Harmonizome 3.0

thioredoxin 2 pseudogene

thioredoxin 2

This nuclear gene encodes a mitochondrial member of the thioredoxin family, a group of small multifunctional redox-active proteins. The encoded protein may play important roles in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis. [provided by RefSeq, Jul 2008]

thioredoxin interacting protein

This gene encodes a thioredoxin-binding protein that is a member of the alpha arrestin protein family. Thioredoxin is a thiol-oxidoreductase that is a major regulator of cellular redox signaling which protects cells from oxidative stress. This protein inhibits the antioxidative function of thioredoxin resulting in the accumulation of reactive oxygen species and cellular stress. This protein also functions as a regulator of cellular metabolism and of endoplasmic reticulum (ER) stress. This protein may also function as a tumor suppressor. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]

thioredoxin 1 pseudogene 7

thioredoxin-related transmembrane protein 4

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, a catalytically active thioredoxin domain, one transmembrane domain and C-terminal ASP/GLU-rich calcium binding domain. Unlike most members of this gene family, it lacks a C-terminal ER-retention sequence. The encoded protein has been shown to have reductase activity in vitro. [provided by RefSeq, Jan 2017]

thioredoxin-related transmembrane protein 1

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, a catalytically active thioredoxin domain, and one transmembrane domain. Unlike most members of this gene family, it lacks a C-terminal ER-retention sequence. The mature membrane-bound protein can both oxidize and reduce disulfide bonds and acts selectively on membrane-associated polypeptides. [provided by RefSeq, Jan 2017]

thioredoxin-related transmembrane protein 3

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The canonical protein encoded by this gene has an N-terminal ER-signal sequence, a catalytically active thioredoxin domain, one transmembrane domain and a C-terminal ER-retention sequence. This gene is expressed in many tissues but has its highest expression in heart and skeletal muscle. It is expressed in the retinal neuroepithelium and lens epithelium in the developing murine eye and haploinsufficiency of this gene in humans and zebrafish is associated with microphthalmia. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Apr 2017]

thioredoxin-related transmembrane protein 2

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, a catalytically active thioredoxin domain, one transmembrane domain and a C-terminal ER-retention sequence. This protein is enriched on the mitochondria-associated-membrane of the ER via palmitoylation of two of its cytosolically exposed cysteines. [provided by RefSeq, Jan 2017]

thioredoxin

The protein encoded by this gene acts as a homodimer and is involved in many redox reactions. The encoded protein is active in the reversible S-nitrosylation of cysteines in certain proteins, which is part of the response to intracellular nitric oxide. This protein is found in the cytoplasm. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011]

thioredoxin pseudogene 6

thioredoxin domain containing 15

This gene encodes a member of the thioredoxin superfamily. Members of this family are characterized by a conserved active motif called the thioredoxin fold that catalyzes disulfide bond formation and isomerization. [provided by RefSeq, Apr 2017]

thioredoxin domain containing 17

Enables peroxidase activity and protein-disulfide reductase (NAD(P)H) activity. Involved in tumor necrosis factor-mediated signaling pathway. Located in cytosol. [provided by Alliance of Genome Resources, Mar 2025]

thioredoxin domain containing 16

Located in endoplasmic reticulum lumen. [provided by Alliance of Genome Resources, Mar 2025]

thioredoxin domain containing 11

Predicted to be located in endoplasmic reticulum membrane. [provided by Alliance of Genome Resources, Mar 2025]

thioredoxin domain containing 12 (endoplasmic reticulum)

This gene encodes a member of the thioredoxin superfamily. Members of this family are characterized by a conserved active motif called the thioredoxin fold that catalyzes disulfide bond formation and isomerization. This protein localizes to the endoplasmic reticulum and has a single atypical active motif. The encoded protein is mainly involved in catalyzing native disulfide bond formation and displays activity similar to protein-disulfide isomerases. This protein may play a role in defense against endoplasmic reticulum stress. Alternate splicing results in both coding and non-coding variants. [provided by RefSeq, Mar 2012]

thioredoxin-related transmembrane protein 2 pseudogene 1

thioredoxin pseudogene 5

thioredoxin pseudogene 4

thioredoxin pseudogene 2

thioredoxin domain containing 9

The protein encoded by this gene is a member of the thioredoxin family. The exact function of this protein is not known but it is associated with cell differentiation. [provided by RefSeq, Jul 2008]

thioredoxin domain containing 8 (spermatozoa)

Involved in spermatogenesis. Located in Golgi apparatus. Biomarker of male infertility. [provided by Alliance of Genome Resources, Mar 2025]

thioredoxin domain containing 2 (spermatozoa)

Enables thioredoxin-disulfide reductase (NADPH) activity. Predicted to be involved in cell redox homeostasis and spermatogenesis. Predicted to act upstream of or within cellular response to reactive oxygen species and flagellated sperm motility. Located in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

thioredoxin domain containing 5 (endoplasmic reticulum)

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal endoplasmic reticulum (ER)-signal sequence, three catalytically active thioredoxin domains and a C-terminal ER-retention sequence. Its expression is induced by hypoxia and its role may be to protect hypoxic cells from apoptosis. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring upstream BLOC1S5 gene. [provided by RefSeq, Dec 2016]

thioredoxin reductase 3 neighbor

thioredoxin-related transmembrane protein 1 pseudogene

thioredoxin-related transmembrane protein 1 pseudogene

thioredoxin reductase 2

The protein encoded by this gene belongs to the pyridine nucleotide-disulfide oxidoreductase family, and is a member of the thioredoxin (Trx) system. Three thioredoxin reductase (TrxR) isozymes are found in mammals. TrxRs are selenocysteine-containing flavoenzymes, which reduce thioredoxins, as well as other substrates, and play a key role in redox homoeostasis. This gene encodes a mitochondrial form important for scavenging reactive oxygen species in mitochondria. It functions as a homodimer containing FAD, and selenocysteine (Sec) at the active site. Sec is encoded by UGA codon that normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, the Sec insertion sequence (SECIS) element, which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternatively spliced transcript variants encoding different isoforms, including a few localized in the cytosol and some lacking the C-terminal Sec residue, have been found for this gene. [provided by RefSeq, Jun 2017]

thioredoxin reductase 3

The protein encoded by this gene belongs to the pyridine nucleotide-disulfide oxidoreductase family, and is a member of the thioredoxin (Trx) system. Three thioredoxin reductase (TrxR) isozymes are found in mammals. TrxRs are selenocysteine-containing flavoenzymes, which reduce thioredoxins, as well as other substrates, and play a key role in redox homoeostasis. This gene encodes the third TrxR, which unlike the other two isozymes, contains an additional N-terminal glutaredoxin (Grx) domain, and shows highest expression in testis. The Grx domain allows this isozyme to participate in both Trx and glutathione systems. It functions as a homodimer containing FAD, and selenocysteine (Sec) at the active site. Sec is encoded by UGA codon that normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, the Sec insertion sequence (SECIS) element, which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternatively spliced transcript variants have been found for this gene. Experimental evidence suggests the use of a non-AUG (CUG) codon as a translation initiation codon (PMID:20018845). [provided by RefSeq, Aug 2017]

thioredoxin reductase 1

The protein encoded by this gene belongs to the pyridine nucleotide-disulfide oxidoreductase family, and is a member of the thioredoxin (Trx) system. Three thioredoxin reductase (TrxR) isozymes are found in mammals. TrxRs are selenocysteine-containing flavoenzymes, which reduce thioredoxins, as well as other substrates, and play a key role in redox homoeostasis. This gene encodes an ubiquitously expressed, cytosolic form of TrxR, which functions as a homodimer containing FAD, and selenocysteine (Sec) at the active site. Sec is encoded by UGA codon that normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, the Sec insertion sequence (SECIS) element, which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing, primarily at the 5' end, results in transcript variants encoding same or different isoforms, including a glutaredoxin-containing isoform that is predominantly expressed in testis. [provided by RefSeq, May 2017]

thioredoxin pseudogene 3

thioredoxin pseudogene 1

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin-like fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GeneRIF Biological Term Annotations

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

From GO Molecular Function Annotations 2015

genes performing the ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the thioredoxin peroxidase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the thioredoxin-disulfide reductase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From HumanCyc Pathways

proteins participating in the thioredoxin pathway pathway from the HumanCyc Pathways dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin/glutathione reductase selenoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

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

From InterPro Predicted Protein Domain Annotations

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

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2023

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

From GO Molecular Function Annotations 2023

genes performing the ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the thioredoxin peroxidase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the thioredoxin-dependent peroxiredoxin activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the L-methionine:thioredoxin-disulfide S-oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the thioredoxin peroxidase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the thioredoxin-dependent peroxiredoxin activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the L-methionine:thioredoxin-disulfide S-oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term fold 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 morphogenesis of an epithelial fold biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the neural fold formation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the neural fold bending biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the neural fold elevation formation biological process from the curated GO Biological Process Annotations 2015 dataset.

From HPO Gene-Disease Associations

genes associated with the abnormality of the aryepiglottic fold phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the prominent nasolabial fold phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the falciform retinal fold phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the thickened nuchal skin fold phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the UBA/THIF-type NAD/FAD binding fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ubiquitin-fold modifier 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Histone-fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Membrane-anchored ubiquitin-fold protein, HCG-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Nucleolar GTP-binding protein 1, Rossman-fold domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATP-grasp fold, subdomain 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATP-grasp fold, subdomain 2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Alpha/Beta hydrolase fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Alpha/beta hydrolase fold-3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Alpha/beta hydrolase fold-1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Alpha/beta hydrolase fold-5 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phenylalanine-tRNA ligase, beta subunit, ferrodoxin-fold anticodon-binding protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Pectin lyase fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the BTB/POZ fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidase C78, ubiquitin fold modifier-specific peptidase 1/ 2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATP-grasp fold, succinyl-CoA synthetase-type protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ubiquitin-fold modifier-conjugating enzyme 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the PAS fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Pectin lyase fold/virulence factor protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATP-grasp fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ribosomal protein S5 domain 2-type fold, subgroup protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Nucleic acid-binding, OB-fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the OB-fold nucleic acid binding domain, AA-tRNA synthetase-type protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the PAS fold-3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATP-grasp fold, RimK-type protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the RNA polymerase Rpb2, OB-fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Rubredoxin-type fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the C-type lectin fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thiamin diphosphate-binding fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ribosomal protein S5 domain 2-type fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Armadillo-type fold 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 MPO Gene-Phenotype Associations

gene mutations causing the abnormal neural fold elevation formation phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal cephalic neural fold morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the failure of head fold formation phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal head fold morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal neural fold formation phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal urogenital fold morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal neural fold morphology phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From TISSUES Text-mining Tissue Protein Expression Evidence Scores

proteins co-occuring with the tissue vocal fold in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Skin Fold (Abnormality) in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Descemet'S Membrane Fold in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Abnormality Of The Aryepiglottic Fold in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Congenital Retinal Fold in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Thickened Nuchal Skin Fold in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Retinal Fold (Finding) in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

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

From DisGeNET Gene-Phenotype Associations

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

From DisGeNET Gene-Phenotype Associations

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

From GO Biological Process Annotations 2023

genes participating in the neural fold bending biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the morphogenesis of an epithelial fold biological process from the curated GO Biological Process Annotations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal head fold morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal neural fold formation phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the retina fold phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal cephalic neural fold morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal neural fold elevation formation phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the absent head fold phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal neural fold morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the abnormal urogenital fold morphology phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025

proteins co-occuring with the tissue Vocal fold in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Subscapular skin fold thickness phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.