캐스크

CASK
캐스크
Protein CASK PDB 1kgd.png
사용 가능한 구조물
PDB직교 검색: PDBe RCSB
식별자
별칭CASK, CAGH39, CAMKUG, CMG, FGS4, LIN2, MICPCH, MRXSNA, TNRC8, 칼슘/칼모듈린 의존 세린 단백질 키나아제(MAGUK 계열), 칼슘/칼모듈린 의존 세린 단백질 키나제, HCASK
외부 IDOMIM: 300172 MGI: 1309489 호몰로Gene: 2736 GeneCard: CASK
직교체
종인간마우스
엔트레스

8573

12361

앙상블

ENSG00000147044

ENSMUSG00000031012

유니프로트

O14936

O70589

RefSeq(mRNA)

NM_001126054
NM_001126055
NM_003688
NM_001367721

NM_001284503
NM_001284504
NM_001284505
NM_009806

RefSeq(단백질)

NP_001119526
NP_001119527
NP_003679
NP_001354650

NP_001271432
NP_001271433
NP_001271434
NP_033936

위치(UCSC)Cr X: 41.51 – 41.92MbCr X: 13.38 – 13.72Mb
PubMed 검색[3][4]
위키다타
인간 보기/편집마우스 보기/편집

말초 혈장막 단백질 CASK는 인간에서 CASK 유전자에 의해 암호화된 단백질이다.[5][6]이 유전자는 CMG 2 (CAMKUGI 단백질 2)와 칼슘/칼모둘린 의존성 세린 단백질 키나아제 3 그리고 막 관련 구아닐레이트 키나제 2의 다른 이름으로도 알려져 있다.

유전자

이 유전자는 X염색체의 짧은 팔(Xp11.4)에 위치한다.그것은 길이가 404,253 베이스로 크릭(마이너스) 가닥 위에 놓여 있다.인코딩된 단백질은 분자량이 105,123 Dalton으로 예측된 926개의 아미노산을 가지고 있다.

함수

이 단백질은 시냅스 트랜섬브레인 단백질 앵커링과 이온 채널 밀거래의 역할을 하는 다도메인 비계 단백질이다.그것은 전사 인자 TBR1과 상호작용하고 네우렉신, 싱데칸을 포함한 몇몇 세포 표면 단백질에 결합한다.

임상적 중요성

이 유전자는 특히 폰틴과 소뇌 저포플라시아를 가진 정신지체 및 소두증을 포함한 X연계 정신지체장애에 관련되어 있다.[7][8]

상호작용

CASK는 다음과 상호 작용하는 것으로 나타났다.

참조

  1. ^ a b c GRCh38: 앙상블 릴리스 89: ENSG00000147044 - 앙상블, 2017년 5월
  2. ^ a b c GRCm38: 앙상블 릴리스 89: ENSMUSG000031012 - 앙상블, 2017년 5월
  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. ^ Dimitratos SD, Stathakis DG, Nelson CA, Woods DF, Bryant PJ (Nov 1998). "The location of human CASK at Xp11.4 identifies this gene as a candidate for X-linked optic atrophy". Genomics. 51 (2): 308–309. doi:10.1006/geno.1998.5404. PMID 9722958.
  6. ^ "Entrez Gene: CASK Calcium/calmodulin-dependent serine protein kinase (MAGUK family)".
  7. ^ Tarpey PS, Smith R, Pleasance E, Whibley A, Edkins S, Hardy C, O'Meara S, Latimer C, Dicks E, Menzies A, Stephens P, Blow M, Greenman C, Xue Y, Tyler-Smith C, Thompson D, Gray K, Andrews J, Barthorpe S, Buck G, Cole J, Dunmore R, Jones D, Maddison M, Mironenko T, Turner R, Turrell K, Varian J, West S, Widaa S, Wray P, Teague J, Butler A, Jenkinson A, Jia M, Richardson D, Shepherd R, Wooster R, Tejada MI, Martinez F, Carvill G, Goliath R, de Brouwer AP, van Bokhoven H, Van Esch H, Chelly J, Raynaud M, Ropers HH, Abidi FE, Srivastava AK, Cox J, Luo Y, Mallya U, Moon J, Parnau J, Mohammed S, Tolmie JL, Shoubridge C, Corbett M, Gardner A, Haan E, Rujirabanjerd S, Shaw M, Vandeleur L, Fullston T, Easton DF, Boyle J, Partington M, Hackett A, Field M, Skinner C, Stevenson RE, Bobrow M, Turner G, Schwartz CE, Gecz J, Raymond FL, Futreal PA, Stratton MR (May 2009). "A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation". Nat. Genet. 41 (5): 535–43. doi:10.1038/ng.367. PMC 2872007. PMID 19377476.
  8. ^ Burglen L, Chantot-Bastaraud S, Garel C, Milh M, Touraine R, Zanni G, Petit F, Afenjar A, Goizet C, Barresi S, Coussement A, Ioos C, Lazaro L, Joriot S, Desguerre I, Lacombe D, des Portes V, Bertini E, Siffroi JP, de Villemeur TB, Rodriguez D (2012). "Spectrum of pontocerebellar hypoplasia in 13 girls and boys with CASK mutations: confirmation of a recognizable phenotype and first description of a male mosaic patient". Orphanet Journal of Rare Diseases. 7 (18): 18. doi:10.1186/1750-1172-7-18. PMC 3351739. PMID 22452838.
  9. ^ a b Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA (May 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025.
  10. ^ a b c d Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (April 2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. 279 (18): 19051–63. doi:10.1074/jbc.M400284200. PMID 14960569.
  11. ^ a b Borg JP, Straight SW, Kaech SM, de Taddéo-Borg M, Kroon DE, Karnak D, Turner RS, Kim SK, Margolis B (November 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. doi:10.1074/jbc.273.48.31633. PMID 9822620.
  12. ^ Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, Kroon DE, Turner RS, Watson SJ, Margolis B (February 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. doi:10.1523/JNEUROSCI.19-04-01307.1999. PMID 9952408.
  13. ^ Schuh K, Uldrijan S, Gambaryan S, Roethlein N, Neyses L (March 2003). "Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK". J. Biol. Chem. 278 (11): 9778–83. doi:10.1074/jbc.M212507200. PMID 12511555.
  14. ^ Wang GS, Hong CJ, Yen TY, Huang HY, Ou Y, Huang TN, Jung WG, Kuo TY, Sheng M, Wang TF, Hsueh YP (April 2004). "Transcriptional modification by a CASK-interacting nucleosome assembly protein". Neuron. 42 (1): 113–28. doi:10.1016/S0896-6273(04)00139-4. PMID 15066269.
  15. ^ a b Chetkovich DM, Bunn RC, Kuo SH, Kawasaki Y, Kohwi M, Bredt DS (August 2002). "Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms". J. Neurosci. 22 (15): 6415–25. doi:10.1523/JNEUROSCI.22-15-06415.2002. PMC 6758133. PMID 12151521.
  16. ^ Nix SL, Chishti AH, Anderson JM, Walther Z (December 2000). "hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions". J. Biol. Chem. 275 (52): 41192–200. doi:10.1074/jbc.M002078200. PMID 10993877.
  17. ^ Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (March 2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells". J. Biol. Chem. 276 (12): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739.
  18. ^ Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (September 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". J. Biol. Chem. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
  19. ^ Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z, Luo X (March 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. 328 (2): 517–21. doi:10.1016/j.bbrc.2005.01.014. PMID 15694377.
  20. ^ Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar MG (September 2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin". Am. J. Pathol. 165 (3): 923–36. doi:10.1016/S0002-9440(10)63354-8. PMC 1618613. PMID 15331416.
  21. ^ Fallon L, Moreau F, Croft BG, Labib N, Gu WJ, Fon EA (January 2002). "Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain". J. Biol. Chem. 277 (1): 486–91. doi:10.1074/jbc.M109806200. PMID 11679592.
  22. ^ a b Zhang Y, Luan Z, Liu A, Hu G (May 2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. 497 (2–3): 99–102. doi:10.1016/S0014-5793(01)02450-4. PMID 11377421.
  23. ^ Cohen AR, Woods DF, Marfatia SM, Walther Z, Chishti AH, Anderson JM, Wood DF (July 1998). "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells". J. Cell Biol. 142 (1): 129–38. doi:10.1083/jcb.142.1.129. PMC 2133028. PMID 9660868.

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