Harmonizome 3.0

From Hub Proteins

Sets of proteins interacting with hub proteins aggregated from data

From Nuclear Receptor Signaling Atlas

Protein-protein interactions inferred from membership in complexes

From Pathway Commons

Protein-protein interactions from low-throughput or high-throughput studies aggregated by Pathway Commons from the following databases: Reactome, NCI Pathways, PhosphoSite, HumanCyc, HPRD, PANTHER, DIP, BioGRID, IntAct, BIND, Transfac, MiRTarBase, Drugbank, Recon X, Comparative Toxicogenomics Database, and KEGG

From Virus MINT

Interactions between viral and human proteins manually curated from literature

From COMPARTMENTS

Protein subcellular localization evidence scores by manual literature curation

From COMPARTMENTS

Protein subcellular localization evidence scores by integrating experimental data

From COMPARTMENTS

Gene-cellular compartment co-occurrence scores from text-mining biomedical abstracts

From CORUM

Proteins participating in complexes by manual literature curation

From Guide to Pharmacology

Protein ligand-receptor interactions curated by experts

From Human Protein Atlas

Semiquantitative protein expression profiles for tissues

From Human Proteome Map

Protein expression profiles for tissues and cell types

From InterPro

Protein domains predicted for gene products based on sequence similarity to known domain signatures

From LOCATE

Subcellular localization of proteins from low-throughput or high-throughput protein localization assays

From Nuclear Receptor Signaling Atlas

Proteins identified in complexes isolated from cultured cells

From Proteomics Database

Protein expression profiles for tissues and cell types reprocessed from many proteomics datasets

From SILAC Phosphoproteomics

Phosphorylation levels of proteins in cell lines following ligand treatment

From TISSUES

Protein tissue expression evidence scores by manual literature curation

From TISSUES

Protein tissue expression evidence scores by integrating experimental data

From TISSUES

Gene-tissue co-occurrence scores from text-mining biomedical abstracts

From Virus MINT

Interactions between viruses and human proteins manually curated from literature

From LOCATE

Subcellular localization of proteins by sequence similarity to localization sequences

From TISSUES

Protein tissue expression evidence scores by manual literature curation

From TISSUES

Protein tissue expression evidence scores by integrating experimental data

From TISSUES

Gene-tissue co-occurrence scores from text-mining biomedical abstracts

From COMPARTMENTS

Protein subcellular localization evidence scores by manual literature curation

From COMPARTMENTS

Protein subcellular localization evidence scores by integrating experimental data

From COMPARTMENTS

Gene-cellular compartment co-occurrence scores from text-mining biomedical abstracts

From Cell Maps for AI

Protein localization assemblies constructed from integrating AP-MS biomolecular interaction and IF imaging data

From Human Protein Atlas

RNA-seq gene expression profiles for cell lines from HPA

From Human Protein Atlas

RNA-seq gene expression profiles for tissues from HPA

From Human Protein Atlas

RNA-seq gene expression profiles for tissue samples from HPA

clathrin interactor 1

This gene encodes a protein with similarity to the epsin family of endocytic adapter proteins. The encoded protein interacts with clathrin, the adapter protein AP-1 and phosphoinositides. This protein may be involved in the formation of clathrin coated vesicles and trafficking between the trans-Golgi network and endosomes. Mutations in this gene are associated with a susceptibility to schizophrenia and psychotic disorders. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2010]

clathrin, light chain A pseudogene

clathrin, heavy chain-like 1

This gene is a member of the clathrin heavy chain family and encodes a major protein of the polyhedral coat of coated pits and vesicles. Chromosomal aberrations involving this gene are associated with meningioma, DiGeorge syndrome, and velo-cardio-facial syndrome. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2009]

clathrin heavy chain linker domain containing 1

sodium channel and clathrin linker 1

This gene encodes an adaptor protein. Studies of a related gene in rat suggest that the encoded protein functions to link clathrin to the sodium channel protein type 10 subunit alpha protein. The encoded protein has also been identified as a component of distal appendages of centrioles that is necessary for ciliogenesis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014]

clathrin, light chain A

Clathrin is a large, soluble protein composed of heavy and light chains. It functions as the main structural component of the lattice-type cytoplasmic face of coated pits and vesicles which entrap specific macromolecules during receptor-mediated endocytosis. This gene encodes one of two clathrin light chain proteins which are believed to function as regulatory elements. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 8 and 12. [provided by RefSeq, May 2010]

clathrin, heavy chain (Hc)

Clathrin is a major protein component of the cytoplasmic face of intracellular organelles, called coated vesicles and coated pits. These specialized organelles are involved in the intracellular trafficking of receptors and endocytosis of a variety of macromolecules. The basic subunit of the clathrin coat is composed of three heavy chains and three light chains. [provided by RefSeq, Jul 2008]

clathrin, light chain B

Clathrin is a large, soluble protein composed of heavy and light chains. It functions as the main structural component of the lattice-type cytoplasmic face of coated pits and vesicles which entrap specific macromolecules during receptor-mediated endocytosis. This gene encodes one of two clathrin light chain proteins which are believed to function as regulatory elements. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2008]

clathrin, light chain A pseudogene

phosphatidylinositol glycan anchor biosynthesis, class C, pseudogene 1

phosphatidylinositol glycan anchor biosynthesis, class C pseudogene 2

phosphatidylinositol transfer protein, cytoplasmic 1

This gene encodes a member of the phosphatidylinositol transfer protein family. The encoded cytoplasmic protein plays a role in multiple processes including cell signaling and lipid metabolism by facilitating the transfer of phosphatidylinositol between membrane compartments. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 1. [provided by RefSeq, May 2012]

phosphatidylinositol glycan anchor biosynthesis, class F, pseudogene 1

phosphatidylinositol glycan anchor biosynthesis, class F, pseudogene 3

phosphatidylinositol glycan anchor biosynthesis, class U pseudogene 1

phosphatidylinositol glycan anchor biosynthesis, class H pseudogene 1

phospholipase C, gamma 2 (phosphatidylinositol-specific)

The protein encoded by this gene is a transmembrane signaling enzyme that catalyzes the conversion of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to 1D-myo-inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) using calcium as a cofactor. IP3 and DAG are second messenger molecules important for transmitting signals from growth factor receptors and immune system receptors across the cell membrane. Mutations in this gene have been found in autoinflammation, antibody deficiency, and immune dysregulation syndrome and familial cold autoinflammatory syndrome 3. [provided by RefSeq, Mar 2014]

phosphatidylinositol 4-kinase, catalytic, alpha pseudogene 2

Predicted to enable kinase activity. Predicted to be involved in phosphatidylinositol phosphate biosynthetic process. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 2

The protein encoded by this gene belongs to the phosphatidylinositol 3,4,5-trisphosphate (PIP3)-dependent Rac exchanger (PREX) family, which are Dbl-type guanine-nucleotide exchange factors for Rac family small G proteins. Structural domains of this protein include the catalytic diffuse B-cell lymphoma homology and pleckstrin homology (DHPH) domain, two disheveled, EGL-10, and pleckstrin homology (DEP) domains, two PDZ domains, and a C-terminal inositol polyphosphate-4 phosphatase (IP4P) domain that is found in one of the isoforms. This protein facilitates the exchange of GDP for GTP on Rac1, allowing the GTP-bound Rac1 to activate downstream effectors. Studies also show that the pleckstrin homology domain of this protein interacts with the phosphatase and tensin homolog (PTEN) gene product to inhibit PTEN phosphatase activity, thus activating the phosphoinositide-3 kinase (PI3K) signaling pathway. Conversely, the PTEN gene product has also been shown to inhibit the GEF activity of this protein. This gene plays a role in insulin-signaling pathways, and either mutations or overexpression of this gene have been observed in some cancers. [provided by RefSeq, Apr 2016]

phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1

The protein encoded by this gene acts as a guanine nucleotide exchange factor for the RHO family of small GTP-binding proteins (RACs). It has been shown to bind to and activate RAC1 by exchanging bound GDP for free GTP. The encoded protein, which is found mainly in the cytoplasm, is activated by phosphatidylinositol-3,4,5-trisphosphate and the beta-gamma subunits of heterotrimeric G proteins. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class Y pseudogene

phosphatidylinositol transfer protein, alpha

This gene encodes a member of a family of lipid-binding proteins that transfer molecules of phosphatidylinositol or phosphatidylcholine between membrane surfaces. The protein is implicated in phospholipase C signaling and in the production of phosphatidylinositol 3,4,5-trisphosphate (PIP3) by phosphoinositide-3-kinase.[provided by RefSeq, Sep 2009]

phosphatidylinositol transfer protein, beta

This gene encodes a cytoplasmic protein that catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes. This transfer activity is required for COPI complex-mediated retrograde transport from the Golgi apparatus to the endoplasmic reticulum. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Sep 2013]

phosphatidylinositol-5-phosphate 4-kinase, type II, alpha

Phosphatidylinositol-5,4-bisphosphate, the precursor to second messengers of the phosphoinositide signal transduction pathways, is thought to be involved in the regulation of secretion, cell proliferation, differentiation, and motility. The protein encoded by this gene is one of a family of enzymes capable of catalyzing the phosphorylation of phosphatidylinositol-5-phosphate on the fourth hydroxyl of the myo-inositol ring to form phosphatidylinositol-5,4-bisphosphate. The amino acid sequence of this enzyme does not show homology to other kinases, but the recombinant protein does exhibit kinase activity. This gene is a member of the phosphatidylinositol-5-phosphate 4-kinase family. [provided by RefSeq, Jul 2008]

phosphatidylinositol-5-phosphate 4-kinase, type II, gamma

Enables 1-phosphatidylinositol-4-phosphate 5-kinase activity and identical protein binding activity. Involved in 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process; negative regulation of insulin receptor signaling pathway; and positive regulation of autophagosome assembly. Located in several cellular components, including autophagosome; cytosol; and nucleoplasm. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol-5-phosphate 4-kinase, type II, beta

The protein encoded by this gene catalyzes the phosphorylation of phosphatidylinositol-5-phosphate on the fourth hydroxyl of the myo-inositol ring to form phosphatidylinositol-5,4-bisphosphate. This gene is a member of the phosphatidylinositol-5-phosphate 4-kinase family. The encoded protein sequence does not show similarity to other kinases, but the protein does exhibit kinase activity. Additionally, the encoded protein interacts with p55 TNF receptor. [provided by RefSeq, Jul 2008]

phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 beta

The protein encoded by this gene belongs to the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking. This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of class II PI3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. The PI3-kinase activity of this protein is sensitive to low nanomolar levels of the inhibitor wortmanin. The C2 domain of this protein was shown to bind phospholipids but not Ca2+, which suggests that this enzyme may function in a calcium-independent manner. [provided by RefSeq, Jul 2008]

phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 alpha

The protein encoded by this gene belongs to the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking. This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of class II PI3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. The PI3-kinase activity of this protein is not sensitive to nanomolar levels of the inhibitor wortmanin. This protein was shown to be able to be activated by insulin and may be involved in integrin-dependent signaling. [provided by RefSeq, Jul 2008]

phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 gamma

The protein encoded by this gene belongs to the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking. This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of class II PI3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. This gene may play a role in several diseases, including type II diabetes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]

phosphatidylinositol-4-phosphate 5-kinase, type I, pseudogene 1

phosphatidylinositol-4-phosphate 5-kinase, type I, pseudogene 2

phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit alpha pseudogene

SMG1 phosphatidylinositol 3-kinase-related kinase

This gene encodes a protein involved in nonsense-mediated mRNA decay (NMD) as part of the mRNA surveillance complex. The protein has kinase activity and is thought to function in NMD by phosphorylating the regulator of nonsense transcripts 1 protein. Alternatively spliced transcript variants have been described, but their full-length nature has yet to be determined. [provided by RefSeq, Mar 2013]

phosphatidylinositol transfer protein, cytoplasmic 1 pseudogene

phosphatidylinositol glycan anchor biosynthesis, class P pseudogene 3

phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit delta pseudogene

phosphatidylinositol glycan anchor biosynthesis, class A, pseudogene 1

phosphatidylinositol glycan anchor biosynthesis, class P

This gene encodes an enzyme involved in the first step of glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells that serves to anchor proteins to the cell surface. The encoded protein is a component of the GPI-N-acetylglucosaminyltransferase complex that catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol (PI). This gene is located in the Down Syndrome critical region on chromosome 21 and is a candidate for the pathogenesis of Down syndrome. This gene has multiple pseudogenes and is a member of the phosphatidylinositol glycan anchor biosynthesis gene family. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Feb 2016]

phosphatidylinositol glycan anchor biosynthesis, class A

This gene encodes a protein required for synthesis of N-acetylglucosaminyl phosphatidylinositol (GlcNAc-PI), the first intermediate in the biosynthetic pathway of GPI anchor. The GPI anchor is a glycolipid found on many blood cells and which serves to anchor proteins to the cell surface. Paroxysmal nocturnal hemoglobinuria, an acquired hematologic disorder, has been shown to result from mutations in this gene. Alternate splice variants have been characterized. A related pseudogene is located on chromosome 12. [provided by RefSeq, Jun 2010]

phosphatidylinositol glycan anchor biosynthesis, class B

This gene encodes a transmembrane protein that is located in the endoplasmic reticulum and is involved in GPI-anchor biosynthesis. The glycosylphosphatidylinositol (GPI) anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This gene is thought to encode a member of a family of dolichol-phosphate-mannose (Dol-P-Man) dependent mannosyltransferases. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class C

This gene encodes an endoplasmic reticulum associated protein that is involved in glycosylphosphatidylinositol (GPI) lipid anchor biosynthesis. The GPI lipid anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. The encoded protein is one subunit of the GPI N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to phosphatidylinositol (PI) on the cytoplasmic side of the endoplasmic reticulum. Two alternatively spliced transcripts that encode the same protein have been found for this gene. A pseudogene on chromosome 11 has also been characterized. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class F

This gene encodes a protein involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor, a glycolipid containing three mannose molecules in its core backbone, is found on many blood cells where it serves to anchor proteins to the cell surface. The encoded protein and another GPI synthesis protein, PIGO, function in the transfer of ethanolaminephosphate to the third mannose in GPI. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class G

This gene encodes an enzyme involved in glycosylphosphatidylinositol-anchor biosynthesis. The encoded protein, which is localized to the endoplasmic reticulum, is involved in transferring ethanoloamine phosphate to mannose 2 of glycosylphosphatidylinositol species H7 to form species H8. Allelic variants of this gene have been associated with intellectual disability, hypotonia, and early-onset seizures. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2016]

phosphatidylinositol glycan anchor biosynthesis, class H

This gene encodes an endoplasmic reticulum associated protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI anchor is a glycolipid found on many blood cells and which serves to anchor proteins to the cell surface. The protein encoded by this gene is a subunit of the GPI N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to phosphatidylinositol (PI) on the cytoplasmic side of the endoplasmic reticulum. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class K

This gene encodes a member of the cysteine protease family C13 that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is a member of the multisubunit enzyme, GPI transamidase and is thought to be its enzymatic component. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class L

This gene encodes an enzyme that catalyzes the second step of glycosylphosphatidylinositol (GPI) biosynthesis, which is the de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI). Study of a similar rat enzyme suggests that this protein localizes to the endoplasmic reticulum. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class M

This gene encodes a transmembrane protein that is located in the endoplasmic reticulum and is involved in GPI-anchor biosynthesis. The glycosylphosphatidylinositol (GPI)-anchor is a glycolipid which contains three mannose molecules in its core backbone. The GPI-anchor is found on many blood cells and serves to anchor proteins to the cell surface. This gene encodes a mannosyltransferase, GPI-MT-I, that transfers the first mannose to GPI on the lumenal side of the endoplasmic reticulum. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class N

This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is expressed in the endoplasmic reticulum and transfers phosphoethanolamine (EtNP) to the first mannose of the GPI anchor. Two alternatively spliced variants, which encode an identical isoform, have been reported. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class O

This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid which contains three mannose molecules in its core backbone. The GPI-anchor is found on many blood cells and serves to anchor proteins to the cell surface. This protein is involved in the transfer of ethanolaminephosphate (EtNP) to the third mannose in GPI. At least three alternatively spliced transcripts encoding two distinct isoforms have been found for this gene. [provided by RefSeq, Jan 2011]

phosphatidylinositol glycan anchor biosynthesis, class Q

This gene is involved in the first step in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This gene encodes a N-acetylglucosaminyl transferase component that is part of the complex that catalyzes transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol (PI). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2012]

phosphatidylinositol glycan anchor biosynthesis, class S

This gene encodes a protein that is involved in GPI-anchor biosynthesis. The glycosylphosphatidylinositol (GPI) anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This gene encodes an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class T

This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 2012]

phosphatidylinositol glycan anchor biosynthesis, class U

The protein encoded by this gene shares similarity with Saccharomyces cerevisiae Cdc91, a predicted integral membrane protein that may function in cell division control. The protein encoded by this gene is the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. [provided by RefSeq, Jul 2008]

phosphatidylinositol glycan anchor biosynthesis, class V

This gene encodes a mannosyltransferase enzyme involved in the biosynthesis of glycosylphosphatidylinositol (GPI). GPI is a complex glycolipid that functions as a membrane anchor for many proteins and plays a role in multiple cellular processes including protein sorting and signal transduction. The encoded protein is localized to the endoplasmic reticulum and transfers the second mannose to the GPI backbone. Mutations in this gene are associated with hyperphosphatasia cognitive disability syndrome. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, Feb 2011]

phosphatidylinositol glycan anchor biosynthesis, class W

The protein encoded by this gene is an inositol acyltransferase that acylates the inositol ring of phosphatidylinositol. This occurs in the endoplasmic reticulum and is a step in the biosynthesis of glycosylphosphatidylinositol (GPI), which anchors many cell surface proteins to the membrane. Defects in this gene are a cause of the age-dependent epileptic encephalopathy West syndrome as well as a syndrome exhibiting hyperphosphatasia and cognitive disability (HPMRS5). [provided by RefSeq, Jul 2017]

phosphatidylinositol glycan anchor biosynthesis, class X

This gene encodes a type I transmembrane protein in the endoplasmic reticulum (ER). The protein is an essential component of glycosylphosphatidylinositol-mannosyltransferase I, which transfers the first of the four mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Studies in rat indicate that the protein is translated from a non-AUG translation initiation site. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2009]

phosphatidylinositol glycan anchor biosynthesis, class Y

The protein encoded by this gene is part of the GPI-N-acetylglucosaminyltransferase (GIP-GnT) complex which initiates the biosynthesis of glycosylphosphatidylinositol (GPI). GPI is synthesized in the endoplasmic reticulum and serves as an anchor for many surface proteins. Proteins containing GPI anchors can have an important role in cell-cell interactions. The transcript for this gene is bicistronic. The downstream open reading frame encodes this GPI-GnT complex protein, while the upstream open reading frame encodes a protein with unknown function, as represented by GeneID:100996939. [provided by RefSeq, Aug 2012]

phosphatidylinositol glycan anchor biosynthesis, class Z

The glycosylphosphatidylinositol (GPI) anchor is a glycolipid found on many blood cells that serves to anchor proteins to the cell surface. This gene encodes a protein that is localized to the endoplasmic reticulum, and is involved in GPI anchor biosynthesis. As shown for the yeast homolog, which is a member of a family of dolichol-phosphate-mannose (Dol-P-Man)-dependent mannosyltransferases, this protein can also add a side-branching fourth mannose to GPI precursors during the assembly of GPI anchors. [provided by RefSeq, Jul 2008]

phosphatidylinositol-4-phosphate 5-kinase-like 1

PIP5KL1 is a phosphoinositide kinase-like protein that lacks intrinsic lipid kinase activity but associates with type I PIPKs (see PIP5K1A; MIM 603275) and may play a role in localization of PIPK activity (Chang et al., 2004 [PubMed 14701839]).[supplied by OMIM, Jun 2009]

phosphatidylinositol-specific phospholipase C, X domain containing 3

Predicted to enable phosphoric diester hydrolase activity. Predicted to be involved in lipid catabolic process and signal transduction. Predicted to be located in cytoplasm. Predicted to be active in glutamatergic synapse. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol transfer protein, membrane-associated 1

PITPNM1 belongs to a family of membrane-associated phosphatidylinositol transfer domain-containing proteins that share homology with the Drosophila retinal degeneration B (rdgB) protein (Ocaka et al., 2005 [PubMed 15627748]).[supplied by OMIM, Mar 2008]

phosphatidylinositol transfer protein, membrane-associated 2

PITPNM2 belongs to a family of membrane-associated phosphatidylinositol transfer domain-containing proteins that share homology with the Drosophila retinal degeneration B (rdgB) protein (Ocaka et al., 2005 [PubMed 15627748]).[supplied by OMIM, Mar 2008]

phosphatidylinositol-specific phospholipase C, X domain containing 2

Predicted to enable phosphoric diester hydrolase activity. Predicted to be involved in lipid catabolic process and signal transduction. Predicted to be located in nucleus. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol-specific phospholipase C, X domain containing 1

This gene is the most terminal protein-coding gene in the pseudoautosomal (PAR) region on chromosomes X and Y. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Mar 2010]

phosphatidylinositol 4-kinase type 2 beta pseudogene

phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit alpha

Phosphatidylinositol 3-kinase is composed of an 85 kDa regulatory subunit and a 110 kDa catalytic subunit. The protein encoded by this gene represents the catalytic subunit, which uses ATP to phosphorylate PtdIns, PtdIns4P and PtdIns(4,5)P2. This gene has been found to be oncogenic and has been implicated in cervical cancers. A pseudogene of this gene has been defined on chromosome 22. [provided by RefSeq, Apr 2016]

phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit delta

Phosphoinositide 3-kinases (PI3Ks) phosphorylate inositol lipids and are involved in the immune response. The protein encoded by this gene is a class I PI3K found primarily in leukocytes. Like other class I PI3Ks (p110-alpha p110-beta, and p110-gamma), the encoded protein binds p85 adapter proteins and GTP-bound RAS. However, unlike the other class I PI3Ks, this protein phosphorylates itself, not p85 protein.[provided by RefSeq, Jul 2010]

phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit gamma

Phosphoinositide 3-kinases (PI3Ks) phosphorylate inositol lipids and are involved in the immune response. The protein encoded by this gene is a class I catalytic subunit of PI3K. Like other class I catalytic subunits (p110-alpha p110-beta, and p110-delta), the encoded protein binds a p85 regulatory subunit to form PI3K. This gene is located in a commonly deleted segment of chromosome 7 previously identified in myeloid leukemias. Several transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jun 2015]

phosphatidylinositol 3-kinase, catalytic subunit type 3

Enables 1-phosphatidylinositol-3-kinase activity. Involved in several processes, including early endosome to late endosome transport; macroautophagy; and phosphatidylinositol-3-phosphate biosynthetic process. Acts upstream of or within autophagy and positive regulation of protein lipidation. Located in autolysosome; late endosome; and midbody. Part of phosphatidylinositol 3-kinase complex, class III. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol 4-kinase type 2 beta

This gene encodes a member of the type II PI4 kinase protein family. The encoded protein is primarily cytosolic and contributes to overall PI4-kinase activity along with other protein family members. This protein is involved in early T cell activation. [provided by RefSeq, Dec 2016]

phosphatidylinositol 4-kinase type 2 alpha

Phosphatidylinositolpolyphosphates (PtdInsPs) are centrally involved in many biologic processes, ranging from cell growth and organization of the actin cytoskeleton to endo- and exocytosis. PI4KII phosphorylates PtdIns at the D-4 position, an essential step in the biosynthesis of PtdInsPs (Barylko et al., 2001 [PubMed 11244087]).[supplied by OMIM, Mar 2008]

phospholipase C, beta 3 (phosphatidylinositol-specific)

This gene encodes a member of the phosphoinositide phospholipase C beta enzyme family that catalyze the production of the secondary messengers diacylglycerol and inositol 1,4,5-triphosphate from phosphatidylinositol in G-protein-linked receptor-mediated signal transduction. Alternative splicing results in multiple transcript variants.[provided by RefSeq, May 2010]

SMG1 phosphatidylinositol 3-kinase-related kinase pseudogene

phosphatidylinositol 4-kinase, catalytic, alpha pseudogene 1

phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit beta

This gene encodes an isoform of the catalytic subunit of phosphoinositide 3-kinase (PI3K). These kinases are important in signaling pathways involving receptors on the outer membrane of eukaryotic cells and are named for their catalytic subunit. The encoded protein is the catalytic subunit for PI3Kbeta (PI3KB). PI3KB has been shown to be part of the activation pathway in neutrophils which have bound immune complexes at sites of injury or infection. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2011]

phosphatidylinositol 4-kinase type 2 alpha pseudogene

phosphatidylinositol glycan anchor biosynthesis, class F, pseudogene 2

phosphatidylinositol-4-phosphate 5-kinase, type I, gamma

This locus encodes a type I phosphatidylinositol 4-phosphate 5-kinase. The encoded protein catalyzes phosphorylation of phosphatidylinositol 4-phosphate, producing phosphatidylinositol 4,5-bisphosphate. This enzyme is found at synapses and has been found to play roles in endocytosis and cell migration. Mutations at this locus have been associated with lethal congenital contractural syndrome. Alternatively spliced transcript variants encoding different isoforms have been described.[provided by RefSeq, Sep 2010]

phosphatidylinositol-4-phosphate 5-kinase, type I, beta

Predicted to enable 1-phosphatidylinositol-4-phosphate 5-kinase activity. Predicted to be involved in phosphatidylinositol phosphate biosynthetic process. Predicted to act upstream of or within phosphatidylinositol biosynthetic process. Located in uropod. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol-4-phosphate 5-kinase, type I, alpha

Enables 1-phosphatidylinositol-4-phosphate 5-kinase activity and kinase binding activity. Involved in several processes, including activation of GTPase activity; focal adhesion assembly; and ruffle assembly. Located in several cellular components, including lamellipodium; nucleus; and ruffle membrane. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol 4-kinase, catalytic, beta

Enables 1-phosphatidylinositol 4-kinase activity and 14-3-3 protein binding activity. Involved in inner ear development. Acts upstream of or within lysosome organization. Located in Golgi membrane. Implicated in autosomal dominant nonsyndromic deafness 87. [provided by Alliance of Genome Resources, Mar 2025]

phosphatidylinositol 4-kinase, catalytic, alpha

This gene encodes a phosphatidylinositol (PI) 4-kinase which catalyzes the first committed step in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. The mammalian PI 4-kinases have been classified into two types, II and III, based on their molecular mass, and modulation by detergent and adenosine. The protein encoded by this gene is a type III enzyme that is not inhibited by adenosine. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Apr 2018]

phosphatidylinositol-4,5-bisphosphate 4-phosphatase 1

TMEM55B catalyzes the degradation of phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) by removing the 4-phosphate (Ungewickell et al., 2005 [PubMed 16365287]).[supplied by OMIM, Mar 2008]

phosphatidylinositol-4,5-bisphosphate 4-phosphatase 2

TMEM55A catalyzes the degradation of phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) by removing the 4-phosphate (Ungewickell et al., 2005 [PubMed 16365287]).[supplied by OMIM, Mar 2008]

SHQ1, H/ACA ribonucleoprotein assembly factor pseudogene 1

dynein assembly factor with WDR repeat domains 1

Predicted to enable ubiquitin-like ligase-substrate adaptor activity. Predicted to be involved in protein polyubiquitination. Predicted to act upstream of with a positive effect on outer dynein arm assembly. Predicted to act upstream of or within with a positive effect on intraciliary transport. Predicted to act upstream of or within several processes, including cerebrospinal fluid circulation; determination of left/right symmetry; and heart development. Predicted to be located in ciliary basal body. Predicted to be part of SCF ubiquitin ligase complex. Implicated in primary ciliary dyskinesia. [provided by Alliance of Genome Resources, Mar 2025]

cytochrome c oxidase assembly factor 1 homolog (S. cerevisiae) pseudogene

SCO1 cytochrome c oxidase assembly protein

Mammalian cytochrome c oxidase (COX) catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane. In yeast, 2 related COX assembly genes, SCO1 and SCO2 (synthesis of cytochrome c oxidase), enable subunits 1 and 2 to be incorporated into the holoprotein. This gene is the human homolog to the yeast SCO1 gene. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) assembly chaperone 4

Predicted to be involved in proteasome assembly. Predicted to be part of protein-containing complex. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) assembly chaperone 1

Enables molecular adaptor activity. Involved in chaperone-mediated protein complex assembly. Located in several cellular components, including Golgi apparatus; endoplasmic reticulum; and nucleoplasm. Part of protein folding chaperone complex. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) assembly chaperone 2

Enables molecular adaptor activity. Involved in chaperone-mediated protein complex assembly. Located in nucleus. Part of protein folding chaperone complex. Implicated in proteosome-associated autoinflammatory syndrome 4. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) assembly chaperone 3

Enables molecular adaptor activity. Involved in chaperone-mediated protein complex assembly. Predicted to be part of protein-containing complex. [provided by Alliance of Genome Resources, Mar 2025]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 1 pseudogene

oxidase (cytochrome c) assembly 1-like

This gene encodes an evolutionarily conserved protein that is localized to the inner mitochondrial membrane. The encoded protein is essential for the translocation of the N-terminal tail of subunit 2 of cytochrome c oxidase, and is involved in the assembly of the cytochrome c oxidase and ATPase complexes of the mitochondrial respiratory chain. [provided by RefSeq, Jul 2016]

COX19 cytochrome c oxidase assembly factor

COX19 encodes a cytochrome c oxidase (COX)-assembly protein. The S. cerevisiae Cox19 protein may play a role in metal transport to the mitochondrial intermembrane space and assembly of complex IV of the mitochondrial respiratory chain (Sacconi et al., 2005 [PubMed 16212937]).[supplied by OMIM, Mar 2008]

iron-sulfur cluster assembly 1 pseudogene 6

iron-sulfur cluster assembly 1 pseudogene 5

iron-sulfur cluster assembly 1 pseudogene 3

iron-sulfur cluster assembly 1 pseudogene 1

dynein, axonemal, assembly factor 5 pseudodgene

nuclear assembly factor 1 ribonucleoprotein

Enables identical protein binding activity and telomerase RNA binding activity. Involved in ribosome biogenesis; telomerase RNA stabilization; and telomerase holoenzyme complex assembly. Acts upstream of or within telomerase RNA localization to Cajal body. Located in cytoplasm and nucleoplasm. Part of sno(s)RNA-containing ribonucleoprotein complex. Implicated in melanoma. [provided by Alliance of Genome Resources, Mar 2025]

iron-sulfur cluster assembly enzyme pseudogene 1

IBA57, iron-sulfur cluster assembly homolog (S. cerevisiae)

The protein encoded by this gene localizes to the mitochondrion and is part of the iron-sulfur cluster assembly pathway. The encoded protein functions late in the biosynthesis of mitochondrial 4Fe-4S proteins. Defects in this gene have been associated with autosomal recessive spastic paraplegia-74 and with multiple mitochondrial dysfunctions syndrome-3. Two transcript variants encoding different isoforms have been found for this gene. The smaller isoform is not likely to be localized to the mitochondrion since it lacks the amino-terminal transit peptide. [provided by RefSeq, Jul 2015]

SAMM50 sorting and assembly machinery component pseudogene 1

nucleosome assembly protein 1-like 1 pseudogene 3

nucleosome assembly protein 1-like 1 pseudogene 2

nucleosome assembly protein 1-like 1 pseudogene 1

Sfi1 homolog, spindle assembly associated (yeast)

Enables phosphatase binding activity. Predicted to be located in cytosol. [provided by Alliance of Genome Resources, Mar 2025]

nucleosome assembly protein 1-like 1

This gene encodes a member of the nucleosome assembly protein (NAP) family. This protein participates in DNA replication and may play a role in modulating chromatin formation and contribute to the regulation of cell proliferation. Alternative splicing results in multiple transcript variants encoding different isoforms; however, not all have been fully described. [provided by RefSeq, Apr 2015]

nucleosome assembly protein 1-like 2

The protein encoded by this intronless gene is a member of the nucleosome assembly protein (NAP) family. The encoded protein represents a class of tissue-specific factors that interact with chromatin to regulate neuronal cell proliferation. [provided by RefSeq, Jan 2011]

nucleosome assembly protein 1-like 3

This gene is intronless and encodes a member of the nucleosome assembly protein (NAP) family. This gene is linked closely to a region of genes responsible for several X-linked cognitive disability syndromes. [provided by RefSeq, Dec 2010]

nucleosome assembly protein 1-like 4

This gene encodes a member of the nucleosome assembly protein (NAP) family which can interact with both core and linker histones. It can shuttle between the cytoplasm and nucleus, suggesting a role as a histone chaperone. This gene is one of several located near the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. [provided by RefSeq, Jul 2008]

nucleosome assembly protein 1-like 5

This gene encodes a protein that shares sequence similarity to nucleosome assembly factors, but may be localized to the cytoplasm rather than the nucleus. Expression of this gene is downregulated in hepatocellular carcinomas. This gene is located within a differentially methylated region (DMR) and is imprinted and paternally expressed. There is a related pseudogene on chromosome 4. [provided by RefSeq, Nov 2015]

nucleosome assembly protein 1-like 6

Predicted to be involved in nucleosome assembly. Predicted to be located in nucleus. [provided by Alliance of Genome Resources, Mar 2025]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 2 pseudogene

COX20 cytochrome c oxidase assembly factor pseudogene 2

COX20 cytochrome c oxidase assembly factor pseudogene 1

SCO1 cytochrome c oxidase assembly protein pseudogene

cytosolic iron-sulfur assembly component 1

Involved in iron-sulfur cluster assembly and protein maturation by iron-sulfur cluster transfer. Located in cytoplasm. Part of MMXD complex and cytosolic [4Fe-4S] assembly targeting complex. [provided by Alliance of Genome Resources, Mar 2025]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 5

The NADH-ubiquinone oxidoreductase complex (complex I) of the mitochondrial respiratory chain catalyzes the transfer of electrons from NADH to ubiquinone, and consists of at least 43 subunits. The complex is located in the inner mitochondrial membrane. This gene encodes a mitochondrial protein that is associated with the matrix face of the mitochondrial inner membrane and is required for complex I assembly. A mutation in this gene results in mitochondrial complex I deficiency. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2009]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 4

NADH:ubiquinone oxidoreductase (complex I) catalyzes the transfer of electrons from NADH to ubiquinone (coenzyme Q) in the first step of the mitochondrial respiratory chain, resulting in the translocation of protons across the inner mitochondrial membrane. This gene encodes a complex I assembly factor. Mutations in this gene are a cause of mitochondrial complex I deficiency. [provided by RefSeq, Oct 2009]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 7

This gene encodes an assembly factor protein which helps in the assembly and stabilization of Complex I, a large multi-subunit enzyme in the mitochondrial respiratory chain. Complex I is involved in several physiological activities in the cell, including metabolite transport and ATP synthesis. The encoded protein is a methyltransferase which methylates Arg85 of a subunit of Complex I in the early stages of its assembly. A pseudogene related to this gene is located on chromosome 8. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2016]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 6

This gene encodes a protein that localizes to mitochondria and contains a predicted phytoene synthase domain. The encoded protein plays an important role in the assembly of complex I (NADH-ubiquinone oxidoreductase) of the mitochondrial respiratory chain through regulation of subunit ND1 biogenesis. Mutations in this gene are associated with complex I enzymatic deficiency. [provided by RefSeq, Nov 2011]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 1

This gene encodes a complex I assembly factor protein. Complex I (NADH-ubiquinone oxidoreductase) catalyzes the transfer of electrons from NADH to ubiquinone (coenzyme Q) in the first step of the mitochondrial respiratory chain, resulting in the translocation of protons across the inner mitochondrial membrane. The encoded protein is required for assembly of complex I, and mutations in this gene are a cause of mitochondrial complex I deficiency. Alternatively spliced transcript variants have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 19. [provided by RefSeq, Dec 2011]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 3

This gene encodes a mitochondrial complex I assembly protein that interacts with complex I subunits. Mutations in this gene cause mitochondrial complex I deficiency, a fatal neonatal disorder of the oxidative phosphorylation system. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2009]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 2

NADH:ubiquinone oxidoreductase (complex I) catalyzes the transfer of electrons from NADH to ubiquinone (coenzyme Q) in the first step of the mitochondrial respiratory chain, resulting in the translocation of protons across the inner mitochondrial membrane. This gene encodes a complex I assembly factor. Mutations in this gene cause progressive encephalopathy resulting from mitochondrial complex I deficiency. [provided by RefSeq, Jul 2008]

chromatin assembly factor 1, subunit A (p150)

Chromatin assembly factor I (CAF1) is a nuclear complex consisting of p50, p60 (CHAF1B; MIM 601245), and p150 (CHAF1A) subunits that assembles histone octamers onto replicating DNA in vitro (Kaufman et al., 1995 [PubMed 7600578]).[supplied by OMIM, Mar 2008]

chromatin assembly factor 1, subunit B (p60)

Chromatin assembly factor I (CAF-I) is required for the assembly of histone octamers onto newly-replicated DNA. CAF-I is composed of three protein subunits, p50, p60, and p150. The protein encoded by this gene corresponds to the p60 subunit and is required for chromatin assembly after replication. The encoded protein is differentially phosphorylated in a cell cycle-dependent manner. In addition, it is normally found in the nucleus except during mitosis, when it is released into the cytoplasm. This protein is a member of the WD-repeat HIR1 family and may also be involved in DNA repair. [provided by RefSeq, Jul 2008]

iron-sulfur cluster assembly 1 homolog (S. cerevisiae) pseudogene

spindle assembly 6 homolog (C. elegans)

The protein encoded by this gene is a central component of centrioles and is necessary for their duplication and function. Centrioles adopt a cartwheel-shaped structure, with the encoded protein forming the hub and spokes inside a microtubule cylinder. Defects in this gene are a cause of autosomal recessive primary microcephaly. [provided by RefSeq, Oct 2016]

COX14 cytochrome c oxidase assembly factor

This gene encodes a small single-pass transmembrane protein that localizes to mitochondria. This protein may play a role in coordinating the early steps of cytochrome c oxidase (COX; also known as complex IV) subunit assembly and, in particular, the synthesis and assembly of the COX I subunit of the holoenzyme. Mutations in this gene have been associated with mitochondrial complex IV deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2012]

dynein, axonemal, assembly factor 2

This gene encodes a highly conserved protein involved in the preassembly of dynein arm complexes which power cilia. These complexes are found in some cilia and are assembled in the cytoplasm prior to transport for cilia formation. Mutations in this gene have been associated with primary ciliary dyskinesia. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Oct 2009]

dynein, axonemal, assembly factor 3

The protein encoded by this gene is required for the assembly of axonemal inner and outer dynein arms and plays a role in assembling dynein complexes for transport into cilia. Defects in this gene are a cause of primary ciliary dyskinesia type 2 (CILD2). Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012]

dynein, axonemal, assembly factor 5

The protein encoded by this gene is essential for the preassembly or stability of axonemal dynein arms, and is found only in organisms with motile cilia and flagella. Mutations in this gene are associated with primary ciliary dyskinesia-18, a disorder characterized by abnormalities of motile cilia. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Feb 2013]

nucleosome assembly protein 1-like 1 pseudogene

NADH dehydrogenase (ubiquinone) complex I, assembly factor 7 pseudogene

iron-sulfur cluster assembly 1 pseudogene 4

iron-sulfur cluster assembly enzyme

This gene encodes a component of the iron-sulfur (Fe-S) cluster scaffold. Fe-S clusters are cofactors that play a role in the function of a diverse set of enzymes, including those that regulate metabolism, iron homeostasis, and oxidative stress response. Alternative splicing results in transcript variants encoding different protein isoforms that localize either to the cytosol or to the mitochondrion. Mutations in this gene have been found in patients with hereditary myopathy with lactic acidosis. A disease-associated mutation in an intron may activate a cryptic splice site, resulting in the production of a splice variant encoding a putatively non-functional protein. A pseudogene of this gene is present on chromosome 1. [provided by RefSeq, Feb 2016]

COX18 cytochrome c oxidase assembly factor

This gene encodes a cytochrome c oxidase assembly protein. The encoded protein is essential for integral membrane protein insertion into the mitochondrial inner membrane. It is also required for cytochrome c oxidase assembly and activity. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014]

COX10 heme A:farnesyltransferase cytochrome c oxidase assembly factor

Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes heme A:farnesyltransferase, which is not a structural subunit but required for the expression of functional COX and functions in the maturation of the heme A prosthetic group of COX. This protein is predicted to contain 7-9 transmembrane domains localized in the mitochondrial inner membrane. A gene mutation, which results in the substitution of a lysine for an asparagine (N204K), is identified to be responsible for cytochrome c oxidase deficiency. In addition, this gene is disrupted in patients with CMT1A (Charcot-Marie-Tooth type 1A) duplication and with HNPP (hereditary neuropathy with liability to pressure palsies) deletion. [provided by RefSeq, Jul 2008]

cytochrome c oxidase assembly homolog 15 (yeast)

Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be essential for the biogenesis of COX formation and may function in the hydroxylation of heme O, according to the yeast mutant studies. This protein is predicted to contain 5 transmembrane domains localized in the mitochondrial inner membrane. Alternative splicing of this gene generates two transcript variants diverging in the 3' region. [provided by RefSeq, Jul 2008]

COX16 cytochrome c oxidase assembly homolog (S. cerevisiae)

Involved in mitochondrial cytochrome c oxidase assembly. Located in mitochondrial inner membrane. Implicated in mitochondrial complex IV deficiency nuclear type 22. [provided by Alliance of Genome Resources, Mar 2025]

SAMM50 sorting and assembly machinery component

This gene encodes a component of the Sorting and Assembly Machinery (SAM) of the mitochondrial outer membrane. The Sam complex functions in the assembly of beta-barrel proteins into the outer mitochondrial membrane.[provided by RefSeq, Jun 2011]

cytochrome c oxidase assembly factor 5

This gene encodes an ortholog of yeast Pet191, which in yeast is a subunit of a large oligomeric complex associated with the mitochondrial inner membrane, and required for the assembly of the cytochrome c oxidase complex. Mutations in this gene are associated with mitochondrial complex IV deficiency, a disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to a severe disease affecting several tissues and organs. [provided by RefSeq, Dec 2011]

cytochrome c oxidase assembly factor 4 homolog (S. cerevisiae)

Predicted to be involved in mitochondrial cytochrome c oxidase assembly. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

cytochrome c oxidase assembly factor 7 (putative)

Involved in respiratory chain complex IV assembly. Located in mitochondrion and nucleoplasm. Is active in mitochondrial intermembrane space. Implicated in spinocerebellar ataxia with axonal neuropathy type 3. [provided by Alliance of Genome Resources, Mar 2025]

cytochrome c oxidase assembly factor 6

This gene encodes a member of the cytochrome c oxidase subunit 6B family. The encoded protein associates with cytochrome c oxidase may act has an cytochrome c oxidase mitochondrial respiratory complex VI assembly factor. Mutations in this gene may be associated with fatal infantile cardiomyopathy. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2014]

cytochrome c oxidase assembly factor 1 homolog (S. cerevisiae)

Involved in mitochondrial cytochrome c oxidase assembly and mitochondrial respiratory chain complex I assembly. Located in cytosol and mitochondrial inner membrane. [provided by Alliance of Genome Resources, Mar 2025]

cytochrome c oxidase assembly factor 3

This gene encodes a member of the cytochrome c oxidase assembly factor family. Studies of a related gene in fly suggest that the encoded protein is localized to mitochondria and is essential for cytochrome c oxidase function. [provided by RefSeq, Nov 2012]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 2 pseudogene

nucleosome assembly protein 1-like 4 pseudogene 2

nucleosome assembly protein 1-like 4 pseudogene 3

iron-sulfur cluster assembly 1 homolog (S. cerevisiae) pseudogene

iron-sulfur cluster assembly 1 homolog (S. cerevisiae) pseudogene

nucleosome assembly protein 1-like 4 pseudogene 1

COPII coat assembly protein SEC16-like

ATP synthase mitochondrial F1 complex assembly factor 2

This gene encodes an assembly factor for the F(1) component of the mitochondrial ATP synthase. This protein binds specifically to the F1 alpha subunit and is thought to prevent this subunit from forming nonproductive homooligomers during enzyme assembly. This gene is located within the Smith-Magenis syndrome region on chromosome 17. An alternatively spliced transcript variant has been described, but its biological validity has not been determined. [provided by RefSeq, Jul 2008]

ATP synthase mitochondrial F1 complex assembly factor 1

This gene encodes an assembly factor for the F(1) component of the mitochondrial ATP synthase. This protein binds specifically to the F1 beta subunit and is thought to prevent this subunit from forming nonproductive homooligomers during enzyme assembly. Alternatively spliced transcript variants have been identified. [provided by RefSeq, Aug 2011]

COX20 cytochrome c oxidase assembly factor

This gene encodes a protein that plays a role in the assembly of cytochrome C oxidase, an important component of the respiratory pathway. It contains two transmembrane helices and localizes to the mitochondrial membrane. Mutations in this gene can cause mitochondrial complex IV deficiency, which results in ataxia and muscle hypotonia. There are multiple pseudogenes for this gene. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2015]

nuclear paraspeckle assembly transcript 1 (non-protein coding)

This gene produces a long non-coding RNA (lncRNA) transcribed from the multiple endocrine neoplasia locus. This lncRNA is retained in the nucleus where it forms the core structural component of the paraspeckle sub-organelles. It may act as a transcriptional regulator for numerous genes, including some genes involved in cancer progression. [provided by RefSeq, Mar 2015]

SCO2 cytochrome c oxidase assembly protein

Cytochrome c oxidase (COX) catalyzes the transfer of electrons from cytochrome c to molecular oxygen, which helps to maintain the proton gradient across the inner mitochondrial membrane that is necessary for aerobic ATP production. Human COX is a multimeric protein complex that requires several assembly factors; this gene encodes one of the COX assembly factors. The encoded protein is a metallochaperone that is involved in the biogenesis of cytochrome c oxidase subunit II. Mutations in this gene are associated with fatal infantile encephalocardiomyopathy and myopia 6. [provided by RefSeq, Oct 2014]

NADH dehydrogenase (ubiquinone) complex I, assembly factor 4 pseudogene 4

NADH dehydrogenase (ubiquinone) complex I, assembly factor 4 pseudogene 3

NADH dehydrogenase (ubiquinone) complex I, assembly factor 4 pseudogene 2

NADH dehydrogenase (ubiquinone) complex I, assembly factor 4 pseudogene 1

mitotic spindle assembly checkpoint protein MAD2A-like

succinate dehydrogenase complex assembly factor 1

The succinate dehydrogenase (SDH) complex (or complex II) of the mitochondrial respiratory chain is composed of 4 individual subunits. The protein encoded by this gene resides in the mitochondria, and is essential for SDH assembly, but does not physically associate with the complex in vivo. Mutations in this gene are associated with SDH-defective infantile leukoencephalopathy (mitochondrial complex II deficiency).[provided by RefSeq, Mar 2010]

succinate dehydrogenase complex assembly factor 2

This gene encodes a mitochondrial assembly factor needed for the flavination of a succinate dehydrogenase complex subunit (SDHA), which is required for activity of the succinate dehydrogenase complex. Mutations in this gene are associated with paraganglioma. [provided by RefSeq, May 2022]

succinate dehydrogenase complex assembly factor 3

Predicted to be involved in mitochondrial respiratory chain complex II assembly; regulation of gluconeogenesis; and succinate metabolic process. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

succinate dehydrogenase complex assembly factor 4

Predicted to enable enzyme activator activity. Involved in cellular respiration and mitochondrial respiratory chain complex II assembly. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

iron-sulfur cluster assembly 1 pseudogene 2

iron-sulfur cluster assembly 1

ISCA1 is a mitochondrial protein involved in the biogenesis and assembly of iron-sulfur clusters, which play a role in electron-transfer reactions (Cozar-Castellano et al., 2004 [PubMed 15262227]).[supplied by OMIM, Mar 2008]

iron-sulfur cluster assembly 2

The protein encoded by this gene is an A-type iron-sulfur cluster (ISC) protein found in mitochondria. The encoded protein appears to be involved in the maturation of mitochondrial iron-sulfur proteins. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2012]

mitochondrial assembly of ribosomal large subunit 1

Enables mitochondrial large ribosomal subunit binding activity. Involved in negative regulation of mitochondrial translation and ribosomal large subunit biogenesis. Located in cytosol and mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

nucleosome assembly protein 1-like 5 pseudogene

ubiquinol-cytochrome c reductase complex assembly factor 1

This gene encodes a transmembrane protein that is structurally similar to the mouse basic fibroblast growth factor repressed ZIC-binding protein. In mouse this protein may be involved in fibroblast growth factor regulated growth control. In humans, polymorphisms in this gene are associated with variation in human height and osteoarthritis. Alternate splicing results in multiple transcript variants. [provided by RefSeq, May 2010]

ubiquinol-cytochrome c reductase complex assembly factor 3

Complex III is a mitochondrial inner membrane protein complex that transfers electrons from ubiquinol to cytochrome c. This gene encodes a protein that functions in complex III assembly. Mutations in this gene result in Mitochondrial complex III deficiency, nuclear type 9. [provided by RefSeq, Dec 2014]

ubiquinol-cytochrome c reductase complex assembly factor 2

This gene encodes a nucleoid protein localized to the mitochondria inner membrane. The encoded protein affects regulation of insulin secretion, mitochondrial ATP production, and myogenesis through modulation of mitochondrial respiratory chain activity. [provided by RefSeq, Oct 2012]

MNAT CDK-activating kinase assembly factor 1

The protein encoded by this gene, along with cyclin H and CDK7, forms the CDK-activating kinase (CAK) enzymatic complex. This complex activates several cyclin-associated kinases and can also associate with TFIIH to activate transcription by RNA polymerase II. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2011]

chromatin assembly factor 1, subunit B (p60) pseudogene

TAM41, mitochondrial translocator assembly and maintenance protein, homolog (S. cerevisiae)

Predicted to enable phosphatidate cytidylyltransferase activity. Predicted to be involved in CDP-diacylglycerol biosynthetic process and cardiolipin biosynthetic process. Is active in mitochondrion. Implicated in combined oxidative phosphorylation deficiency 56. [provided by Alliance of Genome Resources, Mar 2025]

SHQ1, H/ACA ribonucleoprotein assembly factor

SHQ1 assists in the assembly of H/ACA-box ribonucleoproteins that function in the processing of ribosomal RNAs, modification of spliceosomal small nuclear RNAs, and stabilization of telomerase (see MIM 602322) (Grozdanov et al., 2009 [PubMed 19383767]).[supplied by OMIM, Dec 2010]

dynein, axonemal, assembly factor 1

The protein encoded by this gene is cilium-specific and is required for the stability of the ciliary architecture. It is involved in the regulation of microtubule-based cilia and actin-based brush border microvilli. Mutations in this gene are associated with primary ciliary dyskinesia-13. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]

iron-sulfur cluster assembly 2 pseudogene 1

cytosolic iron-sulfur assembly component 2B

Involved in chromosome segregation; iron-sulfur cluster assembly; and protein maturation by iron-sulfur cluster transfer. Located in cytosol; nucleoplasm; and spindle. Part of MMXD complex and cytosolic [4Fe-4S] assembly targeting complex. [provided by Alliance of Genome Resources, Mar 2025]

distal membrane arm assembly component 2 like

This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. This gene encodes the subunit s, also known as factor B, of the proton channel. This subunit is necessary for the energy transduction activity of the ATP synthase complexes. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

formation of mitochondrial complex V assembly factor 1 homolog

Involved in mitochondrial proton-transporting ATP synthase complex assembly. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

cytosolic iron-sulfur assembly component 2A

Predicted to enable metal ion binding activity. Involved in iron-sulfur cluster assembly and protein maturation by iron-sulfur cluster transfer. Located in cytosol and nucleoplasm. Part of cytosolic [4Fe-4S] assembly targeting complex. [provided by Alliance of Genome Resources, Mar 2025]

distal membrane arm assembly component 2

Involved in mitochondrial respiratory chain complex I assembly. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

cytosolic iron-sulfur assembly component 3

Predicted to enable 4 iron, 4 sulfur cluster binding activity and metal ion binding activity. Involved in several processes, including intracellular oxygen homeostasis; iron-sulfur cluster assembly; and response to hypoxia. Part of cytosolic [4Fe-4S] assembly targeting complex. [provided by Alliance of Genome Resources, Mar 2025]

dynein axonemal assembly factor 4

This gene encodes a tetratricopeptide repeat domain-containing protein. The encoded protein interacts with estrogen receptors and the heat shock proteins, Hsp70 and Hsp90. An homologous protein in rat has been shown to function in neuronal migration in the developing neocortex. A chromosomal translocation involving this gene is associated with a susceptibility to developmental dyslexia. Mutations in this gene are associated with deficits in reading and spelling. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the downstream cell cycle progression 1 (CCPG1) gene. [provided by RefSeq, Mar 2011]

ATP23 metallopeptidase and ATP synthase assembly factor homolog

The protein encoded by this gene is amplified in glioblastomas and interacts with the DNA binding subunit of DNA-dependent protein kinase. This kinase is involved in double-strand break repair (DSB), and higher expression of the encoded protein increases the efficiency of DSB. In addition, comparison to orthologous proteins strongly suggests that this protein is a metalloprotease important in the biosynthesis of mitochondrial ATPase. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2016]

dynein axonemal assembly factor 11

The protein encoded by this gene contains several leucine-rich repeat domains and appears to be involved in the motility of cilia. Defects in this gene are a cause of primary ciliary dyskinesia-19 (CILD19). Alternative splicing of this gene results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 4, 11 and 22. [provided by RefSeq, Apr 2016]

lipid droplet assembly factor 1

Involved in lipid droplet formation. Located in endoplasmic reticulum membrane and lipid droplet. [provided by Alliance of Genome Resources, Mar 2025]

dynein axonemal assembly factor 8

Predicted to enable dynein complex binding activity. Predicted to be involved in outer dynein arm assembly. Located in dynein axonemal particle. [provided by Alliance of Genome Resources, Mar 2025]

dynein axonemal assembly factor 9

This gene encodes an uncharacterized protein with a C-terminal coiled-coil region. The gene is located on chromosome 20p13 in a 1.8 Mb region linked to a spinocerebellar ataxia phenotype, but this gene does not appear to be a disease candidate. [provided by RefSeq, Dec 2011]

ubiquinol-cytochrome c reductase complex assembly factor 4

Predicted to be involved in mitochondrial respiratory chain complex III assembly. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

distal membrane arm assembly component 1

Involved in mitochondrial respiratory chain complex I assembly. Located in mitochondrial inner membrane. [provided by Alliance of Genome Resources, Mar 2025]

ubiquinol-cytochrome c reductase complex assembly factor 6

Involved in mitochondrial cytochrome c oxidase assembly and mitochondrial respiratory chain complex III assembly. Located in mitochondrion. Is active in mitochondrial inner membrane. [provided by Alliance of Genome Resources, Mar 2025]

phagosome assembly factor 1

Predicted to be involved in Golgi to plasma membrane protein transport. Located in phagophore assembly site. [provided by Alliance of Genome Resources, Mar 2025]

NADH:ubiquinone oxidoreductase complex assembly factor 8

Involved in mitochondrial respiratory chain complex I assembly. Located in mitochondrial matrix. Implicated in nuclear type mitochondrial complex I deficiency 34. [provided by Alliance of Genome Resources, Mar 2025]

cytochrome c oxidase assembly factor 8

This gene encodes a protein that localizes to the mitochondria, where it stimulates the release of cytochrome c, thereby promoting programmed cell death. Mutations in this gene have been found in individuals with mitochondrial complex IV deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2014]

deuterosome assembly protein 1

Enables identical protein binding activity. Predicted to be involved in centriole replication and de novo centriole assembly involved in multi-ciliated epithelial cell differentiation. Predicted to be located in cytoplasm and membrane. Predicted to be active in centriole and deuterosome. [provided by Alliance of Genome Resources, Mar 2025]

dynein axonemal assembly factor 6

Enables dynein intermediate chain binding activity. Involved in flagellated sperm motility; inner dynein arm assembly; and outer dynein arm assembly. Located in trans-Golgi network. Implicated in primary ciliary dyskinesia 36. [provided by Alliance of Genome Resources, Mar 2025]

ubiquinol-cytochrome c reductase complex assembly factor 5

Enables mitochondrial ribosome binding activity. Involved in mitochondrial cytochrome c oxidase assembly. Located in mitochondrion. Is active in mitochondrial inner membrane. [provided by Alliance of Genome Resources, Mar 2025]

dynein axonemal assembly factor 10

This gene encodes a protein with two WD40 repeat domains thought to be involved in an apoptosis via activation of caspase-3. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2012]

nucleosome assembly protein 1 like 6, pseudogene

Predicted to be involved in nucleosome assembly. Predicted to be located in nucleus. [provided by Alliance of Genome Resources, Mar 2025]

dynein axonemal assembly factor 19

Enables protein homodimerization activity. Involved in axonemal dynein complex assembly; cilium movement; and determination of left/right symmetry. Predicted to be located in axoneme. Predicted to be part of outer dynein arm. Implicated in primary ciliary dyskinesia 17. [provided by Alliance of Genome Resources, Mar 2025]

vacuolar ATPase assembly factor VMA12

The protein encoded by this gene has been observed to localize to the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) and coat protein complex I (COPI) in some human cells. The encoded protein shares some homology with the yeast protein Vma12. Defects in this gene are a cause of congenital disorder of glycosylation, type IIp. [provided by RefSeq, Mar 2016]

40S small subunit processome assembly factor 1

Enables RNA binding activity. Involved in ribosomal small subunit biogenesis. Located in chromosome. Part of small-subunit processome. [provided by Alliance of Genome Resources, Mar 2025]

vacuolar ATPase assembly factor VMA22

The protein encoded by this gene has been observed to localize to the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) and coat protein complex I (COPI) vesicles in some human cells. The encoded protein shares some homology with the yeast V-ATPase assembly factor Vma22p, and the orthologous protein in mouse promotes cell proliferation and suppresses cell death. Defects in this gene are a cause of congenital disorder of glycosylation, type IIo in humans. [provided by RefSeq, Mar 2016]

centrosome assembly and centriole elongation protein

This gene encodes a protein that belongs to the centromere protein family. During cell division, this protein plays a structural role in the maintenance of centrosome integrity and normal spindle morphology, and it is involved in microtubule disassembly at the centrosome. This protein can function as a transcriptional coactivator in the Stat5 signaling pathway, and also as a coactivator of NF-kappaB-mediated transcription, likely via its interaction with the coactivator p300/CREB-binding protein. Mutations in this gene are associated with primary autosomal recessive microcephaly, a disorder characterized by severely reduced brain size and cognitive disability. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Apr 2012]

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-binding clathrin assembly protein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the clathrin coat assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2023

genes participating in the clathrin coat assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin coat assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of clathrin coat assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin coat assembly involved in endocytosis biological process from the curated GO Biological Process Annotations 2025 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Probable cytosolic iron-sulfur protein assembly protein, CIAO1/Cia1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-glycan biosynthesis class S protein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol transfer protein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the phosphatidylinositol 3-kinase/protein kinase B signal transduction biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction biological process from the curated GO Biological Process Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin coat of coated pit cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin adaptor complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-coated vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin coat cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-coated endocytic vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted monoamine transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-coated vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin vesicle coat cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted acetylcholine transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted monoamine transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin coat of endocytic vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted glutamate transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted acetylcholine transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-sculpted glutamate transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin-coated endocytic vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the clathrin coat of trans-golgi network vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin coat of coated pit cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin adaptor complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin-coated vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin coat cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin-coated endocytic vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin-coated vesicle membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin vesicle coat cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin coat of endocytic vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin-coated endocytic vesicle membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the clathrin coat of trans-golgi network vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term clathrin 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 clathrin coat disassembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of clathrin-mediated endocytosis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of clathrin-mediated endocytosis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of clathrin-mediated endocytosis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the clathrin-mediated endocytosis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin coat of coated pit cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin adaptor complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-coated vesicle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin coat cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-coated endocytic vesicle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-sculpted monoamine transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-coated vesicle membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin vesicle coat cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-coated endocytic vesicle membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin coat of endocytic vesicle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-sculpted glutamate transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin-sculpted acetylcholine transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the clathrin coat of trans-golgi network vesicle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the clathrin adaptor activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, mu subunit, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, gamma-adaptin, appendage protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain, linker protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain, propeller repeat protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, mu subunit, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor complex, small chain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Coatomer/clathrin adaptor appendage, Ig-like subdomain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain-related protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain, propeller, N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin light chain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain, linker/propeller domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin alpha-adaptin/coatomer adaptor, appendage, C-terminal subdomain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain, linker, core motif protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin/coatomer adaptor, adaptin-like, N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, mu subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin adaptor, alpha-adaptin, appendage, Ig-like subdomain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clathrin, heavy chain/VPS, 7-fold repeat protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From Phosphosite Textmining Biological Term Annotations

proteins co-occuring with the biological term clathrin in abstracts of publications describing phosphosites from the Phosphosite Textmining Biological Term Annotations dataset.

From Reactome Pathways 2014

proteins participating in the Nef-mediates down modulation of cell surface receptors by recruiting them to clathrin adapters pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Clathrin derived vesicle budding pathway from the Reactome Pathways dataset.

From GO Biological Process Annotations 2023

genes participating in the clathrin-coated vesicle cargo loading, AP-3-mediated biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the clathrin coat disassembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the clathrin-dependent synaptic vesicle endocytosis biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the clathrin-dependent endocytosis of virus by host cell biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the clathrin-coated vesicle cargo loading biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-coated vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-coated endocytic vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-coated endocytic vesicle membrane cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin coat of coated pit cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-coated vesicle membrane cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin coat of trans-Golgi network vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin coat cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted acetylcholine transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted glutamate transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted monoamine transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin adaptor complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin vesicle coat cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin coat of endocytic vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted acetylcholine transport vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted glutamate transport vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the clathrin-sculpted monoamine transport vesicle cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the clathrin adaptor activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From Reactome Pathways 2024

proteins participating in the Cargo recognition for clathrin-mediated endocytosis pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Clathrin-mediated endocytosis pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Nef-mediates down modulation of cell surface receptors by recruiting them to clathrin adapters pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin-coated vesicle cargo loading, AP-3-mediated biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin coat disassembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of clathrin-dependent endocytosis biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin-dependent endocytosis of virus by host cell biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin-dependent synaptic vesicle endocytosis biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the clathrin-coated vesicle cargo loading biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-coated vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-coated endocytic vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-coated endocytic vesicle membrane cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin coat of coated pit cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-coated vesicle membrane cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin coat of trans-Golgi network vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin coat cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted acetylcholine transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted glutamate transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted monoamine transport vesicle membrane cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin adaptor complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin vesicle coat cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin coat of endocytic vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted acetylcholine transport vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted glutamate transport vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the clathrin-sculpted monoamine transport vesicle cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the clathrin adaptor activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-coated vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-coated vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Clathrin coat of endocytic vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-coated pit cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Clathrin coat cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Clathrin coat of coated pit cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Clathrin adaptor complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Clathrin vesicle coat cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Clathrin complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-coated endocytic vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Clathrin coat of trans-Golgi network vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-coated endocytic vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted monoamine transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted monoamine transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted gamma-aminobutyric acid transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted glutamate transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted glutamate transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted acetylcholine transport vesicle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the clathrin-sculpted acetylcholine transport vesicle membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin coat cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-coated vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-coated pit cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin coat of trans-Golgi network vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin coat of endocytic vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin coat of coated pit cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin vesicle coat cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-coated endocytic vesicle membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-coated vesicle membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-coated endocytic vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin adaptor complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Clathrin coat of synaptic vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-sculpted gamma-aminobutyric acid transport vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-sculpted vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-sculpted glutamate transport vesicle membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-sculpted glutamate transport vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-sculpted monoamine transport vesicle cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the clathrin-sculpted monoamine transport vesicle membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Clathrin-mediated endocytosis assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From GAD Gene-Disease Associations

genes associated with the disease activated protein c resistance; blood coagulation disorders; liver diseases; protein c deficiency; protein s deficiency; thrombosis in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease activated protein c resistance; antithrombin iii deficiency; pregnancy complications, hematologic; protein c deficiency; protein s deficiency; puerperal disorders; pulmonary embolism; pulmonary embolisms; thrombophilia; venous thrombosis in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GO Biological Process Annotations 2015

genes participating in the protein-dna complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the heterotrimeric g-protein complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the peptide antigen assembly with mhc class ii protein complex biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the mhc class ii protein complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the polysaccharide assembly with mhc class ii protein complex biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the protein-carbohydrate complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the protein-lipid complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of chaperone-mediated protein complex assembly 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 complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the positive regulation of chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptide antigen assembly with mhc class i protein complex biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the peptide antigen assembly with mhc protein complex biological process from the curated GO Biological Process Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cytochrome c oxidase assembly protein CtaG/Cox11, domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Spindle assembly abnormal protein 6 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the COPII coat assembly protein, Sec16 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Nucleosome assembly protein (NAP) protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cytochrome c oxidase assembly protein PET191 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cytochrome c oxidase assembly protein CtaG/Cox11 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peroxisome assembly protein 12 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the UNC-45/Ring assembly protein 3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cytochrome c oxidase assembly protein COX14 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cytochrome c oxidase assembly protein COX16 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATP12, ATPase F1F0-assembly protein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Vacuolar ATPase assembly integral membrane protein VMA21-like domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Cytochrome oxidase assembly protein 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of protein-containing complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein lipidation involved in autophagosome assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein-containing complex assembly 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-containing complex assembly 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-containing complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the MHC class Ib protein complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the peptide antigen assembly with MHC class I protein complex biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein localization to phagophore assembly site biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the peptide antigen assembly with MHC class II protein complex biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein-lipid complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein-DNA complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the MHC class II protein complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein-RNA complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein localization to kinetochore involved in kinetochore assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the heterotrimeric G-protein complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the MHC class I protein complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the peptide antigen assembly with MHC protein complex biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of protein-containing complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein lipidation involved in autophagosome assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein-containing complex assembly 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-containing complex assembly 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-containing complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the MHC class Ib protein complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptide antigen assembly with MHC class I protein complex biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein localization to phagophore assembly site biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptide antigen assembly with MHC class II protein complex biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein-lipid complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein-DNA complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the MHC class II protein complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein-containing complex assembly involved in synapse maturation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein-RNA complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the heterotrimeric G-protein complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein localization to kinetochore involved in kinetochore assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

genes participating in the MHC class I protein complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the peptide antigen assembly with MHC protein complex biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of chaperone-mediated protein complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Protein folding and complex assembly regulation assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the phosphatidylinositol 3-kinase complex, class iii cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the phosphatidylinositol 3-kinase complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the phosphatidylinositol 3-kinase complex, class i cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the phosphatidylinositol 3-kinase complex, class ib cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the phosphatidylinositol 3-kinase complex, class ia cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the phosphatidylinositol 3-kinase complex, class iii cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the phosphatidylinositol 3-kinase complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the phosphatidylinositol 3-kinase complex, class i cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the phosphatidylinositol 3-kinase complex, class iii, type ii cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the phosphatidylinositol 3-kinase complex, class ib cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the phosphatidylinositol 3-kinase complex, class ia cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the phosphatidylinositol 3-kinase complex, class iii, type i cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From CORUM Protein Complexes

proteins in the Phosphatidylinositol 3-kinase (PIK3CA, PIK3R1) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the Phosphatidylinositol 3-kinase complex (PIK3C3, PIK3R4) protein complex from the CORUM Protein Complexes dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical Phosphatidylinositol 4,5-Diphosphate from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical phosphatidylinositol 3,4-diphosphate from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical Phosphatidylinositol Phosphates from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical dioctanoyl-phosphatidylinositol 4,5-bisphosphate from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical phosphatidylinositol 4-phosphate from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical phosphatidylinositol 3,4,5-triphosphate from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical phosphatidylinositol dimannoside from the curated CTD Gene-Chemical Interactions dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term phosphatidylinositol 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 regulation of phosphatidylinositol dephosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of 1-phosphatidylinositol 4-kinase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of 1-phosphatidylinositol 4-kinase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol-3-phosphate biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of phosphatidylinositol 3-kinase signaling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol 3-kinase signaling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol-mediated signaling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol 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 phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol 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 phosphatidylinositol 3-kinase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of phosphatidylinositol 3-kinase signaling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the insulin receptor signaling pathway via phosphatidylinositol 3-kinase biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of phosphatidylinositol 3-kinase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of phosphatidylinositol 3-kinase signaling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol acyl-chain remodeling biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of phosphatidylinositol 3-kinase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol catabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the phosphatidylinositol biosynthetic 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 phosphatidylinositol biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the phosphatidylinositol 3-kinase complex, class iii cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the phosphatidylinositol 3-kinase complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the phosphatidylinositol 3-kinase complex, class i cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the phosphatidylinositol 3-kinase complex, class iii, type i cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the phosphatidylinositol 3-kinase complex, class iii, type ii cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the phosphatidylinositol 3-kinase complex, class ib cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the phosphatidylinositol 3-kinase complex, class ia cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol phosphate 5-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 1-phosphatidylinositol-3-phosphate 5-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol phosphate 4-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 1-phosphatidylinositol-4-phosphate 5-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol trisphosphate phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-3-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol phospholipase c activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 1-phosphatidylinositol-4-phosphate 3-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-4-phosphate phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol 3-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-4,5-bisphosphate 3-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol monophosphate phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol n-acetylglucosaminyltransferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol 3-kinase regulator activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol phosphate kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol phosphate phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol bisphosphate phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 1-phosphatidylinositol 4-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 1-phosphatidylinositol-3-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 1-phosphatidylinositol-3-kinase regulator activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 1-phosphatidylinositol-5-phosphate 4-kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol bisphosphate kinase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphatidylinositol transporter activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the Phosphatidylinositol-3,4,5-trisphosphate metabolite from the curated HMDB Metabolites of Enzymes dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-4-phosphate 5-kinase, N-terminal domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-4-phosphate 5-kinase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol N-acetylglucosaminyltransferase, GPI19/PIG-P subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-4-phosphate 5-kinase, core protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-4-phosphate 5-kinase, core, subgroup protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol Kinase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phospholipase C, phosphatidylinositol-specific , X domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phospholipase C, phosphatidylinositol-specific, Y domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol 4-kinase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol N-acetylglucosaminyltransferase subunit C protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol 3/4-kinase, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol 3-kinase, C2 domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Bifunctional phosphatidylinositol trisphosphate phosphatase/dual specificity phosphatase PTEN protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol 3-kinase, Vps34 type protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol-4-phosphate 5-kinase, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphatidylinositol 3-/4-kinase, catalytic domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the N-acetylglucosaminyl phosphatidylinositol deacetylase-related protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From KEGG Pathways

proteins participating in the phosphatidylinositol signaling system pathway from the KEGG Pathways dataset.

From Phosphosite Textmining Biological Term Annotations

proteins co-occuring with the biological term phosphatidylinositol-3-kinases in abstracts of publications describing phosphosites from the Phosphosite Textmining Biological Term Annotations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Phosphatidylinositol 4,5-Bisphosphate 5-Phosphatase Deficiency in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Phosphatidylinositol Measurement in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of phosphatidylinositol 3-kinase activity biological process from the curated GO Biological Process Annotations 2023 dataset.