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P04202 (TGFB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transforming growth factor beta-1

Short name=TGF-beta-1

Cleaved into the following chain:

  1. Latency-associated peptide
    Short name=LAP
Gene names
Name:Tgfb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Ref.9

Subunit structure

Homodimer; disulfide-linked, or heterodimer with TGFB2 By similarity. Secreted and stored as a biologically inactive form in the extracellular matrix in a 290 kDa complex (large latent TGF-beta1 complex) containing the TGFB1 homodimer, the latency-associated peptide (LAP), and the latent TGFB1 binding protein-1 (LTBP1). The complex without LTBP1 is known as the'small latent TGF-beta1 complex'. Dissociation of the TGFB1 from LAP is required for growth factor activation and biological activity. Release of the large latent TGF-beta1 complex from the extracellular matrix is carried out by the matrix metalloproteinase MMP3 By similarity. Interacts with CD109 and DPT. Interacts with ASPN By similarity. May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling. 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. Latency-associated peptide interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction. Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Domain

The 'straitjacket' and 'arm' domains encircle the growth factor monomers and are fastened together by strong bonding between Lys-56 and Tyr-103/Tyr-104. Activation of TGF-beta1 requires the binding of integrin alpha-V to an RGD sequence in the prodomain and exertion of force on this domain, which is held in the extracellular matrix by latent TGF-beta binding proteins. The sheer physical force unfastens the straitjacket and releases the active growth factor dimer By similarity.

Post-translational modification

Glycosylated By similarity.

The precursor is cleaved into mature TGF-beta-1 and LAP, which remains non-covalently linked to mature TGF-beta-1 rendering it inactive By similarity.

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   DomainSignal
   Molecular functionGrowth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

SMAD protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

SMAD protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

T cell activation

Inferred from direct assay PubMed 18997793. Source: MGI

T cell differentiation

Inferred from mutant phenotype PubMed 17481928. Source: MGI

T cell homeostasis

Inferred from mutant phenotype PubMed 17481928. Source: MGI

adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains

Inferred from direct assay PubMed 19501566. Source: BHF-UCL

aging

Inferred from electronic annotation. Source: Ensembl

branch elongation involved in mammary gland duct branching

Inferred from mutant phenotype PubMed 18614704. Source: MGI

cell activation

Inferred from direct assay PubMed 21956870. Source: MGI

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

cell death

Inferred from mutant phenotype PubMed 1436033PubMed 8421714. Source: MGI

cell growth

Inferred from electronic annotation. Source: InterPro

cell proliferation

Inferred from direct assay PubMed 12208849. Source: MGI

cell-cell junction organization

Inferred from sequence or structural similarity. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 12646629. Source: MGI

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from direct assay PubMed 7848824. Source: MGI

cellular response to organic cyclic compound

Inferred from sequence or structural similarity. Source: UniProtKB

chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

common-partner SMAD protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

defense response

Traceable author statement PubMed 8421714. Source: MGI

defense response to fungus, incompatible interaction

Inferred from electronic annotation. Source: Ensembl

digestive tract development

Inferred from electronic annotation. Source: Ensembl

embryo development

Inferred from electronic annotation. Source: Ensembl

endoderm development

Inferred from direct assay PubMed 9921650. Source: MGI

epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

evasion or tolerance of host defenses by virus

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix assembly

Inferred from direct assay PubMed 19734317. Source: BHF-UCL

extrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

face morphogenesis

Inferred from expression pattern PubMed 18498113. Source: UniProtKB

female pregnancy

Inferred from electronic annotation. Source: Ensembl

frontal suture morphogenesis

Inferred from electronic annotation. Source: Ensembl

germ cell migration

Inferred from direct assay PubMed 15993878. Source: MGI

hematopoietic progenitor cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluronan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from mutant phenotype PubMed 1436033PubMed 8421714. Source: MGI

inner ear development

Inferred from electronic annotation. Source: Ensembl

lens fiber cell differentiation

Inferred from mutant phenotype PubMed 17215516. Source: MGI

lipopolysaccharide-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

lymph node development

Inferred from mutant phenotype PubMed 1436033. Source: MGI

mammary gland branching involved in thelarche

Inferred from mutant phenotype PubMed 18614704. Source: MGI

mammary gland development

Inferred from direct assay PubMed 1821856. Source: MGI

mitotic cell cycle checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

mononuclear cell proliferation

Inferred from mutant phenotype PubMed 17481928. Source: MGI

myelination

Inferred from electronic annotation. Source: Ensembl

myeloid dendritic cell differentiation

Inferred from mutant phenotype PubMed 17938236. Source: MGI

negative regulation of DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of T cell activation

Inferred from mutant phenotype PubMed 12646629. Source: MGI

negative regulation of T cell proliferation

Inferred from mutant phenotype PubMed 17481928. Source: MGI

negative regulation of blood vessel endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay PubMed 12773577. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of hyaluronan biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of macrophage cytokine production

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of myoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of ossification

Inferred from direct assay PubMed 15820682. Source: MGI

negative regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

negative regulation of skeletal muscle tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15657445. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

organ morphogenesis

Traceable author statement PubMed 8421714. Source: MGI

organ regeneration

Inferred from electronic annotation. Source: Ensembl

ossification involved in bone remodeling

Inferred from electronic annotation. Source: Ensembl

pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 12773577. Source: BHF-UCL

phosphate-containing compound metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NAD+ ADP-ribosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of SMAD protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of blood vessel endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle arrest

Inferred from direct assay PubMed 19056892. Source: MGI

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 15604101. Source: MGI

positive regulation of cellular protein metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of collagen biosynthetic process

Inferred from direct assay PubMed 19734317. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from direct assay PubMed 18794329. Source: MGI

positive regulation of exit from mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 17293613. Source: MGI

positive regulation of histone acetylation

Inferred from direct assay PubMed 15990875. Source: MGI

positive regulation of histone deacetylation

Inferred from direct assay PubMed 15657445PubMed 15990875. Source: MGI

positive regulation of interleukin-17 production

Inferred from direct assay PubMed 19501566. Source: BHF-UCL

positive regulation of isotype switching to IgA isotypes

Inferred from sequence orthology PubMed 14988498. Source: MGI

positive regulation of odontogenesis

Inferred from direct assay PubMed 7848824. Source: MGI

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein localization to nucleus

Inferred from genetic interaction PubMed 21911934. Source: MGI

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell differentiation

Inferred from sequence orthology PubMed 8616889. Source: MGI

positive regulation of superoxide anion generation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15990875PubMed 17951031PubMed 18997793. Source: MGI

positive regulation of transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15100250PubMed 15282343. Source: MGI

protein export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 12208849. Source: MGI

receptor catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA binding

Inferred from direct assay PubMed 15282343. Source: MGI

regulation of actin cytoskeleton reorganization

Inferred from genetic interaction PubMed 21911934. Source: MGI

regulation of binding

Inferred from direct assay PubMed 15282343. Source: MGI

regulation of branching involved in mammary gland duct morphogenesis

Inferred from genetic interaction PubMed 17898001. Source: MGI

regulation of cartilage development

Inferred from direct assay PubMed 20501701. Source: MGI

regulation of cell proliferation

Inferred from direct assay PubMed 11799106. Source: MGI

regulation of protein import into nucleus

Inferred from direct assay PubMed 11799106. Source: MGI

regulation of sodium ion transport

Inferred from direct assay PubMed 16941024. Source: MGI

regulation of striated muscle tissue development

Inferred from direct assay PubMed 11711431. Source: MGI

regulation of transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulatory T cell differentiation

Inferred from direct assay PubMed 15100250. Source: MGI

response to cholesterol

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from sequence or structural similarity. Source: UniProtKB

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to laminar fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from sequence or structural similarity. Source: UniProtKB

response to radiation

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from electronic annotation. Source: Ensembl

salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Traceable author statement PubMed 1436033. Source: MGI

skeletal system development

Traceable author statement PubMed 1436033PubMed 8421714. Source: MGI

tolerance induction to self antigen

Inferred from mutant phenotype PubMed 17481928. Source: MGI

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 12208849PubMed 23868260PubMed 8429908. Source: MGI

ureteric bud development

Inferred from expression pattern PubMed 14656760. Source: UniProtKB

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from direct assay PubMed 2209468. Source: MGI

extracellular space

Inferred from direct assay PubMed 19734317. Source: BHF-UCL

microvillus

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from direct assay PubMed 12208849PubMed 9008713. Source: MGI

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiontransforming growth factor beta receptor binding

Inferred from physical interaction PubMed 17878231. Source: MGI

type II transforming growth factor beta receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 By similarity
Chain30 – 278249Latency-associated peptide
PRO_0000033766
Chain279 – 390112Transforming growth factor beta-1
PRO_0000033767

Regions

Region30 – 7445Straightjacket domain By similarity
Region75 – 271197Arm domain By similarity
Motif244 – 2463Cell attachment site Potential

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) By similarity
Glycosylation1361N-linked (GlcNAc...) By similarity
Glycosylation1761N-linked (GlcNAc...) By similarity
Disulfide bond33Interchain (with C-1350 or C-1375 in LTBP1); in inactive form By similarity
Disulfide bond223Interchain (with C-225) By similarity
Disulfide bond225Interchain (with C-223) By similarity
Disulfide bond285 ↔ 294 By similarity
Disulfide bond293 ↔ 356 By similarity
Disulfide bond322 ↔ 387 By similarity
Disulfide bond326 ↔ 389 By similarity
Disulfide bond355Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
P04202 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 4381A51B711D689E

FASTA39044,310
        10         20         30         40         50         60 
MPPSGLRLLP LLLPLPWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA 

        70         80         90        100        110        120 
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESADPEPEPE ADYYAKEVTR VLMVDRNNAI 

       130        140        150        160        170        180 
YEKTKDISHS IYMFFNTSDI REAVPEPPLL SRAELRLQRL KSSVEQHVEL YQKYSNNSWR 

       190        200        210        220        230        240 
YLGNRLLTPT DTPEWLSFDV TGVVRQWLNQ GDGIQGFRFS AHCSCDSKDN KLHVEINGIS 

       250        260        270        280        290        300 
PKRRGDLGTI HDMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI 

       310        320        330        340        350        360 
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SASPCCVPQA 

       370        380        390 
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS 

« Hide

References

« Hide 'large scale' references
[1]"The murine transforming growth factor-beta precursor."
Derynck R., Jarrett J.A., Chen E.Y., Goeddel D.V.
J. Biol. Chem. 261:4377-4379(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular organization of the gene encoding murine transforming growth factor beta 1."
Guron C., Sudarshan C., Raghow R.
Gene 165:325-326(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[3]"Transforming growth factor-beta 1 sequence and expression: no difference between NOD/Lt and C57Bl/6 mouse strains."
Poirot L., Benoist C., Mathis D.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 and NOD/LT.
Tissue: Spleen.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"P311 binds to the latency associated protein and downregulates the expression of TGF-beta1 and TGF-beta2."
Paliwal S., Shi J., Dhru U., Zhou Y., Schuger L.
Biochem. Biophys. Res. Commun. 315:1104-1109(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NREP.
[6]"Developmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-beta signaling."
Tocharus J., Tsuchiya A., Kajikawa M., Ueta Y., Oka C., Kawaichi M.
Dev. Growth Differ. 46:257-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTRA3.
[7]"HtrA1 serine protease inhibits signaling mediated by Tgfbeta family proteins."
Oka C., Tsujimoto R., Kajikawa M., Koshiba-Takeuchi K., Ina J., Yano M., Tsuchiya A., Ueta Y., Soma A., Kanda H., Matsumoto M., Kawaichi M.
Development 131:1041-1053(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTRA1.
[8]"ADAMTSL6beta protein rescues fibrillin-1 microfibril disorder in a Marfan syndrome mouse model through the promotion of fibrillin-1 assembly."
Saito M., Kurokawa M., Oda M., Oshima M., Tsutsui K., Kosaka K., Nakao K., Ogawa M., Manabe R., Suda N., Ganjargal G., Hada Y., Noguchi T., Teranaka T., Sekiguchi K., Yoneda T., Tsuji T.
J. Biol. Chem. 286:38602-38613(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THSD4.
[9]"Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13177 mRNA. Translation: AAA40423.1.
L42462 expand/collapse EMBL AC list , L42456, L42457, L42458, L42459, L42460, L42461 Genomic DNA. Translation: AAB00138.1.
AJ009862 mRNA. Translation: CAA08900.1.
BC013738 mRNA. Translation: AAH13738.1.
PIRWFMS2. A01396.
RefSeqNP_035707.1. NM_011577.1.
UniGeneMm.248380.

3D structure databases

ProteinModelPortalP04202.
SMRP04202. Positions 30-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204157. 4 interactions.
DIPDIP-48640N.
STRING10090.ENSMUSP00000002678.

PTM databases

PhosphoSiteP04202.

Proteomic databases

PaxDbP04202.
PRIDEP04202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002678; ENSMUSP00000002678; ENSMUSG00000002603.
GeneID21803.
KEGGmmu:21803.
UCSCuc009ftq.1. mouse.

Organism-specific databases

CTD7040.
MGIMGI:98725. Tgfb1.

Phylogenomic databases

eggNOGNOG279949.
HOGENOMHOG000290198.
HOVERGENHBG074115.
InParanoidP04202.
KOK13375.
OMASHSIYMF.
OrthoDBEOG70GMFT.
PhylomeDBP04202.
TreeFamTF318514.

Gene expression databases

ArrayExpressP04202.
BgeeP04202.
CleanExMM_TGFB1.
GenevestigatorP04202.

Family and domain databases

InterProIPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR003939. TGFb1.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERPTHR11848. PTHR11848. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PIRSFPIRSF001787. TGF-beta. 1 hit.
PRINTSPR01423. TGFBETA.
PR01424. TGFBETA1.
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301176.
PMAP-CutDBP04202.
PROP04202.
SOURCESearch...

Entry information

Entry nameTGFB1_MOUSE
AccessionPrimary (citable) accession number: P04202
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: April 16, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot