RAB3A

RAB3A
식별자
에일리어스	RAB3A, 구성원 RAS 종양 유전자 패밀리
외부 ID	OMIM: 179490 MGI: 9784 HomoloGene: 20629 GenCard: RAB3A
유전자 위치(인간)
크르.	19번 염색체(인간)
끝.	18,440,042 bp
유전자 위치(마우스)
크르.	8번 염색체(쥐)
끝.	71,211,323 bp
RNA발현패턴
	상단 표시 위치:
	브로드만 9구역; ; 전전두피질; ; 핵액컴벤스; ; 편도체; ; 창호; ; 시상하부; ; 대상회; ; 척수 신경절; ; 복측 피개부; ; 두정엽;
	추가 참조 표현식 데이터
	추가 참조 표현식 데이터
유전자 존재론
분자 함수	뉴클레오티드 결합; ATP효소결합; GTP 바인딩; 미오신V결합; 단백질C말단결합; GO:0001948 단백질 결합; ATP효소활성화제활성화제; GTP 의존성 단백질 결합; GO:0006184 GTPase 액티비티; GDP-분리억제제결합;
셀룰러 컴포넌트	세포외 소포; 내염색체; 클라트린 분해 모노아민 수송 소포막; 막; 시냅스 소포; 혈장막; 클라트린 분해 감마-아미노낙산수송포막; 클라트린 촉진 아세틸콜린 수송 소포막; 축삭; 터미널 부톤; 아크로솜 소포; 세포내 소기관; 클라트린 자극성 글루탐산수송포막; 세포; 분비 과립막; 시냅스 소포막의 고정 성분; 베시클; 단백질 함유 복합체; 시냅스전활성대; 분비 과립; 세포질핵주위영역;
생물학적 과정	호흡계 과정; ATP 의존성 활성의 양성 조절; 축삭 형성; 폐의 발달; 시냅스성 소포 외세포증; 단기 신경 시냅스 가소성 조절; 유발 신경전달물질 분비; 미토콘드리아 조직; 전기 자극에 대한 반응; 후발달; 구성 분비 경로; 시냅스 전 활성 구역 구조 유지; 글루탐산염 분비; 세포외 조절; 시냅스 전 활성대막으로의 시냅스 소포 융합 조절; 신경근 시냅스 전달; 시냅스 소포 재활용; 촉각 지각; 단백질 수송; 세포외증의 양성 조절; 시냅스 소포 성숙; GO:0010554 신경전달물질 분비; 조절된 분비 경로의 양성 조절; 세포외부증; 호중구 탈과립; 발육 후 단백질 수식; 운송; 세포내단백질; 세포외이식에 관여하는 소포 도킹; 단백질 분비; 랍단백질신호; 혈장막으로의 단백질 국재화; 혈장막 복구; 시냅스 소포 프라이밍 조절; 시냅스 소포 수송; 아크로솜 소포 세포 외전증; 시냅스 소포 외세포증 조절; 칼슘이온조절세포외증; 시냅스 소포 클러스터링;
	출처:아미고 / QuickGO
맞춤법
	5864
	19339
	ENSG00000105649
	ENSMUSG000031840
	P20336
	P63011
	NM_002866
	NM_001166399; NM_009001; NM_001328047; NM_001378892; NM_001378893
	NP_002857; NP_002857.1
	NP_001159871; NP_001314976; NP_033027; NP_001365821; NP_001365822
	위키데이터
인간 보기/편집	마우스 표시/편집

Ras 관련 단백질 Rab-3A는 인간에서 RAB3A ^[5]^[6]^[7]유전자에 의해 암호화되는 단백질이다.그것은 신경세포에서 칼슘에 의해 유발되는 세포외전에 관여한다.

상호 작용

RAB3A는 다음과 상호작용하는 것으로 나타났습니다.

RIMS1,^[8]^[9]
UNC13A,^[10]
RPH3A ^[8]^[11]^[12]및
CHM.^[13]^[14]

레퍼런스

^ ^a ^b ^c GRCh38: 앙상블 릴리즈 89: ENSG00000105649 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리즈 89: ENSMUSG000031840 - 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.
^ Rousseau-Merck MF, Zahraoui A, Bernheim A, Touchot N, Miglierina R, Tavitian A, Berger R (January 1990). "Chromosome mapping of the human ras-related rab3A gene to 19p13.2". Genomics. 5 (4): 694–8. doi:10.1016/0888-7543(89)90110-9. PMID 2687157.
^ Brondyk WH, McKiernan CJ, Fortner KA, Stabila P, Holz RW, Macara IG (March 1995). "Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A". Mol Cell Biol. 15 (3): 1137–43. doi:10.1128/MCB.15.3.1137. PMC 230335. PMID 7532276.
^ "Entrez Gene: RAB3A RAB3A, member RAS oncogene family".
^ ^a ^b Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
^ Betz A, Thakur P, Junge HJ, Ashery U, Rhee JS, Scheuss V, Rosenmund C, Rettig J, Brose N (April 2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron. 30 (1): 183–96. doi:10.1016/s0896-6273(01)00272-0. hdl:11858/00-001M-0000-0012-F596-C. PMID 11343654. S2CID 155875.
^ "Protein unc-13 homolog A". UniProt.
^ Ostermeier C, Brunger AT (February 1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402. S2CID 15162326.
^ Weber E, Jilling T, Kirk KL (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". J. Biol. Chem. 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. PMID 8636125.
^ Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (January 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. 269 (3): 2111–7. doi:10.1016/S0021-9258(17)42142-9. PMID 8294464.
^ Pereira-Leal JB, Strom M, Godfrey RF, Seabra MC (January 2003). "Structural determinants of Rab and Rab Escort Protein interaction: Rab family motifs define a conserved binding surface". Biochem. Biophys. Res. Commun. 301 (1): 92–7. doi:10.1016/s0006-291x(02)02963-7. PMID 12535645.

추가 정보

Khosravi-Far R, Lutz RJ, Cox AD, Conroy L, Bourne JR, Sinensky M, Balch WE, Buss JE, Der CJ (1991). "Isoprenoid modification of rab proteins terminating in CC or CXC motifs". Proc. Natl. Acad. Sci. U.S.A. 88 (14): 6264–8. doi:10.1073/pnas.88.14.6264. PMC 52063. PMID 1648736.
Zahraoui A, Touchot N, Chardin P, Tavitian A (1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion". J. Biol. Chem. 264 (21): 12394–401. doi:10.1016/S0021-9258(18)63872-4. PMID 2501306.
Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA (1995). "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A". Proc. Natl. Acad. Sci. U.S.A. 91 (25): 11963–7. doi:10.1073/pnas.91.25.11963. PMC 45356. PMID 7991565.
McKiernan CJ, Brondyk WH, Macara IG (1993). "The Rab3A GTPase interacts with multiple factors through the same effector domain. Mutational analysis of cross-linking of Rab3A to a putative target protein". J. Biol. Chem. 268 (32): 24449–52. doi:10.1016/S0021-9258(20)80546-8. PMID 8226995.
Trask B, Fertitta A, Christensen M, Youngblom J, Bergmann A, Copeland A, de Jong P, Mohrenweiser H, Olsen A, Carrano A (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers". Genomics. 15 (1): 133–45. doi:10.1006/geno.1993.1021. PMID 8432525.
Johannes L, Perez F, Laran-Chich MP, Henry JP, Darchen F (1996). "Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II". Eur. J. Biochem. 239 (2): 362–8. doi:10.1111/j.1432-1033.1996.0362u.x. PMID 8706741.
Burton JL, Slepnev V, De Camilli PV (1997). "An evolutionarily conserved domain in a subfamily of Rabs is crucial for the interaction with the guanyl nucleotide exchange factor Mss4". J. Biol. Chem. 272 (6): 3663–8. doi:10.1074/jbc.272.6.3663. PMID 9013620.
Geppert M, Goda Y, Stevens CF, Südhof TC (1997). "The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion". Nature. 387 (6635): 810–4. doi:10.1038/42954. PMID 9194562. S2CID 4359038.
Martincic I, Peralta ME, Ngsee JK (1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". J. Biol. Chem. 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. PMID 9341137.
Ostermeier C, Brunger AT (1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402. S2CID 15162326.
Jung YJ, Lee TH, Lee JY, Kim JH, Park JB (1999). "Phosphatidic acid is important to the translocation of Rab3A from the cytosol to phospholipid membranes". NeuroReport. 10 (13): 2859–63. doi:10.1097/00001756-199909090-00029. PMID 10511453.
Sullivan M, Olsen AS, Houslay MD (2000). "Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND". Cell. Signal. 11 (10): 735–42. doi:10.1016/S0898-6568(99)00037-6. PMID 10574328.
Clabecq A, Henry JP, Darchen F (2000). "Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP". J. Biol. Chem. 275 (41): 31786–91. doi:10.1074/jbc.M003705200. PMID 10859313.
Haynes LP, Evans GJ, Morgan A, Burgoyne RD (2001). "A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells". J. Biol. Chem. 276 (13): 9726–32. doi:10.1074/jbc.M006959200. PMID 11134008.
Zhang Y, Luan Z, Liu A, Hu G (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. S2CID 33119468.
Luo HR, Saiardi A, Nagata E, Ye K, Yu H, Jung TS, Luo X, Jain S, Sawa A, Snyder SH (2001). "GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase". Neuron. 31 (3): 439–51. doi:10.1016/S0896-6273(01)00384-1. PMID 11516400. S2CID 10990373.
Piiper A, Leser J, Lutz MP, Beil M, Zeuzem S (2001). "Subcellular distribution and function of Rab3A-D in pancreatic acinar AR42J cells". Biochem. Biophys. Res. Commun. 287 (3): 746–51. doi:10.1006/bbrc.2001.5651. PMID 11563859.
Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". J. Biol. Chem. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.

인간 염색체 19번 유전자에 대한 이 기사는 짧은 글이다.위키피디아를 확장함으로써 위키피디아를 도울 수 있습니다.

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리즈 89: ENSG00000105649 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리즈 89: ENSMUSG000031840 - 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.

[pmid2687157-5] Rousseau-Merck MF, Zahraoui A, Bernheim A, Touchot N, Miglierina R, Tavitian A, Berger R (January 1990). "Chromosome mapping of the human ras-related rab3A gene to 19p13.2". Genomics. 5 (4): 694–8. doi:10.1016/0888-7543(89)90110-9. PMID 2687157.

[pmid7532276-6] Brondyk WH, McKiernan CJ, Fortner KA, Stabila P, Holz RW, Macara IG (March 1995). "Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A". Mol Cell Biol. 15 (3): 1137–43. doi:10.1128/MCB.15.3.1137. PMC 230335. PMID 7532276.

[entrez-7] "Entrez Gene: RAB3A RAB3A, member RAS oncogene family".

[pmid12578829-8] Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.

[pmid11343654-9] Betz A, Thakur P, Junge HJ, Ashery U, Rhee JS, Scheuss V, Rosenmund C, Rettig J, Brose N (April 2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron. 30 (1): 183–96. doi:10.1016/s0896-6273(01)00272-0. hdl:11858/00-001M-0000-0012-F596-C. PMID 11343654. S2CID 155875.

[10] "Protein unc-13 homolog A". UniProt.

[pmid10025402-11] Ostermeier C, Brunger AT (February 1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402. S2CID 15162326.

[pmid8636125-12] Weber E, Jilling T, Kirk KL (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". J. Biol. Chem. 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. PMID 8636125.

[pmid8294464-13] Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (January 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. 269 (3): 2111–7. doi:10.1016/S0021-9258(17)42142-9. PMID 8294464.

[pmid12535645-14] Pereira-Leal JB, Strom M, Godfrey RF, Seabra MC (January 2003). "Structural determinants of Rab and Rab Escort Protein interaction: Rab family motifs define a conserved binding surface". Biochem. Biophys. Res. Commun. 301 (1): 92–7. doi:10.1016/s0006-291x(02)02963-7. PMID 12535645.

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RAB3A

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상호 작용

레퍼런스

추가 정보