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TGF beta receptor 2

From Wikipedia, the free encyclopedia
(Redirected fromTGFBR2)
Protein-coding gene in the species Homo sapiens
TGFBR2
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1KTZ,1M9Z,1PLO,2PJY,3KFD,4P7U,4XJJ,5E92,5E91,5E8V,5E8Y

Identifiers
AliasesTGFBR2, AAT3, FAA3, LDS1B, LDS2, LDS2B, MFS2, RIIC, TAAD2, TGFR-2, TGFbeta-RII, transforming growth factor beta receptor 2, TBR-ii, TBRII
External IDsOMIM:190182;MGI:98729;HomoloGene:2435;GeneCards:TGFBR2;OMA:TGFBR2 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for TGFBR2
Genomic location for TGFBR2
Band3p24.1Start30,606,601bp[1]
End30,694,142bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for TGFBR2
Genomic location for TGFBR2
Band9 F3|9 68.39 cMStart115,913,361bp[2]
End116,004,428bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pericardium

  • tibia

  • parietal pleura

  • epithelium of colon

  • lower lobe of lung

  • visceral pleura

  • vena cava

  • superficial temporal artery

  • cardiac muscle tissue of right atrium

  • synovial joint
Top expressed in
  • left lung lobe

  • gastrula

  • calvaria

  • decidua

  • lymph node

  • stroma of bone marrow

  • sciatic nerve

  • endothelial cell of lymphatic vessel

  • mesenteric lymph nodes

  • molar
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7048

21813

Ensembl

ENSG00000163513

ENSMUSG00000032440

UniProt

P37173

Q62312

RefSeq (mRNA)

NM_001024847
NM_003242

NM_009371
NM_029575

RefSeq (protein)

NP_001020018
NP_003233

NP_033397
NP_083851

Location (UCSC)Chr 3: 30.61 – 30.69 MbChr 9: 115.91 – 116 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transforming growth factor, beta receptor II (70/80kDa) is aTGF beta receptor.TGFBR2 is its humangene.

It is atumor suppressor gene.[5]

Function

[edit]

This gene encodes a member of theserine/threonine protein kinase family and the TGFB receptor subfamily. The encoded protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in this gene have been associated withMarfan syndrome,Loeys-Deitz aortic aneurysm syndrome,Osler–Weber–Rendu syndrome, and the development of various types of tumors. At least 73 disease-causing mutations in this gene have been discovered.[6] Alternatively spliced transcript variants encoding different isoforms have been characterized.[7]

Interactions

[edit]

TGF beta receptor 2 has been shown tointeract with:

Domain architecture

[edit]
Protein domain
Transforming growth factor beta receptor 2 ectodomain
crystal structure of human tgf-beta type ii receptor ligand binding domain
Identifiers
SymbolecTbetaR2
PfamPF08917
InterProIPR015013
Available protein structures:
Pfam  structures /ECOD  
PDBRCSB PDB;PDBe;PDBj
PDBsumstructure summary

TGF beta receptor 2 consists of aC-terminalprotein kinase domain and anN-terminal ectodomain. The ectodomain consists of a compactfold containing nine beta-strands and a singlehelix stabilised by a network of six intra stranddisulphide bonds. Thefolding topology includes a central five-strandedantiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallelbeta-sheets (beta1-beta4, beta3-beta9).[18]

See also

[edit]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000163513Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000032440Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^"TGFBR2 - transforming growth factor, beta receptor II (70/80kDa) - Genetics Home Reference". Archived fromthe original on 2011-08-10. Retrieved2008-09-07.
  6. ^Šimčíková D, Heneberg P (December 2019)."Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases".Scientific Reports.9 (1): 18577.Bibcode:2019NatSR...918577S.doi:10.1038/s41598-019-54976-4.PMC 6901466.PMID 31819097.
  7. ^"Entrez Gene: TGFBR2 transforming growth factor, beta receptor II (70/80kDa)".
  8. ^Yao D, Ehrlich M, Henis YI, Leof EB (Nov 2002)."Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit".Molecular Biology of the Cell.13 (11):4001–12.doi:10.1091/mbc.02-07-0104.PMC 133610.PMID 12429842.
  9. ^Liu JH, Wei S, Burnette PK, Gamero AM, Hutton M, Djeu JY (Jan 1999)."Functional association of TGF-beta receptor II with cyclin B".Oncogene.18 (1):269–75.doi:10.1038/sj.onc.1202263.PMID 9926943.
  10. ^abBarbara NP, Wrana JL, Letarte M (Jan 1999)."Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily".The Journal of Biological Chemistry.274 (2):584–94.doi:10.1074/jbc.274.2.584.PMID 9872992.
  11. ^Guerrero-Esteo M, Sanchez-Elsner T, Letamendia A, Bernabeu C (Aug 2002)."Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II".The Journal of Biological Chemistry.277 (32):29197–209.doi:10.1074/jbc.M111991200.hdl:10261/167807.PMID 12015308.
  12. ^Wrighton KH, Lin X, Feng XH (Jul 2008)."Critical regulation of TGFbeta signaling by Hsp90".Proceedings of the National Academy of Sciences of the United States of America.105 (27):9244–9.Bibcode:2008PNAS..105.9244W.doi:10.1073/pnas.0800163105.PMC 2453700.PMID 18591668.
  13. ^Datta PK, Chytil A, Gorska AE, Moses HL (Dec 1998)."Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling".The Journal of Biological Chemistry.273 (52):34671–4.doi:10.1074/jbc.273.52.34671.PMID 9856985.
  14. ^Datta PK, Moses HL (May 2000)."STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling".Molecular and Cellular Biology.20 (9):3157–67.doi:10.1128/mcb.20.9.3157-3167.2000.PMC 85610.PMID 10757800.
  15. ^Kawabata M, Chytil A, Moses HL (Mar 1995)."Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor".The Journal of Biological Chemistry.270 (10):5625–30.doi:10.1074/jbc.270.10.5625.PMID 7890683.
  16. ^Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti MP (Mar 2001)."Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor".The Journal of Biological Chemistry.276 (9):6727–38.doi:10.1074/jbc.M008340200.PMID 11102446.
  17. ^De Crescenzo G, Pham PL, Durocher Y, O'Connor-McCourt MD (May 2003). "Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding".Journal of Molecular Biology.328 (5):1173–83.doi:10.1016/s0022-2836(03)00360-7.PMID 12729750.
  18. ^abHart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP (Mar 2002). "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex".Nature Structural Biology.9 (3):203–8.doi:10.1038/nsb766.PMID 11850637.S2CID 13322593.
  19. ^Rotzer D, Roth M, Lutz M, Lindemann D, Sebald W, Knaus P (Feb 2001)."Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor".The EMBO Journal.20 (3):480–90.doi:10.1093/emboj/20.3.480.PMC 133482.PMID 11157754.

External links

[edit]
PDB gallery
  • 1ktz: Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3
    1ktz: Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3
  • 1m9z: CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN
    1m9z: CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN
  • 1plo: TRANSFORMING GROWTH FACTOR-BETA TYPE II RECEPTOR EXTRACELLULAR DOMAIN
    1plo: TRANSFORMING GROWTH FACTOR-BETA TYPE II RECEPTOR EXTRACELLULAR DOMAIN
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This article incorporates text from the public domainPfam andInterPro:IPR015013
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