DLGAP1 식별자 별칭 DLGAP1 외부 ID OMIM : 605445 MGI : 1346065 호몰로진 : 31258 GeneCard : DLGAP1 직교체 종 인간 마우스 엔트레스 앙상블 유니프로트 RefSeq(mRNA) RefSeq(단백질) 위치(UCSC) Cr 18: 3.5 – 4.46Mb Cr 17: 70.28 – 71.13Mb PubMed 검색[3] [4] 위키다타
GKAP (Guanylate kinase associated protectrome , GKAP)라고도 알려진 디스크 거대 연관 단백질 1 (DAP-1 )은 인간에서 DLGAP1 유전자 에 의해 인코딩되는 단백질 이다.DAP-1은 뇌의 시냅토솜 준비에서 고농축되며, 시냅스 후 밀도 에 존재하는 것으로 알려져 있다.[5]
함수 이 유전자는 guanylate kinase 관련 단백질(GKAP)이라고 불리는 단백질을 인코딩한다. GKAP는 SHANK 와 PSD-95 단백질에 결합하여 뉴런의 사후 시냅스 밀도의 조립을 용이하게 한다.[6] Dlgap1은 14-amino-acid repeat 5개와 Pro-rich 3개를 가지고 있다.
상호작용 DLGAP1은 다음과 상호 작용하는 것으로 나타났다.
PSD95와 S-SCAM과의 상호작용은 GUM 영역에[13]
참조 ^ a b c GRCh38: 앙상블 릴리스 89: ENSG00000170579 - 앙상블 , 2017년 5월^ a b c GRCm38: 앙상블 릴리스 89: ENSMUSG00000003279 - 앙상블 , 2017년 5월^ "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 .^ "Entrez Gene: DLGAP1 discs, large (Drosophila) homolog-associated protein 1" .^ Hines RM, El-Husseini A (2006). "Mechanisms that regulate neuronal protein clustering at the synapse". In El-Husseini A, Dityatev A (eds.). Molecular mechanisms of synaptogenesis . Berlin: Springer. pp. 72–75. ISBN 978-0-387-32560-6 ^ a b Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y (May 1997). "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density" . J. Biol. Chem . 272 (18): 11943–51. doi :10.1074/jbc.272.18.11943 PMID 9115257 . ^ a b Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (June 1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95" . Genes Cells . 2 (6): 415–24. doi :10.1046/j.1365-2443.1997.1310329.x PMID 9286858 . ^ a b Wu H, Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger ED, Garner CC (November 2000). "Intramolecular interactions regulate SAP97 binding to GKAP" . EMBO J . 19 (21): 5740–51. doi :10.1093/emboj/19.21.5740 . PMC 305801 PMID 11060025 . ^ a b Kim E, Naisbitt S, Hsueh YP, Rao A, Rothschild A, Craig AM, Sheng M (February 1997). "GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules" . J. Cell Biol . 136 (3): 669–78. doi :10.1083/jcb.136.3.669 . PMC 2134290 PMID 9024696 . ^ a b c d Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (June 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein" . J. Neurosci . 20 (12): 4524–34. doi :10.1523/JNEUROSCI.20-12-04524.2000 PMC 6772433 PMID 10844022 . ^ a b Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED (October 1999). "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family". Biochem. Biophys. Res. Commun . 264 (1): 247–52. doi :10.1006/bbrc.1999.1489 . PMID 10527873 . ^ Hirao K, Hata Y, Ide N, Takeuchi M, Irie M, Yao I, et al. (1998). "A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins" . J Biol Chem . 273 (33): 21105–10. doi :10.1074/jbc.273.33.21105 PMID 9694864 . 추가 읽기 Kim E, Naisbitt S, Hsueh YP, et al. (1997). "GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules" . J. Cell Biol . 136 (3): 669–78. doi :10.1083/jcb.136.3.669 . PMC 2134290 PMID 9024696 . Takeuchi M, Hata Y, Hirao K, et al. (1997). "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density" . J. Biol. Chem . 272 (18): 11943–51. doi :10.1074/jbc.272.18.11943 PMID 9115257 . Naisbitt S, Kim E, Weinberg RJ, et al. (1997). "Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90" . J. Neurosci . 17 (15): 5687–96. doi :10.1523/JNEUROSCI.17-15-05687.1997 PMC 6573205 PMID 9221768 . Satoh K, Yanai H, Senda T, et al. (1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95" . Genes Cells . 2 (6): 415–24. doi :10.1046/j.1365-2443.1997.1310329.x PMID 9286858 . Hirao K, Hata Y, Ide N, et al. (1998). "A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins" . J. Biol. Chem . 273 (33): 21105–10. doi :10.1074/jbc.273.33.21105 PMID 9694864 . Deguchi M, Hata Y, Takeuchi M, et al. (1998). "BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein" . J. Biol. Chem . 273 (41): 26269–72. doi :10.1074/jbc.273.41.26269 PMID 9756850 . Kawabe H, Hata Y, Takeuchi M, et al. (1999). "nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP)" . J. Biol. Chem . 274 (43): 30914–8. doi :10.1074/jbc.274.43.30914 PMID 10521485 . Boeckers TM, Winter C, Smalla KH, et al. (1999). "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family". Biochem. Biophys. Res. Commun . 264 (1): 247–52. doi :10.1006/bbrc.1999.1489 . PMID 10527873 . Naisbitt S, Valtschanoff J, Allison DW, et al. (2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein" . J. Neurosci . 20 (12): 4524–34. doi :10.1523/JNEUROSCI.20-12-04524.2000 PMC 6772433 PMID 10844022 . Wu H, Reissner C, Kuhlendahl S, et al. (2000). "Intramolecular interactions regulate SAP97 binding to GKAP" . EMBO J . 19 (21): 5740–51. doi :10.1093/emboj/19.21.5740 . PMC 305801 PMID 11060025 . Haraguchi K, Satoh K, Yanai H, et al. (2001). "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase" . Genes Cells . 5 (11): 905–911. doi :10.1046/j.1365-2443.2000.00374.x PMID 11122378 . Lo KW, Naisbitt S, Fan JS, et al. (2001). "The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif" . J. Biol. Chem . 276 (17): 14059–66. doi :10.1074/jbc.M010320200 PMID 11148209 . Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences" . Proc. Natl. Acad. Sci. U.S.A . 99 (26): 16899–903. doi :10.1073/pnas.242603899 PMC 139241 PMID 12477932 . Im YJ, Lee JH, Park SH, et al. (2004). "Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization" . J. Biol. Chem . 278 (48): 48099–104. doi :10.1074/jbc.M306919200 PMID 12954649 . Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain" . Mol. Cell. Proteomics . 3 (11): 1093–101. doi :10.1074/mcp.M400085-MCP200 PMID 15345747 . Suzuki T, Li W, Zhang JP, et al. (2005). "A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins". Eur. J. Neurosci . 21 (2): 339–50. doi :10.1111/j.1460-9568.2005.03856.x . PMID 15673434 . S2CID 28773407 . Sabio G ; Arthur JS; Kuma Y; et al. (2005). "p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP" . EMBO J . 24 (6): 1134–45. doi :10.1038/sj.emboj.7600578 . PMC 556394 PMID 15729360 .
