P61812 (TGFB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Latency-associated peptide
   Short name=LAP

Gene names

Name:

TGFB2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Aortic aneurysm Disease mutation
Domain	Signal
Molecular function	Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SMAD 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 activation-induced cell death of T cells Inferred from electronic annotation. Source: Compara angiogenesis Traceable author statement PubMed 9611771. Source: UniProtKB axon guidance Inferred from electronic annotation. Source: Compara blood vessel remodeling Inferred from electronic annotation. Source: Compara 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: Compara 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-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 embryonic digestive tract development Inferred from expression pattern PubMed 20875417. Source: DFLAT eye development Inferred from direct assay PubMed 15944186. Source: UniProtKB face morphogenesis Inferred from electronic annotation. Source: Compara glial cell migration Inferred from direct assay PubMed 18431253. Source: BHF-UCL hair follicle morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB hemopoiesis Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Inferred from electronic annotation. Source: Compara 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 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: Compara 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 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 gene expression Inferred from electronic annotation. Source: Compara 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 cascade 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 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 stimulus Inferred from direct assay PubMed 18039789. Source: BHF-UCL salivary gland morphogenesis Inferred from expression pattern PubMed 18080134. Source: BHF-UCL 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
Cellular_component	axon 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: Compara neuronal cell body Inferred from sequence or structural similarity. Source: UniProtKB platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	beta-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 signaling protein serine/threonine kinase activity Inferred from direct assay PubMed 12958365. Source: BHF-UCL 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
APP	P05067	6	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 302

282

Latency-associated peptide

PRO_0000033784

Chain

303 – 414

112

Transforming growth factor beta-2

PRO_0000033785

Amino acid modifications

Glycosylation

72

1

N-linked (GlcNAc...) Potential

Glycosylation

140

1

N-linked (GlcNAc...) Potential

Glycosylation

241

1

N-linked (GlcNAc...) Potential

Disulfide bond

309 ↔ 318

Disulfide bond

317 ↔ 380

Disulfide bond

346 ↔ 411

Disulfide bond

350 ↔ 413

Disulfide bond

379

Interchain

Natural variations

Alternative sequence

116

1

N → TVCPVVTTPSGSVGSLCSRQ SQVLCGYLD in isoform B.

VSP_006417

Natural variant

91

1

R → H. Ref.4 Ref.14
Corresponds to variant rs10482721 [ dbSNP | Ensembl ].

VAR_012708

Natural variant

100 – 104

5

Missing in LDS4.

VAR_068931

Natural variant

207

1

V → L. Ref.4
Corresponds to variant rs10482810 [ dbSNP | Ensembl ].

VAR_018923

Natural variant

299

1

R → W in LDS4. Ref.15

VAR_068932

Natural variant

302

1

R → C in LDS4. Ref.15

VAR_068933

Natural variant

338

1

P → H in LDS4. Ref.15

VAR_068934

Experimental info

Sequence conflict

32

1

F → L in AAA61162. Ref.8

Sequence conflict

116

1

Missing in AAA50405. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

414

Helix Strand Turn

Details...

Helix

306 – 309

4

Beta strand

315 – 320

6

Beta strand

323 – 325

3

Helix

326 – 330

5

Beta strand

335 – 337

3

Beta strand

339 – 342

4

Beta strand

345 – 347

3

Beta strand

354 – 356

3

Helix

359 – 370

12

Helix

372 – 374

3

Beta strand

379 – 382

4

Beta strand

384 – 394

11

Beta strand

397 – 408

12

Beta strand

411 – 414

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 7D9D569E0F4A07D0	FASTA	414	47,748
	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
	Isoform B [UniParc] [UniParc]. Checksum: 5D7A3C2ED51753D5	FASTA	442	50,573
	10 20 30 40 50 60 MHYCVLSAFL ILHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP 70 80 90 100 110 120 EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPP FFPSETVCPV 130 140 150 160 170 180 VTTPSGSVGS LCSRQSQVLC GYLDAIPPTF YRPYFRIVRF DVSAMEKNAS NLVKAEFRVF 190 200 210 220 230 240 RLQNPKARVP EQRIELYQIL KSKDLTSPTQ RYIDSKVVKT RAEGEWLSFD VTDAVHEWLH 250 260 270 280 290 300 HKDRNLGFKI SLHCPCCTFV PSNNYIIPNK SEELEARFAG IDGTSTYTSG DQKTIKSTRK 310 320 330 340 350 360 KNSGKTPHLL LMLLPSYRLE SQQTNRRKKR ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW 370 380 390 400 410 420 KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY 430 440 YIGKTPKIEQ LSNMIVKSCK CS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00220156.
IPI00235354.

PIR

B31249. A29478.
A31249. S06216.

RefSeq

NP_001129071.1. NM_001135599.2.
NP_003229.1. NM_003238.3.

UniGene

Hs.133379.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TFG	X-ray	1.95	A	303-414	[»]
2TGI	X-ray	1.80	A	303-414	[»]

ProteinModelPortal

P61812.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5936N.

IntAct

P61812. 1 interaction.

STRING

9606.ENSP00000355896.

PTM databases

PhosphoSite

P61812.

Polymorphism databases

DMDM

48429157.

Proteomic databases

PaxDb

P61812.

PRIDE

P61812.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366929; ENSP00000355896; ENSG00000092969.
ENST00000366930; ENSP00000355897; ENSG00000092969.

GeneID

7042.

KEGG

hsa:7042.

UCSC

uc001hlm.3. human.
uc001hln.3. human.

Organism-specific databases

CTD

7042.

GeneCards

GC01P218519.

HGNC

HGNC:11768. TGFB2.

MIM

190220. gene.
614816. phenotype.

neXtProt

NX_P61812.

Orphanet

708. Peters anomaly.

PharmGKB

PA36482.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG269146.

HOGENOM

HOG000290198.

HOVERGEN

HBG074115.

KO

K13376.

OMA

RAATCER.

OrthoDB

EOG43TZVH.

Enzyme and pathway databases

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.
hedgehog_2pathway. Signaling events mediated by the Hedgehog family.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

Bgee

P61812.

CleanEx

HS_TGFB2.

Genevestigator

P61812.

GermOnline

ENSG00000092969. Homo sapiens.

Family and domain databases

InterPro

IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR003940. TGFb2.
IPR017948. TGFb_CS.
[Graphical view]

PANTHER

PTHR11848. PTHR11848. 1 hit.

Pfam

PF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]

PIRSF

PIRSF001787. TGF-beta. 1 hit.

PRINTS

PR01423. TGFBETA.
PR01425. TGFBETA2.

SMART

SM00204. TGFB. 1 hit.
[Graphical view]

PROSITE

PS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TGFB2. human.

EvolutionaryTrace

P61812.

GenomeRNAi

7042.

NextBio

27517.

PMAP-CutDB

P61812.

SOURCE

Search...

Entry information

Entry name

TGFB2_HUMAN

Accession

Primary (citable) accession number: P61812
Secondary accession number(s): B4DKC5 , P08112, Q15579, Q15581, Q4VAV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.