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P61812

- TGFB2_HUMAN

UniProt

P61812 - TGFB2_HUMAN

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Protein

Transforming growth factor beta-2

Gene

TGFB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. beta-amyloid binding Source: UniProtKB
  2. cytokine activity Source: UniProtKB
  3. protein heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. receptor binding Source: UniProtKB
  6. receptor signaling protein serine/threonine kinase activity Source: BHF-UCL
  7. transforming growth factor beta receptor binding Source: UniProtKB
  8. type II transforming growth factor beta receptor binding Source: BHF-UCL

GO - Biological processi

  1. activation of protein kinase activity Source: BHF-UCL
  2. angiogenesis Source: UniProtKB
  3. axon guidance Source: Ensembl
  4. blood coagulation Source: Reactome
  5. blood vessel remodeling Source: Ensembl
  6. cardiac epithelial to mesenchymal transition Source: BHF-UCL
  7. cardiac muscle cell proliferation Source: UniProtKB
  8. cardioblast differentiation Source: UniProtKB
  9. cartilage condensation Source: Ensembl
  10. catagen Source: UniProtKB
  11. cell-cell junction organization Source: BHF-UCL
  12. cell-cell signaling Source: ProtInc
  13. cell cycle arrest Source: BHF-UCL
  14. cell death Source: UniProtKB
  15. cell growth Source: InterPro
  16. cell migration Source: BHF-UCL
  17. cell morphogenesis Source: UniProtKB
  18. cell proliferation Source: ProtInc
  19. collagen fibril organization Source: BHF-UCL
  20. dopamine biosynthetic process Source: UniProtKB
  21. embryo development Source: UniProtKB
  22. embryonic digestive tract development Source: DFLAT
  23. epithelial to mesenchymal transition Source: BHF-UCL
  24. extracellular matrix organization Source: Reactome
  25. extrinsic apoptotic signaling pathway Source: BHF-UCL
  26. eye development Source: UniProtKB
  27. face morphogenesis Source: Ensembl
  28. generation of neurons Source: UniProtKB
  29. glial cell migration Source: BHF-UCL
  30. hair follicle development Source: UniProtKB
  31. hair follicle morphogenesis Source: UniProtKB
  32. heart development Source: UniProtKB
  33. heart morphogenesis Source: BHF-UCL
  34. hemopoiesis Source: UniProtKB
  35. menstrual cycle phase Source: BHF-UCL
  36. negative regulation of alkaline phosphatase activity Source: BHF-UCL
  37. negative regulation of cell growth Source: BHF-UCL
  38. negative regulation of cell proliferation Source: UniProtKB
  39. negative regulation of epithelial cell proliferation Source: BHF-UCL
  40. negative regulation of immune response Source: UniProtKB
  41. negative regulation of macrophage cytokine production Source: DFLAT
  42. neuron development Source: UniProtKB
  43. neuron fate commitment Source: Ensembl
  44. neutrophil chemotaxis Source: UniProtKB
  45. odontogenesis Source: BHF-UCL
  46. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  47. platelet activation Source: Reactome
  48. platelet degranulation Source: Reactome
  49. positive regulation of activation-induced cell death of T cells Source: Ensembl
  50. positive regulation of cardioblast differentiation Source: UniProtKB
  51. positive regulation of catagen Source: UniProtKB
  52. positive regulation of cell adhesion mediated by integrin Source: BHF-UCL
  53. positive regulation of cell cycle Source: UniProtKB
  54. positive regulation of cell division Source: UniProtKB-KW
  55. positive regulation of cell growth Source: UniProtKB
  56. positive regulation of cell proliferation Source: UniProtKB
  57. positive regulation of epithelial cell migration Source: BHF-UCL
  58. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  59. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  60. positive regulation of gene expression Source: Ensembl
  61. positive regulation of heart contraction Source: UniProtKB
  62. positive regulation of immune response Source: UniProtKB
  63. positive regulation of integrin biosynthetic process Source: BHF-UCL
  64. positive regulation of neuron apoptotic process Source: UniProtKB
  65. positive regulation of ossification Source: BHF-UCL
  66. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  67. positive regulation of protein secretion Source: BHF-UCL
  68. positive regulation of stress-activated MAPK cascade Source: BHF-UCL
  69. protein phosphorylation Source: BHF-UCL
  70. regulation of transforming growth factor beta2 production Source: BHF-UCL
  71. response to drug Source: UniProtKB
  72. response to hypoxia Source: BHF-UCL
  73. response to progesterone Source: BHF-UCL
  74. response to wounding Source: BHF-UCL
  75. salivary gland morphogenesis Source: BHF-UCL
  76. signal transduction by phosphorylation Source: GOC
  77. SMAD protein import into nucleus Source: BHF-UCL
  78. somatic stem cell division Source: UniProtKB
  79. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  80. wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
SignaLinkiP61812.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:11768. TGFB2.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. endosome Source: Ensembl
  3. extracellular matrix Source: BHF-UCL
  4. extracellular region Source: UniProtKB
  5. extracellular space Source: AgBase
  6. neuronal cell body Source: UniProtKB
  7. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

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.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1045Missing in LDS4. 1 Publication
VAR_068931
Natural varianti299 – 2991R → W in LDS4. 1 Publication
VAR_068932
Natural varianti302 – 3021R → C in LDS4. 1 Publication
VAR_068933
Natural varianti338 – 3381P → H in LDS4. 1 Publication
VAR_068934

Keywords - Diseasei

Aortic aneurysm, Disease mutation

Organism-specific databases

MIMi614816. phenotype.
Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
708. Peters anomaly.
PharmGKBiPA36482.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 302282Latency-associated peptidePRO_0000033784Add
BLAST
Chaini303 – 414112Transforming growth factor beta-2PRO_0000033785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi309 ↔ 318
Disulfide bondi317 ↔ 380
Disulfide bondi346 ↔ 411
Disulfide bondi350 ↔ 413
Disulfide bondi379 – 379Interchain

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

MaxQBiP61812.
PaxDbiP61812.
PRIDEiP61812.

PTM databases

PhosphoSiteiP61812.

Miscellaneous databases

PMAP-CutDBP61812.

Expressioni

Gene expression databases

BgeeiP61812.
CleanExiHS_TGFB2.
GenevestigatoriP61812.

Organism-specific databases

HPAiHPA049818.

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.By similarity1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112900. 10 interactions.
DIPiDIP-5936N.
IntActiP61812. 2 interactions.
STRINGi9606.ENSP00000355896.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi306 – 3094Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi323 – 3253Combined sources
Helixi326 – 3305Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi339 – 3424Combined sources
Beta strandi345 – 3473Combined sources
Beta strandi354 – 3563Combined sources
Helixi359 – 37012Combined sources
Helixi372 – 3743Combined sources
Beta strandi379 – 3824Combined sources
Beta strandi384 – 39411Combined sources
Beta strandi397 – 40812Combined sources
Beta strandi411 – 4144Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TFGX-ray1.95A303-414[»]
2TGIX-ray1.80A303-414[»]
4KXZX-ray2.83A/B/D/E303-414[»]
ProteinModelPortaliP61812.
SMRiP61812. Positions 21-414.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61812.

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG269146.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000290198.
HOVERGENiHBG074115.
InParanoidiP61812.
KOiK13376.
OMAiENAIPPT.
OrthoDBiEOG70GMFT.
PhylomeDBiP61812.
TreeFamiTF318514.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. 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]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PIRSFiPIRSF001787. TGF-beta. 1 hit.
PRINTSiPR01423. TGFBETA.
PR01425. TGFBETA2.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321F → L in AAA61162. (PubMed:1764261)Curated
Sequence conflicti116 – 1161Missing in AAA50405. (PubMed:2850146)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911R → H.2 Publications
Corresponds to variant rs10482721 [ dbSNP | Ensembl ].
VAR_012708
Natural varianti100 – 1045Missing in LDS4. 1 Publication
VAR_068931
Natural varianti207 – 2071V → L.1 Publication
Corresponds to variant rs10482810 [ dbSNP | Ensembl ].
VAR_018923
Natural varianti299 – 2991R → W in LDS4. 1 Publication
VAR_068932
Natural varianti302 – 3021R → C in LDS4. 1 Publication
VAR_068933
Natural varianti338 – 3381P → H in LDS4. 1 Publication
VAR_068934

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei116 – 1161N → TVCPVVTTPSGSVGSLCSRQ SQVLCGYLD in isoform B. 3 PublicationsVSP_006417

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_001135599.2. [P61812-2]
NP_003229.1. NM_003238.3. [P61812-1]
UniGeneiHs.133379.

Genome annotation databases

EnsembliENST00000366929; ENSP00000355896; ENSG00000092969. [P61812-2]
ENST00000366930; ENSP00000355897; ENSG00000092969. [P61812-1]
GeneIDi7042.
KEGGihsa:7042.
UCSCiuc001hlm.3. human.
uc001hln.3. human. [P61812-2]

Polymorphism databases

DMDMi48429157.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

TGF beta-2 entry

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 .
CCDSi CCDS1521.1.
CCDS44318.1. [P61812-2 ]
PIRi A29478. B31249.
S06216. A31249.
RefSeqi NP_001129071.1. NM_001135599.2. [P61812-2 ]
NP_003229.1. NM_003238.3. [P61812-1 ]
UniGenei Hs.133379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TFG X-ray 1.95 A 303-414 [» ]
2TGI X-ray 1.80 A 303-414 [» ]
4KXZ X-ray 2.83 A/B/D/E 303-414 [» ]
ProteinModelPortali P61812.
SMRi P61812. Positions 21-414.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112900. 10 interactions.
DIPi DIP-5936N.
IntActi P61812. 2 interactions.
STRINGi 9606.ENSP00000355896.

PTM databases

PhosphoSitei P61812.

Polymorphism databases

DMDMi 48429157.

Proteomic databases

MaxQBi P61812.
PaxDbi P61812.
PRIDEi P61812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366929 ; ENSP00000355896 ; ENSG00000092969 . [P61812-2 ]
ENST00000366930 ; ENSP00000355897 ; ENSG00000092969 . [P61812-1 ]
GeneIDi 7042.
KEGGi hsa:7042.
UCSCi uc001hlm.3. human.
uc001hln.3. human. [P61812-2 ]

Organism-specific databases

CTDi 7042.
GeneCardsi GC01P218519.
GeneReviewsi TGFB2.
HGNCi HGNC:11768. TGFB2.
HPAi HPA049818.
MIMi 190220. gene.
614816. phenotype.
neXtProti NX_P61812.
Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
708. Peters anomaly.
PharmGKBi PA36482.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG269146.
GeneTreei ENSGT00760000119112.
HOGENOMi HOG000290198.
HOVERGENi HBG074115.
InParanoidi P61812.
KOi K13376.
OMAi ENAIPPT.
OrthoDBi EOG70GMFT.
PhylomeDBi P61812.
TreeFami TF318514.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
SignaLinki P61812.

Miscellaneous databases

ChiTaRSi TGFB2. human.
EvolutionaryTracei P61812.
GeneWikii TGF_beta_2.
GenomeRNAii 7042.
NextBioi 27517.
PMAP-CutDB P61812.
PROi P61812.
SOURCEi Search...

Gene expression databases

Bgeei P61812.
CleanExi HS_TGFB2.
Genevestigatori P61812.

Family and domain databases

Gene3Di 2.10.90.10. 1 hit.
InterProi IPR029034. 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 ]
PANTHERi PTHR11848. PTHR11848. 1 hit.
Pfami PF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view ]
PIRSFi PIRSF001787. TGF-beta. 1 hit.
PRINTSi PR01423. TGFBETA.
PR01425. TGFBETA2.
SMARTi SM00204. TGFB. 1 hit.
[Graphical view ]
SUPFAMi SSF57501. SSF57501. 1 hit.
PROSITEi PS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: VARIANTS LDS4 100-ALA--TYR-104 DEL; TRP-299; CYS-302 AND HIS-338.

Entry informationi

Entry nameiTGFB2_HUMAN
AccessioniPrimary (citable) accession number: P61812
Secondary accession number(s): B4DKC5
, P08112, Q15579, Q15581, Q4VAV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 26, 2014
This is version 129 of the entry and version 1 of the sequence. [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

External Data

Dasty 3