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UniProtKB - P36897 (TGFR1_HUMAN)

Entry version 229 (02 Dec 2020)
Sequence version 1 (01 Jun 1994)
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Protein

TGF-beta receptor type-1

Gene

TGFBR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation.7 Publications

Caution

One report originally reported variant Ile-375 (PubMed:22113417). This variant has been subsequently corrected to Arg-375 by the same authors (Ref. 49).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<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

Mg2+By similarity, Mn2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Kept in an inactive conformation by FKBP1A preventing receptor activation in absence of ligand. CD109 is another inhibitor of the receptor.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei232ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei333Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi211 – 219ATPPROSITE-ProRule annotation9

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionKinase, Receptor, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Differentiation, Growth regulation
LigandATP-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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P36897

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-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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen and Host 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 domaini34 – 126ExtracellularSequence analysisAdd BLAST93
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei127 – 147HelicalSequence analysisAdd BLAST21
Topological domaini148 – 503CytoplasmicSequence analysisAdd BLAST356

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
The disease is caused by mutations affecting the gene represented in this entry. TGFBR1 mutation Gln-487 has been reported to be associated with thoracic aortic aneurysms and dissection (TAAD) (PubMed:16791849). This phenotype, also known as thoracic aortic aneurysms type 5 (AAT5), is distinguised from LDS1 by having aneurysms restricted to thoracic aorta. It is unclear, however, if this condition is fulfilled in individuals bearing Gln-487 mutation, that is why they are considered as LDS1 by the OMIM resource.1 Publication
Disease descriptionAn aortic aneurysm syndrome with widespread systemic involvement, characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. Physical findings include prominent joint laxity, easy bruising, wide and atrophic scars, velvety and translucent skin with easily visible veins, spontaneous rupture of the spleen or bowel, and catastrophic complications of pregnancy, including rupture of the gravid uterus and the arteries, either during pregnancy or in the immediate postpartum period. Some patients have craniosynostosis, exotropy, micrognathia and retrognathia, structural brain abnormalities, and intellectual deficit.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_022344200T → I in LDS1. 1 PublicationCorresponds to variant dbSNP:rs121918712EnsemblClinVar.1
Natural variantiVAR_029481232K → E in LDS1. 1 Publication1
Natural variantiVAR_029482241S → L in LDS1. 2 PublicationsCorresponds to variant dbSNP:rs111854391EnsemblClinVar.1
Natural variantiVAR_066720266D → Y in LDS1. 1 Publication1
Natural variantiVAR_022345318M → R in LDS1. 1 PublicationCorresponds to variant dbSNP:rs121918710EnsemblClinVar.1
Natural variantiVAR_066721351D → G in LDS1. 1 Publication1
Natural variantiVAR_066722375T → R in LDS1. 1 Publication1
Natural variantiVAR_022346400D → G in LDS1. 1 PublicationCorresponds to variant dbSNP:rs121918711EnsemblClinVar.1
Natural variantiVAR_022347487R → P in LDS1. 2 PublicationsCorresponds to variant dbSNP:rs113605875EnsemblClinVar.1
Natural variantiVAR_029484487R → Q in LDS1. 3 PublicationsCorresponds to variant dbSNP:rs113605875EnsemblClinVar.1
Natural variantiVAR_029485487R → W in LDS1. 1 PublicationCorresponds to variant dbSNP:rs111426349EnsemblClinVar.1
Multiple self-healing squamous epithelioma (MSSE)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by multiple skin tumors that undergo spontaneous regression. Tumors appear most often on sun-exposed regions, are locally invasive, and undergo spontaneous resolution over a period of months leaving pitted scars.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06582641C → Y in MSSE; hypomorphic mutation. 1 Publication1
Natural variantiVAR_06582745N → S in MSSE; hypomorphic mutation. 1 PublicationCorresponds to variant dbSNP:rs387906696EnsemblClinVar.1
Natural variantiVAR_06582852G → R in MSSE; hypomorphic mutation. 1 PublicationCorresponds to variant dbSNP:rs587776865EnsemblClinVar.1
Natural variantiVAR_06582983P → L in MSSE; hypomorphic mutation. 1 PublicationCorresponds to variant dbSNP:rs757374917Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi185 – 186TT → 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 Publication2
Mutagenesisi187S → 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 Publication1
Mutagenesisi189S → 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 Publication1
Mutagenesisi191S → 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 Publication1
Mutagenesisi193L → G: Loss of interaction with FKBP1A. 1 Publication1
Mutagenesisi194P → K: Loss of interaction with FKBP1A. 1 Publication1
Mutagenesisi200T → D: Loss of response to TGF-beta. 1 Publication1
Mutagenesisi200T → V: Loss of phosphorylation. Loss of response to TGF-beta. 1 Publication1
Mutagenesisi204T → D: Constitutive activation. 1 Publication1
Mutagenesisi204T → V: Reduced phosphorylation. Reduced response to TGF-beta. 1 Publication1

Keywords - Diseasei

Aortic aneurysm, Craniosynostosis, Disease mutation

Organism-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
MIMi132800, 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 self-healing squamous epithelioma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36485

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P36897, Tchem

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
DB04480, 3-(4-Fluorophenyl)-2-(6-Methylpyridin-2-Yl)-5,6-Dihydro-4h-Pyrrolo[1,2-B]Pyrazole
DB03921, 4-(3-Pyridin-2-Yl-1h-Pyrazol-4-Yl)Quinoline
DB12010, Fostamatinib
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

DrugCentral

More...DrugCentrali		P36897

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 peptidei1 – 331 PublicationAdd BLAST33
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002442334 – 503TGF-beta receptor type-1Add BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi36 ↔ 542 Publications
Disulfide bondi38 ↔ 412 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi45N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi48 ↔ 712 Publications
Disulfide bondi86 ↔ 1002 Publications
Disulfide bondi101 ↔ 1062 Publications
<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 residuei165PhosphoserineCombined sources1
Modified residuei185Phosphothreonine; by TGFBR21 Publication1
Modified residuei186Phosphothreonine; by TGFBR21 Publication1
Modified residuei187Phosphoserine; by TGFBR21 Publication1
Modified residuei189Phosphoserine; by TGFBR21 Publication1
Modified residuei191Phosphoserine; by TGFBR21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, 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-linki391Glycyl 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%5Fprocessing%5Fsection">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

Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding.2 Publications
N-Glycosylated.1 Publication
Ubiquitinated; undergoes ubiquitination catalyzed by several E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the proteasomal and/or lysosomal degradation of the receptor thereby negatively regulating its activity. Deubiquitinated by USP15, leading to stabilization of the protein and enhanced TGF-beta signal. Its ubiquitination and proteasome-mediated degradation is negatively regulated by SDCBP (PubMed:25893292).3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P36897

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P36897

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		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: a multi-organism proteome resource

More...ProteomicsDBi		55234 [P36897-1]
55235 [P36897-2]
55236 [P36897-3]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P36897, 1 site

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

Found in all tissues examined, most abundant in placenta and least abundant in brain and heart. Expressed in a variety of cancer cell lines (PubMed:25893292).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000106799, Expressed in decidua and 220 other tissues

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		ENSG00000106799, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; in the endoplasmic reticulum but also at the cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3.

Interacts with CD109; inhibits TGF-beta receptor activation in keratinocytes.

Interacts with RBPMS.

Interacts (unphosphorylated) with FKBP1A; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation.

Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor.

Interacts with TRAF6 and MAP3K7; induces MAP3K7 activation by TRAF6.

Interacts with PARD6A; involved in TGF-beta induced epithelial to mesenchymal transition.

Interacts with SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1 and SMURF2 to the TGF-beta receptor.

Interacts with USP15 and VPS39.

Interacts with SDCBP (via C-terminus) (PubMed:25893292)

Interacts with CAV1 and this interaction is impaired in the presence of SDCBP (PubMed:25893292).

Interacts with APPL1; interaction is TGF beta dependent; mediates trafficking of the TGFBR1 from the endosomes to the nucleus via microtubules in a TRAF6-dependent manner (PubMed:26583432).

22 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		112904, 199 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, 24 interactors

Molecular INTeraction database

More...MINTi		P36897

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000364133

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P36897, protein

<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

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P36897

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P36897

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini175 – 204GSPROSITE-ProRule annotationAdd BLAST30
Domaini205 – 495Protein kinasePROSITE-ProRule annotationAdd BLAST291

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Motifi193 – 194FKBP1A-binding2

<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

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2052, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156394

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_8_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P36897

Identification of Orthologs from Complete Genome Data

More...OMAi		LMIYICH

Database for complete collections of gene phylogenies

More...PhylomeDBi		P36897

TreeFam database of animal gene trees

More...TreeFami		TF314724

Family and domain databases

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00413

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P36897-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        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
Length:503
Mass (Da):55,960
Last modified:June 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i179F11404725DDCB
GO
Isoform 2 (identifier: P36897-2) [UniParc]FASTAAdd to basket
Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     114-114: T → TGPFS

Show »
Length:507
Mass (Da):56,348
Checksum:i9EFAF4435F30E4C2
GO
Isoform 3 (identifier: P36897-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-191: Missing.

Show »
Length:426
Mass (Da):47,690
Checksum:i97EA2F587AFA08F6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B4DY26B4DY26_HUMAN
Receptor protein serine/threonine k...
TGFBR1
434Annotation score:

Annotation score:4 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>
F8W1R9F8W1R9_HUMAN
Receptor protein serine/threonine k...
TGFBR1
383Annotation score:

Annotation score:2 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>
F8VXZ5F8VXZ5_HUMAN
Receptor protein serine/threonine k...
TGFBR1
114Annotation score:

Annotation score:2 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>
F8VRH6F8VRH6_HUMAN
TGF-beta receptor type-1
TGFBR1
114Annotation score:

Annotation score:2 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>
F8W0K6F8W0K6_HUMAN
TGF-beta receptor type-1
TGFBR1
126Annotation score:

Annotation score:1 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>
H0YHS4H0YHS4_HUMAN
TGF-beta receptor type-1
TGFBR1
122Annotation score:

Annotation score:1 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>
F8VVC4F8VVC4_HUMAN
TGF-beta receptor type-1
TGFBR1
118Annotation score:

Annotation score:1 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02234224 – 26Missing in allele TGFBR1*6A; could be a tumor susceptibility allele. 3
Natural variantiVAR_02234326A → AA in allele TGFBR1*10A; rare polymorphism. 1 Publication1
Natural variantiVAR_06582641C → Y in MSSE; hypomorphic mutation. 1 Publication1
Natural variantiVAR_06582745N → S in MSSE; hypomorphic mutation. 1 PublicationCorresponds to variant dbSNP:rs387906696EnsemblClinVar.1
Natural variantiVAR_06582852G → R in MSSE; hypomorphic mutation. 1 PublicationCorresponds to variant dbSNP:rs587776865EnsemblClinVar.1
Natural variantiVAR_06582983P → L in MSSE; hypomorphic mutation. 1 PublicationCorresponds to variant dbSNP:rs757374917Ensembl.1
Natural variantiVAR_054160139I → V1 PublicationCorresponds to variant dbSNP:rs148176750EnsemblClinVar.1
Natural variantiVAR_041412153V → I1 PublicationCorresponds to variant dbSNP:rs56014374EnsemblClinVar.1
Natural variantiVAR_022344200T → I in LDS1. 1 PublicationCorresponds to variant dbSNP:rs121918712EnsemblClinVar.1
Natural variantiVAR_029481232K → E in LDS1. 1 Publication1
Natural variantiVAR_029482241S → L in LDS1. 2 PublicationsCorresponds to variant dbSNP:rs111854391EnsemblClinVar.1
Natural variantiVAR_066720266D → Y in LDS1. 1 Publication1
Natural variantiVAR_029483267N → H in a patient with Marfan syndrome. 1 Publication1
Natural variantiVAR_041413291Y → C1 PublicationCorresponds to variant dbSNP:rs35974499Ensembl.1
Natural variantiVAR_022345318M → R in LDS1. 1 PublicationCorresponds to variant dbSNP:rs121918710EnsemblClinVar.1
Natural variantiVAR_066721351D → G in LDS1. 1 Publication1
Natural variantiVAR_066722375T → R in LDS1. 1 Publication1
Natural variantiVAR_022346400D → G in LDS1. 1 PublicationCorresponds to variant dbSNP:rs121918711EnsemblClinVar.1
Natural variantiVAR_022347487R → P in LDS1. 2 PublicationsCorresponds to variant dbSNP:rs113605875EnsemblClinVar.1
Natural variantiVAR_029484487R → Q in LDS1. 3 PublicationsCorresponds to variant dbSNP:rs113605875EnsemblClinVar.1
Natural variantiVAR_029485487R → W in LDS1. 1 PublicationCorresponds to variant dbSNP:rs111426349EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041326114T → TGPFS in isoform 2. 1 Publication1
Alternative sequenceiVSP_041327115 – 191Missing in isoform 3. 1 PublicationAdd BLAST77

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L11695 mRNA Translation: AAA16073.1
AF054598 AF054597 Genomic DNA Translation: AAC08998.1
AF035670 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]

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]

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

<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%5Freferences%5Fsection">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:
EMBLi
GenBanki
DDBJi
Links Updated
L11695 mRNA Translation: AAA16073.1
AF054598 AF054597 Genomic DNA Translation: AAC08998.1
AF035670 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
CCDSiCCDS47998.1 [P36897-3]
CCDS6738.1 [P36897-1]
CCDS78413.1 [P36897-2]
PIRiA49432
RefSeqiNP_001124388.1, NM_001130916.2 [P36897-3]
NP_001293139.1, NM_001306210.1 [P36897-2]
NP_004603.1, NM_004612.3 [P36897-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B6CX-ray2.60B/D/F/H162-503[»]
1IASX-ray2.90A/B/C/D/E162-503[»]
1PY5X-ray2.30A175-500[»]
1RW8X-ray2.40A200-500[»]
1TBImodel-A34-114[»]
1VJYX-ray2.00A201-503[»]
2L5SNMR-A31-115[»]
2PJYX-ray3.00C33-111[»]
2WOTX-ray1.85A200-503[»]
2WOUX-ray2.30A200-503[»]
2X7OX-ray3.70A/B/C/D/E162-503[»]
3FAAX-ray3.35A/B/C/D/E162-503[»]
3GXLX-ray1.80A201-503[»]
3HMMX-ray1.70A201-503[»]
3KCFX-ray2.80A/B/C/D/E162-503[»]
3KFDX-ray3.00I/J/K/L31-115[»]
3TZMX-ray1.70A200-503[»]
4X0MX-ray1.68A200-503[»]
4X2FX-ray1.49A200-503[»]
4X2GX-ray1.51A200-503[»]
4X2JX-ray1.69A200-503[»]
4X2KX-ray1.69A200-503[»]
4X2NX-ray1.80A200-503[»]
5E8SX-ray1.45A200-503[»]
5E8TX-ray1.70A200-503[»]
5E8UX-ray2.03A200-503[»]
5E8WX-ray1.86A200-503[»]
5E8XX-ray1.45A200-503[»]
5E8ZX-ray1.51A200-503[»]
5E90X-ray2.05A200-503[»]
5FRIX-ray2.00A200-498[»]
5QIKX-ray1.58A200-503[»]
5QILX-ray1.98A200-503[»]
5QIMX-ray1.75A200-503[»]
5QTZX-ray1.83A200-503[»]
5QU0X-ray1.67A200-503[»]
5USQX-ray2.55A200-498[»]
6B8YX-ray1.65A200-503[»]
6MACX-ray2.34K33-112[»]
BMRBiP36897
SMRiP36897
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi112904, 199 interactors
ComplexPortaliCPX-2544, TGF-beta-3-TGFR complex
CPX-529, TGF-beta-1-TGFR complex
CPX-834, TGF-beta-2-TGFR complex
CORUMiP36897
DIPiDIP-5935N
IntActiP36897, 24 interactors
MINTiP36897
STRINGi9606.ENSP00000364133

Chemistry databases

ChEMBLiCHEMBL4439
DrugBankiDB07267, 2-(6-methylpyridin-2-yl)-N-pyridin-4-ylquinazolin-4-amine
DB04480, 3-(4-Fluorophenyl)-2-(6-Methylpyridin-2-Yl)-5,6-Dihydro-4h-Pyrrolo[1,2-B]Pyrazole
DB03921, 4-(3-Pyridin-2-Yl-1h-Pyrazol-4-Yl)Quinoline
DB12010, Fostamatinib
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
DrugCentraliP36897
GuidetoPHARMACOLOGYi1788

PTM databases

GlyGeniP36897, 1 site
iPTMnetiP36897
PhosphoSitePlusiP36897

Polymorphism and mutation databases

BioMutaiTGFBR1
DMDMi547777

Proteomic databases

EPDiP36897
jPOSTiP36897
MassIVEiP36897
PaxDbiP36897
PeptideAtlasiP36897
PRIDEiP36897
ProteomicsDBi55234 [P36897-1]
55235 [P36897-2]
55236 [P36897-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		29038, 588 antibodies

The DNASU plasmid repository

More...DNASUi		7046

Genome annotation databases

EnsembliENST00000374990; ENSP00000364129; ENSG00000106799 [P36897-3]
ENST00000374994; ENSP00000364133; ENSG00000106799 [P36897-1]
ENST00000552516; ENSP00000447297; ENSG00000106799 [P36897-2]
GeneIDi7046
KEGGihsa:7046
UCSCiuc004azd.4, human [P36897-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7046
DisGeNETi7046
EuPathDBiHostDB:ENSG00000106799.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		TGFBR1
GeneReviewsiTGFBR1
HGNCiHGNC:11772, TGFBR1
HPAiENSG00000106799, Low tissue specificity
MalaCardsiTGFBR1
MIMi132800, phenotype
190181, gene
609192, phenotype
neXtProtiNX_P36897
OpenTargetsiENSG00000106799
Orphaneti91387, Familial thoracic aortic aneurysm and aortic dissection
60030, Loeys-Dietz syndrome
65748, Multiple self-healing squamous epithelioma
PharmGKBiPA36485

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2052, Eukaryota
GeneTreeiENSGT00940000156394
HOGENOMiCLU_000288_8_1_1
InParanoidiP36897
OMAiLMIYICH
PhylomeDBiP36897
TreeFamiTF314724

Enzyme and pathway databases

BRENDAi2.7.10.2, 2681
2.7.11.30, 2681
PathwayCommonsiP36897
ReactomeiR-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-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
SignaLinkiP36897
SIGNORiP36897

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		7046, 36 hits in 856 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		TGFBR1, human
EvolutionaryTraceiP36897

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
PharosiP36897, Tchem

Protein Ontology

More...PROi		PR:P36897
RNActiP36897, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000106799, Expressed in decidua and 220 other tissues
ExpressionAtlasiP36897, baseline and differential
GenevisibleiP36897, HS

Family and domain databases

IDEALiIID00413
InterProiView 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
PANTHERiPTHR23255, PTHR23255, 1 hit
PfamiView protein in Pfam
PF01064, Activin_recp, 1 hit
PF00069, Pkinase, 1 hit
PF08515, TGF_beta_GS, 1 hit
SMARTiView protein in SMART
SM00467, GS, 1 hit
SM00220, S_TKc, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView 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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiTGFR1_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>AccessioniPrimary (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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 2, 2020
This is version 229 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
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