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Protein

Transforming growth factor beta-2

Gene

TGFB2

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

Functioni

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

GO - Molecular functioni

  • amyloid-beta binding Source: UniProtKB
  • cytokine activity Source: UniProtKB
  • growth factor activity Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • signaling receptor binding Source: UniProtKB
  • transforming growth factor beta receptor binding Source: UniProtKB
  • type III transforming growth factor beta receptor binding Source: AgBase
  • type II transforming growth factor beta receptor binding Source: BHF-UCL

GO - Biological processi

  • activation of protein kinase activity Source: BHF-UCL
  • angiogenesis Source: UniProtKB
  • ascending aorta morphogenesis Source: BHF-UCL
  • atrial septum morphogenesis Source: BHF-UCL
  • atrial septum primum morphogenesis Source: BHF-UCL
  • atrioventricular valve morphogenesis Source: BHF-UCL
  • BMP signaling pathway Source: GO_Central
  • cardiac epithelial to mesenchymal transition Source: BHF-UCL
  • cardiac muscle cell proliferation Source: UniProtKB
  • cardiac right ventricle morphogenesis Source: BHF-UCL
  • cardioblast differentiation Source: UniProtKB
  • cell-cell junction organization Source: BHF-UCL
  • cell-cell signaling Source: ProtInc
  • cell cycle arrest Source: BHF-UCL
  • cell death Source: UniProtKB
  • cell development Source: GO_Central
  • cell migration Source: BHF-UCL
  • cell morphogenesis Source: UniProtKB
  • cell proliferation Source: ProtInc
  • collagen fibril organization Source: BHF-UCL
  • cranial skeletal system development Source: BHF-UCL
  • dopamine biosynthetic process Source: UniProtKB
  • embryo development ending in birth or egg hatching Source: UniProtKB
  • embryonic digestive tract development Source: DFLAT
  • embryonic limb morphogenesis Source: BHF-UCL
  • endocardial cushion fusion Source: BHF-UCL
  • endocardial cushion morphogenesis Source: BHF-UCL
  • epithelial to mesenchymal transition Source: BHF-UCL
  • extrinsic apoptotic signaling pathway Source: BHF-UCL
  • eye development Source: UniProtKB
  • generation of neurons Source: UniProtKB
  • glial cell migration Source: BHF-UCL
  • hair follicle development Source: UniProtKB
  • hair follicle morphogenesis Source: UniProtKB
  • heart development Source: UniProtKB
  • heart morphogenesis Source: BHF-UCL
  • heart valve morphogenesis Source: BHF-UCL
  • hemopoiesis Source: UniProtKB
  • inner ear development Source: BHF-UCL
  • kidney development Source: BHF-UCL
  • male gonad development Source: BHF-UCL
  • membranous septum morphogenesis Source: BHF-UCL
  • negative regulation of alkaline phosphatase activity Source: BHF-UCL
  • negative regulation of angiogenesis Source: BHF-UCL
  • negative regulation of cell growth Source: BHF-UCL
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of epithelial cell proliferation Source: BHF-UCL
  • negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of immune response Source: UniProtKB
  • negative regulation of macrophage cytokine production Source: DFLAT
  • negative regulation of Ras protein signal transduction Source: BHF-UCL
  • neural retina development Source: BHF-UCL
  • neural tube closure Source: BHF-UCL
  • neuron development Source: UniProtKB
  • neutrophil chemotaxis Source: UniProtKB
  • odontogenesis Source: BHF-UCL
  • outflow tract septum morphogenesis Source: BHF-UCL
  • pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • pharyngeal arch artery morphogenesis Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of cardioblast differentiation Source: UniProtKB
  • positive regulation of cell adhesion mediated by integrin Source: BHF-UCL
  • positive regulation of cell cycle Source: UniProtKB
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of epithelial cell migration Source: BHF-UCL
  • positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  • positive regulation of heart contraction Source: UniProtKB
  • positive regulation of immune response Source: UniProtKB
  • positive regulation of integrin biosynthetic process Source: BHF-UCL
  • positive regulation of neuron apoptotic process Source: UniProtKB
  • positive regulation of Notch signaling pathway Source: BHF-UCL
  • positive regulation of ossification Source: BHF-UCL
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: GO_Central
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • positive regulation of pri-miRNA transcription by RNA polymerase II Source: BHF-UCL
  • positive regulation of protein secretion Source: BHF-UCL
  • positive regulation of stress-activated MAPK cascade Source: BHF-UCL
  • positive regulation of timing of catagen Source: UniProtKB
  • protein phosphorylation Source: BHF-UCL
  • pulmonary valve morphogenesis Source: BHF-UCL
  • regulation of apoptotic process involved in outflow tract morphogenesis Source: BHF-UCL
  • regulation of timing of catagen Source: UniProtKB
  • regulation of transforming growth factor beta2 production Source: BHF-UCL
  • response to drug Source: UniProtKB
  • response to hypoxia Source: BHF-UCL
  • response to progesterone Source: BHF-UCL
  • response to wounding Source: BHF-UCL
  • salivary gland morphogenesis Source: BHF-UCL
  • secondary palate development Source: BHF-UCL
  • skeletal system development Source: BHF-UCL
  • SMAD protein signal transduction Source: BHF-UCL
  • somatic stem cell division Source: UniProtKB
  • substantia propria of cornea development Source: BHF-UCL
  • transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • uterine wall breakdown Source: BHF-UCL
  • uterus development Source: BHF-UCL
  • ventricular septum morphogenesis Source: BHF-UCL
  • ventricular trabecula myocardium morphogenesis Source: BHF-UCL
  • wound healing Source: UniProtKB

Keywordsi

Molecular functionGrowth factor, Mitogen

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-2129379 Molecules associated with elastic fibres
R-HSA-3000178 ECM proteoglycans
SignaLinkiP61812
SIGNORiP61812

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming growth factor beta-2
Short name:
TGF-beta-2
Alternative name(s):
BSC-1 cell growth inhibitor
Cetermin
Glioblastoma-derived T-cell suppressor factor
Short name:
G-TSF
Polyergin
Cleaved into the following chain:
Gene namesi
Name:TGFB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000092969.11
HGNCiHGNC:11768 TGFB2
MIMi190220 gene
neXtProtiNX_P61812

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

Secreted

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TGFB2 is found in a family with Peters anomaly. Translocation t(1;7)(q41;p21) with HDAC9.1 Publication
Loeys-Dietz syndrome 4 (LDS4)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn aortic aneurysm syndrome with widespread systemic involvement. LDS4 is characterized by arterial tortuosity, aortic dissection, intracranial aneurysm and subarachnoid hemorrhage, hypertelorism, bifid uvula, pectus deformity, bicuspid aortic valve, arachnodactyly, scoliosis, foot deformities, dural ectasia, joint hyperflexibility, and thin skin with easy bruising and striae.
See also OMIM:614816
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068931100 – 104Missing in LDS4. 1 Publication5
Natural variantiVAR_080342102 – 414Missing in LDS4. 1 PublicationAdd BLAST313
Natural variantiVAR_080343229 – 414Missing in LDS4. 1 PublicationAdd BLAST186
Natural variantiVAR_068932299R → W in LDS4. 1 PublicationCorresponds to variant dbSNP:rs863223792EnsemblClinVar.1
Natural variantiVAR_068933302R → C in LDS4. 1 PublicationCorresponds to variant dbSNP:rs869312903Ensembl.1
Natural variantiVAR_068934338P → H in LDS4. 1 PublicationCorresponds to variant dbSNP:rs387907278Ensembl.1
Defects in TGFB2 may be a cause of non-syndromic aortic disease (NSAD). NSAD is a frequently asymptomatic but potentially lethal disease characterized by thoracic aortic aneurysms and dissections without additional syndromic features.1 Publication

Keywords - Diseasei

Aortic aneurysm, Disease mutation

Organism-specific databases

DisGeNETi7042
GeneReviewsiTGFB2
MalaCardsiTGFB2
MIMi614816 phenotype
OpenTargetsiENSG00000092969
Orphaneti91387 Familial thoracic aortic aneurysm and aortic dissection
708 Peters anomaly
PharmGKBiPA36482

Chemistry databases

ChEMBLiCHEMBL3217393

Polymorphism and mutation databases

BioMutaiTGFB2
DMDMi48429157

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003378421 – 302Latency-associated peptideAdd BLAST282
ChainiPRO_0000033785303 – 414Transforming growth factor beta-2Add BLAST112

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi72N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi140N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi241N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi309 ↔ 318
Disulfide bondi317 ↔ 380
Disulfide bondi346 ↔ 411
Disulfide bondi350 ↔ 413
Disulfide bondi379Interchain

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

EPDiP61812
MaxQBiP61812
PeptideAtlasiP61812
PRIDEiP61812
ProteomicsDBi57335
57336 [P61812-2]

PTM databases

iPTMnetiP61812
PhosphoSitePlusiP61812

Miscellaneous databases

PMAP-CutDBiP61812

Expressioni

Gene expression databases

BgeeiENSG00000092969
CleanExiHS_TGFB2
GenevisibleiP61812 HS

Interactioni

Subunit structurei

Homodimer; disulfide-linked (By similarity). Heterodimers with TGFB1 and with TGFB3 have been found in bone (By similarity). Interacts with the serine proteases, HTRA1 and HTRA3 (By similarity). Latency-associated peptide interacts with NREP; the interaction results in a decrease in TGFB2 autoinduction (By similarity). Interacts with ASPN. Interacts with MFAP5 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050677EBI-779581,EBI-77613

GO - Molecular functioni

  • cytokine activity Source: UniProtKB
  • growth factor activity Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • signaling receptor binding Source: UniProtKB
  • transforming growth factor beta receptor binding Source: UniProtKB
  • type III transforming growth factor beta receptor binding Source: AgBase
  • type II transforming growth factor beta receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112900, 8 interactors
ComplexPortaliCPX-605 TGF-beta-2 complex
CPX-834 TGF-beta-2-TGFR complex
DIPiDIP-5936N
IntActiP61812, 2 interactors

Structurei

Secondary structure

1414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi306 – 309Combined sources4
Beta strandi315 – 320Combined sources6
Beta strandi323 – 325Combined sources3
Helixi326 – 330Combined sources5
Beta strandi335 – 337Combined sources3
Beta strandi339 – 342Combined sources4
Beta strandi345 – 347Combined sources3
Beta strandi354 – 356Combined sources3
Helixi359 – 370Combined sources12
Helixi372 – 374Combined sources3
Beta strandi379 – 382Combined sources4
Beta strandi384 – 394Combined sources11
Beta strandi397 – 408Combined sources12
Beta strandi411 – 414Combined sources4

3D structure databases

ProteinModelPortaliP61812
SMRiP61812
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61812

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00910000143982
HOGENOMiHOG000290198
HOVERGENiHBG074115
InParanoidiP61812
KOiK13376
OMAiNERAATC
OrthoDBiEOG091G0BMM
PhylomeDBiP61812
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
IPR003940 TGFb2
IPR017948 TGFb_CS
PANTHERiPTHR11848 PTHR11848, 1 hit
PTHR11848:SF141 PTHR11848:SF141, 1 hit
PfamiView protein in Pfam
PF00019 TGF_beta, 1 hit
PF00688 TGFb_propeptide, 1 hit
PIRSFiPIRSF001787 TGF-beta, 1 hit
PRINTSiPR01423 TGFBETA
PR01425 TGFBETA2
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

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P61812-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHYCVLSAFL ILHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL
60 70 80 90 100
TSPPEDYPEP EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA
110 120 130 140 150
KEVYKIDMPP FFPSENAIPP TFYRPYFRIV RFDVSAMEKN ASNLVKAEFR
160 170 180 190 200
VFRLQNPKAR VPEQRIELYQ ILKSKDLTSP TQRYIDSKVV KTRAEGEWLS
210 220 230 240 250
FDVTDAVHEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP NKSEELEARF
260 270 280 290 300
AGIDGTSTYT SGDQKTIKST RKKNSGKTPH LLLMLLPSYR LESQQTNRRK
310 320 330 340 350
KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC
360 370 380 390 400
PYLWSSDTQH SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI
410
EQLSNMIVKS CKCS
Length:414
Mass (Da):47,748
Last modified:August 1, 1988 - v1
Checksum:i7D9D569E0F4A07D0
GO
Isoform B (identifier: P61812-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-116: N → TVCPVVTTPSGSVGSLCSRQSQVLCGYLD

Show »
Length:442
Mass (Da):50,573
Checksum:i5D7A3C2ED51753D5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32F → L in AAA61162 (PubMed:1764261).Curated1
Sequence conflicti116Missing in AAA50405 (PubMed:2850146).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01270891R → H2 PublicationsCorresponds to variant dbSNP:rs10482721EnsemblClinVar.1
Natural variantiVAR_068931100 – 104Missing in LDS4. 1 Publication5
Natural variantiVAR_080342102 – 414Missing in LDS4. 1 PublicationAdd BLAST313
Natural variantiVAR_018923207V → L1 PublicationCorresponds to variant dbSNP:rs10482810Ensembl.1
Natural variantiVAR_080343229 – 414Missing in LDS4. 1 PublicationAdd BLAST186
Natural variantiVAR_068932299R → W in LDS4. 1 PublicationCorresponds to variant dbSNP:rs863223792EnsemblClinVar.1
Natural variantiVAR_068933302R → C in LDS4. 1 PublicationCorresponds to variant dbSNP:rs869312903Ensembl.1
Natural variantiVAR_072740320R → C Probable disease-associated mutation found in a family with non-syndromic aortic disease. 1 Publication1
Natural variantiVAR_068934338P → H in LDS4. 1 PublicationCorresponds to variant dbSNP:rs387907278Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_006417116N → TVCPVVTTPSGSVGSLCSRQ SQVLCGYLD in isoform B. 3 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00083 mRNA Translation: CAA68279.1
M19154 mRNA Translation: AAA50404.1
M19154 mRNA Translation: AAA50405.1
AY438979 Genomic DNA Translation: AAR05442.1
AK296504 mRNA Translation: BAG59137.1
CH471100 Genomic DNA Translation: EAW93326.1
BC096235 mRNA Translation: AAH96235.1
BC099635 mRNA Translation: AAH99635.1
M87843 Genomic DNA Translation: AAA61162.1
CCDSiCCDS1521.1
CCDS44318.1 [P61812-2]
PIRiA29478 B31249
S06216 A31249
RefSeqiNP_001129071.1, NM_001135599.3 [P61812-2]
NP_003229.1, NM_003238.4 [P61812-1]
UniGeneiHs.133379

Genome annotation databases

EnsembliENST00000366929; ENSP00000355896; ENSG00000092969 [P61812-2]
ENST00000366930; ENSP00000355897; ENSG00000092969 [P61812-1]
GeneIDi7042
KEGGihsa:7042
UCSCiuc001hlm.4 human

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTGFB2_HUMAN
AccessioniPrimary (citable) accession number: P61812
Secondary accession number(s): B4DKC5
, P08112, Q15579, Q15581, Q4VAV9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 20, 2018
This is version 165 of the entry and version 1 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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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