TGFB2
entrez
7042
canonical
uniprot
P61812
canonical
ensembl
ENSG00000092969
resolver
ensp
ENSP00000355896
resolver
ensp
ENSP00000355897
resolver
genesymbol
TGFB2
resolver
hgnc
HGNC:11768
resolver
uniprot
B4DKC5
resolver
uniprot
P08112
resolver
uniprot
Q15579
resolver
uniprot
Q15581
resolver
uniprot
Q4VAV9
resolver
uniprot
Q59EG9
resolver
uniprot_entry
Q59EG9_HUMAN
resolver
uniprot_entry
TGFB2_HUMAN
resolver
uniprot_sec
B4DKC5
resolver
uniprot_sec
P08112
resolver
uniprot_sec
Q15579
resolver
uniprot_sec
Q15581
resolver
uniprot_sec
Q4VAV9
resolver
amino_acid_sequence
MHYCVLSAFLILHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVPEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYRLESQQTNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving TGFB2 is found in a family with Peters anomaly. Translocation t(1;7)(q41;p21) with HDAC9. {ECO:0000269|PubMed:12706107}.; DISEASE: 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. {ECO:0000269|PubMed:22772368, ECO:0000269|PubMed:22772371, ECO:0000269|PubMed:25046559}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Camurati-Engelmann disease 2 (CAEND2) [MIM:606631]: A form of Camurati-Engelmann disease, an autosomal dominant disorder characterized by hyperostosis and sclerosis of the diaphyses of long bones. Sclerotic changes at the skull base may also be present. The disease typically presents in childhood with pain, muscular weakness, and waddling gait. Systemic manifestations such as anemia, leukopenia, and hepatosplenomegaly may also occur. In addition to diaphyseal dysplasia, CAEND2 affected individuals have features of osteopathia striata with cranial sclerosis. {ECO:0000269|PubMed:39014191, ECO:0000269|PubMed:40204055}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: [Transforming growth factor beta-2 proprotein]: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state during storage in extracellular matrix (By similarity). Associates non-covalently with TGF-beta-2 and regulates its activation via interaction with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-2 (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: [Transforming growth factor beta-2]: Multifunctional protein that regulates various processes such as angiogenesis and heart development (PubMed:22772368, PubMed:22772371). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains remain non-covalently linked rendering TGF-beta-2 inactive during storage in extracellular matrix (By similarity). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-2 and maintain it in a latent state during storage in extracellular milieus (By similarity). Once activated following release of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:22772368, ECO:0000269|PubMed:22772371}.
uniprot
proteins
mass_dalton
47748
uniprot
proteins
post_translational_modification
PTM: [Transforming growth factor beta-2 proprotein]: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-2 (TGF-beta-2) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-2 inactive. {ECO:0000250|UniProtKB:P01137}.
uniprot
proteins
protein_family
TGF-beta family
uniprot
proteins
pubmed
11528528
uniprot
proteins
pubmed
12706107
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1631557
uniprot
proteins
pubmed
1641027
uniprot
proteins
pubmed
1764261
uniprot
proteins
pubmed
17827158
uniprot
proteins
pubmed
19651619
uniprot
proteins
pubmed
22772368
uniprot
proteins
pubmed
22772371
uniprot
proteins
pubmed
25046559
uniprot
proteins
pubmed
2850146
uniprot
proteins
pubmed
3162414
uniprot
proteins
pubmed
3322813
uniprot
proteins
pubmed
3476488
uniprot
proteins
pubmed
39014191
uniprot
proteins
pubmed
40204055
uniprot
proteins
pubmed
40774839
uniprot
proteins
sequence_length
414
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted {ECO:0000269|PubMed:39014191}.
uniprot
proteins