UniProtKB - P36897 (TGFR1_HUMAN)
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- BLAST>sp|P36897|TGFR1_HUMAN TGF-beta receptor type-1 OS=Homo sapiens OX=9606 GN=TGFBR1 PE=1 SV=1 MEAAVAAPRPRLLLLVLAAAAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTE TTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPG LGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDL IYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREER SWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVE GMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDS ATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGI HEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGA ARLTALRIKKTLSQLSQQEGIKM
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TGF-beta receptor type-1
TGFBR1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex."
Wieser R., Wrana J.L., Massague J.
EMBO J. 14:2199-2208(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-185; THR-186; SER-187; SER-189 AND SER-191 BY TGFBR2, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF 185-THR-THR-186; SER-187; SER-189; SER-191; THR-200 AND THR-204. - Ref.11"MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma."
Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H., Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H., Wrana J.L., Attisano L.
Cell 86:543-552(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF SMAD2. - Ref.12"MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling."
Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.
Cell 87:1215-1224(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION. - Ref.15"TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling."
Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L.
J. Biol. Chem. 272:27678-27685(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION. - Ref.22"Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity."
Ozdamar B., Bose R., Barrios-Rodiles M., Wang H.R., Zhang Y., Wrana J.L.
Science 307:1603-1609(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EPITHELIAL TO MESENCHYMAL TRANSITION, SUBCELLULAR LOCATION, INTERACTION WITH PARD6A, FUNCTION IN PHOSPHORYLATION OF PARD6A. - Ref.23"Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes."
Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S., Bizet A.A., Philip A.
FASEB J. 20:1525-1527(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELLULAR GROWTH INHIBITION, INTERACTION WITH CD109. - Ref.25"The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner."
Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V., Schuster N., Zhang S., Heldin C.H., Landstrom M.
Nat. Cell Biol. 10:1199-1207(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH TRAF6 AND MAP3K7.
Caution
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.47"Clinical features and genetic analysis of Korean patients with Loeys-Dietz syndrome."
Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K., Lee H.J., Kim D.K.
J. Hum. Genet. 57:52-56(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LDS1 TYR-266; ARG-375 AND GLN-487. - ERRATUM
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Mechanism of TGFbeta receptor inhibition by FKBP12."
Chen Y.G., Liu F., Massague J.
EMBO J. 16:3866-3876(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FKBP1A, ENZYME REGULATION, MUTAGENESIS OF LEU-193 AND PRO-194.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 232 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 333 | Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 211 – 219 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 9 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ATP binding Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- I-SMAD binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- metal ion binding Source: UniProtKB-KW
- protein kinase activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein serine/threonine kinase activity Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- SMAD binding Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transforming growth factor beta-activated receptor activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transforming growth factor beta binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transforming growth factor beta receptor activity, type I Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- type II transforming growth factor beta receptor binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- activation of MAPKK activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- activin receptor signaling pathway Source: AgBase
- angiogenesis involved in coronary vascular morphogenesis Source: BHF-UCL
- anterior/posterior pattern specification Source: BHF-UCL
- apoptotic process Source: UniProtKB-KW
- artery morphogenesis Source: BHF-UCL
- blastocyst development Source: Ensembl
- cardiac epithelial to mesenchymal transition Source: AgBase
- cell cycle arrest Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- cell motility Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cellular response to transforming growth factor beta stimulus Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- collagen fibril organization Source: BHF-UCL
- coronary artery morphogenesis Source: BHF-UCL
- embryonic cranial skeleton morphogenesis Source: BHF-UCL
- endothelial cell activation Source: AgBase
- endothelial cell migration Source: Ensembl
- epicardium morphogenesis Source: BHF-UCL
- epithelial to mesenchymal transition Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- extracellular structure organization Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- germ cell migration Source: BHF-UCL
- heart development Source: AgBase
- intracellular signal transduction Source: AgBase
- in utero embryonic development Source: BHF-UCL
- kidney development Source: BHF-UCL
- lens development in camera-type eye Source: Ensembl
- male gonad development Source: Ensembl
- mesenchymal cell differentiation Source: AgBase
- negative regulation of chondrocyte differentiation Source: BHF-UCL
- negative regulation of endothelial cell proliferation Source: Ensembl
- negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
- neuron fate commitment Source: BHF-UCL
- parathyroid gland development Source: BHF-UCL
- pathway-restricted SMAD protein phosphorylation Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- peptidyl-serine phosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- peptidyl-threonine phosphorylation Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- pharyngeal system development Source: BHF-UCL
- positive regulation of apoptotic signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of cell growth Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of cell migration Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of cell proliferation Source: HGNC <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of cellular component movement Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of endothelial cell proliferation Source: AgBase
- positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
- positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
- positive regulation of filopodium assembly Source: Ensembl
- positive regulation of gene expression Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of occluding junction disassembly Source: BHF-UCL
- positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of protein kinase B signaling Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of SMAD protein signal transduction Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of stress fiber assembly Source: BHF-UCL
- positive regulation of transcription, DNA-templated Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- post-embryonic development Source: Ensembl
- protein deubiquitination Source: Reactome
- protein phosphorylation Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of cardiac muscle cell proliferation Source: BHF-UCL
- regulation of epithelial to mesenchymal transition Source: AgBase
- regulation of gene expression Source: AgBase
- regulation of protein binding Source: Ensembl
- regulation of protein ubiquitination Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of transcription, DNA-templated Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to cholesterol Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- roof of mouth development Source: BHF-UCL
- signal transduction Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- skeletal system development Source: BHF-UCL
- skeletal system morphogenesis Source: BHF-UCL
- thymus development Source: BHF-UCL
- transforming growth factor beta receptor signaling pathway Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ventricular compact myocardium morphogenesis Source: BHF-UCL
- ventricular septum morphogenesis Source: BHF-UCL
- ventricular trabecula myocardium morphogenesis Source: BHF-UCL
- wound healing Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Kinase, Receptor, Serine/threonine-protein kinase, Transferase |
| Biological process | Apoptosis, Differentiation, Growth regulation |
| Ligand | ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.2 2681 2.7.11.30 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2173788 Downregulation of TGF-beta receptor signaling R-HSA-2173789 TGF-beta receptor signaling activates SMADs R-HSA-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) R-HSA-3304356 SMAD2/3 Phosphorylation Motif Mutants in Cancer R-HSA-3315487 SMAD2/3 MH2 Domain Mutants in Cancer R-HSA-3645790 TGFBR2 Kinase Domain Mutants in Cancer R-HSA-3656532 TGFBR1 KD Mutants in Cancer R-HSA-3656535 TGFBR1 LBD Mutants in Cancer R-HSA-5689603 UCH proteinases R-HSA-5689880 Ub-specific processing proteases |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P36897 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P36897 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: TGF-beta receptor type-1 (EC:2.7.11.30)Short name: TGFR-1 Alternative name(s): Activin A receptor type II-like protein kinase of 53kD Activin receptor-like kinase 5 Short name: ALK-5 Short name: ALK5 Serine/threonine-protein kinase receptor R4 Short name: SKR4 TGF-beta type I receptor Transforming growth factor-beta receptor type I Short name: TGF-beta receptor type I Short name: TbetaR-I |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:TGFBR1 Synonyms:ALK5, SKR4 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000106799.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11772 TGFBR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 190181 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P36897 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell membrane 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane."
Gilboa L., Wells R.G., Lodish H.F., Henis Y.I.
J. Cell Biol. 140:767-777(1998) [PubMed] [Europe PMC] [Abstract]Cited for: HOMODIMERIZATION, SUBCELLULAR LOCATION. - Ref.29"Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization."
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.
Oncogene 35:389-401(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SDCBP AND CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION, PROTEASOMAL DEGRADATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane."
Gilboa L., Wells R.G., Lodish H.F., Henis Y.I.
J. Cell Biol. 140:767-777(1998) [PubMed] [Europe PMC] [Abstract]Cited for: HOMODIMERIZATION, SUBCELLULAR LOCATION.
- Cell membrane 2 Publications
Other locations
- tight junction 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity."
Ozdamar B., Bose R., Barrios-Rodiles M., Wang H.R., Zhang Y., Wrana J.L.
Science 307:1603-1609(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EPITHELIAL TO MESENCHYMAL TRANSITION, SUBCELLULAR LOCATION, INTERACTION WITH PARD6A, FUNCTION IN PHOSPHORYLATION OF PARD6A.
- Cell surface 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.29"Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization."
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.
Oncogene 35:389-401(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SDCBP AND CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION, PROTEASOMAL DEGRADATION.
- Membrane raft 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.29"Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization."
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.
Oncogene 35:389-401(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SDCBP AND CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION, PROTEASOMAL DEGRADATION.
- tight junction 1 Publication
Endosome
- endosome Source: Ensembl
Plasma Membrane
- plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transforming growth factor beta receptor complex Source: BHF-UCL <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatori
Other locations
- bicellular tight junction Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cell Source: AgBase
- cell surface Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- intracellular Source: GOC
- intracellular membrane-bounded organelle Source: HPA
- membrane Source: AgBase
- membrane raft Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- receptor complex Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 34 – 126 | ExtracellularSequence analysisAdd BLAST | 93 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 127 – 147 | HelicalSequence analysisAdd BLAST | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 148 – 503 | CytoplasmicSequence analysisAdd BLAST | 356 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell junction, Cell membrane, Membrane, Tight junction<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Loeys-Dietz syndrome 1 (LDS1)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.39"A syndrome of altered cardiovascular, craniofacial, neurocognitive and skeletal development caused by mutations in TGFBR1 or TGFBR2."
Loeys B.L., Chen J., Neptune E.R., Judge D.P., Podowski M., Holm T., Meyers J., Leitch C.C., Katsanis N., Sharifi N., Xu F.L., Myers L.A., Spevak P.J., Cameron D.E., De Backer J.F., Hellemans J., Chen Y., Davis E.C. , Webb C.L., Kress W., Coucke P.J., Rifkin D.B., De Paepe A.M., Dietz H.C.
Nat. Genet. 37:275-281(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LDS1 ILE-200; ARG-318; GLY-400 AND PRO-487. - Ref.41"FBN1, TGFBR1, and the Marfan-craniosynostosis/mental retardation disorders revisited."
Ades L.C., Sullivan K., Biggin A., Haan E.A., Brett M., Holman K.J., Dixon J., Robertson S., Holmes A.D., Rogers J., Bennetts B.
Am. J. Med. Genet. A 140:1047-1058(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LDS1 LEU-241. - Ref.42"Identification and in silico analyses of novel TGFBR1 and TGFBR2 mutations in Marfan syndrome-related disorders."
Matyas G., Arnold E., Carrel T., Baumgartner D., Boileau C., Berger W., Steinmann B.
Hum. Mutat. 27:760-769(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LDS1 LEU-241 AND GLN-487, VARIANT HIS-267. - Ref.43"Aneurysm syndromes caused by mutations in the TGF-beta receptor."
Loeys B.L., Schwarze U., Holm T., Callewaert B.L., Thomas G.H., Pannu H., De Backer J.F., Oswald G.L., Symoens S., Manouvrier S., Roberts A.E., Faravelli F., Greco M.A., Pyeritz R.E., Milewicz D.M., Coucke P.J., Cameron D.E., Braverman A.C. , Byers P.H., De Paepe A.M., Dietz H.C.
N. Engl. J. Med. 355:788-798(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LDS1 GLU-232; TRP-487; PRO-487 AND GLN-487. - Ref.46"Loeys-Dietz syndrome type I and type II: clinical findings and novel mutations in two Italian patients."
Drera B., Ritelli M., Zoppi N., Wischmeijer A., Gnoli M., Fattori R., Calzavara-Pinton P.G., Barlati S., Colombi M.
Orphanet J. Rare Dis. 4:24-24(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LDS1 GLY-351. - Ref.47"Clinical features and genetic analysis of Korean patients with Loeys-Dietz syndrome."
Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K., Lee H.J., Kim D.K.
J. Hum. Genet. 57:52-56(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LDS1 TYR-266; ARG-375 AND GLN-487.
Loeys B.L., Chen J., Neptune E.R., Judge D.P., Podowski M., Holm T., Meyers J., Leitch C.C., Katsanis N., Sharifi N., Xu F.L., Myers L.A., Spevak P.J., Cameron D.E., De Backer J.F., Hellemans J., Chen Y., Davis E.C. , Webb C.L., Kress W., Coucke P.J., Rifkin D.B., De Paepe A.M., Dietz H.C.
Nat. Genet. 37:275-281(2005) [PubMed] [Europe PMC] [Abstract]
Ades L.C., Sullivan K., Biggin A., Haan E.A., Brett M., Holman K.J., Dixon J., Robertson S., Holmes A.D., Rogers J., Bennetts B.
Am. J. Med. Genet. A 140:1047-1058(2006) [PubMed] [Europe PMC] [Abstract]
Matyas G., Arnold E., Carrel T., Baumgartner D., Boileau C., Berger W., Steinmann B.
Hum. Mutat. 27:760-769(2006) [PubMed] [Europe PMC] [Abstract]
Loeys B.L., Schwarze U., Holm T., Callewaert B.L., Thomas G.H., Pannu H., De Backer J.F., Oswald G.L., Symoens S., Manouvrier S., Roberts A.E., Faravelli F., Greco M.A., Pyeritz R.E., Milewicz D.M., Coucke P.J., Cameron D.E., Braverman A.C. , Byers P.H., De Paepe A.M., Dietz H.C.
N. Engl. J. Med. 355:788-798(2006) [PubMed] [Europe PMC] [Abstract]
Drera B., Ritelli M., Zoppi N., Wischmeijer A., Gnoli M., Fattori R., Calzavara-Pinton P.G., Barlati S., Colombi M.
Orphanet J. Rare Dis. 4:24-24(2009) [PubMed] [Europe PMC] [Abstract]
Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K., Lee H.J., Kim D.K.
J. Hum. Genet. 57:52-56(2012) [PubMed] [Europe PMC] [Abstract]
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.42"Identification and in silico analyses of novel TGFBR1 and TGFBR2 mutations in Marfan syndrome-related disorders."
Matyas G., Arnold E., Carrel T., Baumgartner D., Boileau C., Berger W., Steinmann B.
Hum. Mutat. 27:760-769(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LDS1 LEU-241 AND GLN-487, VARIANT HIS-267.
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022344 | 200 | T → I in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029481 | 232 | K → E in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029482 | 241 | S → L in LDS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066720 | 266 | D → Y in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022345 | 318 | M → R in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066721 | 351 | D → G in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066722 | 375 | T → R in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022346 | 400 | D → G in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022347 | 487 | R → P in LDS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029484 | 487 | R → Q in LDS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029485 | 487 | R → W in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Multiple self-healing squamous epithelioma (MSSE)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.48"Multiple self-healing squamous epithelioma is caused by a disease-specific spectrum of mutations in TGFBR1."
Goudie D.R., D'Alessandro M., Merriman B., Lee H., Szeverenyi I., Avery S., O'Connor B.D., Nelson S.F., Coats S.E., Stewart A., Christie L., Pichert G., Friedel J., Hayes I., Burrows N., Whittaker S., Gerdes A.M., Broesby-Olsen S. , Ferguson-Smith M.A., Verma C., Lunny D.P., Reversade B., Lane E.B.
Nat. Genet. 43:365-369(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MSSE TYR-41; SER-45; ARG-52 AND LEU-83.
Goudie D.R., D'Alessandro M., Merriman B., Lee H., Szeverenyi I., Avery S., O'Connor B.D., Nelson S.F., Coats S.E., Stewart A., Christie L., Pichert G., Friedel J., Hayes I., Burrows N., Whittaker S., Gerdes A.M., Broesby-Olsen S. , Ferguson-Smith M.A., Verma C., Lunny D.P., Reversade B., Lane E.B.
Nat. Genet. 43:365-369(2011) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065826 | 41 | C → Y in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065827 | 45 | N → S in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065828 | 52 | G → R in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065829 | 83 | P → L in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 185 – 186 | TT → VV: Loss of phosphorylation on threonine residues. Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with A-187; A-189 and A-191. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 187 | S → A: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-189 and A-191. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 189 | S → A: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-191. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 191 | S → A: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-189. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 193 | L → G: Loss of interaction with FKBP1A. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 194 | P → K: Loss of interaction with FKBP1A. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 200 | T → D: Loss of response to TGF-beta. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 200 | T → V: Loss of phosphorylation. Loss of response to TGF-beta. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 204 | T → D: Constitutive activation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 204 | T → V: Reduced phosphorylation. Reduced response to TGF-beta. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Aortic aneurysm, Craniosynostosis, Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 7046 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | TGFBR1 |
MalaCards human disease database More...MalaCardsi | TGFBR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 132800 phenotype 609192 phenotype |
Open Targets More...OpenTargetsi | ENSG00000106799 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 91387 Familial thoracic aortic aneurysm and aortic dissection 60030 Loeys-Dietz syndrome 65748 Multiple keratoacanthoma, Ferguson-Smith type |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36485 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4439 |
Drug and drug target database More...DrugBanki | DB07267 2-(6-methylpyridin-2-yl)-N-pyridin-4-ylquinazolin-4-amine DB03921 4-(3-Pyridin-2-Yl-1h-Pyrazol-4-Yl)Quinoline DB08450 N-1H-indazol-5-yl-2-(6-methylpyridin-2-yl)quinazolin-4-amine DB07152 N-[4-(5-fluoro-6-methylpyridin-2-yl)-5-quinoxalin-6-yl-1H-imidazol-2-yl]acetamide DB04434 Naphthyridine Inhibitor |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1788 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TGFBR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 547777 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 33 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 33 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000024423 | 34 – 503 | TGF-beta receptor type-1Add BLAST | 470 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 36 ↔ 54 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 38 ↔ 41 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 45 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 48 ↔ 71 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 86 ↔ 100 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 101 ↔ 106 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 165 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 185 | Phosphothreonine; by TGFBR21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 186 | Phosphothreonine; by TGFBR21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 187 | Phosphoserine; by TGFBR21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 189 | Phosphoserine; by TGFBR21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 191 | Phosphoserine; by TGFBR21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 391 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex."
Wieser R., Wrana J.L., Massague J.
EMBO J. 14:2199-2208(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-185; THR-186; SER-187; SER-189 AND SER-191 BY TGFBR2, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF 185-THR-THR-186; SER-187; SER-189; SER-191; THR-200 AND THR-204. - Ref.32"The TGF beta receptor activation process: an inhibitor- to substrate-binding switch."
Huse M., Muir T.W., Xu L., Chen Y.-G., Kuriyan J., Massague J.
Mol. Cell 8:671-682(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 162-503, PHOSPHORYLATION, INTERACTION WITH SMAD2 AND FKBP1A.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Type I transforming growth factor beta receptor maps to 9q22 and exhibits a polymorphism and a rare variant within a polyalanine tract."
Pasche B., Luo Y., Rao P.H., Nimer S.D., Dmitrovsky E., Caron P., Luzzatto L., Offit K., Cordon-Cardo C., Renault B., Satagopan J.M., Murty V.V., Massague J.
Cancer Res. 58:2727-2732(1998) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 34-40, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION, CHARACTERIZATION OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL, VARIANT TGFBR1*10A ALA-26 INS.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor."
Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., Imamura T.
Biochem. J. 386:461-470(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NEDD4L, UBIQUITINATION. - Ref.28"USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma."
Eichhorn P.J., Rodon L., Gonzalez-Junca A., Dirac A., Gili M., Martinez-Saez E., Aura C., Barba I., Peg V., Prat A., Cuartas I., Jimenez J., Garcia-Dorado D., Sahuquillo J., Bernards R., Baselga J., Seoane J.
Nat. Med. 18:429-435(2012) [PubMed] [Europe PMC] [Abstract]Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP15. - Ref.29"Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization."
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.
Oncogene 35:389-401(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SDCBP AND CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION, PROTEASOMAL DEGRADATION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P36897 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P36897 |
PeptideAtlas More...PeptideAtlasi | P36897 |
PRoteomics IDEntifications database More...PRIDEi | P36897 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55234 55235 [P36897-2] 55236 [P36897-3] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P36897 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P36897 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.29"Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization."
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.
Oncogene 35:389-401(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SDCBP AND CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION, PROTEASOMAL DEGRADATION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000106799 |
CleanEx database of gene expression profiles More...CleanExi | HS_TGFBR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P36897 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P36897 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB002441 CAB031481 HPA056473 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex."
Wieser R., Wrana J.L., Massague J.
EMBO J. 14:2199-2208(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-185; THR-186; SER-187; SER-189 AND SER-191 BY TGFBR2, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF 185-THR-THR-186; SER-187; SER-189; SER-191; THR-200 AND THR-204. - Ref.12"MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling."
Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.
Cell 87:1215-1224(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION. - Ref.13"Mechanism of TGFbeta receptor inhibition by FKBP12."
Chen Y.G., Liu F., Massague J.
EMBO J. 16:3866-3876(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FKBP1A, ENZYME REGULATION, MUTAGENESIS OF LEU-193 AND PRO-194. - Ref.14"TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4."
Nakao A., Imamura T., Souchelnytskyi S., Kawabata M., Ishisaki A., Oeda E., Tamaki K., Hanai J., Heldin C.H., Miyazono K., ten Dijke P.
EMBO J. 16:5353-5362(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMAD3. - Ref.15"TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling."
Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L.
J. Biol. Chem. 272:27678-27685(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION. - Ref.16"SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor."
Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.
Cell 95:779-791(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZFYVE9. - Ref.18"Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-beta receptor for degradation."
Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L.
Mol. Cell 6:1365-1375(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMAD7 AND SMURF2, PROTEASOMAL AND LYSOSOMAL DEGRADATION. - Ref.19"Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMAD7 AND SMURF1, PROTEASOMAL DEGRADATION. - Ref.20"TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling."
Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S., McNally J.G., Roberts A.B.
EMBO J. 22:4465-4477(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VPS39. - Ref.21"NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor."
Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., Imamura T.
Biochem. J. 386:461-470(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NEDD4L, UBIQUITINATION. - Ref.22"Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity."
Ozdamar B., Bose R., Barrios-Rodiles M., Wang H.R., Zhang Y., Wrana J.L.
Science 307:1603-1609(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EPITHELIAL TO MESENCHYMAL TRANSITION, SUBCELLULAR LOCATION, INTERACTION WITH PARD6A, FUNCTION IN PHOSPHORYLATION OF PARD6A. - Ref.23"Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes."
Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S., Bizet A.A., Philip A.
FASEB J. 20:1525-1527(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELLULAR GROWTH INHIBITION, INTERACTION WITH CD109. - Ref.25"The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner."
Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V., Schuster N., Zhang S., Heldin C.H., Landstrom M.
Nat. Cell Biol. 10:1199-1207(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH TRAF6 AND MAP3K7. - Ref.29"Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization."
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.
Oncogene 35:389-401(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SDCBP AND CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION, PROTEASOMAL DEGRADATION. - Ref.31"Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12."
Huse M., Chen Y.-G., Massague J., Kuriyan J.
Cell 96:425-436(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 162-503 IN COMPLEX WITH FKBP1A. - Ref.32"The TGF beta receptor activation process: an inhibitor- to substrate-binding switch."
Huse M., Muir T.W., Xu L., Chen Y.-G., Kuriyan J., Massague J.
Mol. Cell 8:671-682(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 162-503, PHOSPHORYLATION, INTERACTION WITH SMAD2 AND FKBP1A. - Ref.33"Synthesis and activity of new aryl- and heteroaryl-substituted 5,6-dihydro-4H-pyrrolo[1,2-b]pyrazole inhibitors of the transforming growth factor-beta type I receptor kinase domain."
Sawyer J.S., Beight D.W., Britt K.S., Anderson B.D., Campbell R.M., Goodson T. Jr., Herron D.K., Li H.-Y., McMillen W.T., Mort N., Parsons S., Smith E.C.R., Wagner J.R., Yan L., Zhang F., Yingling J.M.
Bioorg. Med. Chem. Lett. 14:3581-3584(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-500 IN COMPLEX WITH SYNTHETIC INHIBITOR. - Ref.34"Identification of 1,5-naphthyridine derivatives as a novel series of potent and selective TGF-beta type I receptor inhibitors."
Gellibert F., Woolven J., Fouchet M.-H., Mathews N., Goodland H., Lovegrove V., Laroze A., Nguyen V.-L., Sautet S., Wang R., Janson C., Smith W., Krysa G., Boullay V., De Gouville A.-C., Huet S., Hartley D.
J. Med. Chem. 47:4494-4506(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 201-503 IN COMPLEX WITH SYNTHETIC INHIBITOR. - Ref.35"Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding."
Groppe J., Hinck C.S., Samavarchi-Tehrani P., Zubieta C., Schuermann J.P., Taylor A.B., Schwarz P.M., Wrana J.L., Hinck A.P.
Mol. Cell 29:157-168(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 33-111 IN COMPLEX WITH TGFBR2 AND TGFB3, DISULFIDE BONDS. - Ref.36"Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily."
Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.
J. Biol. Chem. 285:14806-14814(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 31-115 IN COMPLEX WITH TGFBR2 AND TGFB1, RECEPTOR AFFINITY FOR LIGANDS, DISULFIDE BONDS.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Q99IB8 | 5 | EBI-1027557,EBI-6858501 | From Hepatitis C virus genotype 2a (isolate JFH-1). | |
| FKBP1A | P62942 | 2 | EBI-1027557,EBI-1027571 | |
| LRG1 | P02750 | 6 | EBI-16065417,EBI-9083443 | |
| TGFB1 | P01137 | 2 | EBI-1027557,EBI-779636 | |
| YWHAZ | P63104 | 4 | EBI-1027557,EBI-347088 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- I-SMAD binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- SMAD binding Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transforming growth factor beta binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- type II transforming growth factor beta receptor binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112904, 187 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-2544 TGF-beta-3-TGFR complex CPX-529 TGF-beta-1-TGFR complex CPX-834 TGF-beta-2-TGFR complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P36897 |
Database of interacting proteins More...DIPi | DIP-5935N |
Protein interaction database and analysis system More...IntActi | P36897, 46 interactors |
Molecular INTeraction database More...MINTi | P36897 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000364133 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P36897 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 35 – 37 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 42 – 46 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 51 – 57 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 61 – 63 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 69 – 72 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 74 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 77 – 82 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 84 – 86 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 89 – 92 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 94 – 101 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 102 – 105 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 107 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 177 – 183 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 187 – 190 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 191 – 193 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 202 – 204 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 205 – 213 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 215 – 224 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 227 – 234 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 236 – 238 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 239 – 249 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 251 – 253 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 262 – 269 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 271 – 281 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 288 – 294 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 299 – 317 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 322 – 324 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 328 – 330 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 336 – 338 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 339 – 341 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 347 – 349 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 352 – 354 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 356 – 359 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 360 – 363 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 364 – 367 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 368 – 371 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 376 – 378 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 381 – 384 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 393 – 413 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 417 – 419 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 427 – 431 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 438 – 445 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 456 – 460 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 462 – 474 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 479 – 481 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 485 – 497 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P36897 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P36897 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P36897 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 175 – 204 | GSPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 30 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 205 – 495 | Protein kinasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 291 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 193 – 194 | FKBP1A-binding | 2 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Signal, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2052 Eukaryota ENOG410XQT0 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118876 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000230587 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054502 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P36897 |
KEGG Orthology (KO) More...KOi | K04674 |
Identification of Orthologs from Complete Genome Data More...OMAi | GATALQC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0BIU |
Database for complete collections of gene phylogenies More...PhylomeDBi | P36897 |
TreeFam database of animal gene trees More...TreeFami | TF314724 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000472 Activin_recp IPR003605 GS_dom IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS IPR000333 TGFB_receptor |
The PANTHER Classification System More...PANTHERi | PTHR23255 PTHR23255, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01064 Activin_recp, 1 hit PF00069 Pkinase, 1 hit PF08515 TGF_beta_GS, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00467 GS, 1 hit SM00220 S_TKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51256 GS, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT
60 70 80 90 100
DGLCFVSVTE TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC
110 120 130 140 150
CNQDHCNKIE LPTTVKSSPG LGPVELAAVI AGPVCFVCIS LMLMVYICHN
160 170 180 190 200
RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL IYDMTTSGSG SGLPLLVQRT
210 220 230 240 250
IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER SWFREAEIYQ
260 270 280 290 300
TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE
310 320 330 340 350
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA
360 370 380 390 400
DLGLAVRHDS ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD
410 420 430 440 450
IYAMGLVFWE IARRCSIGGI HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL
460 470 480 490 500
RPNIPNRWQS CEALRVMAKI MRECWYANGA ARLTALRIKK TLSQLSQQEG
IKM
The sequence of this isoform differs from the canonical sequence as follows:
114-114: T → TGPFS
10 20 30 40 50
MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT
60 70 80 90 100
DGLCFVSVTE TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC
110 120 130 140 150
CNQDHCNKIE LPTTGPFSVK SSPGLGPVEL AAVIAGPVCF VCISLMLMVY
160 170 180 190 200
ICHNRTVIHH RVPNEEDPSL DRPFISEGTT LKDLIYDMTT SGSGSGLPLL
210 220 230 240 250
VQRTIARTIV LQESIGKGRF GEVWRGKWRG EEVAVKIFSS REERSWFREA
260 270 280 290 300
EIYQTVMLRH ENILGFIAAD NKDNGTWTQL WLVSDYHEHG SLFDYLNRYT
310 320 330 340 350
VTVEGMIKLA LSTASGLAHL HMEIVGTQGK PAIAHRDLKS KNILVKKNGT
360 370 380 390 400
CCIADLGLAV RHDSATDTID IAPNHRVGTK RYMAPEVLDD SINMKHFESF
410 420 430 440 450
KRADIYAMGL VFWEIARRCS IGGIHEDYQL PYYDLVPSDP SVEEMRKVVC
460 470 480 490 500
EQKLRPNIPN RWQSCEALRV MAKIMRECWY ANGAARLTAL RIKKTLSQLS
QQEGIKM
The sequence of this isoform differs from the canonical sequence as follows:
115-191: Missing.
10 20 30 40 50
MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT
60 70 80 90 100
DGLCFVSVTE TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC
110 120 130 140 150
CNQDHCNKIE LPTTGLPLLV QRTIARTIVL QESIGKGRFG EVWRGKWRGE
160 170 180 190 200
EVAVKIFSSR EERSWFREAE IYQTVMLRHE NILGFIAADN KDNGTWTQLW
210 220 230 240 250
LVSDYHEHGS LFDYLNRYTV TVEGMIKLAL STASGLAHLH MEIVGTQGKP
260 270 280 290 300
AIAHRDLKSK NILVKKNGTC CIADLGLAVR HDSATDTIDI APNHRVGTKR
310 320 330 340 350
YMAPEVLDDS INMKHFESFK RADIYAMGLV FWEIARRCSI GGIHEDYQLP
360 370 380 390 400
YYDLVPSDPS VEEMRKVVCE QKLRPNIPNR WQSCEALRVM AKIMRECWYA
410 420
NGAARLTALR IKKTLSQLSQ QEGIKM
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022342 | 24 – 26 | Missing in allele TGFBR1*6A; could be a tumor susceptibility allele. | 3 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022343 | 26 | A → AA in allele TGFBR1*10A; rare polymorphism. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065826 | 41 | C → Y in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065827 | 45 | N → S in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065828 | 52 | G → R in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065829 | 83 | P → L in MSSE; hypomorphic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_054160 | 139 | I → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041412 | 153 | V → I1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022344 | 200 | T → I in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029481 | 232 | K → E in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029482 | 241 | S → L in LDS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066720 | 266 | D → Y in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029483 | 267 | N → H in a patient with Marfan syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041413 | 291 | Y → C1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022345 | 318 | M → R in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066721 | 351 | D → G in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066722 | 375 | T → R in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022346 | 400 | D → G in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022347 | 487 | R → P in LDS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029484 | 487 | R → Q in LDS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029485 | 487 | R → W in LDS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041326 | 114 | T → TGPFS in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041327 | 115 – 191 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 77 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L11695 mRNA Translation: AAA16073.1 AF054598 , AF054590, AF054591, AF054592, AF054593, AF054594, AF054595, AF054596, AF054597 Genomic DNA Translation: AAC08998.1 AF035670 , AF035662, AF035663, AF035664, AF035665, AF035666, AF035667, AF035668, AF035669 Genomic DNA Translation: AAD02042.1 AY497473 Genomic DNA Translation: AAR32097.1 AL162427 Genomic DNA No translation available. BC071181 mRNA Translation: AAH71181.1 AJ619019 mRNA Translation: CAF02096.2 AJ619020 mRNA Translation: CAF02097.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS47998.1 [P36897-3] CCDS6738.1 [P36897-1] CCDS78413.1 [P36897-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A49432 |
NCBI Reference Sequences More...RefSeqi | NP_001124388.1, NM_001130916.2 [P36897-3] NP_001293139.1, NM_001306210.1 [P36897-2] NP_004603.1, NM_004612.3 [P36897-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.494622 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000374990; ENSP00000364129; ENSG00000106799 [P36897-3] ENST00000374994; ENSP00000364133; ENSG00000106799 [P36897-1] ENST00000552516; ENSP00000447297; ENSG00000106799 [P36897-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 7046 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:7046 |
UCSC genome browser More...UCSCi | uc004azd.4 human [P36897-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P36897 | Receptor protein serine/threonine kinase | 503 | |||
| Receptor protein serine/threonine kinase (Fragment) | 475 | ||||
| Receptor protein serine/threonine kinase (Fragment) | 471 | ||||
| Receptor protein serine/threonine kinase | 470 | ||||
| Receptor protein serine/threonine kinase | 470 | ||||
| +14 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| NIEHS-SNPs |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L11695 mRNA Translation: AAA16073.1 AF054598 , AF054590, AF054591, AF054592, AF054593, AF054594, AF054595, AF054596, AF054597 Genomic DNA Translation: AAC08998.1 AF035670 , AF035662, AF035663, AF035664, AF035665, AF035666, AF035667, AF035668, AF035669 Genomic DNA Translation: AAD02042.1 AY497473 Genomic DNA Translation: AAR32097.1 AL162427 Genomic DNA No translation available. BC071181 mRNA Translation: AAH71181.1 AJ619019 mRNA Translation: CAF02096.2 AJ619020 mRNA Translation: CAF02097.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS47998.1 [P36897-3] CCDS6738.1 [P36897-1] CCDS78413.1 [P36897-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A49432 |
NCBI Reference Sequences More...RefSeqi | NP_001124388.1, NM_001130916.2 [P36897-3] NP_001293139.1, NM_001306210.1 [P36897-2] NP_004603.1, NM_004612.3 [P36897-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.494622 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1B6C | X-ray | 2.60 | B/D/F/H | 162-503 | [»] | |
| 1IAS | X-ray | 2.90 | A/B/C/D/E | 162-503 | [»] | |
| 1PY5 | X-ray | 2.30 | A | 175-500 | [»] | |
| 1RW8 | X-ray | 2.40 | A | 200-500 | [»] | |
| 1TBI | model | - | A | 34-114 | [»] | |
| 1VJY | X-ray | 2.00 | A | 201-503 | [»] | |
| 2L5S | NMR | - | A | 31-115 | [»] | |
| 2PJY | X-ray | 3.00 | C | 33-111 | [»] | |
| 2WOT | X-ray | 1.85 | A | 200-503 | [»] | |
| 2WOU | X-ray | 2.30 | A | 200-503 | [»] | |
| 2X7O | X-ray | 3.70 | A/B/C/D/E | 162-503 | [»] | |
| 3FAA | X-ray | 3.35 | A/B/C/D/E | 162-503 | [»] | |
| 3GXL | X-ray | 1.80 | A | 201-503 | [»] | |
| 3HMM | X-ray | 1.70 | A | 201-503 | [»] | |
| 3KCF | X-ray | 2.80 | A/B/C/D/E | 162-503 | [»] | |
| 3KFD | X-ray | 3.00 | I/J/K/L | 31-115 | [»] | |
| 3TZM | X-ray | 1.70 | A | 200-503 | [»] | |
| 4X0M | X-ray | 1.68 | A | 200-503 | [»] | |
| 4X2F | X-ray | 1.49 | A | 200-503 | [»] | |
| 4X2G | X-ray | 1.51 | A | 200-503 | [»] | |
| 4X2J | X-ray | 1.69 | A | 200-503 | [»] | |
| 4X2K | X-ray | 1.69 | A | 200-503 | [»] | |
| 4X2N | X-ray | 1.80 | A | 200-503 | [»] | |
| 5E8S | X-ray | 1.45 | A | 200-503 | [»] | |
| 5E8T | X-ray | 1.70 | A | 200-503 | [»] | |
| 5E8U | X-ray | 2.03 | A | 200-503 | [»] | |
| 5E8W | X-ray | 1.86 | A | 200-503 | [»] | |
| 5E8X | X-ray | 1.45 | A | 200-503 | [»] | |
| 5E8Z | X-ray | 1.51 | A | 200-503 | [»] | |
| 5E90 | X-ray | 2.05 | A | 200-503 | [»] | |
| 5FRI | X-ray | 2.00 | A | 200-498 | [»] | |
| 5USQ | X-ray | 2.55 | A | 200-498 | [»] | |
| 6B8Y | X-ray | 1.65 | A | 200-503 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P36897 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P36897 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112904, 187 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-2544 TGF-beta-3-TGFR complex CPX-529 TGF-beta-1-TGFR complex CPX-834 TGF-beta-2-TGFR complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P36897 |
Database of interacting proteins More...DIPi | DIP-5935N |
Protein interaction database and analysis system More...IntActi | P36897, 46 interactors |
Molecular INTeraction database More...MINTi | P36897 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000364133 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P36897 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4439 |
Drug and drug target database More...DrugBanki | DB07267 2-(6-methylpyridin-2-yl)-N-pyridin-4-ylquinazolin-4-amine DB03921 4-(3-Pyridin-2-Yl-1h-Pyrazol-4-Yl)Quinoline DB08450 N-1H-indazol-5-yl-2-(6-methylpyridin-2-yl)quinazolin-4-amine DB07152 N-[4-(5-fluoro-6-methylpyridin-2-yl)-5-quinoxalin-6-yl-1H-imidazol-2-yl]acetamide DB04434 Naphthyridine Inhibitor |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1788 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P36897 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P36897 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TGFBR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 547777 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P36897 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P36897 |
PeptideAtlas More...PeptideAtlasi | P36897 |
PRoteomics IDEntifications database More...PRIDEi | P36897 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55234 55235 [P36897-2] 55236 [P36897-3] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 7046 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000374990; ENSP00000364129; ENSG00000106799 [P36897-3] ENST00000374994; ENSP00000364133; ENSG00000106799 [P36897-1] ENST00000552516; ENSP00000447297; ENSG00000106799 [P36897-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 7046 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:7046 |
UCSC genome browser More...UCSCi | uc004azd.4 human [P36897-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 7046 |
DisGeNET More...DisGeNETi | 7046 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000106799.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | TGFBR1 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | TGFBR1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11772 TGFBR1 |
Human Protein Atlas More...HPAi | CAB002441 CAB031481 HPA056473 |
MalaCards human disease database More...MalaCardsi | TGFBR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 132800 phenotype 190181 gene 609192 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P36897 |
Open Targets More...OpenTargetsi | ENSG00000106799 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 91387 Familial thoracic aortic aneurysm and aortic dissection 60030 Loeys-Dietz syndrome 65748 Multiple keratoacanthoma, Ferguson-Smith type |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36485 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2052 Eukaryota ENOG410XQT0 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118876 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000230587 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054502 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P36897 |
KEGG Orthology (KO) More...KOi | K04674 |
Identification of Orthologs from Complete Genome Data More...OMAi | GATALQC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0BIU |
Database for complete collections of gene phylogenies More...PhylomeDBi | P36897 |
TreeFam database of animal gene trees More...TreeFami | TF314724 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.2 2681 2.7.11.30 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2173788 Downregulation of TGF-beta receptor signaling R-HSA-2173789 TGF-beta receptor signaling activates SMADs R-HSA-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) R-HSA-3304356 SMAD2/3 Phosphorylation Motif Mutants in Cancer R-HSA-3315487 SMAD2/3 MH2 Domain Mutants in Cancer R-HSA-3645790 TGFBR2 Kinase Domain Mutants in Cancer R-HSA-3656532 TGFBR1 KD Mutants in Cancer R-HSA-3656535 TGFBR1 LBD Mutants in Cancer R-HSA-5689603 UCH proteinases R-HSA-5689880 Ub-specific processing proteases |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P36897 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P36897 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | TGFBR1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P36897 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | TGF_beta_receptor_1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 7046 |
Protein Ontology More...PROi | PR:P36897 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000106799 |
CleanEx database of gene expression profiles More...CleanExi | HS_TGFBR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P36897 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P36897 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000472 Activin_recp IPR003605 GS_dom IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS IPR000333 TGFB_receptor |
The PANTHER Classification System More...PANTHERi | PTHR23255 PTHR23255, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01064 Activin_recp, 1 hit PF00069 Pkinase, 1 hit PF08515 TGF_beta_GS, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00467 GS, 1 hit SM00220 S_TKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51256 GS, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | TGFR1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P36897Primary (citable) accession number: P36897 Secondary accession number(s): Q6IR47, Q706C0, Q706C1 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
| Last sequence update: | June 1, 1994 | |
| Last modified: | July 18, 2018 | |
| This is version 212 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
