Harmonizome 3.0

From Encyclopedia of DNA Elements

Histone site modification profiles for cell lines from ENCODE

From Roadmap Epigenomics

Histone modification profiles for primary cells and tissues

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A-like 4G

Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Predicted to be active in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

peptidyl-tRNA hydrolase 2

The protein encoded by this gene is a mitochondrial protein with two putative domains, an N-terminal mitochondrial localization sequence, and a UPF0099 domain. In vitro assays suggest that this protein possesses peptidyl-tRNA hydrolase activity, to release the peptidyl moiety from tRNA, thereby preventing the accumulation of dissociated peptidyl-tRNA that could reduce the efficiency of translation. This protein also plays a role regulating cell survival and death. It promotes survival as part of an integrin-signaling pathway for cells attached to the extracellular matrix (ECM), but also promotes apoptosis in cells that have lost their attachment to the ECM, a process called anoikos. After loss of cell attachment to the ECM, this protein is phosphorylated, is released from the mitochondria into the cytosol, and promotes caspase-independent apoptosis through interactions with transcriptional regulators. This gene has been implicated in the development and progression of tumors, and mutations in this gene have been associated with an infantile multisystem neurologic, endocrine, and pancreatic disease (INMEPD) characterized by intellectual disability, postnatal microcephaly, progressive cerebellar atrophy, hearing impairment, polyneuropathy, failure to thrive, and organ fibrosis with exocrine pancreas insufficiency (PMID: 25574476). Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Mar 2015]

peptidyl-tRNA hydrolase 1 homolog (S. cerevisiae)

Enables aminoacyl-tRNA hydrolase activity. Involved in rescue of stalled ribosome. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

peptidyl-prolyl cis-trans isomerase A-like

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl arginine deiminase, type I

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type I enzyme is involved in the late stages of epidermal differentiation, where it deiminates filaggrin and keratin K1, which maintains hydration of the stratum corneum, and hence the cutaneous barrier function. This enzyme may also play a role in hair follicle formation. This gene exists in a cluster with four other paralogous genes. [provided by RefSeq, Jul 2008]

peptidyl arginine deiminase, type III

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type III enzyme modulates hair structural proteins, such as filaggrin in the hair follicle and trichohyalin in the inner root sheath, during hair follicle formation. Together with the type I enzyme, this enzyme may also play a role in terminal differentiation of the epidermis. This gene exists in a cluster with four other paralogous genes. [provided by RefSeq, Jul 2008]

peptidyl arginine deiminase, type II

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages. This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous genes. [provided by RefSeq, Jul 2008]

peptidyl arginine deiminase, type IV

This gene is a member of a gene family which encodes enzymes responsible for the conversion of arginine residues to citrulline residues. This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response. [provided by RefSeq, Jul 2008]

peptidyl arginine deiminase, type VI

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. This protein may play a role in cytoskeletal reorganization in the egg and in early embryo development. [provided by RefSeq, Sep 2012]

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase FKBP4 pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

angiotensin I converting enzyme (peptidyl-dipeptidase A) 3, pseudogene

Predicted to be located in acrosomal vesicle. [provided by Alliance of Genome Resources, Mar 2025]

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-tRNA hydrolase domain containing 1

This gene encodes the enzyme peptidyl-tRNA hydrolase. Peptidyl-tRNA hydrolases perform the essential function of recycling peptidyl-tRNAs. Mutations in this gene are associated with autosomal-recessive intellectual disability and parkinsonism. [provided by RefSeq, May 2017]

peptidyl-prolyl cis-trans isomerase A pseudogene

peptidyl-prolyl cis-trans isomerase A pseudogene

arginine-glutamic acid dipeptide (RE) repeats pseudogene 3

lysophosphatidic acid receptor 1

The integral membrane protein encoded by this gene is a lysophosphatidic acid (LPA) receptor from a group known as EDG receptors. These receptors are members of the G protein-coupled receptor superfamily. Utilized by LPA for cell signaling, EDG receptors mediate diverse biologic functions, including proliferation, platelet aggregation, smooth muscle contraction, inhibition of neuroblastoma cell differentiation, chemotaxis, and tumor cell invasion. Many transcript variants encoding a few different isoforms have been identified for this gene. [provided by RefSeq, Oct 2020]

sphingomyelin phosphodiesterase 1, acid lysosomal

The protein encoded by this gene is a lysosomal acid sphingomyelinase that converts sphingomyelin to ceramide. The encoded protein also has phospholipase C activity. Defects in this gene are a cause of Niemann-Pick disease type A (NPA) and Niemann-Pick disease type B (NPB). Multiple transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2010]

sialic acid binding Ig-like lectin 27, pseudogene

gamma-aminobutyric acid (GABA) B receptor, 1

This gene encodes a receptor for gamma-aminobutyric acid (GABA), which is the main inhibitory neurotransmitter in the mammalian central nervous system. This receptor functions as a heterodimer with GABA(B) receptor 2. Defects in this gene may underlie brain disorders such as schizophrenia and epilepsy. Alternative splicing generates multiple transcript variants, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Jan 2016]

N-acetylneuraminic acid phosphatase pseudogene

cellular retinoic acid binding protein 1

This gene encodes a specific binding protein for a vitamin A family member and is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. It is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. [provided by RefSeq, Jul 2008]

lipoic acid synthetase

The protein encoded by this gene belongs to the biotin and lipoic acid synthetases family. Localized in the mitochondrion, this iron-sulfur enzyme catalyzes the final step in the de novo pathway for the biosynthesis of lipoic acid, a potent antioxidant. The deficient expression of this enzyme has been linked to conditions such as diabetes, atherosclerosis and neonatal-onset epilepsy. Alternative splicing occurs at this locus, and several transcript variants encoding distinct isoforms have been identified. [provided by RefSeq, Aug 2020]

sialic acid binding Ig-like lectin 30, pseudogene

stimulated by retinoic acid 6

The protein encoded by this gene is a membrane protein involved in the metabolism of retinol. The encoded protein acts as a receptor for retinol/retinol binding protein complexes. This protein removes the retinol from the complex and transports it across the cell membrane. Defects in this gene are a cause of syndromic microphthalmia type 9 (MCOPS9). Several transcript variants encoding a few different isoforms have been found for this gene. [provided by RefSeq, Dec 2008]

sialic acid binding Ig-like lectin 16 (gene/pseudogene)

Predicted to enable sialic acid binding activity. Involved in positive regulation of defense response to bacterium and positive regulation of interleukin-6 production. Predicted to be located in membrane. Predicted to be active in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid binding Ig-like lectin 14

Predicted to enable sialic acid binding activity. Predicted to be involved in cell adhesion. Predicted to be located in ficolin-1-rich granule membrane and tertiary granule membrane. Predicted to be active in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid binding Ig-like lectin 15

Predicted to be involved in regulation of actin cytoskeleton organization; regulation of bone resorption; and regulation of osteoclast development. Predicted to be located in membrane. Predicted to be part of protein-containing complex. Predicted to be active in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid binding Ig-like lectin 12 (gene/pseudogene)

Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. This gene encodes a member of the SIGLEC3-like subfamily of SIGLECs. Members of this subfamily are characterized by an extracellular V-set immunoglobulin-like domain followed by two C2-set immunoglobulin-like domains, and the cytoplasmic tyrosine-based motifs ITIM and SLAM-like. The encoded protein, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor. This gene is located in a cluster with other SIGLEC3-like genes on 19q13.4. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2013]

sialic acid binding Ig-like lectin 10

SIGLECs are members of the immunoglobulin superfamily that are expressed on the cell surface. Most SIGLECs have 1 or more cytoplasmic immune receptor tyrosine-based inhibitory motifs, or ITIMs. SIGLECs are typically expressed on cells of the innate immune system, with the exception of the B-cell expressed SIGLEC6 (MIM 604405).[supplied by OMIM, Jul 2002]

sialic acid binding Ig-like lectin 11

This gene encodes a member of the sialic acid-binding immunoglobulin-like lectin family. These cell surface lectins are characterized by structural motifs in the immunoglobulin (Ig)-like domains and sialic acid recognition sites in the first Ig V set domain. This family member mediates anti-inflammatory and immunosuppressive signaling. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011]

CCHC-type zinc finger, nucleic acid binding protein

This gene encodes a nucleic-acid binding protein with seven zinc-finger domains. The protein has a preference for binding single stranded DNA and RNA. The protein functions in cap-independent translation of ornithine decarboxylase mRNA, and may also function in sterol-mediated transcriptional regulation. A CCTG expansion from <30 repeats to 75-11000 repeats in the first intron of this gene results in myotonic dystrophy type 2. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2016]

solute carrier family 23 (ascorbic acid transporter), member 2

The absorption of vitamin C into the body and its distribution to organs requires two sodium-dependent vitamin C transporters. This gene encodes one of the two required transporters and the encoded protein accounts for tissue-specific uptake of vitamin C. Previously, this gene had an official symbol of SLC23A1. [provided by RefSeq, Jul 2008]

glucosidase, beta, acid pseudogene 1

N-acetylneuraminic acid phosphatase pseudogene

fatty acid amide hydrolase pseudogene 1

sialic acid binding Ig-like lectin 22, pseudogene

N-acetylneuraminic acid phosphatase pseudogene

fatty acid binding protein 7, brain pseudogene 2

fatty acid binding protein 7, brain pseudogene 1

fragile site, folic acid type, rare, fra(7)(p11.2)

transfer RNA glutamic acid (anticodon UUC)

This record serves to anchor the annotations of this class of tRNAs at multiple locations on the human genome. The placements are predicted using tRNAscan-SE (Lowe, T.M. and Eddy, S.R. 1997. Nucleic Acids Res. 25:955-964, PubMed 9023104).

gamma-aminobutyric acid (GABA) A receptor, rho 1

GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA receptors, which are ligand-gated chloride channels. GABRR1 is a member of the rho subunit family. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2012]

gamma-aminobutyric acid (GABA) A receptor, rho 2

Gamma-aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA receptors, which are ligand-gated chloride channels. The protein encoded by this gene is a member of the rho subunit family and is a component of the GABA type A receptor complex. This gene exists on chromosome 6q next to the gene encoding the rho 1 subunit of the GABA type A receptor, in a region thought to be associated with susceptibility for psychiatric disorders and epilepsy. Polymorphisms in this gene may also be associated with alcohol dependence, and general cognitive ability. [provided by RefSeq, Apr 2016]

gamma-aminobutyric acid (GABA) A receptor, rho 3 (gene/pseudogene)

The neurotransmitter gamma-aminobutyric acid (GABA) functions in the central nervous system to regulate synaptic transmission of neurons. This gene encodes one of three related subunits, which combine as homo- or hetero-pentamers to form GABA(C) receptors. In humans, some individuals contain a single-base polymorphism (dbSNP rs832032) that is predicted to inactivate the gene product. [provided by RefSeq, Jan 2012]

fatty acid synthase

The enzyme encoded by this gene is a multifunctional protein. Its main function is to catalyze the synthesis of palmitate from acetyl-CoA and malonyl-CoA, in the presence of NADPH, into long-chain saturated fatty acids. In some cancer cell lines, this protein has been found to be fused with estrogen receptor-alpha (ER-alpha), in which the N-terminus of FAS is fused in-frame with the C-terminus of ER-alpha. [provided by RefSeq, Jul 2008]

insulin-like growth factor binding protein, acid labile subunit

The protein encoded by this gene is a serum protein that binds insulin-like growth factors, increasing their half-life and their vascular localization. Production of the encoded protein, which contains twenty leucine-rich repeats, is stimulated by growth hormone. Defects in this gene are a cause of acid-labile subunit deficiency, which maifests itself in a delayed and slow puberty. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Mar 2009]

retinoic acid receptor, alpha

This gene represents a nuclear retinoic acid receptor. The encoded protein, retinoic acid receptor alpha, regulates transcription in a ligand-dependent manner. This gene has been implicated in regulation of development, differentiation, apoptosis, granulopoeisis, and transcription of clock genes. Translocations between this locus and several other loci have been associated with acute promyelocytic leukemia. Alternatively spliced transcript variants have been found for this locus.[provided by RefSeq, Sep 2010]

retinoic acid receptor, beta

This gene encodes retinoic acid receptor beta, a member of the thyroid-steroid hormone receptor superfamily of nuclear transcriptional regulators. This receptor localizes to the cytoplasm and to subnuclear compartments. It binds retinoic acid, the biologically active form of vitamin A which mediates cellular signalling in embryonic morphogenesis, cell growth and differentiation. It is thought that this protein limits growth of many cell types by regulating gene expression. The gene was first identified in a hepatocellular carcinoma where it flanks a hepatitis B virus integration site. Alternate promoter usage and differential splicing result in multiple transcript variants. [provided by RefSeq, Mar 2014]

fragile site, folic acid type, rare, fra(10)(q23.3) or fra(10)(q24.2)

retinoic acid receptor, gamma

This gene encodes a retinoic acid receptor that belongs to the nuclear hormone receptor family. Retinoic acid receptors (RARs) act as ligand-dependent transcriptional regulators. When bound to ligands, RARs activate transcription by binding as heterodimers to the retinoic acid response elements (RARE) found in the promoter regions of the target genes. In their unbound form, RARs repress transcription of their target genes. RARs are involved in various biological processes, including limb bud development, skeletal growth, and matrix homeostasis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011]

gamma-aminobutyric acid (GABA) A receptor, beta 1

The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A receptor, beta 1 subunit. It is mapped to chromosome 4p12 in a cluster comprised of genes encoding alpha 4, alpha 2 and gamma 1 subunits of the GABA A receptor. Alteration of this gene is implicated in the pathogenetics of schizophrenia. [provided by RefSeq, Jul 2008]

gamma-aminobutyric acid (GABA) A receptor, beta 3

This gene encodes a member of the ligand-gated ionic channel family. The encoded protein is one the subunits of a multi-subunit chloride channel that serves as the receptor for gamma-aminobutyric acid, a major inhibitory neurotransmitter of the mammalian nervous system. This gene is located on the long arm of chromosome 15 in a cluster with two other genes encoding related subunits of the family. This gene may be associated with the pathogenesis of several disorders including Angelman syndrome, Prader-Willi syndrome, nonsyndromic orofacial clefts, epilepsy and autism. Alternatively spliced transcript variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2013]

fragile site, folic acid type, rare, fra(2)(q13)

fragile site, folic acid type, rare, fra(2)(q11.2)

fragile site, folic acid type, rare, fra(2)(q22.3)

N-acetylneuraminic acid phosphatase

Enables N-acylneuraminate-9-phosphatase activity. Involved in CMP-N-acetylneuraminate biosynthetic process; N-acetylneuraminate biosynthetic process; and glycosylation. Predicted to be active in cytosol. [provided by Alliance of Genome Resources, Mar 2025]

N-acetylneuraminic acid synthase

This gene encodes an enzyme that functions in the biosynthetic pathways of sialic acids. In vitro, the encoded protein uses N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), respectively; however, it exhibits much higher activity toward the Neu5Ac phosphate product. In insect cells, expression of this gene results in Neu5Ac and KDN production. This gene is related to the E. coli sialic acid synthase gene neuB, and it can partially restore sialic acid synthase activity in an E. coli neuB-negative mutant. [provided by RefSeq, Jul 2008]

cellular retinoic acid binding protein 2

This gene encodes a member of the retinoic acid (RA, a form of vitamin A) binding protein family and lipocalin/cytosolic fatty-acid binding protein family. The protein is a cytosol-to-nuclear shuttling protein, which facilitates RA binding to its cognate receptor complex and transfer to the nucleus. It is involved in the retinoid signaling pathway, and is associated with increased circulating low-density lipoprotein cholesterol. Alternatively spliced transcript variants encoding the same protein have been found for this gene.[provided by RefSeq, Dec 2010]

retinoic acid induced 1

This gene is located within the Smith-Magenis syndrome region on chromosome 17. It is highly similar to its mouse counterpart and is expressed at high levels mainly in neuronal tissues. The protein encoded by this gene includes a polymorphic polyglutamine tract in the N-terminal domain. Expression of the mouse counterpart in neurons is induced by retinoic acid. This gene is associated with both the severity of the phenotype and the response to medication in schizophrenic patients. [provided by RefSeq, Jul 2008]

sialic acid binding Ig-like lectin 25, pseudogene

fatty acid amide hydrolase 2

This gene encodes a fatty acid amide hydrolase that shares a conserved protein motif with the amidase signature family of enzymes. The encoded enzyme is able to catalyze the hydrolysis of a broad range of bioactive lipids, including those from the three main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. This enzyme has a preference for monounsaturated acyl chains as a substrate. Alternate splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2017]

glucosidase, beta (bile acid) 2

This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Studies to determine subcellular localization of this protein in the liver indicated that the enzyme was mainly enriched in the microsomal fraction where it appeared to be confined to the endoplasmic reticulum. This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism. [provided by RefSeq, Jul 2008]

glucosidase, beta, acid 3 (gene/pseudogene)

The protein encoded by this gene is a cytosolic enzyme that can hydrolyze several types of glycosides. The enzyme has its highest activity at neutral pH and is predominantly expressed in human liver, kidney, intestine, and spleen. This gene is a polymorphic pseudogene, with the most common allele being the functional allele that encodes the full-length protein. Some individuals contain a single nucleotide polymorphism that results in a premature stop codon in the coding region, and therefore this allele is pseudogenic due to the failure to produce a functional full-length protein. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Apr 2022]

gamma-aminobutyric acid (GABA) A receptor, theta

The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes the theta subunit of the GABA A receptor. The gene is mapped to chromosome Xq28 in a cluster of genes including those that encode the alpha 3 and epsilon subunits of the GABA A receptor. [provided by RefSeq, Jul 2017]

gamma-aminobutyric acid (GABA) A receptor, pi

The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. The subunit encoded by this gene is expressed in several non-neuronal tissues including the uterus and ovaries. This subunit can assemble with known GABA A receptor subunits, and the presence of this subunit alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2014]

gamma-aminobutyric acid (GABA) A receptor, epsilon

The product of this gene belongs to the ligand-gated ionic channel (TC 1.A.9) family. It encodes the gamma-aminobutyric acid (GABA) A receptor which is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes an epsilon subunit. It is mapped to chromosome Xq28 in a cluster comprised of genes encoding alpha 3, beta 4 and theta subunits of the same receptor. Alternatively spliced transcript variants have been identified, but only one is thought to encode a protein. [provided by RefSeq, Oct 2008]

gamma-aminobutyric acid (GABA) A receptor, delta

Gamma-aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. The GABA-A receptor is generally pentameric and there are five types of subunits: alpha, beta, gamma, delta, and rho. This gene encodes the delta subunit. Mutations in this gene have been associated with susceptibility to generalized epilepsy with febrile seizures, type 5. Alternatively spliced transcript variants have been described for this gene, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]

tRNA aspartic acid methyltransferase 1

This gene encodes a protein responsible for the methylation of aspartic acid transfer RNA, specifically at the cytosine-38 residue in the anticodon loop. This enzyme also possesses residual DNA-(cytosine-C5) methyltransferase activity. While similar in sequence and structure to DNA cytosine methyltransferases, this gene is distinct and highly conserved in its function among taxa. [provided by RefSeq, Jun 2010]

hydroxycarboxylic acid receptor 3

Predicted to enable GTP binding activity; nicotinic acid receptor activity; and purinergic nucleotide receptor activity. Predicted to be involved in G protein-coupled receptor signaling pathway. Located in cell junction. [provided by Alliance of Genome Resources, Mar 2025]

hydroxycarboxylic acid receptor 2

Predicted to enable nicotinic acid receptor activity. Involved in neutrophil apoptotic process and positive regulation of neutrophil apoptotic process. Located in cell junction and plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

hydroxycarboxylic acid receptor 1

G protein-coupled receptors (GPCRs, or GPRs), such as GPR81, contain 7 transmembrane domains and transduce extracellular signals through heterotrimeric G proteins.[supplied by OMIM, Feb 2005]

cysteine sulfinic acid decarboxylase

This gene encodes a member of the group 2 decarboxylase family. A similar protein in rodents plays a role in multiple biological processes as the rate-limiting enzyme in taurine biosynthesis, catalyzing the decarboxylation of cysteinesulfinate to hypotaurine. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Sep 2011]

solute carrier family 27 (fatty acid transporter), member 5

The protein encoded by this gene is an isozyme of very long-chain acyl-CoA synthetase (VLCS). It is capable of activating very long-chain fatty-acids containing 24- and 26-carbons. It is expressed in liver and associated with endoplasmic reticulum but not with peroxisomes. Its primary role is in fatty acid elongation or complex lipid synthesis rather than in degradation. This gene has a mouse ortholog. [provided by RefSeq, Jul 2008]

solute carrier family 27 (fatty acid transporter), member 4

This gene encodes a member of a family of fatty acid transport proteins, which are involved in translocation of long-chain fatty acids cross the plasma membrane. This protein is expressed at high levels on the apical side of mature enterocytes in the small intestine, and appears to be the principal fatty acid transporter in enterocytes. Clinical studies suggest this gene as a candidate gene for the insulin resistance syndrome. Mutations in this gene have been associated with ichthyosis prematurity syndrome. [provided by RefSeq, Apr 2010]

solute carrier family 27 (fatty acid transporter), member 6

This gene encodes a member of the fatty acid transport protein family (FATP). FATPs are involved in the uptake of long-chain fatty acids and have unique expression patterns. Alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

solute carrier family 27 (fatty acid transporter), member 3

This gene belongs to a family of integral membrane proteins and encodes a protein that is involved in lipid metabolism. The increased expression of this gene in human neural stem cells derived from induced pluripotent stem cells suggests that it plays an important role in early brain development. Naturally occurring mutations in this gene are associated with autism spectrum disorders. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2017]

solute carrier family 27 (fatty acid transporter), member 2

The protein encoded by this gene is an isozyme of long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme activates long-chain, branched-chain and very-long-chain fatty acids containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney, and is present in both endoplasmic reticulum and peroxisomes, but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked adrenoleukodystrophy. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2009]

lysophosphatidic acid receptor 2

This gene encodes a member of family I of the G protein-coupled receptors, as well as the EDG family of proteins. This protein functions as a lysophosphatidic acid (LPA) receptor and contributes to Ca2+ mobilization, a critical cellular response to LPA in cells, through association with Gi and Gq proteins. An alternative splice variant has been described but its full length sequence has not been determined. [provided by RefSeq, Jul 2008]

lysophosphatidic acid receptor 3

This gene encodes a member of the G protein-coupled receptor family, as well as the EDG family of proteins. This protein functions as a cellular receptor for lysophosphatidic acid and mediates lysophosphatidic acid-evoked calcium mobilization. This receptor couples predominantly to G(q/11) alpha proteins. [provided by RefSeq, Jul 2008]

lysophosphatidic acid receptor 6

The protein encoded by this gene belongs to the family of G-protein coupled receptors, that are preferentially activated by adenosine and uridine nucleotides. This gene aligns with an internal intron of the retinoblastoma susceptibility gene in the reverse orientation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2009]

lysophosphatidic acid receptor 4

This gene encodes a member of the lysophosphatidic acid receptor family. It may also be related to the P2Y receptors, a family of receptors that bind purine and pyrimidine nucleotides and are coupled to G proteins. The encoded protein may play a role in monocytic differentiation. [provided by RefSeq, Feb 2009]

lysophosphatidic acid receptor 5

This gene encodes a member of the rhodopsin class of G protein-coupled transmembrane receptors. This protein transmits extracellular signals from lysophosphatidic acid to cells through heterotrimeric G proteins and mediates numerous cellular processes. Many G protein receptors serve as targets for pharmaceutical drugs. Transcript variants of this gene have been described.[provided by RefSeq, Dec 2008]

fatty acid desaturase 1

The protein encoded by this gene is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization. [provided by RefSeq, Jul 2008]

fatty acid desaturase 3

The protein encoded by this gene is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization. [provided by RefSeq, Jul 2008]

fatty acid desaturase 2

The protein encoded by this gene is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2013]

fatty acid desaturase 6

Predicted to enable oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water. Predicted to be involved in lipid metabolic process. Predicted to be located in membrane. [provided by Alliance of Genome Resources, Mar 2025]

fatty acid binding protein 5 pseudogene 1

fatty acid binding protein 5 pseudogene 3

Predicted to enable fatty acid binding activity. Predicted to be involved in fatty acid transport. Predicted to be active in cytosol and nucleus. [provided by Alliance of Genome Resources, Mar 2025]

fatty acid binding protein 5 pseudogene 2

fatty acid binding protein 5 pseudogene 5

fatty acid binding protein 5 pseudogene 4

fatty acid binding protein 5 pseudogene 7

fatty acid binding protein 5 pseudogene 6

fatty acid binding protein 5 pseudogene 9

fatty acid binding protein 5 pseudogene 8

G protein-coupled bile acid receptor 1

This gene encodes a member of the G protein-coupled receptor (GPCR) superfamily. This enzyme functions as a cell surface receptor for bile acids. Treatment of cells expressing this GPCR with bile acids induces the production of intracellular cAMP, activation of a MAP kinase signaling pathway, and internalization of the receptor. The receptor is implicated in the suppression of macrophage functions and regulation of energy homeostasis by bile acids. Alternative splicing results in multiple transcript variants encoding the same protein. [provided by RefSeq, Jul 2008]

sialic acid binding Ig-like lectin 28, pseudogene

N-acylsphingosine amidohydrolase (acid ceramidase) 1

This gene encodes a member of the acid ceramidase family of proteins. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed. Processing of this preproprotein generates alpha and beta subunits that heterodimerize to form the mature lysosomal enzyme, which catalyzes the degradation of ceramide into sphingosine and free fatty acid. This enzyme is overexpressed in multiple human cancers and may play a role in cancer progression. Mutations in this gene are associated with the lysosomal storage disorder, Farber lipogranulomatosis, and a neuromuscular disorder, spinal muscular atrophy with progressive myoclonic epilepsy. [provided by RefSeq, Oct 2015]

gamma-aminobutyric acid (GABA) A receptor, gamma 3

This gene encodes a gamma-aminobutyric acid (GABA) receptor. GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. GABA-A receptors are pentameric, consisting of proteins from several subunit classes: alpha, beta, gamma, delta and rho. The protein encoded by this gene is a gamma subunit, which contains the benzodiazepine binding site. Two transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Aug 2012]

gamma-aminobutyric acid (GABA) A receptor, gamma 2

This gene encodes a gamma-aminobutyric acid (GABA) receptor. GABA is the major inhibitory neurotransmitter in the mammlian brain, where it acts at GABA-A receptors, which are ligand-gated chloride channels. GABA-A receptors are pentameric, consisting of proteins from several subunit classes: alpha, beta, gamma, delta and rho. Mutations in this gene have been associated with epilepsy and febrile seizures. Multiple transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]

gamma-aminobutyric acid (GABA) A receptor, gamma 1

The protein encoded by this gene belongs to the ligand-gated ionic channel family. It is an integral membrane protein and plays an important role in inhibiting neurotransmission by binding to the benzodiazepine receptor and opening an integral chloride channel. This gene is clustered with three other family members on chromosome 4. [provided by RefSeq, Jul 2008]

sialic acid binding Ig-like lectin 20, pseudogene

retinoic acid receptor responder (tazarotene induced) 2

This gene encodes a secreted chemotactic protein that initiates chemotaxis via the ChemR23 G protein-coupled seven-transmembrane domain ligand. Expression of this gene is upregulated by the synthetic retinoid tazarotene and occurs in a wide variety of tissues. The active protein has several roles, including that as an adipokine and as an antimicrobial protein with activity against bacteria and fungi. [provided by RefSeq, Nov 2014]

retinoic acid receptor responder (tazarotene induced) 3

Retinoids exert biologic effects such as potent growth inhibitory and cell differentiation activities and are used in the treatment of hyperproliferative dermatological diseases. These effects are mediated by specific nuclear receptor proteins that are members of the steroid and thyroid hormone receptor superfamily of transcriptional regulators. RARRES1, RARRES2, and RARRES3 are genes whose expression is upregulated by the synthetic retinoid tazarotene. RARRES3 is thought act as a tumor suppressor or growth regulator. [provided by RefSeq, Jul 2008]

retinoic acid receptor responder (tazarotene induced) 1

This gene was identified as a retinoid acid (RA) receptor-responsive gene. It encodes a type 1 membrane protein. The expression of this gene is upregulated by tazarotene as well as by retinoic acid receptors. The expression of this gene is found to be downregulated in prostate cancer, which is caused by the methylation of its promoter and CpG island. Alternatively spliced transcript variant encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]

sialic acid acetylesterase

This gene encodes an enzyme which removes 9-O-acetylation modifications from sialic acids. Mutations in this gene are associated with susceptibility to autoimmune disease 6. Multiple transcript variants encoding different isoforms, found either in the cytosol or in the lysosome, have been found for this gene.[provided by RefSeq, Feb 2011]

fragile site, folic acid type, rare, fra(5)(q35)

retinoic acid receptor responder protein 2 pseudogene

ATH1, acid trehalase-like 1 (yeast)

Enables protein-glucosylgalactosylhydroxylysine glucosidase activity. Involved in carbohydrate metabolic process. Located in cytosol. [provided by Alliance of Genome Resources, Mar 2025]

fatty acid binding protein 5 pseudogene 15

fatty acid binding protein 5 pseudogene 14

fatty acid binding protein 5 pseudogene 10

fatty acid binding protein 5 pseudogene 12

nucleic acid binding protein 2

Single-stranded DNA (ssDNA)-binding proteins, such as OBFC2B, are ubiquitous and essential for a variety of DNA metabolic processes, including replication, recombination, and detection and repair of damage (Richard et al., 2008 [PubMed 18449195]).[supplied by OMIM, Jun 2008]

nucleic acid binding protein 1

Single-stranded DNA (ssDNA)-binding proteins, such as OBFC2A, are ubiquitous and essential for a variety of DNA metabolic processes, including replication, recombination, and detection and repair of damage (Richard et al., 2008 [PubMed 18449195]).[supplied by OMIM, Jun 2008]

solute carrier family 27 (fatty acid transporter), member 1

Enables biotin transmembrane transporter activity; efflux transmembrane transporter activity; and long-chain fatty acid transmembrane transporter activity. Involved in several processes, including glycerophospholipid biosynthetic process; lipid transport across blood-brain barrier; and monocarboxylic acid transport. Located in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

fragile site, folic acid type, rare, fra(16)(p13.11)

There are several phenotypes associated with variation in pericentric region of chromosome 16: see the 16p12.2-p11.2 deletion syndrome (MIM 613604); see MIM 611913 for a deletion or duplication at 16p11.2 associated with autism (AUTS14); and see MIM 613444 for a 220-kb deletion at 16p11.2 associated with isolated severe early-onset obesity and obesity with developmental delay.[supplied by OMIM, Nov 2010]

all-trans retinoic acid-induced differentiation factor

This gene is thought to be involved in apoptosis, and may also be involved in hematopoietic development and differentiation. The use of alternative splice sites and promotors result in multiple transcript variants encoding different isoforms.[provided by RefSeq, Dec 2009]

solute carrier family 10 (sodium/bile acid cotransporter), member 2

This gene encodes a sodium/bile acid cotransporter. This transporter is the primary mechanism for uptake of intestinal bile acids by apical cells in the distal ileum. Bile acids are the catabolic product of cholesterol metabolism, so this protein is also critical for cholesterol homeostasis. Mutations in this gene cause primary bile acid malabsorption (PBAM); muatations in this gene may also be associated with other diseases of the liver and intestines, such as familial hypertriglyceridemia (FHTG). [provided by RefSeq, Mar 2010]

solute carrier family 10 (sodium/bile acid cotransporter), member 6

Predicted to enable bile acid:sodium symporter activity. Predicted to be involved in bile acid and bile salt transport. Predicted to be located in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid-binding Ig-like lectin 14

pipecolic acid oxidase

Enables L-pipecolate oxidase activity and sarcosine oxidase activity. Involved in L-lysine catabolic process to acetyl-CoA via L-pipecolate. Located in peroxisome. [provided by Alliance of Genome Resources, Mar 2025]

transfer RNA glutamic acid (anticodon CUC)

This record serves to anchor the annotations of this class of tRNAs at multiple locations on the human genome. The placements are predicted using tRNAscan-SE (Lowe, T.M. and Eddy, S.R. 1997. Nucleic Acids Res. 25:955-964, PubMed 9023104).

Uric acid concentration, serum, QTL6

Uric acid concentration, serum, QTL5

Uric acid concentration, serum, QTL4

Uric acid concentration, serum, QTL3

fatty acid binding protein 12

Predicted to enable fatty acid binding activity. Predicted to be involved in fatty acid transport. Predicted to be active in cytosol and nucleus. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid binding Ig-like lectin 17, pseudogene

fragile site, folic acid type, rare, fra(8)(q22.3)

glucosidase, beta, acid

This gene encodes a lysosomal membrane protein that cleaves the beta-glucosidic linkage of glycosylceramide, an intermediate in glycolipid metabolism. Mutations in this gene cause Gaucher disease, a lysosomal storage disease characterized by an accumulation of glucocerebrosides. A related pseudogene is approximately 12 kb downstream of this gene on chromosome 1. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2010]

mitochondria-localized glutamic acid-rich protein

Predicted to be involved in several processes, including axonal transport; cellular response to gonadotropin-releasing hormone; and nervous system development. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidic acid phosphatase type 2C

The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is similar to phosphatidic acid phosphatase type 2A (PPAP2A) and type 2B (PPAP2B). All three proteins contain 6 transmembrane regions, and a consensus N-glycosylation site. This protein has been shown to possess membrane associated PAP activity. Three alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

phosphatidic acid phosphatase type 2B

The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is a membrane glycoprotein localized at the cell plasma membrane. It has been shown to actively hydrolyze extracellular lysophosphatidic acid and short-chain phosphatidic acid. The expression of this gene is found to be enhanced by epidermal growth factor in Hela cells. [provided by RefSeq, Mar 2010]

phosphatidic acid phosphatase type 2A

The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in synthesis of glycerolipids and in phospholipase D-mediated signal transduction. This enzyme is an integral membrane glycoprotein that plays a role in the hydrolysis and uptake of lipids from extracellular space. Alternate splicing results in multiple transcript variants of this gene. [provided by RefSeq, May 2013]

1-acylglycerol-3-phosphate O-acyltransferase 6 (lysophosphatidic acid acyltransferase, zeta) pseudogene

stimulated by retinoic acid 8

This gene encodes a retinoic acid-responsive protein. A homologous protein in mouse has been shown to be involved in the regulation of meiotic initiation in both spermatogenesis and oogenesis, though feature differences between the mouse and human proteins suggest that these homologs are not entirely functionally equivalent. It is thought that this gene may play a role in spermatogenesis in humans. [provided by RefSeq, Nov 2010]

bone morphogenetic protein/retinoic acid inducible neural-specific 3

This gene is overexpressed in pituitary tumors but is underexpressed in tongue squamous cell carcinomas, ulcerative colitis, and peri-implantitis. Polymorphisms that increase expression of this gene have been shown to increase vascular inflammation, and an association of this gene with myocardial infarction has been demonstrated. Finally, hypermethylation of this gene may find usefulness as a biomarker for gastric cancer. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015]

bone morphogenetic protein/retinoic acid inducible neural-specific 2

Predicted to be involved in cellular response to retinoic acid; central nervous system neuron differentiation; and negative regulation of mitotic cell cycle. Predicted to act upstream of or within locomotion and nervous system development. Predicted to be located in extracellular region. Predicted to be active in cytoplasm; dendrite; and neuronal cell body. Implicated in oral squamous cell carcinoma. [provided by Alliance of Genome Resources, Mar 2025]

bone morphogenetic protein/retinoic acid inducible neural-specific 1

This gene is located within a chromosomal region that shows loss of heterozygosity in some bladder cancers. It contains a 5' CpG island that may be a frequent target of hypermethylation, and it may undergo hypermethylation-based silencing in some bladder cancers. [provided by RefSeq, Jul 2008]

solute carrier family 9, subfamily C (Na+-transporting carboxylic acid decarboxylase), member 1

Predicted to enable potassium:proton antiporter activity and sodium:proton antiporter activity. Predicted to be involved in potassium ion transmembrane transport; regulation of intracellular pH; and sodium ion import across plasma membrane. Predicted to act upstream of or within flagellated sperm motility. Predicted to be located in membrane and motile cilium. Predicted to be active in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

iron/zinc purple acid phosphatase-like protein

Purple acid phosphatases (PAPs), including PAPL, are a family of binuclear metallohydrolases that have been identified in plants, animals, and fungi (Flanagan et al., 2006 [PubMed 16793224]).[supplied by OMIM, Mar 2008]

fragile site, folic acid type, rare, fra(10)(q23.3) or fra(10)(q24.2) candidate 1

The protein encoded by this gene is a nuclear phosphoprotein of unknown function. This gene contains a tandem CGG repeat region within a CpG island that normally consists of 8-14 repeats but can expand to over 200 repeats. The repeat region is within the 5' UTR of some transcript variants, but is intronic to another variant. The expanded repeat allele is a fragile site and becomes hypermethylated, causing a reduction in gene expression. A disease phenotype has not been associated with expanded alleles. This gene is found within the rare FRA10A folate-sensitive fragile site. [provided by RefSeq, Dec 2016]

transfer RNA aspartic acid (anticodon GUC)

This record serves to anchor the annotations of this class of tRNAs at multiple locations on the human genome. The placements are predicted using tRNAscan-SE (Lowe, T.M. and Eddy, S.R. 1997. Nucleic Acids Res. 25:955-964, PubMed 9023104).

solute carrier family 23 (ascorbic acid transporter), member 1

The absorption of vitamin C into the body and its distribution to organs requires two sodium-dependent vitamin C transporters. This gene encodes one of the two transporters. The encoded protein is active in bulk vitamin C transport involving epithelial surfaces. Previously, this gene had an official symbol of SLC23A2. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2008]

fatty acid binding protein 6, ileal

This gene encodes the ileal fatty acid binding protein. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP6 and FABP1 (the liver fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. Transcript variants generated by alternate transcription promoters and/or alternate splicing have been found for this gene. [provided by RefSeq, Jul 2008]

fatty acid binding protein 7, brain

The gene encodes a small, highly conserved cytoplasmic protein that bind long-chain fatty acids and other hydrophobic ligands. The encoded protein is important in the establishment of the radial glial fiber in the developing brain. Alternative splicing and promoter usage results in multiple transcript variants encoding different isoforms. Pseudogenes of this gene are found on multiple chromosomes. [provided by RefSeq, Jan 2016]

fatty acid binding protein 4, adipocyte

FABP4 encodes the fatty acid binding protein found in adipocytes. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. [provided by RefSeq, Jul 2008]

fatty acid binding protein 5 (psoriasis-associated)

This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs may play roles in fatty acid uptake, transport, and metabolism. Polymorphisms in this gene are associated with type 2 diabetes. The human genome contains many pseudogenes similar to this locus.[provided by RefSeq, Feb 2011]

fatty acid binding protein 2, intestinal

The protein encoded by this gene is an intracellular fatty acid-binding protein that participates in the uptake, intracellular metabolism, and transport of long-chain fatty acids. The encoded protein is also involved in the modulation of cell growth and proliferation. This protein binds saturated long-chain fatty acids with high affinity, and may act as a lipid sensor to maintain energy homeostasis. [provided by RefSeq, Aug 2017]

fatty acid binding protein 3, muscle and heart

The intracellular fatty acid-binding proteins (FABPs) belongs to a multigene family. FABPs are divided into at least three distinct types, namely the hepatic-, intestinal- and cardiac-type. They form 14-15 kDa proteins and are thought to participate in the uptake, intracellular metabolism and/or transport of long-chain fatty acids. They may also be responsible in the modulation of cell growth and proliferation. Fatty acid-binding protein 3 gene contains four exons and its function is to arrest growth of mammary epithelial cells. This gene is a candidate tumor suppressor gene for human breast cancer. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2016]

gamma-aminobutyric acid (GABA) A receptor, alpha 5

GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. Transcript variants utilizing three different alternative non-coding first exons have been described. [provided by RefSeq, Jul 2008]

gamma-aminobutyric acid (GABA) A receptor, alpha 4

Gamma-aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. This gene encodes subunit alpha-4, which is involved in the etiology of autism and eventually increases autism risk through interaction with another subunit, gamma-aminobutyric acid receptor beta-1 (GABRB1). Alternatively spliced transcript variants encoding different isoforms have been found in this gene.[provided by RefSeq, Feb 2011]

gamma-aminobutyric acid (GABA) A receptor, alpha 6

GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. [provided by RefSeq, Jul 2008]

gamma-aminobutyric acid (GABA) A receptor, alpha 1

This gene encodes a gamma-aminobutyric acid (GABA) receptor. GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. GABA-A receptors are pentameric, consisting of proteins from several subunit classes: alpha, beta, gamma, delta and rho. Mutations in this gene cause juvenile myoclonic epilepsy and childhood absence epilepsy type 4. Multiple transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008]

gamma-aminobutyric acid (GABA) A receptor, alpha 3

GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. [provided by RefSeq, Jul 2008]

gamma-aminobutyric acid (GABA) A receptor, alpha 2

GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2013]

sialic acid binding Ig-like lectin 21, pseudogene

sialic acid binding Ig-like lectin 8

Sialic acid-binding immunoglobulin (Ig)-like lectins, or SIGLECs (e.g., CD33 (MIM 159590)), are a family of type 1 transmembrane proteins each having a unique expression pattern, mostly in hemopoietic cells. SIGLEC8 is a member of the CD33-like subgroup of SIGLECs, which are localized to 19q13.3-q13.4 and have 2 conserved cytoplasmic tyrosine-based motifs: an immunoreceptor tyrosine-based inhibitory motif, or ITIM (see MIM 604964), and a motif homologous to one identified in signaling lymphocyte activation molecule (SLAM; MIM 603492) that mediates an association with SLAM-associated protein (SAP; MIM 300490) (summarized by Foussias et al., 2000 [PubMed 11095983]).[supplied by OMIM, May 2010]

sialic acid binding Ig-like lectin 9

Predicted to enable monosaccharide binding activity and sialic acid binding activity. Predicted to be involved in cell adhesion. Predicted to act upstream of or within negative regulation of inflammatory response and negative regulation of phagocytosis, engulfment. Predicted to be located in external side of plasma membrane. Predicted to be active in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid binding Ig-like lectin 5

This gene encodes a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. These cell surface lectins are characterized by structural motifs in the immunoglobulin (Ig)-like domains and sialic acid recognition sites in the first Ig V set domain. The encoded protein is a member of the CD33-related subset of Siglecs and inhibits the activation of several cell types including monocytes, macrophages and neutrophils. Binding of group B Streptococcus (GBS) to the encoded protein plays a role in GBS immune evasion. [provided by RefSeq, Feb 2012]

sialic acid binding Ig-like lectin 6

This gene encodes a member of the SIGLEC (sialic acid binding immunoglobulin-like lectin) family of proteins. The encoded transmembrane receptor binds sialyl-TN glycans and leptin. Placental expression of the encoded protein is upregulated in preeclampsia. [provided by RefSeq, Jul 2016]

sialic acid binding Ig-like lectin 7

Predicted to enable sialic acid binding activity. Predicted to be involved in cell adhesion. Predicted to be located in membrane. Predicted to be active in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid binding Ig-like lectin 1, sialoadhesin

This gene encodes a member of the immunoglobulin superfamily. The encoded protein is a lectin-like adhesion molecule that binds glycoconjugate ligands on cell surfaces in a sialic acid-dependent manner. It is a type I transmembrane protein expressed only by a subpopulation of macrophages and is involved in mediating cell-cell interactions. The protein plays an important role in multiple human diseases and bacterial and viral infections has been shown to enhance SARS-CoV-2 infection. [provided by RefSeq, Dec 2021]

free fatty acid receptor 4

This gene encodes a G protein-coupled receptor (GPR) which belongs to the rhodopsin family of GPRs. The encoded protein functions as a receptor for free fatty acids, including omega-3, and participates in suppressing anti-inflammatory responses and insulin sensitizing. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2012]

retinoic acid early transcript 1K pseudogene

retinoic acid early transcript 1M pseudogene

glucuronic acid epimerase

Enables calcium ion binding activity; heparosan-N-sulfate-glucuronate 5-epimerase activity; and protein homodimerization activity. Involved in heparan sulfate proteoglycan biosynthetic process. Predicted to be located in Golgi membrane. Predicted to be active in Golgi apparatus. Implicated in cerebrovascular disease and hypertension. [provided by Alliance of Genome Resources, Mar 2025]

sialic acid binding Ig-like lectin 26, pseudogene

gamma-aminobutyric acid (GABA) B receptor, 2

The multi-pass membrane protein encoded by this gene belongs to the G-protein coupled receptor 3 family and GABA-B receptor subfamily. The GABA-B receptors inhibit neuronal activity through G protein-coupled second-messenger systems, which regulate the release of neurotransmitters, and the activity of ion channels and adenylyl cyclase. This receptor subunit forms an active heterodimeric complex with GABA-B receptor subunit 1, neither of which is effective on its own. Allelic variants of this gene have been associated with nicotine dependence.[provided by RefSeq, Jan 2010]

sialic acid binding Ig-like lectin 18, pseudogene

fragile site, folic acid type, rare, fra(22)(q13)

glucosidase, alpha; acid

This gene encodes lysosomal alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. The encoded preproprotein is proteolytically processed to generate multiple intermediate forms and the mature form of the enzyme. Defects in this gene are the cause of glycogen storage disease II, also known as Pompe's disease, which is an autosomal recessive disorder with a broad clinical spectrum. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]

fatty acid binding protein 1, liver

This gene encodes the fatty acid binding protein found in liver. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. This protein and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. [provided by RefSeq, Mar 2011]

fragile site, folic acid type, rare, fra(X)(q28) E

fragile site, folic acid type, rare, fra(X)(q27.3) A (macroorchidism, mental retardation)

retinoic acid induced 2

Retinoic acid plays a critical role in development, cellular growth, and differentiation. The specific function of this retinoic acid-induced gene has not yet been determined but it may play a role in development. The chromosomal location of this gene designates it to be a candidate for diseases such as Nance-Horan syndrome, sensorineural deafness, non-specific X-linked cognitive disability, oral-facial-digital syndrome, and Fried syndrome. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Feb 2010]

sialic acid binding Ig-like lectin 31, pseudogene

ribonucleic acid export 1

Mutations in the Schizosaccharomyces pombe Rae1 and Saccharomyces cerevisiae Gle2 genes have been shown to result in accumulation of poly(A)-containing mRNA in the nucleus, suggesting that the encoded proteins are involved in RNA export. The protein encoded by this gene is a homolog of yeast Rae1. It contains four WD40 motifs, and has been shown to localize to distinct foci in the nucleoplasm, to the nuclear rim, and to meshwork-like structures throughout the cytoplasm. This gene is thought to be involved in nucleocytoplasmic transport, and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. Alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

sialic acid binding Ig-like lectin 29, pseudogene

fatty acid 2-hydroxylase

This gene encodes a protein that catalyzes the synthesis of 2-hydroxysphingolipids, a subset of sphingolipids that contain 2-hydroxy fatty acids. Sphingolipids play roles in many cellular processes and their structural diversity arises from modification of the hydrophobic ceramide moiety, such as by 2-hydroxylation of the N-acyl chain, and the existence of many different head groups. Mutations in this gene have been associated with leukodystrophy dysmyelinating with spastic paraparesis with or without dystonia.[provided by RefSeq, Mar 2010]

stimulated by retinoic acid 13

Enables DNA binding activity. Contributes to double-stranded DNA binding activity. Involved in interstrand cross-link repair; replication fork processing; and resolution of meiotic recombination intermediates. Part of chromosome and nucleus. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidic acid phosphatase type 2 domain containing 1B

Enables diacylglycerol diphosphate phosphatase activity and phosphatidate phosphatase activity. Involved in phospholipid dephosphorylation. Predicted to be located in cytoplasm and plasma membrane. Predicted to be active in membrane. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidic acid phosphatase type 2 domain containing 1A

Enables diacylglycerol diphosphate phosphatase activity; identical protein binding activity; and phosphatidate phosphatase activity. Involved in phospholipid dephosphorylation and regulation of calcium ion import. Predicted to be located in plasma membrane. Predicted to be active in membrane. Biomarker of breast cancer. [provided by Alliance of Genome Resources, Mar 2025]

fatty acid desaturase 2 pseudogene 1

Predicted to enable oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water. Predicted to be involved in lipid metabolic process. Predicted to be located in endoplasmic reticulum membrane. [provided by Alliance of Genome Resources, Mar 2025]

fatty acid binding protein 9, testis

Predicted to enable long-chain fatty acid binding activity. Predicted to be involved in long-chain fatty acid transport. Predicted to be located in cytoplasm. Predicted to be active in cytosol and nucleus. [provided by Alliance of Genome Resources, Mar 2025]

retinoic acid receptor responder (tazarotene induced) 2 pseudogene 8

retinoic acid receptor responder (tazarotene induced) 2 pseudogene 2

retinoic acid receptor responder (tazarotene induced) 2 pseudogene 1

retinoic acid receptor responder (tazarotene induced) 2 pseudogene 4

Aromatic alpha-keto acid reductase

free fatty acid receptor 2

This gene encodes a member of the GP40 family of G protein-coupled receptors that are clustered together on chromosome 19. The encoded protein is a receptor for short chain free fatty acids and may be involved in the inflammatory response and in regulating lipid plasma levels. [provided by RefSeq, Apr 2009]

free fatty acid receptor 3

Enables G protein-coupled receptor activity. Involved in adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway and cellular response to fatty acid. Located in plasma membrane. [provided by Alliance of Genome Resources, Mar 2025]

retinoic acid early transcript 1E

This gene belong to the RAET1 family, which consists of major histocompatibility complex (MHC) class I-related genes located in a cluster on chromosome 6q24.2-q25.3. This and RAET1G protein differ from other RAET1 proteins in that they have type I membrane-spanning sequences at their C termini rather than glycosylphosphatidylinositol anchor sequences. This protein functions as a ligand for NKG2D receptor, which is expressed on the surface of several types of immune cells, and is involved in innate and adaptive immune responses. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Aug 2011]

retinoic acid early transcript 1G

This gene encodes a member of the major histocompatibility complex (MHC) class I family of proteins. Although the encoded protein includes C-terminal transmembrane and cytoplasmic domains, proteolytic processing results in the removal of these domains and subsequent tethering to the plasma membrane by a glycosylphosphatidylinositol (GPI)-anchor. The encoded protein is one of several related ligands of the natural killer group 2, member D (NKG2D) receptor, which functions as an activating receptor in innate and adaptive immunity. This gene is present in a gene cluster on chromosome 6. [provided by RefSeq, Jul 2015]

retinoic acid early transcript 1F pseudogene

retinoic acid early transcript 1L

RAET1L belongs to the RAET1 family of major histocompatibility complex (MHC) class I-related genes, which are located within a 180-kb cluster on chromosome 6q24.2-q25.3. The REAT1 genes encode glycoproteins that contain extracellular alpha-1 and alpha-2 domains, but they lack the membrane proximal Ig-like alpha-3 domain. Most RAET1 glycoproteins are anchored to the membrane via glycosylphosphatidylinositol (GPI) linkage (Radosavljevic et al., 2002 [PubMed 11827464]).[supplied by OMIM, Mar 2008]

sphingomyelin phosphodiesterase, acid-like 3B

Enables phosphoric diester hydrolase activity. Predicted to be involved in membrane lipid catabolic process; negative regulation of inflammatory response; and negative regulation of toll-like receptor signaling pathway. Located in extracellular exosome. [provided by Alliance of Genome Resources, Mar 2025]

sphingomyelin phosphodiesterase, acid-like 3A

Enables phosphoric diester hydrolase activity and zinc ion binding activity. Involved in negative regulation of cGAS/STING signaling pathway and nucleoside triphosphate catabolic process. Located in extracellular exosome. Is active in extracellular space. [provided by Alliance of Genome Resources, Mar 2025]

lipase A, lysosomal acid, cholesterol esterase

This gene encodes lipase A, the lysosomal acid lipase (also known as cholesterol ester hydrolase). This enzyme functions in the lysosome to catalyze the hydrolysis of cholesteryl esters and triglycerides. Mutations in this gene can result in Wolman disease and cholesteryl ester storage disease. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jan 2014]

lipase B, lysosomal acid

fragile site, folic acid type, rare, fra(6)(p23)

gamma-aminobutyric acid (GABA) A receptor, beta 2

The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A receptor, beta 2 subunit. It is mapped to chromosome 5q34 in a cluster comprised of genes encoding alpha 1 and gamma 2 subunits of the GABA A receptor. Alternative splicing of this gene generates 2 transcript variants, differing by a 114 bp insertion. [provided by RefSeq, Jul 2008]

proline rich Gla (G-carboxyglutamic acid) 4 (transmembrane)

Enables WW domain binding activity. Predicted to be involved in blood coagulation. Located in plasma membrane. Biomarker of cholangiocarcinoma. [provided by Alliance of Genome Resources, Mar 2025]

proline rich Gla (G-carboxyglutamic acid) 1

This gene encodes a vitamin K-dependent, gamma-carboxyglutamic acid (Gla)-containing, single-pass transmembrane protein. This protein contains a Gla domain at the N-terminus, preceded by a propeptide sequence required for post-translational gamma-carboxylation of specific glutamic acid residues by a vitamin K-dependent gamma-carboxylase. The C-terminus is proline-rich containing PPXY and PXXP motifs found in a variety of signaling and cytoskeletal proteins. This gene is highly expressed in the spinal cord. Several alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Mar 2010]

proline rich Gla (G-carboxyglutamic acid) 2

The protein encoded by this gene is a single-pass transmembrane protein containing an N-terminal gamma-carboxyglutamic acid (Gla) domain and tandem Pro/Leu-Pro-Xaa-Tyr (PY) motifs at its C-terminal end. The Gla domain is exposed on the cell surface while the PY motifs are cytoplasmic. The PY motifs of the encoded protein have been shown to interact with YAP1, a WW domain-containing protein. Therefore, it is thought that the encoded protein may be part of a signal transduction pathway. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2015]

proline rich Gla (G-carboxyglutamic acid) 3 (transmembrane)

This gene encodes a protein which contains a vitamin K-dependent carboxylation/gamma-carboxyglutamic domain. The encoded protein is a member of a family of vitamin K-dependent transmembrane proteins which contain a glutamate-rich extracellular domain. [provided by RefSeq, Aug 2011]

acid phosphatase 5, tartrate resistant

This gene encodes an iron containing glycoprotein which catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. It is the most basic of the acid phosphatases and is the only form not inhibited by L(+)-tartrate. [provided by RefSeq, Aug 2008]

acid phosphatase 6, lysophosphatidic

This gene encodes a member of the histidine acid phosphatase protein family. The encoded protein hydrolyzes lysophosphatidic acid, which is involved in G protein-coupled receptor signaling, lipid raft modulation, and in balancing lipid composition within the cell. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2016]

acid phosphatase 1, soluble

The product of this gene belongs to the phosphotyrosine protein phosphatase family of proteins. It functions as an acid phosphatase and a protein tyrosine phosphatase by hydrolyzing protein tyrosine phosphate to protein tyrosine and orthophosphate. This enzyme also hydrolyzes orthophosphoric monoesters to alcohol and orthophosphate. This gene is genetically polymorphic, and three common alleles segregating at the corresponding locus give rise to six phenotypes. Each allele appears to encode at least two electrophoretically different isozymes, Bf and Bs, which are produced in allele-specific ratios. Multiple alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Aug 2008]

acid phosphatase 2, lysosomal

The protein encoded by this gene belongs to the histidine acid phosphatase family, which hydrolyze orthophosphoric monoesters to alcohol and phosphate. This protein is localized to the lysosomal membrane, and is chemically and genetically distinct from the red cell acid phosphatase. Mice lacking this gene showed multiple defects, including bone structure alterations, lysosomal storage defects, and an increased tendency towards seizures. An enzymatically-inactive allele of this gene in mice showed severe growth retardation, hair-follicle abnormalities, and an ataxia-like phenotype. Alternatively spliced transcript variants have been found for this gene. A C-terminally extended isoform is also predicted to be produced by the use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism. [provided by RefSeq, Oct 2017]

acid phosphatase, testicular

Acid phosphatases are enzymes capable of hydrolyzing orthophosphoric acid esters in an acid medium. This gene is up-regulated by androgens and is down-regulated by estrogens in the prostate cancer cell line. This gene exhibits a lower level of expression in testicular cancer tissues than in normal tissues. The protein encoded by this gene has structural similarity to prostatic and lysosomal acid phosphatases. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]

acid phosphatase, prostate

This gene encodes an enzyme that catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. It is synthesized under androgen regulation and is secreted by the epithelial cells of the prostate gland. An alternatively spliced transcript variant encoding a longer isoform has been found for this gene. This isoform contains a transmembrane domain and is localized in the plasma membrane-endosomal-lysosomal pathway. [provided by RefSeq, Sep 2008]

N-acylethanolamine acid amidase

Enables DNA-binding transcription factor binding activity and hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides. Involved in several processes, including N-acylethanolamine metabolic process; N-acylphosphatidylethanolamine metabolic process; and sphingosine metabolic process. Located in lysosome and membrane. [provided by Alliance of Genome Resources, Mar 2025]

arginine-glutamic acid dipeptide (RE) repeats

This gene encodes a member of the atrophin family of arginine-glutamic acid (RE) dipeptide repeat-containing proteins. The encoded protein co-localizes with a transcription factor in the nucleus, and its overexpression triggers apoptosis. A similar protein in mouse associates with histone deacetylase and is thought to function as a transcriptional co-repressor during embryonic development. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

cytidine monophospho-N-acetylneuraminic acid hydroxylase, pseudogene

Sialic acids are terminal components of the carbohydrate chains of glycoconjugates involved in ligand-receptor, cell-cell, and cell-pathogen interactions. The two most common forms of sialic acid found in mammalian cells are N-acetylneuraminic acid (Neu5Ac) and its hydroxylated derivative, N-glycolylneuraminic acid (Neu5Gc). Studies of sialic acid distribution show that Neu5Gc is not detectable in normal human tissues although it was an abundant sialic acid in other mammals. Neu5Gc is, in actuality, immunogenic in humans. The absense of Neu5Gc in humans is due to a deletion within the human gene CMAH encoding cytidine monophosphate-N-acetylneuraminic acid hydroxylase, an enzyme responsible for Neu5Gc biosynthesis. Sequences encoding the mouse, pig, and chimpanzee hydroxylase enzymes were obtained by cDNA cloning and found to be highly homologous. However, the homologous human cDNA differs from these cDNAs by a 92-bp deletion in the 5' region. This deletion, corresponding to exon 6 of the mouse hydroxylase gene, causes a frameshift mutation and premature termination of the polypeptide chain in human. It seems unlikely that the truncated human hydroxylase mRNA encodes for an active enzyme explaining why Neu5Gc is undetectable in normal human tissues. Human genomic DNA also shows evidence of this deletion which does not occur in the genomes of African great apes. Nonetheless, the CMAH gene maps to 6p21.32 in humans and great apes indicating that mutation of the CMAH gene occurred following human divergence from chimpanzees and bonobos. [provided by RefSeq, Jul 2008]

phosphatidic acid phosphatase type 2 domain containing 3

Predicted to enable sphingosine-1-phosphate phosphatase activity. Predicted to act upstream of or within negative regulation of myotube differentiation. Predicted to be located in endoplasmic reticulum membrane and nucleus. Predicted to be active in membrane and nuclear envelope. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidic acid phosphatase type 2 domain containing 2

Enables isoprenoid diphosphate phosphatase activity and phosphatase activity. Involved in several processes, including phospholipid dephosphorylation; phospholipid metabolic process; and positive regulation of neutrophil activation. Located in endoplasmic reticulum membrane and nuclear membrane. [provided by Alliance of Genome Resources, Mar 2025]

solute carrier family 10 (sodium/bile acid cotransporter), member 1

The protein encoded by this gene belongs to the sodium/bile acid cotransporter family, which are integral membrane glycoproteins that participate in the enterohepatic circulation of bile acids. Two homologous transporters are involved in the reabsorption of bile acids; the ileal sodium/bile acid cotransporter with an apical cell localization that absorbs bile acids from the intestinal lumen, bile duct and kidney, and the liver-specific sodium/bile acid cotransporter, represented by this protein, that is found in the basolateral membranes of hepatocytes. Bile acids are the catabolic product of cholesterol metabolism, hence this protein is important for cholesterol homeostasis. [provided by RefSeq, Oct 2011]

fragile site, folic acid type, rare, fra(11)(q13.3)

branched chain keto acid dehydrogenase E1, beta polypeptide

This gene encodes the E1 beta subunit of branched-chain keto acid dehydrogenase, which is a multienzyme complex associated with the inner membrane of mitochondria. This enzyme complex functions in the catabolism of branched-chain amino acids. Mutations in this gene have been associated with maple syrup urine disease (MSUD), type 1B, a disease characterized by a maple syrup odor to the urine in addition to mental and physical retardation and feeding problems. Alternative splicing at this locus results in multiple transcript variants. [provided by RefSeq, Jan 2016]

branched chain keto acid dehydrogenase E1, alpha polypeptide

The branched-chain alpha-keto acid (BCAA) dehydrogenase (BCKD) complex is an innter mitochondrial enzyme complex that catalyzes the second major step in the catabolism of the branched-chain amino acids leucine, isoleucine, and valine. The BCKD complex consists of three catalytic components: a heterotetrameric (alpha2-beta2) branched-chain alpha-keto acid decarboxylase (E1), a dihydrolipoyl transacylase (E2), and a dihydrolipoamide dehydrogenase (E3). This gene encodes the alpha subunit of the decarboxylase (E1) component. Mutations in this gene result in maple syrup urine disease, type IA. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Sep 2009]

cytidine monophosphate N-acetylneuraminic acid synthetase

This gene encodes an enzyme that converts N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc). This process is important in the formation of sialylated glycoprotein and glycolipids. This modification plays a role in cell-cell communications and immune responses. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]

retinoic acid induced 14

Predicted to enable actin binding activity. Predicted to be involved in cell differentiation and spermatogenesis. Located in cytosol; fibrillar center; and nucleoplasm. [provided by Alliance of Genome Resources, Mar 2025]

fragile site, folic acid type, rare, fra(1)(p21.3)

solute carrier family 35 (CMP-sialic acid transporter), member A1

The protein encoded by this gene is found in the membrane of the Golgi apparatus, where it transports nucleotide sugars into the Golgi. One such nucleotide sugar is CMP-sialic acid, which is imported into the Golgi by the encoded protein and subsequently glycosylated. Defects in this gene are a cause of congenital disorder of glycosylation type 2F (CDG2F). Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Dec 2009]

acid sensing (proton gated) ion channel family member 5

This gene belongs to the amiloride-sensitive Na+ channel and degenerin (NaC/DEG) family, members of which have been identified in many animal species ranging from the nematode to human. The amiloride-sensitive Na(+) channel encoded by this gene is primarily expressed in the small intestine, however, its exact function is not known. [provided by RefSeq, Jul 2008]

acid sensing (proton gated) ion channel family member 4

This gene belongs to the superfamily of acid-sensing ion channels, which are proton-gated, amiloride-sensitive sodium channels. These channels have been implicated in synaptic transmission, pain perception as well as mechanoperception. This gene is predominantly expressed in the pituitary gland, and was considered a candidate for paroxysmal dystonic choreoathetosis (PDC), a movement disorder, however, no correlation was found between mutations in this gene and PDC. [provided by RefSeq, Feb 2012]

acid sensing (proton gated) ion channel 1

This gene encodes a member of the acid-sensing ion channel (ASIC) family of proteins, which are part of the degenerin/epithelial sodium channel (DEG/ENaC) superfamily. Members of the ASIC family are sensitive to amiloride and function in neurotransmission. The encoded proteins function in learning, pain transduction, touch sensation, and development of memory and fear. Alternatively spliced transcript variants have been described. [provided by RefSeq, Feb 2012]

acid sensing (proton gated) ion channel 3

This gene encodes a member of the degenerin/epithelial sodium channel (DEG/ENaC) superfamily. The members of this family are amiloride-sensitive sodium channels that contain intracellular N and C termini, two hydrophobic transmembrane regions, and a large extracellular loop, which has many cysteine residues with conserved spacing. The member encoded by this gene is an acid sensor and may play an important role in the detection of lasting pH changes. In addition, a heteromeric association between this member and acid-sensing (proton-gated) ion channel 2 has been observed as proton-gated channels sensitive to gadolinium. Alternatively spliced transcript variants have been described. [provided by RefSeq, Feb 2012]

acid sensing (proton gated) ion channel 2

This gene encodes a member of the degenerin/epithelial sodium channel (DEG/ENaC) superfamily. The members of this family are amiloride-sensitive sodium channels that contain intracellular N and C termini, 2 hydrophobic transmembrane regions, and a large extracellular loop, which has many cysteine residues with conserved spacing. The member encoded by this gene may play a role in neurotransmission. In addition, a heteromeric association between this member and acid-sensing (proton-gated) ion channel 3 has been observed to co-assemble into proton-gated channels sensitive to gadolinium. Alternative splicing has been observed at this locus and two variants, encoding distinct isoforms, have been identified. [provided by RefSeq, Feb 2012]

fragile site, folic acid type, rare, fra(19)(p13)

sialic acid binding Ig-like lectin 24, pseudogene

fatty acid binding protein 3, pseudogene 2

fragile site, folic acid type, rare, fra(20)(p11.23)

fragile site, folic acid type, rare, fra(9)(q32)

fragile site, folic acid type, rare, fra(9)(p21)

ELOVL fatty acid elongase 6

Fatty acid elongases (EC 6.2.1.3), such as ELOVL6, use malonyl-CoA as a 2-carbon donor in the first and rate-limiting step of fatty acid elongation (Moon et al., 2001 [PubMed 11567032]).[supplied by OMIM, Mar 2008]

ELOVL fatty acid elongase 7

Enables fatty acid elongase activity. Involved in fatty acid elongation, polyunsaturated fatty acid; fatty acid elongation, saturated fatty acid; and very long-chain fatty acid biosynthetic process. Located in endoplasmic reticulum. [provided by Alliance of Genome Resources, Mar 2025]

ELOVL fatty acid elongase 4

This gene encodes a membrane-bound protein which is a member of the ELO family, proteins which participate in the biosynthesis of fatty acids. Consistent with the expression of the encoded protein in photoreceptor cells of the retina, mutations and small deletions in this gene are associated with Stargardt-like macular dystrophy (STGD3) and autosomal dominant Stargardt-like macular dystrophy (ADMD), also referred to as autosomal dominant atrophic macular degeneration. [provided by RefSeq, Jul 2008]

ELOVL fatty acid elongase 5

This gene belongs to the ELO family. It is highly expressed in the adrenal gland and testis, and encodes a multi-pass membrane protein that is localized in the endoplasmic reticulum. This protein is involved in the elongation of long-chain polyunsaturated fatty acids. Mutations in this gene have been associated with spinocerebellar ataxia-38 (SCA38). Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Sep 2014]

ELOVL fatty acid elongase 2

Enables fatty acid elongase activity. Involved in fatty acid elongation, polyunsaturated fatty acid and very long-chain fatty acid biosynthetic process. Located in endoplasmic reticulum. [provided by Alliance of Genome Resources, Mar 2025]

ELOVL fatty acid elongase 3

This gene encodes a protein that belongs to the GNS1/SUR4 family. Members of this family play a role in elongation of long chain fatty acids to provide precursors for synthesis of sphingolipids and ceramides. [provided by RefSeq, Jul 2013]

ELOVL fatty acid elongase 1

Enables fatty acid elongase activity. Involved in fatty acid biosynthetic process and sphingolipid biosynthetic process. Located in endoplasmic reticulum. [provided by Alliance of Genome Resources, Mar 2025]

free fatty acid receptor 1

This gene encodes a member of the GP40 family of G protein-coupled receptors that are clustered together on chromosome 19. The encoded protein is a receptor for medium and long chain free fatty acids and may be involved in the metabolic regulation of insulin secretion. Polymorphisms in this gene may be associated with type 2 diabetes. [provided by RefSeq, Apr 2009]

nucleic acid binding protein 2 pseudogene

fatty acid binding protein 5 pseudogene 11

fatty acid hydroxylase domain containing 2

Predicted to enable C-4 methylsterol oxidase activity. Involved in positive regulation of megakaryocyte differentiation and positive regulation of protein phosphorylation. Located in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

fragile site, folic acid type, rare, fra(12)(q13.1)

FRA12A is a folate-sensitive chromosomal fragile site prone to breakage. No consistent phenotype has been observed with FRA12A, and it can be inherited without phenotypic effect (Berg et al., 2000 [PubMed 10955484]). However, mental retardation with or without other anomalies has been described in patients with over 40% of cells expressing FRA12A (Winnepenninckx et al., 2007).[supplied by OMIM, Mar 2008]

fragile site, folic acid type, rare, fra(12)(q24.13)

fatty acid amide hydrolase

This gene encodes a protein that is responsible for the hydrolysis of a number of primary and secondary fatty acid amides, including the neuromodulatory compounds anandamide and oleamide. [provided by RefSeq, Jul 2008]

acid phosphatase 3

This gene encodes an enzyme that catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. It is synthesized under androgen regulation and is secreted by the epithelial cells of the prostate gland. An alternatively spliced transcript variant encoding a longer isoform has been found for this gene. This isoform contains a transmembrane domain and is localized in the plasma membrane-endosomal-lysosomal pathway. [provided by RefSeq, Sep 2008]

acid phosphatase 4

Acid phosphatases are enzymes capable of hydrolyzing orthophosphoric acid esters in an acid medium. This gene is up-regulated by androgens and is down-regulated by estrogens in the prostate cancer cell line. This gene exhibits a lower level of expression in testicular cancer tissues than in normal tissues. The protein encoded by this gene has structural similarity to prostatic and lysosomal acid phosphatases. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]

acid phosphatase 7, tartrate resistant (putative)

Purple acid phosphatases (PAPs), including PAPL, are a family of binuclear metallohydrolases that have been identified in plants, animals, and fungi (Flanagan et al., 2006 [PubMed 16793224]).[supplied by OMIM, Mar 2008]

fatty acid desaturase 2B, pseudogene

Predicted to enable oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water. Predicted to be involved in lipid metabolic process. Predicted to be located in endoplasmic reticulum membrane. [provided by Alliance of Genome Resources, Mar 2025]

palmitic acid regulated anti-inflammatory lncRNA

From GO Biological Process Annotations 2015

genes participating in the peptidyl-amino acid modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-amino acid modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-amino acid modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine modification to peptidyl-hypusine biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-lysine modification to peptidyl-hypusine biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-aspartic acid modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-glutamic acid modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-glutamic acid modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-aspartic acid modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-glutamic acid modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-aspartic acid modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-glycine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-glutamine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-methionine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-alanine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-tryptophan modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-asparagine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-threonine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-serine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-proline modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-tyrosine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-histidine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-cysteine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-arginine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-methionine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-proline modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-arginine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-threonine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-serine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-glycine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-tyrosine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-cysteine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-glutamine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-histidine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-alanine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-methionine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-lysine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-arginine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-threonine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-serine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-glycine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-tyrosine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-cysteine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-glutamine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-proline modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-histidine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-s-diacylglycerol-l-cysteine biosynthetic process from peptidyl-cysteine biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-diphthamide biosynthetic process from peptidyl-histidine biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-diphthamide biosynthetic process from peptidyl-histidine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-S-diacylglycerol-L-cysteine biosynthetic process from peptidyl-cysteine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-S-diacylglycerol-L-cysteine biosynthetic process from peptidyl-cysteine biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-glutamic acid carboxylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-glutamic acid acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-aspartic acid hydroxylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-glutamic acid carboxylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-aspartic acid acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-glutamic acid acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-aspartic acid autophosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-aspartic acid hydroxylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-aspartic acid phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the N-terminal peptidyl-aspartic acid acetylation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the N-terminal peptidyl-glutamic acid acetylation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptidyl-glutamic acid carboxylation biological process from the curated GO Biological Process Annotations 2025 dataset.

From Biocarta Pathways

proteins participating in the the prc2 complex sets long-term gene silencing through modification of histone tails pathway from the Biocarta Pathways dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term modification in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of histone modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the trna thio-modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein modification by small protein conjugation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the trna wobble base modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification of morphology or physiology of other organism involved in symbiotic interaction biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of protein modification process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of histone modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of histone modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of mrna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the mitochondrial rna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the mitochondrial trna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the covalent chromatin modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of protein modification process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of mrna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the lipoprotein modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the rrna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the actin modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the heparan sulfate proteoglycan biosynthetic process, enzymatic modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification of morphology or physiology of other organism biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the snrna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of chromatin modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the mrna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein modification process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the lipid modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the chromatin modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the post-translational protein modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of transcription from rna polymerase ii promoter by histone modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification by host of symbiont morphology or physiology biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification by host of symbiont molecular function biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification by virus of host mrna processing biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the trna wobble uridine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cellular protein modification process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the dna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the histone modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the trna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the co-translational protein modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of protein modification process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the macromolecule modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the mitochondrial trna wobble uridine modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the rna modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification-dependent protein catabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification-dependent macromolecule catabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of chromatin modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptide modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of chromatin modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of transcription from rna polymerase ii promoter by histone modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein modification by small protein removal biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the histone h3-k9 modification biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the modification by symbiont of host morphology or physiology biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2015 dataset.

From HumanCyc Pathways

proteins participating in the terminal O-glycans residues modification pathway from the HumanCyc Pathways dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the tRNA-i(6)A37 modification enzyme MiaB protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the tRNA modification GTPase MnmE domain 2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Chromatin modification-related protein Eaf7/MRGBP protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ribosomal S6 modification enzyme RimK/Lysine biosynthesis enzyme LysX protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the tRNA modification GTPase MnmE C-terminal domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Modification methylase HemK protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the tRNA modification GTPase MnmE protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From Reactome Pathways 2014

proteins participating in the Post-translational modification: synthesis of GPI-anchored proteins pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Post-translational protein modification pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Transport to the Golgi and subsequent modification pathway from the Reactome Pathways dataset.

From GO Biological Process Annotations 2023

genes participating in the protein modification process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the tRNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the heparan sulfate proteoglycan biosynthetic process, enzymatic modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein modification by small protein conjugation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the post-translational protein modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the tRNA wobble uridine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the histone modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of protein modification process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the tRNA thio-modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the RNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of modification of synaptic structure biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the modification of postsynaptic actin cytoskeleton biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the mRNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the co-translational protein modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of modification of postsynaptic structure biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of modification of postsynaptic actin cytoskeleton biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the modification of synaptic structure biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the tRNA wobble cytosine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the snRNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the actin modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the tRNA threonylcarbamoyladenosine modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the modification of dendritic spine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the rRNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein modification by small protein removal biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the mitochondrial tRNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of histone modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the modification-dependent protein catabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptide modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the lipid modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of protein modification process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the macromolecule modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of protein modification process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the DNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the tRNA wobble base modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the modification of postsynaptic structure biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the modification-dependent macromolecule catabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the lipid modification by small protein conjugation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the mitochondrial RNA modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the histone H3-K9 modification biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the poly-ADP-D-ribose modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the ADP-D-ribose modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the K48-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the K6-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the ubiquitin modification-dependent histone binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the K63-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the K11-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the ubiquitination-like modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term modification of postsynaptic actin cytoskeleton from the SynGO Synaptic Gene Annotations dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term regulation of modification of postsynaptic structure from the SynGO Synaptic Gene Annotations dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term regulation of modification of postsynaptic actin cytoskeleton from the SynGO Synaptic Gene Annotations dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term modification of postsynaptic structure from the SynGO Synaptic Gene Annotations dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term regulation of modification of synapse structure, modulating synaptic transmission from the SynGO Synaptic Gene Annotations dataset.

From SynGO Synaptic Gene Annotations

genes associated with the synaptic term modification of synaptic structure, modulating synaptic transmission from the SynGO Synaptic Gene Annotations dataset.

From Reactome Pathways 2024

proteins participating in the Post-translational modification: synthesis of GPI-anchored proteins pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Post-translational protein modification pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Transport to the Golgi and subsequent modification pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the rRNA modification in the mitochondrion pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the rRNA modification in the nucleus and cytosol pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the tRNA modification in the mitochondrion pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the tRNA modification in the nucleus and cytosol pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein modification process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the tRNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein modification by small protein conjugation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the mRNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the post-translational protein modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the tRNA wobble uridine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of protein modification process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the tRNA thio-modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the RNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of modification of synaptic structure biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the modification of postsynaptic actin cytoskeleton biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of post-translational protein modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the co-translational protein modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of modification of postsynaptic structure biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of modification of postsynaptic actin cytoskeleton biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the modification of synaptic structure biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the tRNA wobble cytosine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of translational initiation by tRNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the snRNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein histidyl modification to diphthamide biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the actin modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the tRNA threonylcarbamoyladenosine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the rRNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the mitochondrial RNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein modification by small protein removal biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the mitochondrial tRNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the modification-dependent protein catabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptide modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the mitochondrial tRNA wobble uridine modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the lipid modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of protein modification process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the macromolecule modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of protein modification process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein modification by small protein conjugation or removal biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the DNA modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the tRNA wobble base modification biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the modification of postsynaptic structure biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the modification-dependent macromolecule catabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the lipid modification by small protein conjugation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the poly-ADP-D-ribose modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the ADP-D-ribose modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the K48-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the K6-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the K63-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the K11-linked polyubiquitin modification-dependent protein binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Chromatin modification and transcriptional regulation 1 assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Chromatin modification and transcriptional regulation 2 assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Regulation of gene expression and protein modification assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Regulation of apoptosis and RNA modification assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term peptidyl in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-serine dimethylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-arginine n-methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-diphthamide metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-cysteine s-trans-nitrosylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-glycine n-myristoylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of peptidyl-tyrosine autophosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-histidine dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-tyrosine dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-serine trimethylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-serine phosphorylation of stat protein biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-tyrosine autophosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine trimethylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-l-cysteine s-palmitoylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine n6-acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-serine methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-tyrosine autophosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine desuccinylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of peptidyl-cysteine s-nitrosylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-proline dimethylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine monomethylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-tyrosine autophosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-arginine omega-n-methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of n-terminal peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-cysteine s-nitrosylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-serine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-pyrromethane cofactor linkage biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-serine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-serine trans-autophosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-serine octanoylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-proline hydroxylation to 3-hydroxy-l-proline biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-proline hydroxylation to 4-hydroxy-l-proline biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-arginine methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-serine autophosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-methionine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-histidine hydroxylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein-pyridoxal-5-phosphate linkage via peptidyl-n6-pyridoxal phosphate-l-lysine biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of peptidyl-serine dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-cysteine s-nitrosylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine deacetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-l-cysteine n-palmitoylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-asparagine hydroxylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-tyrosine sulfation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine dimethylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-cysteine s-nitrosylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-proline methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine demalonylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-serine dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-threonine dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-arginine methylation, to symmetrical-dimethyl arginine biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-serine dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-glutamine methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of n-terminal peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-arginine methylation, to asymmetrical-dimethyl arginine biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the internal peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein peptidyl-prolyl isomerization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-alanine methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-serine dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of peptidyl-serine phosphorylation of stat protein biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-cysteine methylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the n-terminal peptidyl-alanine trimethylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-proline hydroxylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-cysteine oxidation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine hydroxylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptidyl-lysine hydroxylation to 5-hydroxy-l-lysine biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-prolyl cis-trans isomerase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-cysteine s-nitrosylase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-dipeptidase inhibitor activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-proline 3-dioxygenase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-lysine n-acetyltransferase activity, acting on acetyl phosphate as donor molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-dipeptidase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-lysine 5-dioxygenase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-proline 4-dioxygenase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-histidine dioxygenase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-asparagine 3-dioxygenase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the peptidyl-proline dioxygenase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-glycine alpha-amidating monooxygenase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-prolyl cis-trans isomerase, FKBP-type, domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidase M2, peptidyl-dipeptidase A protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-tRNA hydrolase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-prolyl cis-trans isomerase, PpiC-type protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-tRNA hydrolase, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cyclophilin-type peptidyl-prolyl cis-trans isomerase E protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cyclophilin-type peptidyl-prolyl cis-trans isomerase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-tRNA hydrolase, PTH2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-prolyl cis-trans isomerase, FKBP-type protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidyl-tRNA hydrolase II domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-glutamate ADP-deribosylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine trimethylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine monomethylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine dimethylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine hydroxylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-tyrosine dephosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-arginine N-methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-arginine methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-threonine dephosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein peptidyl-prolyl isomerization biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-tyrosine sulfation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-glycine N-myristoylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-tyrosine autophosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-cysteine S-nitrosylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-serine autophosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-serine trans-autophosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-serine dephosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the internal peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-tyrosine autophosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-serine phosphorylation of STAT protein biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-cysteine S-trans-nitrosylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-cysteine S-nitrosylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-proline hydroxylation to 4-hydroxy-L-proline biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-cysteine S-nitrosylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-serine dephosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-cysteine methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-tyrosine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of peptidyl-serine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-serine phosphorylation of STAT protein biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine oxidation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-cysteine oxidation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine deacetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-glutamine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-methionine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-serine dephosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-tyrosine autophosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of N-terminal peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine propionylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine crotonylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine butyrylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-arginine hydroxylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-L-cysteine N-palmitoylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-L-cysteine S-palmitoylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-arginine methylation, to symmetrical-dimethyl arginine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-histidine methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-proline hydroxylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine glutarylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-lysine acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-arginine methylation, to asymmetrical-dimethyl arginine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-serine octanoylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-cysteine deglycation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-arginine deglycation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine deglycation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-glycine methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-proline dimethylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-serine dimethylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-serine trimethylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-histidine dephosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-serine ADP-deribosylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine demalonylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine desuccinylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-lysine N6-acetylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-glutamine methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-threonine autophosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of peptidyl-lysine crotonylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-proline methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-histidine methylation, to form tele-methylhistidine biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the N-terminal peptidyl-alanine methylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptidyl-proline hydroxylation to 3-hydroxy-L-proline biological process from the curated GO Biological Process Annotations 2023 dataset.