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P61812 (TGFB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Latency-associated peptide
    Short name=LAP
Gene names
Name:TGFB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 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. Ref.11

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.

Involvement in disease

A chromosomal aberration involving TGFB2 is found in a family with Peters anomaly. Translocation t(1;7)(q41;p21) with HDAC9.

Loeys-Dietz syndrome 4 (LDS4) [MIM:614816]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseAortic aneurysm
Disease mutation
   DomainSignal
   Molecular functionGrowth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein import into nucleus

Inferred from direct assay PubMed 17192487. Source: BHF-UCL

activation of protein kinase activity

Inferred from direct assay PubMed 17192487PubMed 17960115. Source: BHF-UCL

angiogenesis

Traceable author statement PubMed 9611771. Source: UniProtKB

axon guidance

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

cardiac epithelial to mesenchymal transition

Inferred from direct assay PubMed 10092230. Source: BHF-UCL

cardiac muscle cell proliferation

Inferred from direct assay PubMed 15896309. Source: UniProtKB

cardioblast differentiation

Inferred from direct assay PubMed 15896309. Source: UniProtKB

cartilage condensation

Inferred from electronic annotation. Source: Ensembl

catagen

Inferred from direct assay PubMed 15955085. Source: UniProtKB

cell cycle arrest

Inferred from direct assay PubMed 18223299. Source: BHF-UCL

cell death

Inferred from direct assay PubMed 16227582. Source: UniProtKB

cell growth

Inferred from electronic annotation. Source: InterPro

cell migration

Inferred from direct assay PubMed 10092230. Source: BHF-UCL

cell morphogenesis

Inferred from direct assay PubMed 15896309. Source: UniProtKB

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

cell-cell junction organization

Inferred from direct assay PubMed 18505915. Source: BHF-UCL

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

collagen fibril organization

Inferred from direct assay PubMed 16891397. Source: BHF-UCL

dopamine biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

embryo development

Traceable author statement PubMed 2119582. Source: UniProtKB

embryonic digestive tract development

Inferred from expression pattern PubMed 20875417. Source: DFLAT

epithelial to mesenchymal transition

Inferred from direct assay PubMed 10092230PubMed 18223299. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 17217916. Source: BHF-UCL

eye development

Inferred from direct assay PubMed 15944186. Source: UniProtKB

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

generation of neurons

Traceable author statement PubMed 15944186. Source: UniProtKB

glial cell migration

Inferred from direct assay PubMed 18431253. Source: BHF-UCL

hair follicle development

Inferred from direct assay PubMed 10433821. Source: UniProtKB

hair follicle morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

heart development

Inferred from direct assay PubMed 15896309. Source: UniProtKB

heart morphogenesis

Inferred from direct assay PubMed 10092230. Source: BHF-UCL

hemopoiesis

Inferred from sequence or structural similarity. Source: UniProtKB

menstrual cycle phase

Inferred from expression pattern PubMed 18039789. Source: BHF-UCL

negative regulation of alkaline phosphatase activity

Inferred from direct assay PubMed 18358889. Source: BHF-UCL

negative regulation of cell growth

Inferred from direct assay PubMed 18358889. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from direct assay PubMed 15944186. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from direct assay PubMed 17217916. Source: BHF-UCL

negative regulation of immune response

Traceable author statement PubMed 9611771. Source: UniProtKB

negative regulation of macrophage cytokine production

Inferred from direct assay PubMed 20875417. Source: DFLAT

neuron development

Inferred from sequence or structural similarity. Source: UniProtKB

neuron fate commitment

Inferred from electronic annotation. Source: Ensembl

neutrophil chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

odontogenesis

Non-traceable author statement PubMed 18078367. Source: BHF-UCL

pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 11157754PubMed 18358889. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of activation-induced cell death of T cells

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardioblast differentiation

Inferred from direct assay PubMed 15896309. Source: UniProtKB

positive regulation of catagen

Inferred from direct assay PubMed 15955085. Source: UniProtKB

positive regulation of cell adhesion mediated by integrin

Inferred from direct assay PubMed 17960115PubMed 18223299. Source: BHF-UCL

positive regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell growth

Inferred from direct assay PubMed 15896309PubMed 20573232. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 15896309. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from direct assay PubMed 17960115. Source: BHF-UCL

positive regulation of epithelial to mesenchymal transition

Inferred from direct assay PubMed 17999987PubMed 18505915. Source: BHF-UCL

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart contraction

Inferred from direct assay PubMed 15896309. Source: UniProtKB

positive regulation of immune response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of integrin biosynthetic process

Inferred from direct assay PubMed 17960115. Source: BHF-UCL

positive regulation of neuron apoptotic process

Inferred from direct assay PubMed 16227582. Source: UniProtKB

positive regulation of ossification

Inferred from expression pattern PubMed 17401695. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 18223299. Source: BHF-UCL

positive regulation of protein secretion

Inferred from direct assay PubMed 18505915. Source: BHF-UCL

positive regulation of stress-activated MAPK cascade

Inferred from direct assay PubMed 17192487. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay PubMed 18358889. Source: BHF-UCL

regulation of transforming growth factor beta2 production

Inferred from mutant phenotype PubMed 12411310. Source: BHF-UCL

response to drug

Inferred from direct assay PubMed 20573232. Source: UniProtKB

response to hypoxia

Inferred from mutant phenotype PubMed 12411310. Source: BHF-UCL

response to progesterone

Inferred from direct assay PubMed 18039789. Source: BHF-UCL

response to wounding

Inferred from expression pattern PubMed 16891397PubMed 18040277. Source: BHF-UCL

salivary gland morphogenesis

Inferred from expression pattern PubMed 18080134. Source: BHF-UCL

signal transduction by phosphorylation

Inferred from direct assay PubMed 12958365. Source: GOC

somatic stem cell division

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 11157754PubMed 18358889. Source: BHF-UCL

wound healing

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from direct assay PubMed 18049952. Source: BHF-UCL

extracellular region

Inferred from direct assay PubMed 16227582. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionbeta-amyloid binding

Inferred from direct assay PubMed 16227582. Source: UniProtKB

cytokine activity

Traceable author statement PubMed 9611771. Source: UniProtKB

protein heterodimerization activity

Traceable author statement PubMed 9611771. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 2119582. Source: UniProtKB

receptor binding

Inferred from mutant phenotype PubMed 16227582. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from direct assay PubMed 12958365. Source: BHF-UCL

transforming growth factor beta receptor binding

Inferred from direct assay PubMed 16227582. Source: UniProtKB

type II transforming growth factor beta receptor binding

Inferred from direct assay PubMed 11157754. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050676EBI-779581,EBI-77613

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P61812-1)

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.
Isoform B (identifier: P61812-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 302282Latency-associated peptide
PRO_0000033784
Chain303 – 414112Transforming growth factor beta-2
PRO_0000033785

Amino acid modifications

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

Natural variations

Alternative sequence1161N → TVCPVVTTPSGSVGSLCSRQ SQVLCGYLD in isoform B.
VSP_006417
Natural variant911R → H. Ref.4 Ref.14
Corresponds to variant rs10482721 [ dbSNP | Ensembl ].
VAR_012708
Natural variant100 – 1045Missing in LDS4.
VAR_068931
Natural variant2071V → L. Ref.4
Corresponds to variant rs10482810 [ dbSNP | Ensembl ].
VAR_018923
Natural variant2991R → W in LDS4. Ref.15
VAR_068932
Natural variant3021R → C in LDS4. Ref.15
VAR_068933
Natural variant3381P → H in LDS4. Ref.15
VAR_068934

Experimental info

Sequence conflict321F → L in AAA61162. Ref.8
Sequence conflict1161Missing in AAA50405. Ref.3

Secondary structure

........................... 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 7D9D569E0F4A07D0

FASTA41447,748
        10         20         30         40         50         60 
MHYCVLSAFL ILHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP 

        70         80         90        100        110        120 
EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPP FFPSENAIPP 

       130        140        150        160        170        180 
TFYRPYFRIV RFDVSAMEKN ASNLVKAEFR VFRLQNPKAR VPEQRIELYQ ILKSKDLTSP 

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

       250        260        270        280        290        300 
NKSEELEARF AGIDGTSTYT SGDQKTIKST RKKNSGKTPH LLLMLLPSYR LESQQTNRRK 

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

       370        380        390        400        410 
SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI EQLSNMIVKS CKCS 

« Hide

Isoform B [UniParc] [UniParc].

Checksum: 5D7A3C2ED51753D5
Show »

FASTA44250,573

References

« Hide 'large scale' references
[1]"Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-beta gene family."
de Martin R., Haendler B., Hofer-Warbinek R., Gaugitsch H., Wrann M., Schluesener H., Seifert J.M., Bodmer S., Fontana A., Hofer E.
EMBO J. 6:3673-3677(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"Transforming growth factor-beta 2: cDNA cloning and sequence analysis."
Madisen L., Webb N.R., Rose T.M., Marquardt H., Ikeda T., Twardzik D.R., Seyedin S., Purchio A.F.
DNA 7:1-8(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[3]"Structural and sequence analysis of TGF-beta 2 cDNA clones predicts two different precursor proteins produced by alternative mRNA splicing."
Webb N.R., Madisen L., Rose T.M., Purchio A.F.
DNA 7:493-497(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
[4]NIEHS SNPs program
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-91 AND LEU-207.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Thalamus.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
[8]"Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter."
Noma T., Glick A.B., Geiser A.G., O'Reilly M.A., Miller J., Roberts A.B., Sporn M.B.
Growth Factors 4:247-255(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
Tissue: Lung.
[9]"Complete amino acid sequence of human transforming growth factor type beta 2."
Marquardt H., Lioubin M.N., Ikeda T.
J. Biol. Chem. 262:12127-12131(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 303-414.
[10]"Molecular characterization of a familial translocation implicates disruption of HDAC9 and possible position effect on TGFbeta2 in the pathogenesis of Peters' anomaly."
David D., Cardoso J., Marques B., Marques R., Silva E.D., Santos H., Boavida M.G.
Genomics 81:489-503(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH HDAC9.
[11]"Mechanisms for asporin function and regulation in articular cartilage."
Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.
J. Biol. Chem. 282:32185-32192(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASPN.
[12]"Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily."
Daopin S., Piez K.A., Ogawa Y., Davies D.R.
Science 257:369-373(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[13]"An unusual feature revealed by the crystal structure at 2.2-A resolution of human transforming growth factor-beta 2."
Schlunegger M.P., Gruetter M.G.
Nature 358:430-434(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[14]"Two novel polymorphisms in the human transforming growth factor beta 2 gene."
Alansari A., Hajeer A.H., Bayat A., Eyre S., Carthy D., Ollier W.E.
Genes Immun. 2:295-296(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-91.
[15]"Loss-of-function mutations in TGFB2 cause a syndromic presentation of thoracic aortic aneurysm."
Lindsay M.E., Schepers D., Bolar N.A., Doyle J.J., Gallo E., Fert-Bober J., Kempers M.J., Fishman E.K., Chen Y., Myers L., Bjeda D., Oswald G., Elias A.F., Levy H.P., Anderlid B.M., Yang M.H., Bongers E.M., Timmermans J. expand/collapse author list , Braverman A.C., Canham N., Mortier G.R., Brunner H.G., Byers P.H., Van Eyk J., Van Laer L., Dietz H.C., Loeys B.L.
Nat. Genet. 44:922-927(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS4 100-ALA--TYR-104 DEL; TRP-299; CYS-302 AND HIS-338.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

TGF beta-2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB31249. A29478.
A31249. S06216.
RefSeqNP_001129071.1. NM_001135599.2.
NP_003229.1. NM_003238.3.
UniGeneHs.133379.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TFGX-ray1.95A303-414[»]
2TGIX-ray1.80A303-414[»]
ProteinModelPortalP61812.
SMRP61812. Positions 21-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112900. 10 interactions.
DIPDIP-5936N.
IntActP61812. 1 interaction.
STRING9606.ENSP00000355896.

PTM databases

PhosphoSiteP61812.

Polymorphism databases

DMDM48429157.

Proteomic databases

PaxDbP61812.
PRIDEP61812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366929; ENSP00000355896; ENSG00000092969. [P61812-2]
ENST00000366930; ENSP00000355897; ENSG00000092969. [P61812-1]
GeneID7042.
KEGGhsa:7042.
UCSCuc001hlm.3. human.
uc001hln.3. human. [P61812-2]

Organism-specific databases

CTD7042.
GeneCardsGC01P218519.
HGNCHGNC:11768. TGFB2.
HPAHPA049818.
MIM190220. gene.
614816. phenotype.
neXtProtNX_P61812.
Orphanet91387. Familial thoracic aortic aneurysm and aortic dissection.
708. Peters anomaly.
PharmGKBPA36482.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269146.
HOGENOMHOG000290198.
HOVERGENHBG074115.
KOK13376.
OMAENAIPPT.
OrthoDBEOG70GMFT.
PhylomeDBP61812.
TreeFamTF318514.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
SignaLinkP61812.

Gene expression databases

BgeeP61812.
CleanExHS_TGFB2.
GenevestigatorP61812.

Family and domain databases

InterProIPR001839. 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]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTGFB2. human.
EvolutionaryTraceP61812.
GeneWikiTGF_beta_2.
GenomeRNAi7042.
NextBio27517.
PMAP-CutDBP61812.
PROP61812.
SOURCESearch...

Entry information

Entry nameTGFB2_HUMAN
AccessionPrimary (citable) accession number: P61812
Secondary accession number(s): B4DKC5 expand/collapse secondary AC list , P08112, Q15579, Q15581, Q4VAV9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM