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Entry version 223 (08 May 2019)
Sequence version 2 (17 Oct 2006)
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Protein

TGF-beta receptor type-2

Gene

TGFBR2

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 I serine/threonine kinase receptor, TGFBR1, 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 TGFRB1 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.1 Publication

<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. 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei277ATPPROSITE-ProRule annotation1
<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 sitei379Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi250 – 258ATPPROSITE-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

GO - Biological processi

<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

Reactome - a knowledgebase of biological pathways and processes

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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-3642279 TGFBR2 MSI Frameshift 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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P37173

SIGNOR Signaling Network Open Resource

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SIGNORi
P37173

<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-2 (EC:2.7.11.30)
Short name:
TGFR-2
Alternative name(s):
TGF-beta type II receptor
Transforming growth factor-beta receptor type II
Short name:
TGF-beta receptor type II
Short name:
TbetaR-II
<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:TGFBR2
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 3

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:11773 TGFBR2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
190182 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P37173

<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_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 domaini23 – 166ExtracellularSequence analysisAdd BLAST144
<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>Transmembranei167 – 187HelicalSequence analysisAdd BLAST21
Topological domaini188 – 567CytoplasmicSequence analysisAdd BLAST380

Keywords - Cellular componenti

Cell membrane, Membrane

<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

Hereditary non-polyposis colorectal cancer 6 (HNPCC6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected.
See also OMIM:614331
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_008156315T → M in HNPCC6. 2 PublicationsCorresponds to variant dbSNP:rs34833812EnsemblClinVar.1
Esophageal cancer (ESCR)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage.
See also OMIM:133239
Loeys-Dietz syndrome 2 (LDS2)10 Publications
The disease is caused by mutations affecting the gene represented in this entry. TGFBR2 mutations Cys-460 and His-460 have been reported to be associated with thoracic aortic aneurysms and dissection (TAAD). This phenotype, also known as thoracic aortic aneurysms type 3 (AAT3), is distinguised from LDS2 by having aneurysms restricted to thoracic aorta. As individuals carrying these mutations also exhibit descending aortic disease and aneurysms of other arteries (PubMed:16027248), they have been considered as LDS2 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.
See also OMIM:610168
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076167190R → H in LDS2. 1 PublicationCorresponds to variant dbSNP:rs780542125Ensembl.1
Natural variantiVAR_076168247D → V in LDS2. 1 PublicationCorresponds to variant dbSNP:rs761231369Ensembl.1
Natural variantiVAR_066723306Q → HE in LDS2. 1 Publication1
Natural variantiVAR_022351308L → P in LDS2; has a negative effect on TGF-beta signaling. 2 PublicationsCorresponds to variant dbSNP:rs28934568EnsemblClinVar.1
Natural variantiVAR_076169325T → P in LDS2. 1 Publication1
Natural variantiVAR_022352336Y → N in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893812EnsemblClinVar.1
Natural variantiVAR_022353355A → P in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893813EnsemblClinVar.1
Natural variantiVAR_076170357G → R in LDS2. 1 Publication1
Natural variantiVAR_022354357G → W in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893814EnsemblClinVar.1
Natural variantiVAR_066724377H → R in LDS2. 1 Publication1
Natural variantiVAR_066725446D → N in LDS2. 1 PublicationCorresponds to variant dbSNP:rs886039551EnsemblClinVar.1
Natural variantiVAR_022358449S → F in LDS2; has a negative effect on TGF-beta signaling. 2 PublicationsCorresponds to variant dbSNP:rs104893807EnsemblClinVar.1
Natural variantiVAR_066726457M → K in LDS2. 1 Publication1
Natural variantiVAR_029760460R → C in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893811EnsemblClinVar.1
Natural variantiVAR_029761460R → H in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893816EnsemblClinVar.1
Natural variantiVAR_066727509G → V in LDS2. 1 PublicationCorresponds to variant dbSNP:rs863223853EnsemblClinVar.1
Natural variantiVAR_066728510I → F in LDS2. 1 Publication1
Natural variantiVAR_066729510I → S in LDS2. 1 Publication1
Natural variantiVAR_066730514C → R in LDS2. 1 PublicationCorresponds to variant dbSNP:rs193922664EnsemblClinVar.1
Natural variantiVAR_066731521W → R in LDS2. 1 Publication1
Natural variantiVAR_022360528R → C in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893810EnsemblClinVar.1
Natural variantiVAR_022361528R → H in LDS2. 2 PublicationsCorresponds to variant dbSNP:rs104893815EnsemblClinVar.1
Natural variantiVAR_076171530T → I in LDS2. 1 Publication1
Natural variantiVAR_022362537R → C in LDS2; has a negative effect on TGF-beta signaling. 1 PublicationCorresponds to variant dbSNP:rs104893809EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi277K → R: Abolishes kinase activity, TGF-beta signaling and interaction with DAXX. 1 Publication1

Keywords - Diseasei

Aortic aneurysm, Disease mutation, Hereditary nonpolyposis colorectal cancer

Organism-specific databases

DisGeNET

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DisGeNETi
7048

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
TGFBR2

MalaCards human disease database

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MalaCardsi
TGFBR2
MIMi133239 phenotype
610168 phenotype
614331 phenotype

Open Targets

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OpenTargetsi
ENSG00000163513

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
91387 Familial thoracic aortic aneurysm and aortic dissection
60030 Loeys-Dietz syndrome
144 Lynch syndrome
284973 Marfan syndrome type 2
99977 Squamous cell carcinoma of the esophagus

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36486

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4267

Drug and drug target database

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DrugBanki
DB04077 Glycerol

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1795

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TGFBR2

Domain mapping of disease mutations (DMDM)

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DMDMi
116242818

<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 – 221 PublicationAdd BLAST22
<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_000002442623 – 567TGF-beta receptor type-2Add BLAST545

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 bondi51 ↔ 845 Publications
Disulfide bondi54 ↔ 715 Publications
Disulfide bondi61 ↔ 675 Publications
<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>Glycosylationi70N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi77 ↔ 1015 Publications
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi121 ↔ 1365 Publications
Disulfide bondi138 ↔ 1435 Publications
Glycosylationi154N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei409PhosphoserineBy similarity1
Modified residuei548PhosphoserineCombined sources1
Modified residuei553PhosphoserineBy similarity1

<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

Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P37173

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P37173

MaxQB - The MaxQuant DataBase

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MaxQBi
P37173

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P37173

PeptideAtlas

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PeptideAtlasi
P37173

PRoteomics IDEntifications database

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PRIDEi
P37173

ProteomicsDB human proteome resource

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ProteomicsDBi
55264
55265 [P37173-2]

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1979

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P37173

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P37173

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000163513 Expressed in 231 organ(s), highest expression level in metanephric glomerulus

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P37173 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P37173 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB073537

<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

Homodimer. 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 TGFRB1 and TGFRB2 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 DAXX. Interacts with TCTEX1D4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with and is activated by SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2. Interacts with VPS39; this interaction is independent of the receptor kinase activity and of the presence of TGF-beta.8 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112906, 88 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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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

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CORUMi
P37173

Database of interacting proteins

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DIPi
DIP-5939N

Protein interaction database and analysis system

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IntActi
P37173, 29 interactors

Molecular INTeraction database

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MINTi
P37173

STRING: functional protein association networks

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STRINGi
9606.ENSP00000351905

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P37173

<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

1567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KTZX-ray2.15B38-159[»]
1M9ZX-ray1.05A49-159[»]
1PLONMR-A38-159[»]
2PJYX-ray3.00B42-149[»]
3KFDX-ray3.00E/F/G/H38-153[»]
4P7UX-ray1.50A49-159[»]
4XJJX-ray1.40A50-159[»]
5E8VX-ray1.69A237-549[»]
5E8YX-ray2.05A237-549[»]
5E91X-ray2.42A237-549[»]
5E92X-ray2.08A237-549[»]
5QINX-ray1.57A237-549[»]
5TX4X-ray1.88A38-153[»]
5TY4electron microscopy2.90A47-149[»]

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

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SMRi
P37173

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P37173

<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_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>Domaini244 – 544Protein kinasePROSITE-ProRule annotationAdd BLAST301

<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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3653 Eukaryota
ENOG410XS2Z LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157527

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231495

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P37173

KEGG Orthology (KO)

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KOi
K04388

Identification of Orthologs from Complete Genome Data

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OMAi
NDMMVTD

Database of Orthologous Groups

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OrthoDBi
426838at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P37173

TreeFam database of animal gene trees

More...
TreeFami
TF314724

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008271 Ser/Thr_kinase_AS
IPR000333 TGFB_receptor
IPR017194 Transform_growth_fac-b_typ-2
IPR015013 Transforming_GF_b_rcpt_2_ecto

The PANTHER Classification System

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PANTHERi
PTHR23255 PTHR23255, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08917 ecTbetaR2, 1 hit
PF07714 Pkinase_Tyr, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF037393 TGFRII, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00653 ACTIVIN2R

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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 (2)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 2 <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 basket
Isoform 1 (identifier: P37173-1) [UniParc]FASTAAdd 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.

« Hide
        10         20         30         40         50
MGRGLLRGLW PLHIVLWTRI ASTIPPHVQK SVNNDMIVTD NNGAVKFPQL
60 70 80 90 100
CKFCDVRFST CDNQKSCMSN CSITSICEKP QEVCVAVWRK NDENITLETV
110 120 130 140 150
CHDPKLPYHD FILEDAASPK CIMKEKKKPG ETFFMCSCSS DECNDNIIFS
160 170 180 190 200
EEYNTSNPDL LLVIFQVTGI SLLPPLGVAI SVIIIFYCYR VNRQQKLSST
210 220 230 240 250
WETGKTRKLM EFSEHCAIIL EDDRSDISST CANNINHNTE LLPIELDTLV
260 270 280 290 300
GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDINLK
310 320 330 340 350
HENILQFLTA EERKTELGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL
360 370 380 390 400
GSSLARGIAH LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL
410 420 430 440 450
SLRLDPTLSV DDLANSGQVG TARYMAPEVL ESRMNLENVE SFKQTDVYSM
460 470 480 490 500
ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE HPCVESMKDN VLRDRGRPEI
510 520 530 540 550
PSFWLNHQGI QMVCETLTEC WDHDPEARLT AQCVAERFSE LEHLDRLSGR
560
SCSEEKIPED GSLNTTK
Length:567
Mass (Da):64,568
Last modified:October 17, 2006 - v2
<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:iC541DA751FFBDBEB
GO
Isoform 2 (identifier: P37173-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-32: SV → SDVEMEAQKDEIICPSCNRTAHPLRHI

Show »
Length:592
Mass (Da):67,457
Checksum:i8ADCBA70F95E1CBB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti381K → N in BAA09332 (PubMed:8973329).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02051036M → V1 PublicationCorresponds to variant dbSNP:rs17025864EnsemblClinVar.1
Natural variantiVAR_04141461C → R in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_03607073I → V in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_076167190R → H in LDS2. 1 PublicationCorresponds to variant dbSNP:rs780542125Ensembl.1
Natural variantiVAR_017606191V → I2 PublicationsCorresponds to variant dbSNP:rs56105708EnsemblClinVar.1
Natural variantiVAR_076168247D → V in LDS2. 1 PublicationCorresponds to variant dbSNP:rs761231369Ensembl.1
Natural variantiVAR_066723306Q → HE in LDS2. 1 Publication1
Natural variantiVAR_022351308L → P in LDS2; has a negative effect on TGF-beta signaling. 2 PublicationsCorresponds to variant dbSNP:rs28934568EnsemblClinVar.1
Natural variantiVAR_008156315T → M in HNPCC6. 2 PublicationsCorresponds to variant dbSNP:rs34833812EnsemblClinVar.1
Natural variantiVAR_076169325T → P in LDS2. 1 Publication1
Natural variantiVAR_041415328H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_022352336Y → N in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893812EnsemblClinVar.1
Natural variantiVAR_022353355A → P in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893813EnsemblClinVar.1
Natural variantiVAR_076170357G → R in LDS2. 1 Publication1
Natural variantiVAR_022354357G → W in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893814EnsemblClinVar.1
Natural variantiVAR_041416373M → I1 PublicationCorresponds to variant dbSNP:rs35719192EnsemblClinVar.1
Natural variantiVAR_066724377H → R in LDS2. 1 Publication1
Natural variantiVAR_022355387V → M in a breast tumor. 2 PublicationsCorresponds to variant dbSNP:rs35766612EnsemblClinVar.1
Natural variantiVAR_022356435N → S in a breast tumor; signaling of TGF-beta significantly inhibited. 1 Publication1
Natural variantiVAR_028063439V → A4 PublicationsCorresponds to variant dbSNP:rs1050833Ensembl.1
Natural variantiVAR_066725446D → N in LDS2. 1 PublicationCorresponds to variant dbSNP:rs886039551EnsemblClinVar.1
Natural variantiVAR_022357447V → A in a breast tumor; signaling of TGF-beta significantly inhibited. 1 Publication1
Natural variantiVAR_022358449S → F in LDS2; has a negative effect on TGF-beta signaling. 2 PublicationsCorresponds to variant dbSNP:rs104893807EnsemblClinVar.1
Natural variantiVAR_022359452L → M in a breast tumor; signaling of TGF-beta significantly inhibited. 1 Publication1
Natural variantiVAR_066726457M → K in LDS2. 1 Publication1
Natural variantiVAR_029760460R → C in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893811EnsemblClinVar.1
Natural variantiVAR_029761460R → H in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893816EnsemblClinVar.1
Natural variantiVAR_041417490N → S in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_066727509G → V in LDS2. 1 PublicationCorresponds to variant dbSNP:rs863223853EnsemblClinVar.1
Natural variantiVAR_066728510I → F in LDS2. 1 Publication1
Natural variantiVAR_066729510I → S in LDS2. 1 Publication1
Natural variantiVAR_066730514C → R in LDS2. 1 PublicationCorresponds to variant dbSNP:rs193922664EnsemblClinVar.1
Natural variantiVAR_066731521W → R in LDS2. 1 Publication1
Natural variantiVAR_015816526E → Q in esophageal cancer. 1 PublicationCorresponds to variant dbSNP:rs121918714EnsemblClinVar.1
Natural variantiVAR_022360528R → C in LDS2. 1 PublicationCorresponds to variant dbSNP:rs104893810EnsemblClinVar.1
Natural variantiVAR_022361528R → H in LDS2. 2 PublicationsCorresponds to variant dbSNP:rs104893815EnsemblClinVar.1
Natural variantiVAR_076171530T → I in LDS2. 1 Publication1
Natural variantiVAR_022362537R → C in LDS2; has a negative effect on TGF-beta signaling. 1 PublicationCorresponds to variant dbSNP:rs104893809EnsemblClinVar.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_01215731 – 32SV → SDVEMEAQKDEIICPSCNRT AHPLRHI in isoform 2. 2 Publications2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M85079 mRNA Translation: AAA61164.1
D28131 mRNA Translation: BAA05673.1
U52246
, U52240, U52241, U52242, U52244, U52245 Genomic DNA Translation: AAB17553.1
U69152
, U69146, U69147, U69148, U69149, U69150, U69151 Genomic DNA Translation: AAB40916.1
D50683 mRNA Translation: BAA09332.1
AY675319 Genomic DNA Translation: AAT70724.1
AK300383 mRNA Translation: BAG62117.1
CH471055 Genomic DNA Translation: EAW64412.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2648.1 [P37173-1]
CCDS33727.1 [P37173-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A42100

NCBI Reference Sequences

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RefSeqi
NP_001020018.1, NM_001024847.2 [P37173-2]
NP_003233.4, NM_003242.5 [P37173-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000295754; ENSP00000295754; ENSG00000163513 [P37173-1]
ENST00000359013; ENSP00000351905; ENSG00000163513 [P37173-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
7048

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:7048

UCSC genome browser

More...
UCSCi
uc003cen.4 human [P37173-1]

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_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:
EMBLi
GenBanki
DDBJi
Links Updated
M85079 mRNA Translation: AAA61164.1
D28131 mRNA Translation: BAA05673.1
U52246
, U52240, U52241, U52242, U52244, U52245 Genomic DNA Translation: AAB17553.1
U69152
, U69146, U69147, U69148, U69149, U69150, U69151 Genomic DNA Translation: AAB40916.1
D50683 mRNA Translation: BAA09332.1
AY675319 Genomic DNA Translation: AAT70724.1
AK300383 mRNA Translation: BAG62117.1
CH471055 Genomic DNA Translation: EAW64412.1
CCDSiCCDS2648.1 [P37173-1]
CCDS33727.1 [P37173-2]
PIRiA42100
RefSeqiNP_001020018.1, NM_001024847.2 [P37173-2]
NP_003233.4, NM_003242.5 [P37173-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KTZX-ray2.15B38-159[»]
1M9ZX-ray1.05A49-159[»]
1PLONMR-A38-159[»]
2PJYX-ray3.00B42-149[»]
3KFDX-ray3.00E/F/G/H38-153[»]
4P7UX-ray1.50A49-159[»]
4XJJX-ray1.40A50-159[»]
5E8VX-ray1.69A237-549[»]
5E8YX-ray2.05A237-549[»]
5E91X-ray2.42A237-549[»]
5E92X-ray2.08A237-549[»]
5QINX-ray1.57A237-549[»]
5TX4X-ray1.88A38-153[»]
5TY4electron microscopy2.90A47-149[»]
SMRiP37173
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112906, 88 interactors
ComplexPortaliCPX-2544 TGF-beta-3-TGFR complex
CPX-529 TGF-beta-1-TGFR complex
CPX-834 TGF-beta-2-TGFR complex
CORUMiP37173
DIPiDIP-5939N
IntActiP37173, 29 interactors
MINTiP37173
STRINGi9606.ENSP00000351905

Chemistry databases

BindingDBiP37173
ChEMBLiCHEMBL4267
DrugBankiDB04077 Glycerol
GuidetoPHARMACOLOGYi1795

PTM databases

GlyConnecti1979
iPTMnetiP37173
PhosphoSitePlusiP37173

Polymorphism and mutation databases

BioMutaiTGFBR2
DMDMi116242818

Proteomic databases

EPDiP37173
jPOSTiP37173
MaxQBiP37173
PaxDbiP37173
PeptideAtlasiP37173
PRIDEiP37173
ProteomicsDBi55264
55265 [P37173-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7048
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295754; ENSP00000295754; ENSG00000163513 [P37173-1]
ENST00000359013; ENSP00000351905; ENSG00000163513 [P37173-2]
GeneIDi7048
KEGGihsa:7048
UCSCiuc003cen.4 human [P37173-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7048
DisGeNETi7048

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TGFBR2
GeneReviewsiTGFBR2

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0024332
HGNCiHGNC:11773 TGFBR2
HPAiCAB073537
MalaCardsiTGFBR2
MIMi133239 phenotype
190182 gene
610168 phenotype
614331 phenotype
neXtProtiNX_P37173
OpenTargetsiENSG00000163513
Orphaneti91387 Familial thoracic aortic aneurysm and aortic dissection
60030 Loeys-Dietz syndrome
144 Lynch syndrome
284973 Marfan syndrome type 2
99977 Squamous cell carcinoma of the esophagus
PharmGKBiPA36486

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3653 Eukaryota
ENOG410XS2Z LUCA
GeneTreeiENSGT00940000157527
HOGENOMiHOG000231495
InParanoidiP37173
KOiK04388
OMAiNDMMVTD
OrthoDBi426838at2759
PhylomeDBiP37173
TreeFamiTF314724

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
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-3642279 TGFBR2 MSI Frameshift 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
SignaLinkiP37173
SIGNORiP37173

Miscellaneous databases

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

More...
ChiTaRSi
TGFBR2 human
EvolutionaryTraceiP37173

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TGF_beta_receptor_2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
7048

Protein Ontology

More...
PROi
PR:P37173

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000163513 Expressed in 231 organ(s), highest expression level in metanephric glomerulus
ExpressionAtlasiP37173 baseline and differential
GenevisibleiP37173 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008271 Ser/Thr_kinase_AS
IPR000333 TGFB_receptor
IPR017194 Transform_growth_fac-b_typ-2
IPR015013 Transforming_GF_b_rcpt_2_ecto
PANTHERiPTHR23255 PTHR23255, 1 hit
PfamiView protein in Pfam
PF08917 ecTbetaR2, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF037393 TGFRII, 1 hit
PRINTSiPR00653 ACTIVIN2R
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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 nameiTGFR2_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: P37173
Secondary accession number(s): B4DTV5
, Q15580, Q6DKT6, Q99474
<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 historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: May 8, 2019
This is version 223 of the entry and version 2 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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