Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P01137 (TGFB1_HUMAN)

Entry version 256 (07 Oct 2020)
Sequence version 2 (01 Feb 1991)
Previous versions | rss
Add a publicationFeedback
Protein

Transforming growth factor beta-1 proprotein

Gene

TGFB1

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

Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively.1 Publication1 Publication
Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix (PubMed:28117447). Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1 (PubMed:2022183, PubMed:8617200, PubMed:8939931, PubMed:19750484, PubMed:22278742, PubMed:19651619). Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia (Probable). Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:22278742, PubMed:19651619). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447).1 Publication7 Publications
Transforming growth factor beta-1: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix (PubMed:29109152). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus (PubMed:2022183, PubMed:8617200, PubMed:8939931, PubMed:19750484, PubMed:22278742, PubMed:19651619). TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). Once activated following release of LAP, TGF-beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (PubMed:20207738). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency-associated peptide chain (LAP) and 'milieu molecules' (By similarity). Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (By similarity). At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development (By similarity). At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP) (PubMed:25310401). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus (PubMed:25893292, PubMed:29483653, PubMed:30696809). Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (PubMed:25893292, PubMed:30696809).By similarity13 Publications

Miscellaneous

TGF-beta-1 is inactivated by fresolimumab (also named GC1008), a monoclonal-neutralizing antibody.1 Publication

<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 functionGrowth factor, Mitogen

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P01137

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-114608, Platelet degranulation
R-HSA-168277, Influenza Virus Induced Apoptosis
R-HSA-202733, Cell surface interactions at the vascular wall
R-HSA-2129379, Molecules associated with elastic fibres
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-3000170, Syndecan interactions
R-HSA-3000178, ECM proteoglycans
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-381340, Transcriptional regulation of white adipocyte differentiation
R-HSA-5689603, UCH proteinases
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
R-HSA-8941855, RUNX3 regulates CDKN1A transcription
R-HSA-8941858, Regulation of RUNX3 expression and activity
R-HSA-8951936, RUNX3 regulates p14-ARF

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

More...SignaLinki		P01137

SIGNOR Signaling Network Open Resource

More...SIGNORi		P01137

<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:
Transforming growth factor beta-1 proprotein
Cleaved into the following 2 chains:
Latency-associated peptide4 Publications
Short name:
LAP
Transforming growth factor beta-14 Publications
Short name:
TGF-beta-1
<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:TGFB1Imported
Synonyms:TGFB
<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: Unplaced

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000105329.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:11766, TGFB1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		190180, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P01137

<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

Keywords - Cellular componenti

Extracellular matrix, Secreted

<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

Camurati-Engelmann disease (CAEND)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by hyperostosis and sclerosis of the diaphyses of long bones. The disease typically presents in early childhood with pain, muscular weakness and waddling gait, and in some cases other features such as exophthalmos, facial paralysis, hearing difficulties and loss of vision.
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_01760781Y → H in CAEND; leads to TGF-beta-1 intracellular accumulation. 2 Publications1
Natural variantiVAR_017608218R → C in CAEND; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. 4 Publications1
Natural variantiVAR_017609218R → H in CAEND. 1 Publication1
Natural variantiVAR_017610222H → D in CAEND; sporadic case; higher levels of active TGF-beta-1 in the culture medium. 1 Publication1
Natural variantiVAR_067303223C → G in CAEND. 1 Publication1
Natural variantiVAR_067304223C → R in CAEND. 1 Publication1
Natural variantiVAR_017611225C → R in CAEND; higher levels of active TGF-beta-1 in the culture medium. 3 Publications1
Inflammatory bowel disease, immunodeficiency, and encephalopathy (IBDIMDE)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by severe infantile inflammatory bowel disease manifesting as bloody diarrhea and failure to thrive, global developmental delay, epilepsy, brain atrophy and encephalopathy. Affected individuals suffer from recurrent infections associated with impaired T-cell response to stimulation and decreased T-cell subsets, including regulatory and helper T cells.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08158445R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication1
Natural variantiVAR_081585110R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication1
Natural variantiVAR_081586387C → R in IBDIMDE; loss of TGFB1-mediated activation of SMAD signaling; mutant TGFB1 is not secreted. 1 Publication1

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>Mutagenesisi33C → S: Abolishes interchain disulfide bond with LTBP1 and/or LRRC32, and subsequent regulation of activation of TGF-beta-1. 2 Publications1
Mutagenesisi75E → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication1
Mutagenesisi158L → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication1
Mutagenesisi160L → A or R: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication1
Mutagenesisi193P → A or R: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication1
Mutagenesisi232 – 236LQVDI → GQGDG: Strongly inhibits integrin-binding and activation of TGF-beta-1. 1 Publication5
Mutagenesisi234 – 236VDI → GDG: Strongly inhibits integrin-binding and activation of TGF-beta-1. 1 Publication3
Mutagenesisi237N → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication1
Mutagenesisi254N → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication1
Mutagenesisi257 – 260FLLL → GLLG: Strongly inhibits integrin-binding and activation of TGF-beta-1. 1 Publication4
Mutagenesisi278R → A: Prevents cleavage and subsequent maturation of the protein. Generated in order to mimic the structure of the Transforming growth factor beta-1 proprotein. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		7040

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

More...GeneReviewsi		TGFB1

MalaCards human disease database

More...MalaCardsi		TGFB1
MIMi131300, phenotype
618213, phenotype

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

More...Orphaneti		1328, Camurati-Engelmann disease
586, Cystic fibrosis
565788, Infantile inflammatory bowel disease with neurological involvement

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA350

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P01137, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1795178

Drug and drug target database

More...DrugBanki		DB10770, Foreskin fibroblast (neonatal)
DB10772, Foreskin keratinocyte (neonatal)
DB00070, Hyaluronidase (ovine)
DB01162, Terazosin
DB06205, Vorhyaluronidase alfa

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TGFB1

Domain mapping of disease mutations (DMDM)

More...DMDMi		135674

<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 – 291 PublicationAdd BLAST29
<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_000003376230 – 278Latency-associated peptide4 PublicationsAdd BLAST249
ChainiPRO_0000033763279 – 390Transforming growth factor beta-14 PublicationsAdd BLAST112

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 bondi33Interchain (with C-1359 or C-1384 in LTBP1); in inactive form1 Publication
<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>Glycosylationi82N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Glycosylationi136N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi176N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi223Interchain (with C-225)Combined sources2 Publications
Disulfide bondi225Interchain (with C-223)Combined sources2 Publications
Disulfide bondi285 ↔ 294Combined sources4 Publications
Disulfide bondi293 ↔ 356Combined sources4 Publications
Disulfide bondi322 ↔ 387Combined sources4 Publications
Disulfide bondi326 ↔ 389Combined sources4 Publications
Disulfide bondi355InterchainCombined sources3 Publications

<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

Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive.1 Publication
N-glycosylated (PubMed:3162913, PubMed:2493139, PubMed:28117447). Deglycosylation leads to activation of Transforming growth factor beta-1 (TGF-beta-1); mechanisms triggering deglycosylation-driven activation of TGF-beta-1 are however unclear (PubMed:2493139).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei278 – 279Cleavage; by FURIN1 Publication2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P01137

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P01137

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P01137

MaxQB - The MaxQuant DataBase

More...MaxQBi		P01137

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

More...PaxDbi		P01137

PeptideAtlas

More...PeptideAtlasi		P01137

PRoteomics IDEntifications database

More...PRIDEi		P01137

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51337

2D gel databases

USC-OGP 2-DE database

More...OGPi		P01137

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1835, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P01137, 3 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01137

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

More...PhosphoSitePlusi		P01137

<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

Highly expressed in bone (PubMed:11746498, PubMed:17827158). Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA) (PubMed:11746498, PubMed:17827158). Colocalizes with ASPN in chondrocytes within OA lesions of articular cartilage (PubMed:17827158).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000105329, Expressed in granulocyte and 181 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P01137, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000105329, 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; disulfide-linked (PubMed:20207738, PubMed:25209176, PubMed:28117447, PubMed:29109152).

Interacts with the serine proteases, HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated signaling. The HTRA protease activity is required for this inhibition (By similarity). May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling (By similarity).

Interacts with CD109, DPT and ASPN (PubMed:9895299, PubMed:16754747, PubMed:17827158). Latency-associated peptide: Homodimer; disulfide-linked (PubMed:28117447, PubMed:29109152). Latency-associated peptide:

Interacts with Transforming growth factor beta-1 (TGF-beta-1) chain; interaction is non-covalent and maintains (TGF-beta-1) in a latent state; each Latency-associated peptide (LAP) monomer interacts with TGF-beta-1 in the other monomer (PubMed:29109152). Latency-associated peptide:

Interacts with LTBP1; leading to regulate activation of TGF-beta-1 (PubMed:2022183, PubMed:8617200, PubMed:8939931). Latency-associated peptide:

Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:22278742, PubMed:19651619).

Interacts with LRRC33/NRROS; leading to regulate activation of TGF-beta-1 in macrophages and microglia (Probable). Latency-associated peptide:

Interacts (via cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). Latency-associated peptide:

Interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction (By similarity). Latency-associated peptide:

Interacts with HSP90AB1; inhibits latent TGFB1 activation (PubMed:20599762). Transforming growth factor beta-1: Homodimer; disulfide-linked (PubMed:20207738, PubMed:25209176, PubMed:28117447, PubMed:29109152). Transforming growth factor beta-1:

Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (PubMed:20207738).

By similarity1 Publication14 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		112898, 247 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-529, TGF-beta-1-TGFR complex
CPX-602, TGF-beta-1 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P01137

Database of interacting proteins

More...DIPi		DIP-5934N

Protein interaction database and analysis system

More...IntActi		P01137, 95 interactors

Molecular INTeraction database

More...MINTi		P01137

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000221930

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P01137

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P01137, 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

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Small Angle Scattering Biological Data Bank

More...SASBDBi		P01137

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

More...SMRi		P01137

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		P01137

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 74Straightjacket domainBy similarityAdd BLAST45
Regioni75 – 271Arm domainBy similarityAdd BLAST197
Regioni226 – 252Bowtie tail1 PublicationAdd BLAST27

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>Motifi244 – 246Cell attachment site1 Publication3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The 'straitjacket' and 'arm' domains encircle the Transforming growth factor beta-1 (TGF-beta-1) monomers and are fastened together by strong bonding between Lys-56 and Tyr-103/Tyr-104.By similarity
The cell attachment site motif mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8) (PubMed:28117447). The motif locates to a long loop in the arm domain called the bowtie tail (PubMed:28117447). Integrin-binding stabilizes an alternative conformation of the bowtie tail (PubMed:28117447). Activation by integrin requires force application by the actin cytoskeleton, which is resisted by the 'milieu molecules' (such as LTBP1, LRRC32/GARP and/or LRRC33/NRROS), resulting in distortion of the prodomain and release of the active TGF-beta-1 (PubMed:28117447).1 Publication

<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 TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3900, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_039840_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01137

KEGG Orthology (KO)

More...KOi		K13375

Database of Orthologous Groups

More...OrthoDBi		853728at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P01137

TreeFam database of animal gene trees

More...TreeFami		TF318514

Family and domain databases

Database of protein disorder

More...DisProti		DP01252

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.10.90.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00534

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029034, Cystine-knot_cytokine
IPR001839, TGF-b_C
IPR001111, TGF-b_propeptide
IPR016319, TGF-beta
IPR015615, TGF-beta-rel
IPR003939, TGFb1
IPR017948, TGFb_CS

The PANTHER Classification System

More...PANTHERi		PTHR11848, PTHR11848, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00019, TGF_beta, 1 hit
PF00688, TGFb_propeptide, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001787, TGF-beta, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01423, TGFBETA
PR01424, TGFBETA1

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00204, TGFB, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57501, SSF57501, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00250, TGF_BETA_1, 1 hit
PS51362, TGF_BETA_2, 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P01137-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPPSGLRLLL LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR 
        60         70         80         90        100
GQILSKLRLA SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE 
       110        120        130        140        150
ADYYAKEVTR VLMVETHNEI YDKFKQSTHS IYMFFNTSEL REAVPEPVLL 
       160        170        180        190        200
SRAELRLLRL KLKVEQHVEL YQKYSNNSWR YLSNRLLAPS DSPEWLSFDV 
       210        220        230        240        250
TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT TGRRGDLATI 
       260        270        280        290        300
HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI 
       310        320        330        340        350
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA 
       360        370        380        390
SAAPCCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS
Length:390
Mass (Da):44,341
Last modified:February 1, 1991 - 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:i75391614250288FE
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A499FJK2A0A499FJK2_HUMAN
Transforming growth factor beta
TGFB1
390Annotation 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>
M0R2S0M0R2S0_HUMAN
Transforming growth factor beta-1 p...
TGFB1
120Annotation 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>

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 conflicti159R → RR in CAA26580 (PubMed:3861940).Curated1

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

In post-menopausal Japanese women, the frequency of Leu-10 is higher in subjects with osteoporosis than in controls.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01617110L → P Associated with higher bone mineral density and lower frequency of vertebral fractures in Japanese post-menopausal women. 3 PublicationsCorresponds to variant dbSNP:rs1800470Ensembl.1
Natural variantiVAR_01617225R → P1 PublicationCorresponds to variant dbSNP:rs1800471EnsemblClinVar.1
Natural variantiVAR_08158445R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication1
Natural variantiVAR_01760781Y → H in CAEND; leads to TGF-beta-1 intracellular accumulation. 2 Publications1
Natural variantiVAR_081585110R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication1
Natural variantiVAR_017608218R → C in CAEND; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. 4 Publications1
Natural variantiVAR_017609218R → H in CAEND. 1 Publication1
Natural variantiVAR_017610222H → D in CAEND; sporadic case; higher levels of active TGF-beta-1 in the culture medium. 1 Publication1
Natural variantiVAR_067303223C → G in CAEND. 1 Publication1
Natural variantiVAR_067304223C → R in CAEND. 1 Publication1
Natural variantiVAR_017611225C → R in CAEND; higher levels of active TGF-beta-1 in the culture medium. 3 Publications1
Natural variantiVAR_016173263T → I. Corresponds to variant dbSNP:rs1800472EnsemblClinVar.1
Natural variantiVAR_081586387C → R in IBDIMDE; loss of TGFB1-mediated activation of SMAD signaling; mutant TGFB1 is not secreted. 1 Publication1

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
X05839 X05850 Genomic DNA Translation: CAA29283.1
X02812 mRNA Translation: CAA26580.1
BT007245 mRNA Translation: AAP35909.1
AK291907 mRNA Translation: BAF84596.1
CH471126 Genomic DNA Translation: EAW57032.1
BC001180 mRNA Translation: AAH01180.1
BC000125 mRNA Translation: AAH00125.1
BC022242 mRNA Translation: AAH22242.1
M38449 mRNA Translation: AAA36735.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33031.1

Protein sequence database of the Protein Information Resource

More...PIRi		A27513, WFHU2

NCBI Reference Sequences

More...RefSeqi		NP_000651.3, NM_000660.6

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7040

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7040

UCSC genome browser

More...UCSCi		uc002oqh.4, human

Keywords - Coding sequence diversityi

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

Wikipedia

TGF beta-1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05839 X05850 Genomic DNA Translation: CAA29283.1
X02812 mRNA Translation: CAA26580.1
BT007245 mRNA Translation: AAP35909.1
AK291907 mRNA Translation: BAF84596.1
CH471126 Genomic DNA Translation: EAW57032.1
BC001180 mRNA Translation: AAH01180.1
BC000125 mRNA Translation: AAH00125.1
BC022242 mRNA Translation: AAH22242.1
M38449 mRNA Translation: AAA36735.1
CCDSiCCDS33031.1
PIRiA27513, WFHU2
RefSeqiNP_000651.3, NM_000660.6

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
1KLANMR-A/B279-390[»]
1KLCNMR-A/B279-390[»]
1KLDNMR-A/B279-390[»]
3KFDX-ray3.00A/B/C/D279-390[»]
4KV5X-ray3.00A/B/C/D279-390[»]
5FFOX-ray3.49C/D/G/H34-390[»]
5VQPX-ray2.90A30-390[»]
6OM2X-ray2.77E/F242-252[»]
6P7JX-ray3.50A30-278[»]
SASBDBiP01137
SMRiP01137
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi112898, 247 interactors
ComplexPortaliCPX-529, TGF-beta-1-TGFR complex
CPX-602, TGF-beta-1 complex
CORUMiP01137
DIPiDIP-5934N
IntActiP01137, 95 interactors
MINTiP01137
STRINGi9606.ENSP00000221930

Chemistry databases

BindingDBiP01137
ChEMBLiCHEMBL1795178
DrugBankiDB10770, Foreskin fibroblast (neonatal)
DB10772, Foreskin keratinocyte (neonatal)
DB00070, Hyaluronidase (ovine)
DB01162, Terazosin
DB06205, Vorhyaluronidase alfa

PTM databases

GlyConnecti1835, 1 N-Linked glycan (1 site)
GlyGeniP01137, 3 sites
iPTMnetiP01137
PhosphoSitePlusiP01137

Polymorphism and mutation databases

BioMutaiTGFB1
DMDMi135674

2D gel databases

OGPiP01137

Proteomic databases

EPDiP01137
jPOSTiP01137
MassIVEiP01137
MaxQBiP01137
PaxDbiP01137
PeptideAtlasiP01137
PRIDEiP01137
ProteomicsDBi51337

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P01137, 5 sequenced antibodies

The DNASU plasmid repository

More...DNASUi		7040

Genome annotation databases

GeneIDi7040
KEGGihsa:7040
UCSCiuc002oqh.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7040
DisGeNETi7040
EuPathDBiHostDB:ENSG00000105329.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		TGFB1
GeneReviewsiTGFB1
HGNCiHGNC:11766, TGFB1
HPAiENSG00000105329, Low tissue specificity
MalaCardsiTGFB1
MIMi131300, phenotype
190180, gene
618213, phenotype
neXtProtiNX_P01137
Orphaneti1328, Camurati-Engelmann disease
586, Cystic fibrosis
565788, Infantile inflammatory bowel disease with neurological involvement
PharmGKBiPA350

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3900, Eukaryota
HOGENOMiCLU_039840_0_0_1
InParanoidiP01137
KOiK13375
OrthoDBi853728at2759
PhylomeDBiP01137
TreeFamiTF318514

Enzyme and pathway databases

PathwayCommonsiP01137
ReactomeiR-HSA-114608, Platelet degranulation
R-HSA-168277, Influenza Virus Induced Apoptosis
R-HSA-202733, Cell surface interactions at the vascular wall
R-HSA-2129379, Molecules associated with elastic fibres
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-3000170, Syndecan interactions
R-HSA-3000178, ECM proteoglycans
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-381340, Transcriptional regulation of white adipocyte differentiation
R-HSA-5689603, UCH proteinases
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
R-HSA-8941855, RUNX3 regulates CDKN1A transcription
R-HSA-8941858, Regulation of RUNX3 expression and activity
R-HSA-8951936, RUNX3 regulates p14-ARF
SignaLinkiP01137
SIGNORiP01137

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		7040, 2 hits in 879 CRISPR screens

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

More...ChiTaRSi		TGFB1, human
EvolutionaryTraceiP01137

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TGF_beta_1

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

More...GenomeRNAii		7040
PharosiP01137, Tchem

Protein Ontology

More...PROi		PR:P01137
RNActiP01137, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000105329, Expressed in granulocyte and 181 other tissues
GenevisibleiP01137, HS

Family and domain databases

DisProtiDP01252
Gene3Di2.10.90.10, 1 hit
IDEALiIID00534
InterProiView protein in InterPro
IPR029034, Cystine-knot_cytokine
IPR001839, TGF-b_C
IPR001111, TGF-b_propeptide
IPR016319, TGF-beta
IPR015615, TGF-beta-rel
IPR003939, TGFb1
IPR017948, TGFb_CS
PANTHERiPTHR11848, PTHR11848, 1 hit
PfamiView protein in Pfam
PF00019, TGF_beta, 1 hit
PF00688, TGFb_propeptide, 1 hit
PIRSFiPIRSF001787, TGF-beta, 1 hit
PRINTSiPR01423, TGFBETA
PR01424, TGFBETA1
SMARTiView protein in SMART
SM00204, TGFB, 1 hit
SUPFAMiSSF57501, SSF57501, 1 hit
PROSITEiView protein in PROSITE
PS00250, TGF_BETA_1, 1 hit
PS51362, TGF_BETA_2, 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 nameiTGFB1_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: P01137
Secondary accession number(s): A8K792, Q9UCG4
<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: July 21, 1986
Last sequence update: February 1, 1991
Last modified: October 7, 2020
This is version 256 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again