TGFBR2

Transformirajući faktor rasta beta receptor 2 ektodomena
Transformirajući faktor rasta beta receptor 2 ektodomena
	<img src="//upload.wikimedia.org/wikipedia/commons/thumb/3/39/PDB_1m9z_EBI.jpg/220px-PDB_1m9z_EBI.jpg" decoding="async" width="220" height="165" class="mw-file-element" data-file-width="800" data-file-height="600"> Kristalna struktura ljudskog domena vezanja liganda za receptor tgf-beta tipa ii
Identifikatori
Simbol	ecTbetaR2

TGFBR2
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1KTZ, 1M9Z, 1PLO, 2PJY, 3KFD, 4P7U, 4XJJ, 5E92, 5E91, 5E8V, 5E8Y
Identifikatori
Aliasi	TGFBR2
Vanjski ID-jevi	OMIM: 190182 MGI: 98729 HomoloGene: 2435 GeneCards: TGFBR2
Lokacija gena (čovjek)
Hrom.	Hromosom 3 (čovjek)
Kraj	30,694,142 bp
Lokacija gena (miš)
Hrom.	Hromosom 9 (miš)
Kraj	116,004,428 bp
Obrazac RNK ekspresije
	; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• transforming growth factor beta-activated receptor activity; • kinase activity; • ATP binding; • type III transforming growth factor beta receptor binding; • protein kinase activity; • transforming growth factor beta receptor activity, type II; • vezivanje iona metala; • protein serine/threonine kinase activity; • aktivnost sa transferazom; • type I transforming growth factor beta receptor binding; • mitogen-activated protein kinase kinase kinase binding; • GO:0001948, GO:0016582 vezivanje za proteine; • SMAD binding; • nucleotide binding; • glycosaminoglycan binding; • transforming growth factor beta binding; • transmembrane receptor protein serine/threonine kinase activity; • signaling receptor activity; • growth factor binding;
Ćelijska komponenta	• citoplazma; • citosol; • membrana; • Kaveole; • cell surface; • Lipidni splav; • integral component of membrane; • receptor complex; • ćelijska membrana; • integral component of plasma membrane; • external side of plasma membrane;
Biološki proces	• growth plate cartilage development; • response to cholesterol; • lens fiber cell apoptotic process; • response to steroid hormone; • positive regulation of T cell tolerance induction; • receptor-mediated endocytosis; • response to organic substance; • Vaskulogeneza; • protein phosphorylation; • positive regulation of B cell tolerance induction; • positive regulation of reactive oxygen species metabolic process; • blood vessel development; • positive regulation of mesenchymal cell proliferation; • animal organ regeneration; • animal organ morphogenesis; • transforming growth factor beta receptor signaling pathway; • embryo implantation; • negative regulation of cell population proliferation; • GO:0097285 apoptoza; • pathway-restricted SMAD protein phosphorylation; • common-partner SMAD protein phosphorylation; • bronchus morphogenesis; • lung development; • response to mechanical stimulus; • positive regulation of epithelial cell migration; • in utero embryonic development; • negative regulation of transforming growth factor beta receptor signaling pathway; • heart development; • cartilage development; • positive regulation of tolerance induction to self antigen; • branching involved in blood vessel morphogenesis; • positive regulation of skeletal muscle tissue regeneration; • Ježev signalni put; • negative regulation of cardiac muscle cell proliferation; • Notch signaling pathway; • Ćelijska diferencijacija; • Fosforilacija; • response to nutrient; • mammary gland morphogenesis; • Zarastanje rana; • response to glucose; • positive regulation of epithelial to mesenchymal transition; • positive regulation of angiogenesis; • response to estrogen; • Gastrulacija; • Regulacija ekspresije gena; • embryonic cranial skeleton morphogenesis; • peptidyl-threonine phosphorylation; • trachea formation; • lung lobe morphogenesis; • positive regulation of smooth muscle cell proliferation; • lung morphogenesis; • GO:1904578 response to organic cyclic compound; • trachea morphogenesis; • GO:0010260 starenje; • myeloid dendritic cell differentiation; • bronchus development; • brain development; • transmembrane receptor protein serine/threonine kinase signaling pathway; • lens development in camera-type eye; • regulation of cell population proliferation; • GO:0035404 peptidyl-serine phosphorylation; • positive regulation of cell population proliferation; • embryonic hemopoiesis; • growth plate cartilage chondrocyte growth; • regulation of growth; • positive regulation of NK T cell differentiation; • digestive tract development; • activation of protein kinase activity; • response to hypoxia; • heart looping; • outflow tract septum morphogenesis; • membranous septum morphogenesis; • outflow tract morphogenesis; • atrioventricular valve morphogenesis; • tricuspid valve morphogenesis; • cardiac left ventricle morphogenesis; • endocardial cushion fusion; • ventricular septum morphogenesis; • positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; • cell proliferation involved in endocardial cushion morphogenesis; • positive regulation of CD4-positive, alpha-beta T cell proliferation; • superior endocardial cushion morphogenesis; • inferior endocardial cushion morphogenesis; • miRNA transport; • secondary palate development; • pattern specification process;
	Izvori:Amigo / QuickGO
Ortolozi
	7048
	21813
	ENSG00000163513
	ENSMUSG00000032440
	P37173
	Q62312
	NM_001024847; NM_003242
	NM_009371; NM_029575
	NP_001020018; NP_003233
	NP_033397; NP_083851
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Beta receptor II transformirajućeg faktora rasta (70/80kDa) je beta receptor TGF. TGFBR2 je ljudski gen.

To je gen supresije tumora.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 567 aminokiselina, a molekulska težina 645.68 Da.^[6]

10	20	30	40	50
MGRGLLRGLW	PLHIVLWTRI	ASTIPPHVQK	SVNNDMIVTD	NNGAVKFPQL
CKFCDVRFST	CDNQKSCMSN	CSITSICEKP	QEVCVAVWRK	NDENITLETV
CHDPKLPYHD	FILEDAASPK	CIMKEKKKPG	ETFFMCSCSS	DECNDNIIFS
EEYNTSNPDL	LLVIFQVTGI	SLLPPLGVAI	SVIIIFYCYR	VNRQQKLSST
WETGKTRKLM	EFSEHCAIIL	EDDRSDISST	CANNINHNTE	LLPIELDTLV
GKGRFAEVYK	AKLKQNTSEQ	FETVAVKIFP	YEEYASWKTE	KDIFSDINLK
HENILQFLTA	EERKTELGKQ	YWLITAFHAK	GNLQEYLTRH	VISWEDLRKL
GSSLARGIAH	LHSDHTPCGR	PKMPIVHRDL	KSSNILVKND	LTCCLCDFGL
SLRLDPTLSV	DDLANSGQVG	TARYMAPEVL	ESRMNLENVE	SFKQTDVYSM
ALVLWEMTSR	CNAVGEVKDY	EPPFGSKVRE	HPCVESMKDN	VLRDRGRPEI
PSFWLNHQGI	QMVCETLTEC	WDHDPEARLT	AQCVAERFSE	LEHLDRLSGR
SCSEEKIPED	GSLNTTK

Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

Arhitektura domena

TGF beta receptor 2 sastoji se od C-terminal a domena protein-kinaze i N-terminalnog ektodomena. Ektodomen se sastoji od kompaktnog nabora koji sadrži devet beta-lanaca i jedan alfa-heliks stabiliziran mrežom od šest unutrašnjih lanaca disulfidne veze. Topologija presavijanja uključuje središnji petolančani antiparalelni beta-list, u središtu dugačak osam ostataka, prekriven drugim slojem koji se sastoji od dva segmenta lančanih antiparalelnih beta-listova (beta1-beta4, beta3-beta9).^[7]

Funkcija

Ovaj gen kodira člana porodice serin / treonin protein kinaza i potporodice TGFB receptora. Kodirani protein je transmembranski protein koji ima domen protein-kinaze, tvori heterodimerni kompleks sa drugim receptorskim proteinom i veže TGF-beta. Ovaj kompleks receptora/liganda fosforilira proteine, koji zatim ulaze u jedro i regulišu transkripciju podskupine gena povezanih sa ffjska proliferacija|proliferacijom ćelija]]. Mutacije u ovom genu povezane su s Marfanovim sindromom, Loeys-Deitzovim sindromom aneurizme aorte, Osler-Weber-Renduovim sindromom i razvojem različitih vrsta tumora. Karakterizirane su alternativno spojene varijante transkripta koje kodiraju različite izoforme.^[8]

Interakcije

Pokazano je da TGF beta receptor 2 interakcije sa:

AP2B1,^[9]
Ciklin B2,^[10]
Endoglin,^[11]^[12]
Član A citosolnog proteina alfa od 90kDa^[13]
STRAP,^[14]^[15]
TGF beta receptor 1,^[16]^[17] and
Transformiirajći faktor rasta beta 3.^[7]^[11]^[18]^[19]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000163513 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000032440 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "TGFBR2 - transforming growth factor, beta receptor II (70/80kDa) - Genetics Home Reference". Arhivirano s originala, 10. 8. 2011. Pristupljeno 7. 9. 2008.
^ "UniProt, P37173". Pristupljeno 18. 7. 2021.
^ ^a ^b Hart 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.
^ "Entrez Gene: TGFBR2 transforming growth factor, beta receptor II (70/80kDa)".
^ 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.
^ 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.
^ ^a ^b Barbara 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.
^ 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. PMID 12015308.
^ 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. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668.
^ 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.
^ Datta PK, Moses HL (maj 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.
^ 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.
^ 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.
^ De Crescenzo G, Pham PL, Durocher Y, O'Connor-McCourt MD (maj 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.
^ 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.

Vanjski linkovi

GeneReviews/NIH/NCBI/UW entry on Thoracic Aortic Aneurysms and Aortic Dissections

Šablon:Geni za supresiju tumora

Ovaj članak uključuje tekst iz javnog domena Pfam i InterPro: IPR015013

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000163513 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000032440 - Ensembl, maj 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.

[urlTGFBR2_-_transforming_growth_factor,_beta_receptor_II_(70/80kDa)_-_Genetics_Home_Reference-5] "TGFBR2 - transforming growth factor, beta receptor II (70/80kDa) - Genetics Home Reference". Arhivirano s originala, 10. 8. 2011. Pristupljeno 7. 9. 2008.

[UniProt-6] "UniProt, P37173". Pristupljeno 18. 7. 2021.

[pmid11850637-7] Hart 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.

[8] "Entrez Gene: TGFBR2 transforming growth factor, beta receptor II (70/80kDa)".

[pmid12429842-9] 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.

[pmid9926943-10] 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.

[pmid9872992-11] Barbara 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.

[pmid12015308-12] 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. PMID 12015308.

[pmid18591668-13] 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. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668.

[pmid9856985-14] 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.

[pmid10757800-15] Datta PK, Moses HL (maj 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.

[pmid7890683-16] 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.

[pmid11102446-17] 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.

[pmid12729750-18] De Crescenzo G, Pham PL, Durocher Y, O'Connor-McCourt MD (maj 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.

[pmid11157754-19] 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.

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Transformirajući faktor rasta beta receptor 2 ektodomena
Kristalna struktura ljudskog domena vezanja liganda za receptor tgf-beta tipa ii
Identifikatori
Simbol	ecTbetaR2