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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
Latency-associated peptide: 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). Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (PubMed:25893292).By similarity11 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

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 functionGrowth factor, Mitogen

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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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-3315487 SMAD2/3 MH2 Domain 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

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SignaLinki
P01137

SIGNOR Signaling Network Open Resource

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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_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:
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_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:TGFB1Imported
Synonyms:TGFB
<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 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000105329.9

Human Gene Nomenclature Database

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HGNCi
HGNC:11766 TGFB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
190180 gene

neXtProt; the human protein knowledge platform

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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; 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.
See also OMIM:131300
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

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>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

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DisGeNETi
7040

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

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GeneReviewsi
TGFB1

MalaCards human disease database

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MalaCardsi
TGFB1
MIMi131300 phenotype

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

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Orphaneti
1328 Camurati-Engelmann disease
586 Cystic fibrosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA350

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1795178

Drug and drug target database

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DrugBanki
DB00070 Hyaluronidase
DB06205 Hyaluronidase (Human Recombinant)

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TGFB1

Domain mapping of disease mutations (DMDM)

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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.<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_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>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_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

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
Latency-associated peptide: 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

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EPDi
P01137

MaxQB - The MaxQuant DataBase

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MaxQBi
P01137

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

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PaxDbi
P01137

PeptideAtlas

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PeptideAtlasi
P01137

PRoteomics IDEntifications database

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PRIDEi
P01137

ProteomicsDB human proteome resource

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ProteomicsDBi
51337

2D gel databases

USC-OGP 2-DE database

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OGPi
P01137

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1835

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P01137

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

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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

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Bgeei
ENSG00000105329 Expressed in 170 organ(s), highest expression level in leukocyte

CleanEx database of gene expression profiles

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CleanExi
HS_TGFB1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P01137 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P01137 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000361
CAB073543

<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; 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_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
112898, 70 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-529 TGF-beta-1-TGFR complex
CPX-602 TGF-beta-1 complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P01137

Database of interacting proteins

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DIPi
DIP-5934N

Protein interaction database and analysis system

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IntActi
P01137, 84 interactors

Molecular INTeraction database

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MINTi
P01137

STRING: functional protein association networks

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STRINGi
9606.ENSP00000221930

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P01137

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P01137

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

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SMRi
P01137

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
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

Latency-associated peptide: 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
Latency-associated peptide: 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
ENOG410XT8Z LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000290198

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG074115

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P01137

KEGG Orthology (KO)

More...
KOi
K13375

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0BMM

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P01137

TreeFam database of animal gene trees

More...
TreeFami
TF318514

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.10.90.10, 1 hit

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_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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is 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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
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_in_disease">'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_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
Natural variantiVAR_016173263T → I. Corresponds to variant dbSNP:rs1800472EnsemblClinVar.1

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
, X05840, X05843, X05844, X05849, 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

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.645227

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000221930; ENSP00000221930; ENSG00000105329

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_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

Wikipedia

TGF beta-1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05839
, X05840, X05843, X05844, X05849, 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
UniGeneiHs.645227

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[»]
ProteinModelPortaliP01137
SMRiP01137
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112898, 70 interactors
ComplexPortaliCPX-529 TGF-beta-1-TGFR complex
CPX-602 TGF-beta-1 complex
CORUMiP01137
DIPiDIP-5934N
IntActiP01137, 84 interactors
MINTiP01137
STRINGi9606.ENSP00000221930

Chemistry databases

BindingDBiP01137
ChEMBLiCHEMBL1795178
DrugBankiDB00070 Hyaluronidase
DB06205 Hyaluronidase (Human Recombinant)

PTM databases

GlyConnecti1835
iPTMnetiP01137
PhosphoSitePlusiP01137

Polymorphism and mutation databases

BioMutaiTGFB1
DMDMi135674

2D gel databases

OGPiP01137

Proteomic databases

EPDiP01137
MaxQBiP01137
PaxDbiP01137
PeptideAtlasiP01137
PRIDEiP01137
ProteomicsDBi51337

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7040
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221930; ENSP00000221930; ENSG00000105329
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

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0015152
HGNCiHGNC:11766 TGFB1
HPAiCAB000361
CAB073543
MalaCardsiTGFB1
MIMi131300 phenotype
190180 gene
neXtProtiNX_P01137
Orphaneti1328 Camurati-Engelmann disease
586 Cystic fibrosis
PharmGKBiPA350

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3900 Eukaryota
ENOG410XT8Z LUCA
HOGENOMiHOG000290198
HOVERGENiHBG074115
InParanoidiP01137
KOiK13375
OrthoDBiEOG091G0BMM
PhylomeDBiP01137
TreeFamiTF318514

Enzyme and pathway databases

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-3315487 SMAD2/3 MH2 Domain 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

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

Protein Ontology

More...
PROi
PR:P01137

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000105329 Expressed in 170 organ(s), highest expression level in leukocyte
CleanExiHS_TGFB1
ExpressionAtlasiP01137 baseline and differential
GenevisibleiP01137 HS

Family and domain databases

Gene3Di2.10.90.10, 1 hit
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...

<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_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: July 21, 1986
Last sequence update: February 1, 1991
Last modified: November 7, 2018
This is version 241 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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