UniProtKB - P01137 (TGFB1_HUMAN)
Transforming growth factor beta-1 proprotein
TGFB1
Functioni
Miscellaneous
GO - Molecular functioni
- antigen binding Source: UniProtKB
- cytokine activity Source: GO_Central
- enzyme binding Source: BHF-UCL
- growth factor activity Source: UniProtKB-KW
- identical protein binding Source: IntAct
- type III transforming growth factor beta receptor binding Source: AgBase
- type II transforming growth factor beta receptor binding Source: BHF-UCL
- type I transforming growth factor beta receptor binding Source: AgBase
GO - Biological processi
- aortic valve morphogenesis Source: BHF-UCL
- ATP biosynthetic process Source: BHF-UCL
- BMP signaling pathway Source: GO_Central
- cell-cell junction organization Source: BHF-UCL
- cell cycle arrest Source: BHF-UCL
- cell migration Source: UniProtKB
- cellular response to organic cyclic compound Source: UniProtKB
- cellular response to transforming growth factor beta stimulus Source: BHF-UCL
- chondrocyte differentiation Source: UniProtKB
- common-partner SMAD protein phosphorylation Source: UniProtKB
- connective tissue replacement involved in inflammatory response wound healing Source: BHF-UCL
- cytokine-mediated signaling pathway Source: Reactome
- embryonic liver development Source: BHF-UCL
- epidermal growth factor receptor signaling pathway Source: BHF-UCL
- epithelial to mesenchymal transition Source: UniProtKB
- extracellular matrix assembly Source: BHF-UCL
- extrinsic apoptotic signaling pathway Source: BHF-UCL
- heart development Source: BHF-UCL
- heart valve morphogenesis Source: BHF-UCL
- hematopoietic progenitor cell differentiation Source: UniProtKB
- hyaluronan catabolic process Source: UniProtKB
- inflammatory response Source: UniProtKB
- leukocyte migration Source: Reactome
- lipopolysaccharide-mediated signaling pathway Source: UniProtKB
- lymph node development Source: UniProtKB
- macrophage derived foam cell differentiation Source: BHF-UCL
- MAPK cascade Source: UniProtKB
- membrane protein intracellular domain proteolysis Source: UniProtKB
- mitotic cell cycle checkpoint Source: BHF-UCL
- negative regulation of biomineral tissue development Source: BHF-UCL
- negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
- negative regulation of cell-cell adhesion Source: BHF-UCL
- negative regulation of cell cycle Source: HGNC-UCL
- negative regulation of cell differentiation Source: CACAO
- negative regulation of cell growth Source: BHF-UCL
- negative regulation of cell population proliferation Source: BHF-UCL
- negative regulation of cytolysis Source: ARUK-UCL
- negative regulation of epithelial cell proliferation Source: BHF-UCL
- negative regulation of extracellular matrix disassembly Source: BHF-UCL
- negative regulation of fat cell differentiation Source: UniProtKB
- negative regulation of gene expression Source: BHF-UCL
- negative regulation of gene silencing by miRNA Source: BHF-UCL
- negative regulation of hyaluronan biosynthetic process Source: UniProtKB
- negative regulation of macrophage cytokine production Source: DFLAT
- negative regulation of mitotic cell cycle Source: BHF-UCL
- negative regulation of myoblast differentiation Source: UniProtKB
- negative regulation of pri-miRNA transcription by RNA polymerase II Source: BHF-UCL
- negative regulation of production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
- negative regulation of protein localization to plasma membrane Source: UniProtKB
- negative regulation of protein phosphorylation Source: BHF-UCL
- negative regulation of skeletal muscle tissue development Source: UniProtKB
- negative regulation of transcription, DNA-templated Source: UniProtKB
- negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
- neural tube closure Source: BHF-UCL
- neural tube development Source: BHF-UCL
- ossification involved in bone remodeling Source: BHF-UCL
- pathway-restricted SMAD protein phosphorylation Source: UniProtKB
- phosphate-containing compound metabolic process Source: BHF-UCL
- platelet degranulation Source: Reactome
- positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
- positive regulation of bone mineralization Source: BHF-UCL
- positive regulation of canonical Wnt signaling pathway Source: CACAO
- positive regulation of cardiac muscle cell differentiation Source: BHF-UCL
- positive regulation of cell division Source: UniProtKB-KW
- positive regulation of cell migration Source: BHF-UCL
- positive regulation of cell population proliferation Source: BHF-UCL
- positive regulation of cellular protein metabolic process Source: BHF-UCL
- positive regulation of chemotaxis Source: BHF-UCL
- positive regulation of collagen biosynthetic process Source: UniProtKB
- positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
- positive regulation of extracellular matrix assembly Source: BHF-UCL
- positive regulation of fibroblast migration Source: BHF-UCL
- positive regulation of gene expression Source: UniProtKB
- positive regulation of interleukin-17 production Source: BHF-UCL
- positive regulation of isotype switching to IgA isotypes Source: MGI
- positive regulation of MAP kinase activity Source: BHF-UCL
- positive regulation of microglia differentiation Source: UniProtKB
- positive regulation of NAD+ ADP-ribosyltransferase activity Source: BHF-UCL
- positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
- positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
- positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
- positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
- positive regulation of phosphatidylinositol 3-kinase activity Source: BHF-UCL
- positive regulation of pri-miRNA transcription by RNA polymerase II Source: BHF-UCL
- positive regulation of production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
- positive regulation of protein-containing complex assembly Source: BHF-UCL
- positive regulation of protein dephosphorylation Source: BHF-UCL
- positive regulation of protein import into nucleus Source: BHF-UCL
- positive regulation of protein kinase B signaling Source: BHF-UCL
- positive regulation of protein localization to nucleus Source: BHF-UCL
- positive regulation of protein phosphorylation Source: BHF-UCL
- positive regulation of protein secretion Source: BHF-UCL
- positive regulation of SMAD protein signal transduction Source: BHF-UCL
- positive regulation of superoxide anion generation Source: BHF-UCL
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- positive regulation of transcription regulatory region DNA binding Source: BHF-UCL
- positive regulation of vascular endothelial growth factor production Source: BHF-UCL
- positive regulation of vascular permeability Source: UniProtKB
- protein export from nucleus Source: UniProtKB
- protein kinase B signaling Source: UniProtKB
- protein phosphorylation Source: UniProtKB
- receptor catabolic process Source: BHF-UCL
- regulation of binding Source: UniProtKB
- regulation of blood vessel remodeling Source: BHF-UCL
- regulation of cell migration Source: BHF-UCL
- regulation of cell population proliferation Source: GO_Central
- regulation of DNA binding Source: UniProtKB
- regulation of protein import into nucleus Source: UniProtKB
- regulation of SMAD protein signal transduction Source: UniProtKB
- regulation of striated muscle tissue development Source: UniProtKB
- regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
- response to cholesterol Source: BHF-UCL
- response to estradiol Source: BHF-UCL
- response to progesterone Source: BHF-UCL
- response to wounding Source: BHF-UCL
- salivary gland morphogenesis Source: BHF-UCL
- SMAD protein complex assembly Source: BHF-UCL
- SMAD protein signal transduction Source: GO_Central
- transforming growth factor beta receptor signaling pathway Source: BHF-UCL
- transforming growth factor beta receptor signaling pathway involved in heart development Source: BHF-UCL
- vasculogenesis Source: BHF-UCL
- ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
Keywordsi
Molecular function | Growth factor, Mitogen |
Enzyme and pathway databases
PathwayCommonsi | P01137 |
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 |
SignaLinki | P01137 |
SIGNORi | P01137 |
Names & Taxonomyi
Protein namesi | Recommended name: Transforming growth factor beta-1 proproteinCleaved into the following 2 chains: |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000105329.9 |
HGNCi | HGNC:11766, TGFB1 |
MIMi | 190180, gene |
neXtProti | NX_P01137 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix 1 Publication
Extracellular region or secreted
- Secreted 2 Publications
Extracellular region or secreted
- blood microparticle Source: UniProtKB
- collagen-containing extracellular matrix Source: BHF-UCL
- extracellular matrix Source: UniProtKB
- extracellular region Source: Reactome
- extracellular space Source: BHF-UCL
Golgi apparatus
- Golgi lumen Source: Reactome
Nucleus
- nucleus Source: BHF-UCL
Plasma Membrane
- plasma membrane Source: Reactome
Other locations
- cell surface Source: BHF-UCL
- cytoplasm Source: BHF-UCL
- platelet alpha granule lumen Source: Reactome
Keywords - Cellular componenti
Extracellular matrix, SecretedPathology & Biotechi
Involvement in diseasei
Camurati-Engelmann disease (CAEND)5 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_017607 | 81 | Y → H in CAEND; leads to TGF-beta-1 intracellular accumulation. 2 Publications | 1 | |
Natural variantiVAR_017608 | 218 | R → C in CAEND; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. 4 Publications | 1 | |
Natural variantiVAR_017609 | 218 | R → H in CAEND. 1 Publication | 1 | |
Natural variantiVAR_017610 | 222 | H → D in CAEND; sporadic case; higher levels of active TGF-beta-1 in the culture medium. 1 Publication | 1 | |
Natural variantiVAR_067303 | 223 | C → G in CAEND. 1 Publication | 1 | |
Natural variantiVAR_067304 | 223 | C → R in CAEND. 1 Publication | 1 | |
Natural variantiVAR_017611 | 225 | C → R in CAEND; higher levels of active TGF-beta-1 in the culture medium. 3 Publications | 1 |
Inflammatory bowel disease, immunodeficiency, and encephalopathy (IBDIMDE)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081584 | 45 | R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication | 1 | |
Natural variantiVAR_081585 | 110 | R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication | 1 | |
Natural variantiVAR_081586 | 387 | C → R in IBDIMDE; loss of TGFB1-mediated activation of SMAD signaling; mutant TGFB1 is not secreted. 1 Publication | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 33 | C → S: Abolishes interchain disulfide bond with LTBP1 and/or LRRC32, and subsequent regulation of activation of TGF-beta-1. 2 Publications | 1 | |
Mutagenesisi | 75 | E → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication | 1 | |
Mutagenesisi | 158 | L → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication | 1 | |
Mutagenesisi | 160 | L → A or R: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication | 1 | |
Mutagenesisi | 193 | P → A or R: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication | 1 | |
Mutagenesisi | 232 – 236 | LQVDI → GQGDG: Strongly inhibits integrin-binding and activation of TGF-beta-1. 1 Publication | 5 | |
Mutagenesisi | 234 – 236 | VDI → GDG: Strongly inhibits integrin-binding and activation of TGF-beta-1. 1 Publication | 3 | |
Mutagenesisi | 237 | N → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication | 1 | |
Mutagenesisi | 254 | N → A: Does not affect integrin-binding or activation of TGF-beta-1. 1 Publication | 1 | |
Mutagenesisi | 257 – 260 | FLLL → GLLG: Strongly inhibits integrin-binding and activation of TGF-beta-1. 1 Publication | 4 | |
Mutagenesisi | 278 | R → 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 Publication | 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNETi | 7040 |
GeneReviewsi | TGFB1 |
MalaCardsi | TGFB1 |
MIMi | 131300, phenotype 618213, phenotype |
Orphaneti | 1328, Camurati-Engelmann disease 586, Cystic fibrosis 565788, Infantile inflammatory bowel disease with neurological involvement |
PharmGKBi | PA350 |
Miscellaneous databases
Pharosi | P01137, Tchem |
Chemistry databases
ChEMBLi | CHEMBL1795178 |
DrugBanki | DB10770, Foreskin fibroblast (neonatal) DB10772, Foreskin keratinocyte (neonatal) DB14740, Hyaluronidase DB06205, Hyaluronidase (human recombinant) DB00070, Hyaluronidase (ovine) DB01162, Terazosin |
Polymorphism and mutation databases
BioMutai | TGFB1 |
DMDMi | 135674 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 29 | 1 PublicationAdd BLAST | 29 | |
ChainiPRO_0000033762 | 30 – 278 | Latency-associated peptide4 PublicationsAdd BLAST | 249 | |
ChainiPRO_0000033763 | 279 – 390 | Transforming growth factor beta-14 PublicationsAdd BLAST | 112 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 33 | Interchain (with C-1359 or C-1384 in LTBP1); in inactive form1 Publication | ||
Glycosylationi | 82 | N-linked (GlcNAc...) asparagineCombined sources3 Publications | 1 | |
Glycosylationi | 136 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 176 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 223 | Interchain (with C-225)Combined sources2 Publications | ||
Disulfide bondi | 225 | Interchain (with C-223)Combined sources2 Publications | ||
Disulfide bondi | 285 ↔ 294 | Combined sources4 Publications | ||
Disulfide bondi | 293 ↔ 356 | Combined sources4 Publications | ||
Disulfide bondi | 322 ↔ 387 | Combined sources4 Publications | ||
Disulfide bondi | 326 ↔ 389 | Combined sources4 Publications | ||
Disulfide bondi | 355 | InterchainCombined sources3 Publications |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 278 – 279 | Cleavage; by FURIN1 Publication | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, GlycoproteinProteomic databases
EPDi | P01137 |
jPOSTi | P01137 |
MassIVEi | P01137 |
MaxQBi | P01137 |
PaxDbi | P01137 |
PeptideAtlasi | P01137 |
PRIDEi | P01137 |
ProteomicsDBi | 51337 |
2D gel databases
OGPi | P01137 |
PTM databases
GlyConnecti | 1835, 1 N-Linked glycan (1 site) |
GlyGeni | P01137, 3 sites |
iPTMneti | P01137 |
PhosphoSitePlusi | P01137 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000105329, Expressed in granulocyte and 181 other tissues |
Genevisiblei | P01137, HS |
Organism-specific databases
HPAi | ENSG00000105329, Low tissue specificity |
Interactioni
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 PublicationsBinary interactionsi
Hide detailsP01137
Latency-associated peptide (PRO_0000033762)
With | #Exp. | IntAct |
---|---|---|
PSG1 [P11464] | 2 | EBI-15487336,EBI-716740 |
GO - Molecular functioni
- cytokine activity Source: GO_Central
- enzyme binding Source: BHF-UCL
- growth factor activity Source: UniProtKB-KW
- identical protein binding Source: IntAct
- type III transforming growth factor beta receptor binding Source: AgBase
- type II transforming growth factor beta receptor binding Source: BHF-UCL
- type I transforming growth factor beta receptor binding Source: AgBase
Protein-protein interaction databases
BioGRIDi | 112898, 249 interactors |
ComplexPortali | CPX-529, TGF-beta-1-TGFR complex CPX-602, TGF-beta-1 complex |
CORUMi | P01137 |
DIPi | DIP-5934N |
IntActi | P01137, 95 interactors |
MINTi | P01137 |
STRINGi | 9606.ENSP00000221930 |
Chemistry databases
BindingDBi | P01137 |
Miscellaneous databases
RNActi | P01137, protein |
Structurei
Secondary structure
3D structure databases
SASBDBi | P01137 |
SMRi | P01137 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P01137 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 30 – 74 | Straightjacket domainBy similarityAdd BLAST | 45 | |
Regioni | 75 – 271 | Arm domainBy similarityAdd BLAST | 197 | |
Regioni | 226 – 252 | Bowtie tail1 PublicationAdd BLAST | 27 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 244 – 246 | Cell attachment site1 Publication | 3 |
Domaini
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG3900, Eukaryota |
HOGENOMi | CLU_039840_0_0_1 |
InParanoidi | P01137 |
OrthoDBi | 853728at2759 |
PhylomeDBi | P01137 |
TreeFami | TF318514 |
Family and domain databases
DisProti | DP01252 |
Gene3Di | 2.10.90.10, 1 hit |
IDEALi | IID00534 |
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 |
PANTHERi | PTHR11848, PTHR11848, 1 hit |
Pfami | View protein in Pfam PF00019, TGF_beta, 1 hit PF00688, TGFb_propeptide, 1 hit |
PIRSFi | PIRSF001787, TGF-beta, 1 hit |
PRINTSi | PR01423, TGFBETA PR01424, TGFBETA1 |
SMARTi | View protein in SMART SM00204, TGFB, 1 hit |
SUPFAMi | SSF57501, SSF57501, 1 hit |
PROSITEi | View protein in PROSITE PS00250, TGF_BETA_1, 1 hit PS51362, TGF_BETA_2, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A499FJK2 | A0A499FJK2_HUMAN | Transforming growth factor beta | TGFB1 | 390 | Annotation score: | ||
M0R2S0 | M0R2S0_HUMAN | Transforming growth factor beta-1 p... | TGFB1 | 120 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 159 | R → RR in CAA26580 (PubMed:3861940).Curated | 1 |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_016171 | 10 | L → 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_016172 | 25 | R → P1 PublicationCorresponds to variant dbSNP:rs1800471EnsemblClinVar. | 1 | |
Natural variantiVAR_081584 | 45 | R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication | 1 | |
Natural variantiVAR_017607 | 81 | Y → H in CAEND; leads to TGF-beta-1 intracellular accumulation. 2 Publications | 1 | |
Natural variantiVAR_081585 | 110 | R → C in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreated TGFB1. 1 Publication | 1 | |
Natural variantiVAR_017608 | 218 | R → C in CAEND; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. 4 Publications | 1 | |
Natural variantiVAR_017609 | 218 | R → H in CAEND. 1 Publication | 1 | |
Natural variantiVAR_017610 | 222 | H → D in CAEND; sporadic case; higher levels of active TGF-beta-1 in the culture medium. 1 Publication | 1 | |
Natural variantiVAR_067303 | 223 | C → G in CAEND. 1 Publication | 1 | |
Natural variantiVAR_067304 | 223 | C → R in CAEND. 1 Publication | 1 | |
Natural variantiVAR_017611 | 225 | C → R in CAEND; higher levels of active TGF-beta-1 in the culture medium. 3 Publications | 1 | |
Natural variantiVAR_016173 | 263 | T → I. Corresponds to variant dbSNP:rs1800472EnsemblClinVar. | 1 | |
Natural variantiVAR_081586 | 387 | C → R in IBDIMDE; loss of TGFB1-mediated activation of SMAD signaling; mutant TGFB1 is not secreted. 1 Publication | 1 |
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 |
CCDSi | CCDS33031.1 |
PIRi | A27513, WFHU2 |
RefSeqi | NP_000651.3, NM_000660.6 |
Genome annotation databases
GeneIDi | 7040 |
KEGGi | hsa:7040 |
UCSCi | uc002oqh.4, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
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 |
CCDSi | CCDS33031.1 |
PIRi | A27513, WFHU2 |
RefSeqi | NP_000651.3, NM_000660.6 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KLA | NMR | - | A/B | 279-390 | [»] | |
1KLC | NMR | - | A/B | 279-390 | [»] | |
1KLD | NMR | - | A/B | 279-390 | [»] | |
3KFD | X-ray | 3.00 | A/B/C/D | 279-390 | [»] | |
4KV5 | X-ray | 3.00 | A/B/C/D | 279-390 | [»] | |
5FFO | X-ray | 3.49 | C/D/G/H | 34-390 | [»] | |
5VQP | X-ray | 2.90 | A | 30-390 | [»] | |
6OM2 | X-ray | 2.77 | E/F | 242-252 | [»] | |
6P7J | X-ray | 3.50 | A | 30-278 | [»] | |
SASBDBi | P01137 | |||||
SMRi | P01137 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 112898, 249 interactors |
ComplexPortali | CPX-529, TGF-beta-1-TGFR complex CPX-602, TGF-beta-1 complex |
CORUMi | P01137 |
DIPi | DIP-5934N |
IntActi | P01137, 95 interactors |
MINTi | P01137 |
STRINGi | 9606.ENSP00000221930 |
Chemistry databases
BindingDBi | P01137 |
ChEMBLi | CHEMBL1795178 |
DrugBanki | DB10770, Foreskin fibroblast (neonatal) DB10772, Foreskin keratinocyte (neonatal) DB14740, Hyaluronidase DB06205, Hyaluronidase (human recombinant) DB00070, Hyaluronidase (ovine) DB01162, Terazosin |
PTM databases
GlyConnecti | 1835, 1 N-Linked glycan (1 site) |
GlyGeni | P01137, 3 sites |
iPTMneti | P01137 |
PhosphoSitePlusi | P01137 |
Polymorphism and mutation databases
BioMutai | TGFB1 |
DMDMi | 135674 |
2D gel databases
OGPi | P01137 |
Proteomic databases
EPDi | P01137 |
jPOSTi | P01137 |
MassIVEi | P01137 |
MaxQBi | P01137 |
PaxDbi | P01137 |
PeptideAtlasi | P01137 |
PRIDEi | P01137 |
ProteomicsDBi | 51337 |
Protocols and materials databases
ABCDi | P01137, 10 sequenced antibodies |
DNASUi | 7040 |
Genome annotation databases
GeneIDi | 7040 |
KEGGi | hsa:7040 |
UCSCi | uc002oqh.4, human |
Organism-specific databases
CTDi | 7040 |
DisGeNETi | 7040 |
EuPathDBi | HostDB:ENSG00000105329.9 |
GeneCardsi | TGFB1 |
GeneReviewsi | TGFB1 |
HGNCi | HGNC:11766, TGFB1 |
HPAi | ENSG00000105329, Low tissue specificity |
MalaCardsi | TGFB1 |
MIMi | 131300, phenotype 190180, gene 618213, phenotype |
neXtProti | NX_P01137 |
Orphaneti | 1328, Camurati-Engelmann disease 586, Cystic fibrosis 565788, Infantile inflammatory bowel disease with neurological involvement |
PharmGKBi | PA350 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3900, Eukaryota |
HOGENOMi | CLU_039840_0_0_1 |
InParanoidi | P01137 |
OrthoDBi | 853728at2759 |
PhylomeDBi | P01137 |
TreeFami | TF318514 |
Enzyme and pathway databases
PathwayCommonsi | P01137 |
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 |
SignaLinki | P01137 |
SIGNORi | P01137 |
Miscellaneous databases
BioGRID-ORCSi | 7040, 2 hits in 850 CRISPR screens |
ChiTaRSi | TGFB1, human |
EvolutionaryTracei | P01137 |
GeneWikii | TGF_beta_1 |
GenomeRNAii | 7040 |
Pharosi | P01137, Tchem |
PROi | PR:P01137 |
RNActi | P01137, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000105329, Expressed in granulocyte and 181 other tissues |
Genevisiblei | P01137, HS |
Family and domain databases
DisProti | DP01252 |
Gene3Di | 2.10.90.10, 1 hit |
IDEALi | IID00534 |
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 |
PANTHERi | PTHR11848, PTHR11848, 1 hit |
Pfami | View protein in Pfam PF00019, TGF_beta, 1 hit PF00688, TGFb_propeptide, 1 hit |
PIRSFi | PIRSF001787, TGF-beta, 1 hit |
PRINTSi | PR01423, TGFBETA PR01424, TGFBETA1 |
SMARTi | View protein in SMART SM00204, TGFB, 1 hit |
SUPFAMi | SSF57501, SSF57501, 1 hit |
PROSITEi | View protein in PROSITE PS00250, TGF_BETA_1, 1 hit PS51362, TGF_BETA_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TGFB1_HUMAN | |
Accessioni | P01137Primary (citable) accession number: P01137 Secondary accession number(s): A8K792, Q9UCG4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | February 1, 1991 | |
Last modified: | December 2, 2020 | |
This is version 257 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations