EPH receptor A2

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EPH receptor A2

PDB prikaz baziran na 1mqb.
Dostupne strukture
1MQB, 2E8N, 2K9Y, 2KSO, 2X10, 2X11, 3C8X, 3CZU, 3FL7, 3HEI, 3HPN, 3KKA, 3MBW, 3MX0, 3SKJ, 4P2K, 4P2W, 4PDO
Identifikatori
SimboliEPHA2; ARCC2; CTPA; CTPP1; CTRCT6; ECK
Vanjski IDOMIM: 176946 MGI: 95278 HomoloGene: 20929 GeneCards: EPHA2 Gene
EC broj2.7.10.1
Ontologija gena
Molekulska funkcija aktivnost transmembranske receptorske proteinske tirozinske kinaze
aktivnost efrinskog receptora
proteinsko vezivanje
Ćelijska komponenta ćelijska membrana
integralna komponenta ćelijske membrane
fokalna adhezija
Biološki proces razviće skeletalnog sistema
angiogeneza
vaskulogeneza
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez196913836
EnsemblENSG00000142627ENSMUSG00000006445
UniProtP29317Q03145
Ref. Sekv. (iRNK)NM_004431NM_010139
Ref. Sekv. (protein)NP_004422NP_034269
Lokacija (UCSC)Chr 1:
16.45 - 16.48 Mb
Chr 4:
141.3 - 141.33 Mb
PubMed pretraga[1][2]

EPH receptor A2 (efrinski receptor 2 tipa A) protein je koji je kod ljudi kodiran EPHA2 genom.[1][2]

Ovaj gen je pripadnik grupe efrinskih receptora iz familije proteinskih turozinskih kinaza. EPH i EPH-srodni receptori uzimaju učešća u posredovanju događaja razvića, posebno u nervnom sistemu. Receptori EPH podfamilije tipično imaju jedan kinazni domen, ekstracelularni region koji sadrži domen bogat cisteinom i dva ponavljanja fibronektinskog tipa III. Efrinski receptori se dele u dve grupe na bazi sličnosti sekvenci njihovih ekstracelularnih domena i njihovih afiniteta vezivanja liganda efrina A i efrina B.[2]

Interakcije

EPH receptor A2 formira interakcije sa PIK3R1,[3] Grb2,[4] ACP1[5] i SHC1.[4]

Reference

  1. Sulman EP, Tang XX, Allen C, Biegel JA, Pleasure DE, Brodeur GM, Ikegaki N (April 1997). „ECK, a human EPH-related gene, maps to 1p36.1, a common region of alteration in human cancers”. Genomics 40 (2): 371–4. DOI:10.1006/geno.1996.4569. PMID 9119409. 
  2. 2,0 2,1 „Entrez Gene: EPHA2 EPH receptor A2”. 
  3. Pandey, A; Lazar D F; Saltiel A R; Dixit V M (December 1994). „Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity”. J. Biol. Chem. (UNITED STATES) 269 (48): 30154–7. ISSN 0021-9258. PMID 7982920. 
  4. 4,0 4,1 Pratt, Rebecca L; Kinch Michael S (October 2002). „Activation of the EphA2 tyrosine kinase stimulates the MAP/ERK kinase signaling cascade”. Oncogene (England) 21 (50): 7690–9. DOI:10.1038/sj.onc.1205758. ISSN 0950-9232. PMID 12400011. 
  5. Kikawa, Keith D; Vidale Derika R; Van Etten Robert L; Kinch Michael S (October 2002). „Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation”. J. Biol. Chem. (United States) 277 (42): 39274–9. DOI:10.1074/jbc.M207127200. ISSN 0021-9258. PMID 12167657. 

Literatura

  • Flanagan JG, Vanderhaeghen P (1998). „The ephrins and Eph receptors in neural development.”. Annu. Rev. Neurosci. 21: 309–45. DOI:10.1146/annurev.neuro.21.1.309. PMID 9530499. 
  • Zhou R (1998). „The Eph family receptors and ligands.”. Pharmacol. Ther. 77 (3): 151–81. DOI:10.1016/S0163-7258(97)00112-5. PMID 9576626. 
  • Holder N, Klein R (1999). „Eph receptors and ephrins: effectors of morphogenesis.”. Development 126 (10): 2033–44. PMID 10207129. 
  • Wilkinson DG (2000). „Eph receptors and ephrins: regulators of guidance and assembly.”. Int. Rev. Cytol. 196: 177–244. DOI:10.1016/S0074-7696(00)96005-4. PMID 10730216. 
  • Xu Q, Mellitzer G, Wilkinson DG (2001). „Roles of Eph receptors and ephrins in segmental patterning.”. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 355 (1399): 993–1002. DOI:10.1098/rstb.2000.0635. PMC 1692797. PMID 11128993. 
  • Wilkinson DG (2001). „Multiple roles of EPH receptors and ephrins in neural development.”. Nat. Rev. Neurosci. 2 (3): 155–64. DOI:10.1038/35058515. PMID 11256076. 
  • Kinch MS, Carles-Kinch K (2003). „Overexpression and functional alterations of the EphA2 tyrosine kinase in cancer.”. Clin. Exp. Metastasis 20 (1): 59–68. DOI:10.1023/A:1022546620495. PMID 12650608. 
  • Walker-Daniels J, Hess AR, Hendrix MJ, Kinch MS (2003). „Differential regulation of EphA2 in normal and malignant cells.”. Am. J. Pathol. 162 (4): 1037–42. DOI:10.1016/S0002-9440(10)63899-0. PMC 1851246. PMID 12651595. 
  • Lindberg RA, Hunter T (1991). „cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases”. Mol. Cell. Biol. 10 (12): 6316–24. PMC 362907. PMID 2174105. 
  • Pandey A, Shao H, Marks RM, et al. (1995). „Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-alpha-induced angiogenesis”. Science 268 (5210): 567–9. DOI:10.1126/science.7536959. PMID 7536959. 
  • Pandey A, Duan H, Dixit VM (1995). „Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase”. J. Biol. Chem. 270 (33): 19201–4. DOI:10.1074/jbc.270.33.19201. PMID 7543898. 
  • Ruiz JC, Robertson EJ (1994). „The expression of the receptor-protein tyrosine kinase gene, eck, is highly restricted during early mouse development”. Mech. Dev. 46 (2): 87–100. DOI:10.1016/0925-4773(94)90078-7. PMID 7918100. 
  • Davis S, Gale NW, Aldrich TH, et al. (1994). „Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity”. Science 266 (5186): 816–9. DOI:10.1126/science.7973638. PMID 7973638. 
  • Pandey A, Lazar DF, Saltiel AR, Dixit VM (1994). „Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity”. J. Biol. Chem. 269 (48): 30154–7. PMID 7982920. 
  • Ganju P, Shigemoto K, Brennan J, et al. (1994). „The Eck receptor tyrosine kinase is implicated in pattern formation during gastrulation, hindbrain segmentation and limb development”. Oncogene 9 (6): 1613–24. PMID 8183555. 
  • Gale NW, Holland SJ, Valenzuela DM, et al. (1996). „Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis”. Neuron 17 (1): 9–19. DOI:10.1016/S0896-6273(00)80276-7. PMID 8755474. 
  • Kozlosky CJ, VandenBos T, Park L, et al. (1997). „LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain”. Cytokine 9 (8): 540–9. DOI:10.1006/cyto.1997.0199. PMID 9245480. 
  • Ephnomenclaturecommittee, (1997). „Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee”. Cell 90 (3): 403–4. DOI:10.1016/S0092-8674(00)80500-0. PMID 9267020. 
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PDB Galerija
1mqb: Kristalna struktura efrinske A2 (ephA2) receptorske proteinske kinaze
1mqb: Kristalna struktura efrinske A2 (ephA2) receptorske proteinske kinaze  
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FGFR1 • FGFR2 • FGFR3 • FGFR4
VEGFR1 • VEGFR2 • VEGFR3 • VEGFR4
MET • RON
NTRK1 • NTRK2 • NTRK3
EPH receptorska familija
EPHA1 • EPHA2 • EPHA3 • EPHA4 • EPHA5 • EPHA6 • EPHA7 • EPHA8 • EPHB1 • EPHB2 • EPHB3 • EPHB4 • EPHB5 • EPHB6 • EPHX
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DDR receptorska familija
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ROS1
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AATYK • AATYK2 • AATYK3
AXL receptorska familija
AXL • MER • TYRO3
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nekategorisani
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ABL familija
ABL1 • ARG
ACK familija
ACK1 • TNK1
CSK familija
CSK • MATK
FAK familija
FAK • PYK2
FES familija
FES • FER
FRK familija
FRK • BRK • SRMS
JAK familija
JAK1 • JAK2 • JAK3 • TYK2
SRC-A familija
SRC • FGR • FYN • YES1
SRC-B familija
BLK • HCK • LCK • LYN
TEC familija
TEC • BMX • BTK • ITK • TXK
SYK familija
SYK • ZAP70
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6