DB stringclasses 1
value | DB_Object_ID stringlengths 6 10 | DB_Object_Symbol stringlengths 2 11 | Qualifier stringclasses 21
values | GO_ID stringlengths 10 10 | DB_Reference stringlengths 9 34 | Evidence_Code stringclasses 1
value | Aspect stringclasses 3
values | DB_Object_Name stringlengths 5 112 | DB_Object_Synonym stringlengths 2 114 ⌀ | DB_Object_Type stringclasses 1
value | Taxon stringclasses 106
values | Date int64 20M 20.3M | Assigned_By stringclasses 30
values | Annotation_Extension stringlengths 19 521 ⌀ | PMID stringlengths 4 8 ⌀ | GO_Name stringlengths 4 187 ⌀ | Title stringlengths 24 381 ⌀ | Abstract stringlengths 101 3.97k ⌀ |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
UniProtKB | A0A024RBG1 | NUDT4B | located_in | GO:0005829 | GO_REF:0000052 | IDA | C | Diphosphoinositol polyphosphate phosphohydrolase NUDT4B | NUDT4B | protein | taxon:9606 | 20,241,022 | HPA | null | null | cytosol | null | null |
UniProtKB | A0A075B6N1 | TRBV19 | part_of | GO:0042105 | PMID:21081917 | IDA | C | T cell receptor beta variable 19 | TRBV19 | protein | taxon:9606 | 20,200,113 | UniProt | null | 21081917 | alpha-beta T cell receptor complex | The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation. | Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable β-domain of TCR (TCRVβ). They induce a massive release of cytokines, which can lead to diseases such as food poisoning and toxic sh... |
UniProtKB | A0A087WT01 | TRAV27 | part_of | GO:0042105 | PMID:21081917 | IDA | C | T cell receptor alpha variable 27 | TRAV27 | protein | taxon:9606 | 20,200,113 | UniProt | null | 21081917 | alpha-beta T cell receptor complex | The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation. | Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable β-domain of TCR (TCRVβ). They induce a massive release of cytokines, which can lead to diseases such as food poisoning and toxic sh... |
UniProtKB | A0A087X1C5 | CYP2D7 | NOT|enables | GO:0070330 | PMID:18838503 | IDA | F | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 18838503 | aromatase activity | Expression and functional analysis of CYP2D6.24, CYP2D6.26, CYP2D6.27, and CYP2D7 isozymes. | The objectives of this study were to compare the drug-metabolizing activity of human CYP2D6.24 (I297L), CYP2D6.26 (I369T), and CYP2D6.27 (E410K) allelic isoforms with wild-type CYP2D6.1 and to express the CYP2D7 protein derived from an indel polymorphism (CYP2D7 138delT) and investigate its possible codeine O-demethyla... |
UniProtKB | A0A087X1C5 | CYP2D7 | NOT|involved_in | GO:0006805 | PMID:18838503 | IDA | P | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 18838503 | xenobiotic metabolic process | Expression and functional analysis of CYP2D6.24, CYP2D6.26, CYP2D6.27, and CYP2D7 isozymes. | The objectives of this study were to compare the drug-metabolizing activity of human CYP2D6.24 (I297L), CYP2D6.26 (I369T), and CYP2D6.27 (E410K) allelic isoforms with wild-type CYP2D6.1 and to express the CYP2D7 protein derived from an indel polymorphism (CYP2D7 138delT) and investigate its possible codeine O-demethyla... |
UniProtKB | A0A087X1C5 | CYP2D7 | NOT|involved_in | GO:0042178 | PMID:18838503 | IDA | P | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 18838503 | xenobiotic catabolic process | Expression and functional analysis of CYP2D6.24, CYP2D6.26, CYP2D6.27, and CYP2D7 isozymes. | The objectives of this study were to compare the drug-metabolizing activity of human CYP2D6.24 (I297L), CYP2D6.26 (I369T), and CYP2D6.27 (E410K) allelic isoforms with wild-type CYP2D6.1 and to express the CYP2D7 protein derived from an indel polymorphism (CYP2D7 138delT) and investigate its possible codeine O-demethyla... |
UniProtKB | A0A087X1C5 | CYP2D7 | enables | GO:0070330 | PMID:15051713 | IDA | F | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 15051713 | aromatase activity | A frameshift mutation and alternate splicing in human brain generate a functional form of the pseudogene cytochrome P4502D7 that demethylates codeine to morphine. | A frameshift mutation 138delT generates an open reading frame in the pseudogene, cytochrome P4502D7 (CYP2D7), and an alternate spliced functional transcript of CYP2D7 containing partial inclusion of intron 6 was identified in human brain but not in liver or kidney from the same individual. mRNA and protein of the brain... |
UniProtKB | A0A087X1C5 | CYP2D7 | involved_in | GO:0006805 | PMID:15051713 | IDA | P | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 15051713 | xenobiotic metabolic process | A frameshift mutation and alternate splicing in human brain generate a functional form of the pseudogene cytochrome P4502D7 that demethylates codeine to morphine. | A frameshift mutation 138delT generates an open reading frame in the pseudogene, cytochrome P4502D7 (CYP2D7), and an alternate spliced functional transcript of CYP2D7 containing partial inclusion of intron 6 was identified in human brain but not in liver or kidney from the same individual. mRNA and protein of the brain... |
UniProtKB | A0A087X1C5 | CYP2D7 | involved_in | GO:0042178 | PMID:15051713 | IDA | P | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 15051713 | xenobiotic catabolic process | A frameshift mutation and alternate splicing in human brain generate a functional form of the pseudogene cytochrome P4502D7 that demethylates codeine to morphine. | A frameshift mutation 138delT generates an open reading frame in the pseudogene, cytochrome P4502D7 (CYP2D7), and an alternate spliced functional transcript of CYP2D7 containing partial inclusion of intron 6 was identified in human brain but not in liver or kidney from the same individual. mRNA and protein of the brain... |
UniProtKB | A0A087X1C5 | CYP2D7 | located_in | GO:0005737 | PMID:15051713 | IDA | C | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 15051713 | cytoplasm | A frameshift mutation and alternate splicing in human brain generate a functional form of the pseudogene cytochrome P4502D7 that demethylates codeine to morphine. | A frameshift mutation 138delT generates an open reading frame in the pseudogene, cytochrome P4502D7 (CYP2D7), and an alternate spliced functional transcript of CYP2D7 containing partial inclusion of intron 6 was identified in human brain but not in liver or kidney from the same individual. mRNA and protein of the brain... |
UniProtKB | A0A087X1C5 | CYP2D7 | located_in | GO:0005739 | PMID:18838503 | IDA | C | Cytochrome P450 2D7 | CYP2D7 | protein | taxon:9606 | 20,150,123 | UniProt | null | 18838503 | mitochondrion | Expression and functional analysis of CYP2D6.24, CYP2D6.26, CYP2D6.27, and CYP2D7 isozymes. | The objectives of this study were to compare the drug-metabolizing activity of human CYP2D6.24 (I297L), CYP2D6.26 (I369T), and CYP2D6.27 (E410K) allelic isoforms with wild-type CYP2D6.1 and to express the CYP2D7 protein derived from an indel polymorphism (CYP2D7 138delT) and investigate its possible codeine O-demethyla... |
UniProtKB | A0A096LP01 | SMIM26 | located_in | GO:0005739 | PMID:33386847 | IDA | C | Small integral membrane protein 26 | SMIM26|LINC00493 | protein | taxon:9606 | 20,240,108 | UniProt | null | 33386847 | mitochondrion | Identification and analysis of short open reading frames (sORFs) in the initially annotated noncoding RNA LINC00493 from human cells. | Whole transcriptome analyses have revealed that mammalian genomes are massively transcribed, resulting in the production of huge numbers of transcripts with unknown functions (TUFs). Previous research has categorized most TUFs as noncoding RNAs (ncRNAs) because most previously studied TUFs do not encode open reading fr... |
UniProtKB | A0A096LP01 | SMIM26 | located_in | GO:0005741 | PMID:37009826 | IDA | C | Small integral membrane protein 26 | SMIM26|LINC00493 | protein | taxon:9606 | 20,240,108 | UniProt | null | 37009826 | mitochondrial outer membrane | LINC00493-encoded microprotein SMIM26 exerts anti-metastatic activity in renal cell carcinoma. | Human microproteins encoded by long non-coding RNAs (lncRNA) have been increasingly discovered, however, complete functional characterization of these emerging proteins is scattered. Here, we show that LINC00493-encoded SMIM26, an understudied microprotein localized in mitochondria, is tendentiously downregulated in cl... |
UniProtKB | A0A0B4J2F0 | PIGBOS1 | located_in | GO:0005741 | PMID:31653868 | IDA | C | Protein PIGBOS1 | PIGBOS1 | protein | taxon:9606 | 20,191,030 | UniProt | null | 31653868 | mitochondrial outer membrane | Regulation of the ER stress response by a mitochondrial microprotein. | Cellular homeostasis relies on having dedicated and coordinated responses to a variety of stresses. The accumulation of unfolded proteins in the endoplasmic reticulum (ER) is a common stress that triggers a conserved pathway called the unfolded protein response (UPR) that mitigates damage, and dysregulation of UPR unde... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | enables | GO:0003677 | PMID:29983246 | IDA | F | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,329 | UniProt | null | 29983246 | DNA binding | The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. | Cellular homeostasis is coordinated through communication between mitochondria and the nucleus, organelles that each possess their own genomes. Whereas the mitochondrial genome is regulated by factors encoded in the nucleus, the nuclear genome is currently not known to be actively controlled by factors encoded in the m... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0001649 | PMID:30468456 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,329 | UniProt | null | 30468456 | osteoblast differentiation | MOTS-c improves osteoporosis by promoting osteogenic differentiation of bone marrow mesenchymal stem cells via TGF-β/Smad pathway. | <h4>Objective</h4>To explore whether MOTS-c could improve osteoporosis by promoting osteogenic differentiation of rat bone mesenchymal stem cells (BMSCs) via transforming growth factor-β (TGF-β)/Smad pathway.<h4>Materials and methods</h4>Rat BMSCs were isolated and cultured, followed by osteogenic and lipid differentia... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0006357 | PMID:29983246 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,329 | UniProt | null | 29983246 | regulation of transcription by RNA polymerase II | The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. | Cellular homeostasis is coordinated through communication between mitochondria and the nucleus, organelles that each possess their own genomes. Whereas the mitochondrial genome is regulated by factors encoded in the nucleus, the nuclear genome is currently not known to be actively controlled by factors encoded in the m... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0032147 | PMID:25738459 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,160,627 | UniProt | null | 25738459 | activation of protein kinase activity | The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance. | Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA. ... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0033687 | PMID:31081069 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,329 | UniProt | null | 31081069 | osteoblast proliferation | MOTS-c improves osteoporosis by promoting the synthesis of type I collagen in osteoblasts via TGF-β/SMAD signaling pathway. | <h4>Objective</h4>To investigate whether MOTS-c can regulate the synthesis of type I collagen in osteoblasts by regulating TGF-β/SMAD pathway, thereby improving osteoporosis.<h4>Materials and methods</h4>Viability of hFOB1.19 cells treated with MOTS-c was detected by CCK-8 assay. The mRNA and protein levels of TGF-β, S... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0043610 | PMID:25738459 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,160,627 | UniProt | null | 25738459 | regulation of carbohydrate utilization | The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance. | Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA. ... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0048630 | PMID:33554779 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,330 | UniProt | null | 33554779 | skeletal muscle tissue growth | MOTS-c reduces myostatin and muscle atrophy signaling. | Obesity and type 2 diabetes are metabolic diseases, often associated with sarcopenia and muscle dysfunction. MOTS-c, a mitochondrial-derived peptide, acts as a systemic hormone and has been implicated in metabolic homeostasis. Although MOTS-c improves insulin sensitivity in skeletal muscle, whether MOTS-c impacts muscl... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0071902 | PMID:33554779 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,330 | UniProt | null | 33554779 | positive regulation of protein serine/threonine kinase activity | MOTS-c reduces myostatin and muscle atrophy signaling. | Obesity and type 2 diabetes are metabolic diseases, often associated with sarcopenia and muscle dysfunction. MOTS-c, a mitochondrial-derived peptide, acts as a systemic hormone and has been implicated in metabolic homeostasis. Although MOTS-c improves insulin sensitivity in skeletal muscle, whether MOTS-c impacts muscl... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:0072522 | PMID:25738459 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,160,627 | UniProt | null | 25738459 | purine-containing compound biosynthetic process | The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance. | Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA. ... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | involved_in | GO:2001145 | PMID:33554779 | IDA | P | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,330 | UniProt | null | 33554779 | negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity | MOTS-c reduces myostatin and muscle atrophy signaling. | Obesity and type 2 diabetes are metabolic diseases, often associated with sarcopenia and muscle dysfunction. MOTS-c, a mitochondrial-derived peptide, acts as a systemic hormone and has been implicated in metabolic homeostasis. Although MOTS-c improves insulin sensitivity in skeletal muscle, whether MOTS-c impacts muscl... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | located_in | GO:0005615 | PMID:25738459 | IDA | C | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,160,223 | UniProt | null | 25738459 | extracellular space | The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance. | Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA. ... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | located_in | GO:0005634 | PMID:29983246 | IDA | C | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,329 | UniProt | null | 29983246 | nucleus | The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. | Cellular homeostasis is coordinated through communication between mitochondria and the nucleus, organelles that each possess their own genomes. Whereas the mitochondrial genome is regulated by factors encoded in the nucleus, the nuclear genome is currently not known to be actively controlled by factors encoded in the m... |
UniProtKB | A0A0C5B5G6 | MT-RNR1 | located_in | GO:0005739 | PMID:29983246 | IDA | C | Mitochondrial-derived peptide MOTS-c | MT-RNR1 | protein | taxon:9606 | 20,210,329 | UniProt | null | 29983246 | mitochondrion | The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. | Cellular homeostasis is coordinated through communication between mitochondria and the nucleus, organelles that each possess their own genomes. Whereas the mitochondrial genome is regulated by factors encoded in the nucleus, the nuclear genome is currently not known to be actively controlled by factors encoded in the m... |
UniProtKB | A0A0K2S4Q6 | CD300H | NOT|enables | GO:0042803 | PMID:26221034 | IDA | F | Protein CD300H | CD300H | protein | taxon:9606 | 20,180,831 | UniProt | null | 26221034 | protein homodimerization activity | Identification and Characterization of CD300H, a New Member of the Human CD300 Immunoreceptor Family. | Recruitment of circulating monocytes and neutrophils to infection sites is essential for host defense against infections. Here, we identified a previously unannotated gene that encodes an immunoglobulin-like receptor, designated CD300H, which is located in the CD300 gene cluster. CD300H has a short cytoplasmic tail and... |
UniProtKB | A0A0K2S4Q6 | CD300H | involved_in | GO:0030593 | PMID:26221034 | IDA | P | Protein CD300H | CD300H | protein | taxon:9606 | 20,160,428 | UniProt | null | 26221034 | neutrophil chemotaxis | Identification and Characterization of CD300H, a New Member of the Human CD300 Immunoreceptor Family. | Recruitment of circulating monocytes and neutrophils to infection sites is essential for host defense against infections. Here, we identified a previously unannotated gene that encodes an immunoglobulin-like receptor, designated CD300H, which is located in the CD300 gene cluster. CD300H has a short cytoplasmic tail and... |
UniProtKB | A0A0U1RRE5 | NBDY | involved_in | GO:0000956 | PMID:27918561 | IDA | P | Negative regulator of P-body association | NBDY|LINC01420 | protein | taxon:9606 | 20,170,116 | UniProt | null | 27918561 | nuclear-transcribed mRNA catabolic process | A human microprotein that interacts with the mRNA decapping complex. | Proteomic detection of non-annotated microproteins indicates the translation of hundreds of small open reading frames (smORFs) in human cells, but whether these microproteins are functional or not is unknown. Here, we report the discovery and characterization of a 7-kDa human microprotein we named non-annotated P-body ... |
UniProtKB | A0A0U1RRE5 | NBDY | involved_in | GO:0010607 | PMID:27918561 | IDA | P | Negative regulator of P-body association | NBDY|LINC01420 | protein | taxon:9606 | 20,170,116 | UniProt | null | 27918561 | negative regulation of cytoplasmic mRNA processing body assembly | A human microprotein that interacts with the mRNA decapping complex. | Proteomic detection of non-annotated microproteins indicates the translation of hundreds of small open reading frames (smORFs) in human cells, but whether these microproteins are functional or not is unknown. Here, we report the discovery and characterization of a 7-kDa human microprotein we named non-annotated P-body ... |
UniProtKB | A0A0U1RRE5 | NBDY | located_in | GO:0000932 | PMID:27918561 | IDA | C | Negative regulator of P-body association | NBDY|LINC01420 | protein | taxon:9606 | 20,170,113 | UniProt | null | 27918561 | P-body | A human microprotein that interacts with the mRNA decapping complex. | Proteomic detection of non-annotated microproteins indicates the translation of hundreds of small open reading frames (smORFs) in human cells, but whether these microproteins are functional or not is unknown. Here, we report the discovery and characterization of a 7-kDa human microprotein we named non-annotated P-body ... |
UniProtKB | A0A1B0GTB2 | TUNAR | involved_in | GO:0032469 | PMID:34513312 | IDA | P | Protein TUNAR | TUNAR | protein | taxon:9606 | 20,220,211 | UniProt | null | 34513312 | endoplasmic reticulum calcium ion homeostasis | A putative long noncoding RNA-encoded micropeptide maintains cellular homeostasis in pancreatic β cells. | Micropeptides (microproteins) encoded by transcripts previously annotated as long noncoding RNAs (lncRNAs) are emerging as important mediators of fundamental biological processes in health and disease. Here, we applied two computational tools to identify putative micropeptides encoded by lncRNAs that are expressed in t... |
UniProtKB | A0A1B0GTB2 | TUNAR | involved_in | GO:0035774 | PMID:34513312 | IDA | P | Protein TUNAR | TUNAR | protein | taxon:9606 | 20,220,211 | UniProt | null | 34513312 | positive regulation of insulin secretion involved in cellular response to glucose stimulus | A putative long noncoding RNA-encoded micropeptide maintains cellular homeostasis in pancreatic β cells. | Micropeptides (microproteins) encoded by transcripts previously annotated as long noncoding RNAs (lncRNAs) are emerging as important mediators of fundamental biological processes in health and disease. Here, we applied two computational tools to identify putative micropeptides encoded by lncRNAs that are expressed in t... |
UniProtKB | A0A1B0GTB2 | TUNAR | located_in | GO:0005783 | PMID:34513312 | IDA | C | Protein TUNAR | TUNAR | protein | taxon:9606 | 20,220,211 | UniProt | null | 34513312 | endoplasmic reticulum | A putative long noncoding RNA-encoded micropeptide maintains cellular homeostasis in pancreatic β cells. | Micropeptides (microproteins) encoded by transcripts previously annotated as long noncoding RNAs (lncRNAs) are emerging as important mediators of fundamental biological processes in health and disease. Here, we applied two computational tools to identify putative micropeptides encoded by lncRNAs that are expressed in t... |
UniProtKB | A0A1B0GVM2 | TCAF2C | located_in | GO:0005886 | GO_REF:0000052 | IDA | C | Peptidase M60 domain-containing protein | TCAF2C | protein | taxon:9606 | 20,241,022 | HPA | null | null | plasma membrane | null | null |
UniProtKB | A0A1B0GVM2 | TCAF2C | located_in | GO:0030054 | GO_REF:0000052 | IDA | C | Peptidase M60 domain-containing protein | TCAF2C | protein | taxon:9606 | 20,241,022 | HPA | null | null | cell junction | null | null |
UniProtKB | A0A1B0GVQ0 | SPAAR | colocalizes_with | GO:0046611 | PMID:28024296 | IDA | C | Small regulatory polypeptide of amino acid response | SPAAR|LINC00961|SPAR | protein | taxon:9606 | 20,170,110 | UniProt | null | 28024296 | lysosomal proton-transporting V-type ATPase complex | mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR polypeptide. | Although long non-coding RNAs (lncRNAs) are non-protein-coding transcripts by definition, recent studies have shown that a fraction of putative small open reading frames within lncRNAs are translated. However, the biological significance of these hidden polypeptides is still unclear. Here we identify and functionally c... |
UniProtKB | A0A1B0GVQ0 | SPAAR | located_in | GO:0005765 | PMID:28024296 | IDA | C | Small regulatory polypeptide of amino acid response | SPAAR|LINC00961|SPAR | protein | taxon:9606 | 20,170,110 | UniProt | null | 28024296 | lysosomal membrane | mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR polypeptide. | Although long non-coding RNAs (lncRNAs) are non-protein-coding transcripts by definition, recent studies have shown that a fraction of putative small open reading frames within lncRNAs are translated. However, the biological significance of these hidden polypeptides is still unclear. Here we identify and functionally c... |
UniProtKB | A0A1B0GVQ0 | SPAAR | located_in | GO:0031902 | PMID:28024296 | IDA | C | Small regulatory polypeptide of amino acid response | SPAAR|LINC00961|SPAR | protein | taxon:9606 | 20,170,110 | UniProt | null | 28024296 | late endosome membrane | mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR polypeptide. | Although long non-coding RNAs (lncRNAs) are non-protein-coding transcripts by definition, recent studies have shown that a fraction of putative small open reading frames within lncRNAs are translated. However, the biological significance of these hidden polypeptides is still unclear. Here we identify and functionally c... |
UniProtKB | A0A3B3IS91 | POLGARF | located_in | GO:0005615 | PMID:32958672 | IDA | C | POLG alternative reading frame | POLGARF | protein | taxon:9606 | 20,210,716 | UniProt | null | 32958672 | extracellular space | Unusually efficient CUG initiation of an overlapping reading frame in <i>POLG</i> mRNA yields novel protein POLGARF. | While near-cognate codons are frequently used for translation initiation in eukaryotes, their efficiencies are usually low (<10% compared to an AUG in optimal context). Here, we describe a rare case of highly efficient near-cognate initiation. A CUG triplet located in the 5' leader of <i>POLG</i> messenger RNA (mRNA) i... |
UniProtKB | A0A3B3IS91 | POLGARF | located_in | GO:0005730 | PMID:32958672 | IDA | C | POLG alternative reading frame | POLGARF | protein | taxon:9606 | 20,210,716 | UniProt | null | 32958672 | nucleolus | Unusually efficient CUG initiation of an overlapping reading frame in <i>POLG</i> mRNA yields novel protein POLGARF. | While near-cognate codons are frequently used for translation initiation in eukaryotes, their efficiencies are usually low (<10% compared to an AUG in optimal context). Here, we describe a rare case of highly efficient near-cognate initiation. A CUG triplet located in the 5' leader of <i>POLG</i> messenger RNA (mRNA) i... |
UniProtKB | A0A455ZAR2 | LINC-PINT | located_in | GO:0005634 | PMID:30367041 | IDA | C | Transcriptional regulator PINT87aa | LINC-PINT | protein | taxon:9606 | 20,211,105 | UniProt | null | 30367041 | nucleus | A peptide encoded by circular form of LINC-PINT suppresses oncogenic transcriptional elongation in glioblastoma. | Circular RNAs (circRNAs) are a large class of transcripts in the mammalian genome. Although the translation of circRNAs was reported, additional coding circRNAs and the functions of their translated products remain elusive. Here, we demonstrate that an endogenous circRNA generated from a long noncoding RNA encodes regu... |
UniProtKB | A0A590UK10 | ARHGEF18 | located_in | GO:0005829 | GO_REF:0000052 | IDA | C | Rho guanine nucleotide exchange factor 18 | ARHGEF18 | protein | taxon:9606 | 20,241,022 | HPA | null | null | cytosol | null | null |
UniProtKB | A0A590UK10 | ARHGEF18 | located_in | GO:0005886 | GO_REF:0000052 | IDA | C | Rho guanine nucleotide exchange factor 18 | ARHGEF18 | protein | taxon:9606 | 20,241,022 | HPA | null | null | plasma membrane | null | null |
UniProtKB | A0A590UK83 | SMIM45 | located_in | GO:0005634 | PMID:36593289 | IDA | C | Small integral membrane protein 45 | SMIM45|LINC00634 | protein | taxon:9606 | 20,230,214 | UniProt | null | 36593289 | nucleus | De novo genes with an lncRNA origin encode unique human brain developmental functionality. | Human de novo genes can originate from neutral long non-coding RNA (lncRNA) loci and are evolutionarily significant in general, yet how and why this all-or-nothing transition to functionality happens remains unclear. Here, in 74 human/hominoid-specific de novo genes, we identified distinctive U1 elements and RNA splice... |
UniProtKB | A0A590UK83 | SMIM45 | located_in | GO:0005737 | PMID:36593289 | IDA | C | Small integral membrane protein 45 | SMIM45|LINC00634 | protein | taxon:9606 | 20,230,214 | UniProt | null | 36593289 | cytoplasm | De novo genes with an lncRNA origin encode unique human brain developmental functionality. | Human de novo genes can originate from neutral long non-coding RNA (lncRNA) loci and are evolutionarily significant in general, yet how and why this all-or-nothing transition to functionality happens remains unclear. Here, in 74 human/hominoid-specific de novo genes, we identified distinctive U1 elements and RNA splice... |
UniProtKB | A0A5B9 | TRBC2 | located_in | GO:0005886 | PMID:31461748 | IDA | C | T cell receptor beta constant 2 | TRBC2|TCRBC2 | protein | taxon:9606 | 20,241,220 | ComplexPortal | null | 31461748 | plasma membrane | Structural basis of assembly of the human T cell receptor-CD3 complex. | The αβ T cell receptor (TCR), in association with the CD3γε-CD3δε-CD3ζζ signalling hexamer, is the primary determinant of T cell development and activation, and of immune responses to foreign antigens. The mechanism of assembly of the TCR-CD3 complex remains unknown. Here we report a cryo-electron microscopy structure ... |
UniProtKB | A0A6Q8PH20 | CAST | located_in | GO:0005783 | GO_REF:0000052 | IDA | C | Calpastatin | CAST | protein | taxon:9606 | 20,241,022 | HPA | null | null | endoplasmic reticulum | null | null |
UniProtKB | A0A6Q8PH20 | CAST | located_in | GO:0005829 | GO_REF:0000052 | IDA | C | Calpastatin | CAST | protein | taxon:9606 | 20,241,022 | HPA | null | null | cytosol | null | null |
UniProtKB | A0A7P0TBJ1 | HAPSTR2 | located_in | GO:0005634 | PMID:36631436 | IDA | C | HUWE1-associated protein modifying stress responses 2 | HAPSTR2 | protein | taxon:9606 | 20,230,117 | UniProt | null | 36631436 | nucleus | The HAPSTR2 retrogene buffers stress signaling and resilience in mammals. | We recently identified HAPSTR1 (C16orf72) as a key component in a novel pathway which regulates the cellular response to molecular stressors, such as DNA damage, nutrient scarcity, and protein misfolding. Here, we identify a functional paralog to HAPSTR1: HAPSTR2. HAPSTR2 formed early in mammalian evolution, via genomi... |
UniProtKB | A0A8I5KW96 | AK4P3 | located_in | GO:0005739 | GO_REF:0000052 | IDA | C | Adenylate kinase 4, mitochondrial | AK4P3|AK3L1|AK4 | protein | taxon:9606 | 20,241,022 | HPA | null | null | mitochondrion | null | null |
UniProtKB | A0AV96 | RBM47 | enables | GO:0003723 | PMID:24038582 | IDA | F | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,929 | UniProt | null | 24038582 | RNA binding | rbm47, a novel RNA binding protein, regulates zebrafish head development. | <h4>Background</h4>Vertebrate trunk induction requires inhibition of bone morphogenetic protein (BMP) signaling, whereas vertebrate head induction requires concerted inhibition of both Wnt and BMP signaling. RNA binding proteins play diverse roles in embryonic development and their roles in vertebrate head development ... |
UniProtKB | A0AV96 | RBM47 | enables | GO:0003723 | PMID:24916387 | IDA | F | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,915 | UniProt | null | 24916387 | RNA binding | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AV96 | RBM47 | enables | GO:0003730 | PMID:34160127 | IDA | F | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,221,007 | UniProt | null | 34160127 | mRNA 3'-UTR binding | RNA-binding protein RBM47 stabilizes IFNAR1 mRNA to potentiate host antiviral activity. | The type I interferon (IFN-I, IFN-α/β)-mediated immune response is the first line of host defense against invading viruses. IFN-α/β binds to IFN-α/β receptors (IFNARs) and triggers the expression of IFN-stimulated genes (ISGs). Thus, stabilization of IFNARs is important for prolonging antiviral activity. Here, we repor... |
UniProtKB | A0AV96 | RBM47 | enables | GO:0140767 | PMID:24916387 | IDA | F | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,926 | UniProt | part_of(GO:0016554),occurs_in(GO:0005634),has_input(UniProtKB:P41238),has_input(SO:0000234) | 24916387 | enzyme-substrate adaptor activity | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AV96 | RBM47 | enables | GO:0140767 | PMID:24916387 | IDA | F | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,221,007 | UniProt | null | 24916387 | enzyme-substrate adaptor activity | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AV96 | RBM47 | involved_in | GO:0000381 | PMID:31358901 | IDA | P | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,221,010 | UniProt | null | 31358901 | regulation of alternative mRNA splicing, via spliceosome | RBM47-regulated alternative splicing of TJP1 promotes actin stress fiber assembly during epithelial-to-mesenchymal transition. | Morphological and functional changes in cells during the epithelial-mesenchymal transition (EMT) process are known to be regulated by alternative splicing. However, only a few splicing factors involved in EMT have been reported and their underlying mechanisms remain largely unknown. Here, we showed that an isoform of t... |
UniProtKB | A0AV96 | RBM47 | involved_in | GO:0016554 | PMID:24916387 | IDA | P | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,926 | UniProt | null | 24916387 | cytidine to uridine editing | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AV96 | RBM47 | involved_in | GO:0016554 | PMID:24916387 | IDA | P | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,221,010 | UniProt | null | 24916387 | cytidine to uridine editing | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AV96 | RBM47 | involved_in | GO:0016554 | PMID:30844405 | IDA | P | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,221,010 | UniProt | null | 30844405 | cytidine to uridine editing | Comparison of RNA Editing Activity of APOBEC1-A1CF and APOBEC1-RBM47 Complexes Reconstituted in HEK293T Cells. | RNA editing is an important form of regulating gene expression and activity. APOBEC1 cytosine deaminase was initially characterized as pairing with a cofactor, A1CF, to form an active RNA editing complex that specifically targets APOB RNA in regulating lipid metabolism. Recent studies revealed that APOBEC1 may be invol... |
UniProtKB | A0AV96 | RBM47 | involved_in | GO:0070935 | PMID:34160127 | IDA | P | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,221,007 | UniProt | null | 34160127 | 3'-UTR-mediated mRNA stabilization | RNA-binding protein RBM47 stabilizes IFNAR1 mRNA to potentiate host antiviral activity. | The type I interferon (IFN-I, IFN-α/β)-mediated immune response is the first line of host defense against invading viruses. IFN-α/β binds to IFN-α/β receptors (IFNARs) and triggers the expression of IFN-stimulated genes (ISGs). Thus, stabilization of IFNARs is important for prolonging antiviral activity. Here, we repor... |
UniProtKB | A0AV96 | RBM47 | located_in | GO:0005634 | PMID:24038582 | IDA | C | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,929 | UniProt | null | 24038582 | nucleus | rbm47, a novel RNA binding protein, regulates zebrafish head development. | <h4>Background</h4>Vertebrate trunk induction requires inhibition of bone morphogenetic protein (BMP) signaling, whereas vertebrate head induction requires concerted inhibition of both Wnt and BMP signaling. RNA binding proteins play diverse roles in embryonic development and their roles in vertebrate head development ... |
UniProtKB | A0AV96 | RBM47 | located_in | GO:0005634 | PMID:24916387 | IDA | C | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,915 | UniProt | null | 24916387 | nucleus | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AV96 | RBM47 | located_in | GO:0005737 | PMID:24916387 | IDA | C | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,916 | UniProt | null | 24916387 | cytoplasm | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AV96 | RBM47 | part_of | GO:0030895 | PMID:24916387 | IDA | C | RNA-binding protein 47 | RBM47 | protein | taxon:9606 | 20,220,927 | UniProt | null | 24916387 | apolipoprotein B mRNA editing enzyme complex | C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. | Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where... |
UniProtKB | A0AVF1 | IFT56 | part_of | GO:0030991 | PMID:26980730 | IDA | C | Intraflagellar transport protein 56 | IFT56|TTC26 | protein | taxon:9606 | 20,191,022 | MGI | null | 26980730 | intraciliary transport particle A | Overall Architecture of the Intraflagellar Transport (IFT)-B Complex Containing Cluap1/IFT38 as an Essential Component of the IFT-B Peripheral Subcomplex. | Intraflagellar transport (IFT) is essential for assembly and maintenance of cilia and flagella as well as ciliary motility and signaling. IFT is mediated by multisubunit complexes, including IFT-A, IFT-B, and the BBSome, in concert with kinesin and dynein motors. Under high salt conditions, purified IFT-B complex disso... |
UniProtKB | A0AVI4 | TMEM129 | enables | GO:0061630 | PMID:24807418 | IDA | F | E3 ubiquitin-protein ligase TM129 | TMEM129 | protein | taxon:9606 | 20,180,312 | ParkinsonsUK-UCL | part_of(GO:0036503) | 24807418 | ubiquitin protein ligase activity | A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation. | Misfolded ER proteins are retrotranslocated into the cytosol for degradation via the ubiquitin-proteasome system. The human cytomegalovirus protein US11 exploits this ER-associated protein degradation (ERAD) pathway to downregulate HLA class I molecules in virus-infected cells, thereby evading elimination by cytotoxic ... |
UniProtKB | A0AVI4 | TMEM129 | involved_in | GO:0000209 | PMID:24807418 | IDA | P | E3 ubiquitin-protein ligase TM129 | TMEM129 | protein | taxon:9606 | 20,150,415 | ParkinsonsUK-UCL | null | 24807418 | protein polyubiquitination | A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation. | Misfolded ER proteins are retrotranslocated into the cytosol for degradation via the ubiquitin-proteasome system. The human cytomegalovirus protein US11 exploits this ER-associated protein degradation (ERAD) pathway to downregulate HLA class I molecules in virus-infected cells, thereby evading elimination by cytotoxic ... |
UniProtKB | A0AVI4 | TMEM129 | involved_in | GO:0006511 | PMID:24807418 | IDA | P | E3 ubiquitin-protein ligase TM129 | TMEM129 | protein | taxon:9606 | 20,231,121 | ParkinsonsUK-UCL | part_of(GO:0036503) | 24807418 | ubiquitin-dependent protein catabolic process | A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation. | Misfolded ER proteins are retrotranslocated into the cytosol for degradation via the ubiquitin-proteasome system. The human cytomegalovirus protein US11 exploits this ER-associated protein degradation (ERAD) pathway to downregulate HLA class I molecules in virus-infected cells, thereby evading elimination by cytotoxic ... |
UniProtKB | A0AVI4 | TMEM129 | located_in | GO:0005783 | PMID:24807418 | IDA | C | E3 ubiquitin-protein ligase TM129 | TMEM129 | protein | taxon:9606 | 20,150,415 | ParkinsonsUK-UCL | null | 24807418 | endoplasmic reticulum | A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation. | Misfolded ER proteins are retrotranslocated into the cytosol for degradation via the ubiquitin-proteasome system. The human cytomegalovirus protein US11 exploits this ER-associated protein degradation (ERAD) pathway to downregulate HLA class I molecules in virus-infected cells, thereby evading elimination by cytotoxic ... |
UniProtKB | A0AVK6 | E2F8 | enables | GO:0000978 | PMID:16179649 | IDA | F | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,131,029 | NTNU_SB | null | 16179649 | RNA polymerase II cis-regulatory region sequence-specific DNA binding | Characterization of E2F8, a novel E2F-like cell-cycle regulated repressor of E2F-activated transcription. | The E2F family of transcription factors are downstream effectors of the retinoblastoma protein, pRB, pathway and are essential for the timely regulation of genes necessary for cell-cycle progression. Here we describe the characterization of human and murine E2F8, a new member of the E2F family. Sequence analysis of E2F... |
UniProtKB | A0AVK6 | E2F8 | enables | GO:0000987 | PMID:22903062 | IDA | F | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,180,425 | UniProt | null | 22903062 | cis-regulatory region sequence-specific DNA binding | E2F7 and E2F8 promote angiogenesis through transcriptional activation of VEGFA in cooperation with HIF1. | The E2F family of transcription factors plays an important role in controlling cell-cycle progression. While this is their best-known function, we report here novel functions for the newest members of the E2F family, E2F7 and E2F8 (E2F7/8). We show that simultaneous deletion of E2F7/8 in zebrafish and mice leads to sev... |
UniProtKB | A0AVK6 | E2F8 | enables | GO:0001227 | PMID:16179649 | IDA | F | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,131,013 | NTNU_SB | null | 16179649 | DNA-binding transcription repressor activity, RNA polymerase II-specific | Characterization of E2F8, a novel E2F-like cell-cycle regulated repressor of E2F-activated transcription. | The E2F family of transcription factors are downstream effectors of the retinoblastoma protein, pRB, pathway and are essential for the timely regulation of genes necessary for cell-cycle progression. Here we describe the characterization of human and murine E2F8, a new member of the E2F family. Sequence analysis of E2F... |
UniProtKB | A0AVK6 | E2F8 | enables | GO:1990837 | PMID:28473536 | IDA | F | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,200,608 | ARUK-UCL | null | 28473536 | sequence-specific double-stranded DNA binding | Impact of cytosine methylation on DNA binding specificities of human transcription factors. | The majority of CpG dinucleotides in the human genome are methylated at cytosine bases. However, active gene regulatory elements are generally hypomethylated relative to their flanking regions, and the binding of some transcription factors (TFs) is diminished by methylation of their target sequences. By analysis of 542... |
UniProtKB | A0AVK6 | E2F8 | involved_in | GO:0000122 | PMID:16179649 | IDA | P | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,140,322 | NTNU_SB | has_input(NCBI_Gene:1869) | 16179649 | negative regulation of transcription by RNA polymerase II | Characterization of E2F8, a novel E2F-like cell-cycle regulated repressor of E2F-activated transcription. | The E2F family of transcription factors are downstream effectors of the retinoblastoma protein, pRB, pathway and are essential for the timely regulation of genes necessary for cell-cycle progression. Here we describe the characterization of human and murine E2F8, a new member of the E2F family. Sequence analysis of E2F... |
UniProtKB | A0AVK6 | E2F8 | located_in | GO:0005654 | GO_REF:0000052 | IDA | C | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,241,022 | HPA | null | null | nucleoplasm | null | null |
UniProtKB | A0AVK6 | E2F8 | located_in | GO:0005730 | GO_REF:0000052 | IDA | C | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,241,022 | HPA | null | null | nucleolus | null | null |
UniProtKB | A0AVK6 | E2F8 | located_in | GO:0005829 | GO_REF:0000052 | IDA | C | Transcription factor E2F8 | E2F8 | protein | taxon:9606 | 20,241,022 | HPA | null | null | cytosol | null | null |
UniProtKB | A0AVT1 | UBA6 | located_in | GO:0005737 | GO_REF:0000054 | IDA | C | Ubiquitin-like modifier-activating enzyme 6 | UBA6|MOP4|UBE1L2 | protein | taxon:9606 | 20,100,607 | LIFEdb | null | null | cytoplasm | null | null |
UniProtKB | A0FGR8 | ESYT2 | enables | GO:0005509 | PMID:24373768 | IDA | F | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,140,527 | UniProt | null | 24373768 | calcium ion binding | Structure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2. | Contacts between the endoplasmic reticulum and the plasma membrane involve extended synaptotagmins (E-Syts) in mammals or tricalbins in yeast, proteins with multiple C₂ domains. One of the tandem C₂ domains of E-Syt2 is predicted to bind Ca²⁺, but no Ca²⁺-dependent function has been attributed to this protein. We have ... |
UniProtKB | A0FGR8 | ESYT2 | enables | GO:0005544 | PMID:17360437 | IDA | F | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,131,121 | FlyBase | null | 17360437 | calcium-dependent phospholipid binding | E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains. | C(2) domains are autonomously folded protein modules that generally act as Ca(2+)- and phospholipid-binding domains and/or as protein-protein interaction domains. We now report the primary structures and biochemical properties of a family of evolutionarily conserved mammalian proteins, referred to as E-Syts, for extend... |
UniProtKB | A0FGR8 | ESYT2 | enables | GO:0008429 | PMID:24847877 | IDA | F | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,140,527 | UniProt | null | 24847877 | phosphatidylethanolamine binding | Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. | Growing evidence suggests that close appositions between the endoplasmic reticulum (ER) and other membranes, including appositions with the plasma membrane (PM), mediate exchange of lipids between these bilayers. The mechanisms of such exchange, which allows lipid transfer independently of vesicular transport, remain p... |
UniProtKB | A0FGR8 | ESYT2 | enables | GO:0031210 | PMID:24847877 | IDA | F | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,140,527 | UniProt | null | 24847877 | phosphatidylcholine binding | Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. | Growing evidence suggests that close appositions between the endoplasmic reticulum (ER) and other membranes, including appositions with the plasma membrane (PM), mediate exchange of lipids between these bilayers. The mechanisms of such exchange, which allows lipid transfer independently of vesicular transport, remain p... |
UniProtKB | A0FGR8 | ESYT2 | enables | GO:0035091 | PMID:24847877 | IDA | F | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,140,527 | UniProt | null | 24847877 | phosphatidylinositol binding | Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. | Growing evidence suggests that close appositions between the endoplasmic reticulum (ER) and other membranes, including appositions with the plasma membrane (PM), mediate exchange of lipids between these bilayers. The mechanisms of such exchange, which allows lipid transfer independently of vesicular transport, remain p... |
UniProtKB | A0FGR8 | ESYT2 | located_in | GO:0005789 | PMID:23791178 | IDA | C | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,140,528 | UniProt | null | 23791178 | endoplasmic reticulum membrane | PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins. | Most available information on endoplasmic reticulum (ER)-plasma membrane (PM) contacts in cells of higher eukaryotes concerns proteins implicated in the regulation of Ca(2+) entry. However, growing evidence suggests that such contacts play more general roles in cell physiology, pointing to the existence of additionally... |
UniProtKB | A0FGR8 | ESYT2 | located_in | GO:0005829 | GO_REF:0000052 | IDA | C | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,241,022 | HPA | null | null | cytosol | null | null |
UniProtKB | A0FGR8 | ESYT2 | located_in | GO:0005886 | GO_REF:0000052 | IDA | C | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,241,022 | HPA | null | null | plasma membrane | null | null |
UniProtKB | A0FGR8 | ESYT2 | located_in | GO:0005886 | PMID:17360437 | IDA | C | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,131,121 | FlyBase | null | 17360437 | plasma membrane | E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains. | C(2) domains are autonomously folded protein modules that generally act as Ca(2+)- and phospholipid-binding domains and/or as protein-protein interaction domains. We now report the primary structures and biochemical properties of a family of evolutionarily conserved mammalian proteins, referred to as E-Syts, for extend... |
UniProtKB | A0FGR8 | ESYT2 | located_in | GO:0044232 | PMID:23791178 | IDA | C | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,140,528 | UniProt | null | 23791178 | organelle membrane contact site | PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins. | Most available information on endoplasmic reticulum (ER)-plasma membrane (PM) contacts in cells of higher eukaryotes concerns proteins implicated in the regulation of Ca(2+) entry. However, growing evidence suggests that such contacts play more general roles in cell physiology, pointing to the existence of additionally... |
UniProtKB | A0FGR8 | ESYT2 | located_in | GO:0140268 | PMID:27044890 | IDA | C | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,200,227 | UniProt | null | 27044890 | endoplasmic reticulum-plasma membrane contact site | Dynamic formation of ER-PM junctions presents a lipid phosphatase to regulate phosphoinositides. | Endoplasmic reticulum-plasma membrane (ER-PM) contact sites play an integral role in cellular processes such as excitation-contraction coupling and store-operated calcium entry (SOCE). Another ER-PM assembly is one tethered by the extended synaptotagmins (E-Syt). We have discovered that at steady state, E-Syt2 position... |
UniProtKB | A0FGR8 | ESYT2 | located_in | GO:0140268 | PMID:30220461 | IDA | C | Extended synaptotagmin-2 | ESYT2|FAM62B|KIAA1228 | protein | taxon:9606 | 20,181,015 | UniProt | null | 30220461 | endoplasmic reticulum-plasma membrane contact site | Aster Proteins Facilitate Nonvesicular Plasma Membrane to ER Cholesterol Transport in Mammalian Cells. | The mechanisms underlying sterol transport in mammalian cells are poorly understood. In particular, how cholesterol internalized from HDL is made available to the cell for storage or modification is unknown. Here, we describe three ER-resident proteins (Aster-A, -B, -C) that bind cholesterol and facilitate its removal ... |
UniProtKB | A0FGR9 | ESYT3 | located_in | GO:0005789 | PMID:23791178 | IDA | C | Extended synaptotagmin-3 | ESYT3|FAM62C | protein | taxon:9606 | 20,140,528 | UniProt | null | 23791178 | endoplasmic reticulum membrane | PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins. | Most available information on endoplasmic reticulum (ER)-plasma membrane (PM) contacts in cells of higher eukaryotes concerns proteins implicated in the regulation of Ca(2+) entry. However, growing evidence suggests that such contacts play more general roles in cell physiology, pointing to the existence of additionally... |
UniProtKB | A0FGR9 | ESYT3 | located_in | GO:0005886 | PMID:17360437 | IDA | C | Extended synaptotagmin-3 | ESYT3|FAM62C | protein | taxon:9606 | 20,131,121 | FlyBase | null | 17360437 | plasma membrane | E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains. | C(2) domains are autonomously folded protein modules that generally act as Ca(2+)- and phospholipid-binding domains and/or as protein-protein interaction domains. We now report the primary structures and biochemical properties of a family of evolutionarily conserved mammalian proteins, referred to as E-Syts, for extend... |
UniProtKB | A0FGR9 | ESYT3 | located_in | GO:0009898 | PMID:23791178 | IDA | C | Extended synaptotagmin-3 | ESYT3|FAM62C | protein | taxon:9606 | 20,230,323 | UniProt | null | 23791178 | cytoplasmic side of plasma membrane | PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins. | Most available information on endoplasmic reticulum (ER)-plasma membrane (PM) contacts in cells of higher eukaryotes concerns proteins implicated in the regulation of Ca(2+) entry. However, growing evidence suggests that such contacts play more general roles in cell physiology, pointing to the existence of additionally... |
UniProtKB | A0FGR9 | ESYT3 | located_in | GO:0044232 | PMID:23791178 | IDA | C | Extended synaptotagmin-3 | ESYT3|FAM62C | protein | taxon:9606 | 20,140,528 | UniProt | null | 23791178 | organelle membrane contact site | PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins. | Most available information on endoplasmic reticulum (ER)-plasma membrane (PM) contacts in cells of higher eukaryotes concerns proteins implicated in the regulation of Ca(2+) entry. However, growing evidence suggests that such contacts play more general roles in cell physiology, pointing to the existence of additionally... |
UniProtKB | A0FGR9 | ESYT3 | located_in | GO:0140268 | PMID:30220461 | IDA | C | Extended synaptotagmin-3 | ESYT3|FAM62C | protein | taxon:9606 | 20,181,015 | UniProt | null | 30220461 | endoplasmic reticulum-plasma membrane contact site | Aster Proteins Facilitate Nonvesicular Plasma Membrane to ER Cholesterol Transport in Mammalian Cells. | The mechanisms underlying sterol transport in mammalian cells are poorly understood. In particular, how cholesterol internalized from HDL is made available to the cell for storage or modification is unknown. Here, we describe three ER-resident proteins (Aster-A, -B, -C) that bind cholesterol and facilitate its removal ... |
UniProtKB | A0JLT2 | MED19 | located_in | GO:0005634 | PMID:24882805 | IDA | C | Mediator of RNA polymerase II transcription subunit 19 | MED19|LCMR1 | protein | taxon:9606 | 20,250,731 | ComplexPortal | null | 24882805 | nucleus | Subunit architecture and functional modular rearrangements of the transcriptional mediator complex. | The multisubunit Mediator, comprising ∼30 distinct proteins, plays an essential role in gene expression regulation by acting as a bridge between DNA-binding transcription factors and the RNA polymerase II (RNAPII) transcription machinery. Efforts to uncover the Mediator mechanism have been hindered by a poor understand... |
UniProtKB | A0JNW5 | BLTP3B | enables | GO:0062069 | PMID:20163565 | IDA | F | Bridge-like lipid transfer protein family member 3B | BLTP3B|KIAA0701|SHIP164|UHRF1BP1L | protein | taxon:9606 | 20,180,913 | UniProt | null | 20163565 | GARP complex binding | A novel syntaxin 6-interacting protein, SHIP164, regulates syntaxin 6-dependent sorting from early endosomes. | Membrane fusion is dependent on the function of SNAREs and their alpha-helical SNARE motifs that form SNARE complexes. The Habc domains at the N-termini of some SNAREs can interact with their associated SNARE motif, Sec1/Munc18 (SM) proteins, tethering proteins or adaptor proteins, suggesting that they play an importan... |
UniProtKB | A0JNW5 | BLTP3B | enables | GO:0120013 | PMID:35499567 | IDA | F | Bridge-like lipid transfer protein family member 3B | BLTP3B|KIAA0701|SHIP164|UHRF1BP1L | protein | taxon:9606 | 20,220,831 | UniProt | null | 35499567 | lipid transfer activity | SHIP164 is a chorein motif lipid transfer protein that controls endosome-Golgi membrane traffic. | Cellular membranes differ in protein and lipid composition as well as in the protein-lipid ratio. Thus, progression of membranous organelles along traffic routes requires mechanisms to control bilayer lipid chemistry and their abundance relative to proteins. The recent structural and functional characterization of VPS1... |
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Dataset Description
This dataset integrates Gene Ontology (GO) annotations (filtered to experimental evidence, IDA) with bibliographic data from Europe PMC.
Each record links a biological entity (gene/protein) to a GO term and the supporting scientific publication (Title and Abstract).
Columns
- DB, DB_Object_ID, DB_Object_Symbol — Source database and gene/protein identifiers
- Qualifier — Relationship qualifier (e.g.,
NOT,contributes_to) - GO_ID, GO_Name — GO term and its descriptive name
- DB_Reference — Supporting reference (PubMed or other)
- Evidence_Code — Experimental evidence type (e.g.,
IDA) - Aspect — Ontology branch (
P= process,F= function,C= component) - DB_Object_Name, DB_Object_Synonym, DB_Object_Type — Entity metadata
- Taxon — Organism taxonomy ID
- Date, Assigned_By, Annotation_Extension — Annotation metadata
- PMID — PubMed ID for the supporting publication
- Title, Abstract — Publication title and abstract text (fetched from Europe PMC)
Summary
This dataset forms a structured link between curated GO annotations and natural language descriptions of the underlying biology — suitable for:
- Biological reasoning
- Text mining
- Literature-grounded machine learning (ML) datasets
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