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Protein

Transforming growth factor beta-1 proprotein

Gene

TGFB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGrowth factor, Mitogen

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

Names & Taxonomyi

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
Gene namesi
Name:TGFB1Imported
Synonyms:TGFB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105329.9
HGNCiHGNC:11766 TGFB1
MIMi190180 gene
neXtProtiNX_P01137

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

Pathology & Biotechi

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
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
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

DisGeNETi7040
GeneReviewsiTGFB1
MalaCardsiTGFB1
MIMi131300 phenotype
Orphaneti1328 Camurati-Engelmann disease
586 Cystic fibrosis
PharmGKBiPA350

Chemistry databases

ChEMBLiCHEMBL1795178
DrugBankiDB00070 Hyaluronidase
DB06205 Hyaluronidase (Human Recombinant)

Polymorphism and mutation databases

BioMutaiTGFB1
DMDMi135674

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000003376230 – 278Latency-associated peptide4 PublicationsAdd BLAST249
ChainiPRO_0000033763279 – 390Transforming growth factor beta-14 PublicationsAdd BLAST112

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33Interchain (with C-1359 or C-1384 in LTBP1); in inactive form1 Publication
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

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
Sitei278 – 279Cleavage; by FURIN1 Publication2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

EPDiP01137
MaxQBiP01137
PaxDbiP01137
PeptideAtlasiP01137
PRIDEiP01137
ProteomicsDBi51337

2D gel databases

OGPiP01137

PTM databases

GlyConnecti1835
iPTMnetiP01137
PhosphoSitePlusiP01137

Expressioni

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

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

Organism-specific databases

HPAiCAB000361
CAB073543

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 Publications

Binary interactionsi

GO - Molecular functioni

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

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP01137
SMRiP01137
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01137

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 74Straightjacket domainBy similarityAdd BLAST45
Regioni75 – 271Arm domainBy similarityAdd BLAST197
Regioni226 – 252Bowtie tail1 PublicationAdd BLAST27

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi244 – 246Cell attachment site1 Publication3

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

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3900 Eukaryota
ENOG410XT8Z LUCA
HOGENOMiHOG000290198
HOVERGENiHBG074115
InParanoidiP01137
KOiK13375
OrthoDBiEOG091G0BMM
PhylomeDBiP01137
TreeFamiTF318514

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

Sequence (1+)i

Sequence statusi: Complete.

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
Checksum:i75391614250288FE
GO

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:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti159R → RR in CAA26580 (PubMed:3861940).Curated1

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:
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

Genome annotation databases

EnsembliENST00000221930; ENSP00000221930; ENSG00000105329
GeneIDi7040
KEGGihsa:7040
UCSCiuc002oqh.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar 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
CCDSiCCDS33031.1
PIRiA27513 WFHU2
RefSeqiNP_000651.3, NM_000660.6
UniGeneiHs.645227

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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

DNASUi7040
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221930; ENSP00000221930; ENSG00000105329
GeneIDi7040
KEGGihsa:7040
UCSCiuc002oqh.4 human

Organism-specific databases

CTDi7040
DisGeNETi7040
EuPathDBiHostDB:ENSG00000105329.9
GeneCardsiTGFB1
GeneReviewsiTGFB1
H-InvDBiHIX0015152
HGNCiHGNC:11766 TGFB1
HPAiCAB000361
CAB073543
MalaCardsiTGFB1
MIMi131300 phenotype
190180 gene
neXtProtiNX_P01137
Orphaneti1328 Camurati-Engelmann disease
586 Cystic fibrosis
PharmGKBiPA350
GenAtlasiSearch...

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

ChiTaRSiTGFB1 human
EvolutionaryTraceiP01137
GeneWikiiTGF_beta_1
GenomeRNAii7040
PROiPR:P01137
SOURCEiSearch...

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
ProtoNetiSearch...

Entry informationi

Entry nameiTGFB1_HUMAN
AccessioniPrimary (citable) accession number: P01137
Secondary accession number(s): A8K792, Q9UCG4
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.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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