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P61812

- TGFB2_HUMAN

UniProt

P61812 - TGFB2_HUMAN

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
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    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 binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. receptor binding Source: UniProtKB
    7. receptor signaling protein serine/threonine kinase activity Source: BHF-UCL
    8. transforming growth factor beta receptor binding Source: UniProtKB
    9. 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

    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. extracellular matrix Source: BHF-UCL
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: AgBase
    5. neuronal cell body Source: UniProtKB
    6. platelet alpha granule lumen Source: Reactome

    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.
    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 – 3094
    Beta strandi315 – 3206
    Beta strandi323 – 3253
    Helixi326 – 3305
    Beta strandi335 – 3373
    Beta strandi339 – 3424
    Beta strandi345 – 3473
    Beta strandi354 – 3563
    Helixi359 – 37012
    Helixi372 – 3743
    Beta strandi379 – 3824
    Beta strandi384 – 39411
    Beta strandi397 – 40812
    Beta strandi411 – 4144

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TFGX-ray1.95A303-414[»]
    2TGIX-ray1.80A303-414[»]
    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.
    HOGENOMiHOG000290198.
    HOVERGENiHBG074115.
    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

    MHYCVLSAFL ILHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL    50
    TSPPEDYPEP EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA 100
    KEVYKIDMPP FFPSENAIPP TFYRPYFRIV RFDVSAMEKN ASNLVKAEFR 150
    VFRLQNPKAR VPEQRIELYQ ILKSKDLTSP TQRYIDSKVV KTRAEGEWLS 200
    FDVTDAVHEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP NKSEELEARF 250
    AGIDGTSTYT SGDQKTIKST RKKNSGKTPH LLLMLLPSYR LESQQTNRRK 300
    KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC 350
    PYLWSSDTQH SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI 400
    EQLSNMIVKS CKCS 414
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    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.
    HOGENOMi HOG000290198.
    HOVERGENi HBG074115.
    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

    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: October 1, 2014
    This is version 127 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