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P27090 (TGFB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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-2

Short name=TGF-beta-2

Cleaved into the following chain:

  1. Latency-associated peptide
    Short name=LAP
Gene names
Name:Tgfb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

TGF-beta 2 has suppressive effects on interleukin-2 dependent T-cell growth.

Subunit structure

Homodimer; disulfide-linked By similarity. Heterodimers with TGFB1 and with TGFB3 have been found in bone By similarity. Interacts with ASPN By similarity. Interacts with the serine proteases HTRA1 and HTRA3. Latency-associated peptide interacts with NREP; the interaction results in a decrease in TGFB2 autoinduction. Ref.3 Ref.4 Ref.5

Subcellular location

Secreted.

Post-translational modification

The precursor is cleaved into mature TGF-beta-2 and LAP, which remains non-covalently linked to mature TGF-beta-2 rendering it inactive By similarity.

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGrowth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

activation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

axon guidance

Inferred from mutant phenotype PubMed 15528466. Source: MGI

blood vessel development

Inferred from mutant phenotype PubMed 15528466. Source: MGI

blood vessel remodeling

Inferred from mutant phenotype PubMed 12393102. Source: MGI

cardiac epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

cardiac left ventricle morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

cardiac muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

cardiac right ventricle morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

cardioblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

cartilage condensation

Inferred from genetic interaction PubMed 8565825. Source: MGI

catagen

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

cell death

Inferred from sequence or structural similarity. Source: UniProtKB

cell growth

Inferred from electronic annotation. Source: InterPro

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

cell morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction organization

Inferred from sequence or structural similarity. Source: UniProtKB

collagen fibril organization

Inferred from sequence or structural similarity. Source: UniProtKB

dopamine biosynthetic process

Inferred from mutant phenotype PubMed 16257223. Source: UniProtKB

embryonic digestive tract development

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix organization

Inferred from mutant phenotype PubMed 11784073PubMed 15528466. Source: MGI

extrinsic apoptotic signaling pathway

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

eye development

Inferred from sequence or structural similarity. Source: UniProtKB

face morphogenesis

Inferred from expression pattern PubMed 18498113. Source: UniProtKB

glial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

hair follicle development

Inferred from mutant phenotype PubMed 10433821. Source: UniProtKB

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 10433821. Source: UniProtKB

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

heart morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

hemopoiesis

Inferred from mutant phenotype PubMed 14707111. Source: UniProtKB

menstrual cycle phase

Inferred from electronic annotation. Source: Ensembl

negative regulation of alkaline phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

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 keratinocyte differentiation

Non-traceable author statement PubMed 10433821. Source: UniProtKB

negative regulation of macrophage cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

neuron development

Inferred from mutant phenotype PubMed 16257223. Source: UniProtKB

neuron fate commitment

Inferred from direct assay PubMed 15744664. Source: MGI

neutrophil chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

outflow tract morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

pathway-restricted SMAD protein phosphorylation

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

positive regulation of activation-induced cell death of T cells

Inferred from direct assay PubMed 8206089. Source: MGI

positive regulation of cardioblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of catagen

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell adhesion mediated by integrin

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle

Inferred from mutant phenotype PubMed 14707111. Source: UniProtKB

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from direct assay PubMed 8206089. Source: MGI

positive regulation of gene expression

Inferred from direct assay PubMed 18498113. Source: UniProtKB

positive regulation of heart contraction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of immune response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of integrin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ossification

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of stress-activated MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of apoptotic process

Inferred from mutant phenotype PubMed 12393102. Source: MGI

regulation of transforming growth factor beta2 production

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

response to progesterone

Inferred from sequence or structural similarity. Source: UniProtKB

salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

signal transduction by phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal system development

Inferred from mutant phenotype PubMed 15531369. Source: MGI

somatic stem cell division

Inferred from direct assay PubMed 14707111. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

ventricular septum morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

wound healing

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from direct assay PubMed 16257223. Source: UniProtKB

endosome

Inferred from direct assay PubMed 21266196. Source: UniProt

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 8164195. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 16257223. Source: UniProtKB

   Molecular_functionbeta-amyloid binding

Inferred from sequence or structural similarity. Source: UniProtKB

growth factor activity

Traceable author statement PubMed 16257223. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

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 – 2020 Potential
Chain21 – 302282Latency-associated peptide
PRO_0000033786
Chain303 – 414112Transforming growth factor beta-2
PRO_0000033787

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Disulfide bond309 ↔ 318 By similarity
Disulfide bond317 ↔ 380 By similarity
Disulfide bond346 ↔ 411 By similarity
Disulfide bond350 ↔ 413 By similarity
Disulfide bond379Interchain By similarity

Experimental info

Sequence conflict95 – 962DE → EQ in CAA40672. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P27090 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: DB37A7C38881F286

FASTA41447,589
        10         20         30         40         50         60 
MHYCVLSTFL LLHLVPVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP 

        70         80         90        100        110        120 
DEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPS HLPSENAIPP 

       130        140        150        160        170        180 
TFYRPYFRIV RFDVSTMEKN ASNLVKAEFR VFRLQNPKAR VAEQRIELYQ ILKSKDLTSP 

       190        200        210        220        230        240 
TQRYIDSKVV KTRAEGEWLS FDVTDAVQEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP 

       250        260        270        280        290        300 
NKSEELEARF AGIDGTSTYA SGDQKTIKST RKKTSGKTPH LLLMLLPSYR LESQQSSRRK 

       310        320        330        340        350        360 
KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH 

       370        380        390        400        410 
TKVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGNTPKI EQLSNMIVKS CKCS 

« Hide

References

« Hide 'large scale' references
[1]"Murine transforming growth factor-beta 2 cDNA sequence and expression in adult tissues and embryos."
Miller D.A., Lee A., Pelton R.W., Chen E.Y., Moses H.L., Derynck R.
Mol. Endocrinol. 3:1108-1114(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Mammary tumor.
[3]"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.
[4]"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.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57413 mRNA. Translation: CAA40672.1.
BC011170 mRNA. Translation: AAH11170.1.
CCDSCCDS15601.1.
PIRWFMSB2. A40148.
RefSeqNP_033393.2. NM_009367.3.
UniGeneMm.18213.

3D structure databases

ProteinModelPortalP27090.
SMRP27090. Positions 21-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204160. 2 interactions.
IntActP27090. 1 interaction.
MINTMINT-4121010.

PTM databases

PhosphoSiteP27090.

Proteomic databases

PaxDbP27090.
PRIDEP27090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045288; ENSMUSP00000043849; ENSMUSG00000039239.
GeneID21808.
KEGGmmu:21808.
UCSCuc007dzo.2. mouse.

Organism-specific databases

CTD7042.
MGIMGI:98726. Tgfb2.

Phylogenomic databases

eggNOGNOG269146.
GeneTreeENSGT00620000087687.
HOGENOMHOG000290198.
HOVERGENHBG074115.
InParanoidQ91VP5.
KOK13376.
OMAENAIPPT.
OrthoDBEOG70GMFT.
TreeFamTF318514.

Gene expression databases

ArrayExpressP27090.
BgeeP27090.
CleanExMM_TGFB2.
GenevestigatorP27090.

Family and domain databases

Gene3D2.10.90.10. 1 hit.
InterProIPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR003940. TGFb2.
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.
PR01425. TGFBETA2.
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMSSF57501. SSF57501. 1 hit.
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTGFB2. mouse.
NextBio301190.
PROP27090.
SOURCESearch...

Entry information

Entry nameTGFB2_MOUSE
AccessionPrimary (citable) accession number: P27090
Secondary accession number(s): Q91VP5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 129 of the entry and version 2 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