혈관확장제 자극인단백질

VASP
사용 가능한 구조
PDB	Ortholog 검색: PDBe RCSB
PDB ID 코드 목록
	1EGX, 1USD, 1USE, 2PAV, 2PBD, 3CHW
식별자
에일리어스	VASP, 혈관확장제 자극인단백질, 혈관확장제 자극인단백질
외부 ID	OMIM : 601703 MGI : 109268 HomoloGene : 7592 GenCard : VASP
유전자 위치(인간)
크르.	19번 염색체(인간)
끝.	45,526,983 bp
유전자 위치(마우스)
크르.	7번 염색체(쥐)
끝.	1,9005,742 bp
RNA발현패턴
	상단 표시 위치:
	단구; ; 복정맥; ; 비장; ; 피; ; 직장; ; 흉부 대동맥; ; 상행 대동맥; ; 좌측 자궁관; ; 우관상 동맥; ; 좌폐 상엽;
	추가 참조 표현식 데이터
	추가 참조 표현식 데이터
유전자 존재론
분자 함수	프로파일린 결합; SH3 도메인바인딩; GO:0001948, GO:0016582 단백질 결합; 액틴 결합; 카드헤린 결합;
셀룰러 컴포넌트	세포 투영; 막; 국소 접착; 이세포밀접합; 필로포듐; 혈장막; 세포 접합; 액틴 세포골격; 세포외 엑소좀; 세포골격; 층상 지방막; 라멜리포듐; 필로포듐막; 세포질; 세포;
생물학적 과정	액틴 필라멘트 중합 양성 조절; 축삭 유도; 신경관 폐쇄; 액틴 중합 또는 탈중합; 단백질 호모테트라미라이제이션; 액틴세포골격조직; 셀 접합 조립체;
	출처:아미고 / QuickGO
맞춤법
	7408
	22323
	ENSG00000125753
	ENSMUSG000030403
	P50552
	P70460
	NM_001008736; NM_003370
	NM_001282021; NM_001282022; NM_009499
	NP_003361
	NP_001268950; NP_001268951; NP_033525
	위키데이터
인간 보기/편집	마우스 표시/편집

Vasodilator 자극 인단백질은 VASP ^[5]^[6]유전자에 의해 인간에게 암호화되는 단백질이다.

기능.

혈관확장제 자극인산단백질(VASP)은 Ena-VASP 단백질군의 구성원이다.Ena-VASP 패밀리 멤버는 E/DFPPPXD/E 모티브를 포함한 단백질을 결합하고 Ena-VASP 단백질을 국소 접착 세포막에 표적화하는 N-말단 EVH1 도메인을 포함한다.단백질의 중간 영역에서 가족 구성원은 SH3와 WW 도메인을 포함하는 단백질을 결합하는 프롤린이 풍부한 영역을 가진다.C 말단 EVH2 도메인은 사분해를 매개하고 G 및 F 액틴을 결합합니다.VASP는 필라멘트 형태의 액틴 형성과 관련이 있으며 세포 접착 및 운동성에 광범위한 역할을 할 가능성이 있다.VASP는 또한 인테그린-세포외 매트릭스 상호작용을 조절하는 세포내 신호전달 경로에 관여할 수 있다.VASP는 고리형 뉴클레오티드 의존성 키나아제 PKA 및 PKG에 ^[6]의해 조절된다.

상호 작용

혈관확장제 자극 인단백질은 Zyxin,^[7]^[8] Profilin 1, ^[7]PFN2와 ^[7]^[9]상호작용하는 것으로 나타났다.

레퍼런스

^ ^a ^b ^c GRCh38: 앙상블 릴리즈 89: ENSG00000125753 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리즈 89: ENSMUSG000030403 - 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.
^ Zimmer M, Fink T, Fischer L, Hauser W, Scherer K, Lichter P, Walter U (January 1997). "Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization". Genomics. 36 (2): 227–33. doi:10.1006/geno.1996.0457. PMID 8812448.
^ ^a ^b "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".
^ ^a ^b ^c Harbeck, B; Hüttelmaier S; Schluter K; Jockusch B M; Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.
^ Drees, B; Friederich E; Fradelizi J; Louvard D; Beckerle M C; Golsteyn R M (July 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. ISSN 0021-9258. PMID 10801818.
^ Reinhard, M; Giehl K; Abel K; Haffner C; Jarchau T; Hoppe V; Jockusch B M; Walter U (April 1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. ISSN 0261-4189. PMC 398250. PMID 7737110.

추가 정보

Reinhard M, Halbrügge M, Scheer U, et al. (1992). "The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts". EMBO J. 11 (6): 2063–70. doi:10.1002/j.1460-2075.1992.tb05264.x. PMC 556672. PMID 1318192.
Halbrügge M, Eigenthaler M, Polke C, Walter U (1992). "Protein phosphorylation regulated by cyclic nucleotide-dependent protein kinases in cell extracts and in intact human lymphocytes". Cell. Signal. 4 (2): 189–99. doi:10.1016/0898-6568(92)90082-J. PMID 1319722.
Reinhard M, Jouvenal K, Tripier D, Walter U (1995). "Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7956–60. Bibcode:1995PNAS...92.7956R. doi:10.1073/pnas.92.17.7956. PMC 41265. PMID 7644520.
Reinhard M, Giehl K, Abel K, et al. (1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. PMC 398250. PMID 7737110.
Haffner C, Jarchau T, Reinhard M, et al. (1995). "Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP". EMBO J. 14 (1): 19–27. doi:10.1002/j.1460-2075.1995.tb06971.x. PMC 398048. PMID 7828592.
Horstrup K, Jablonka B, Hönig-Liedl P, et al. (1994). "Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition". Eur. J. Biochem. 225 (1): 21–7. doi:10.1111/j.1432-1033.1994.00021.x. PMID 7925440.
Butt E, Abel K, Krieger M, et al. (1994). "cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets". J. Biol. Chem. 269 (20): 14509–17. doi:10.1016/S0021-9258(17)36652-8. PMID 8182057.
Laurent V, Loisel TP, Harbeck B, et al. (1999). "Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes". J. Cell Biol. 144 (6): 1245–58. doi:10.1083/jcb.144.6.1245. PMC 2150578. PMID 10087267.
Bachmann C, Fischer L, Walter U, Reinhard M (1999). "The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation". J. Biol. Chem. 274 (33): 23549–57. doi:10.1074/jbc.274.33.23549. PMID 10438535.
Petit MM, Fradelizi J, Golsteyn RM, et al. (2000). "LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity". Mol. Biol. Cell. 11 (1): 117–29. doi:10.1091/mbc.11.1.117. PMC 14761. PMID 10637295.
Krause M, Sechi AS, Konradt M, et al. (2000). "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton". J. Cell Biol. 149 (1): 181–94. doi:10.1083/jcb.149.1.181. PMC 2175102. PMID 10747096.
Drees B, Friederich E, Fradelizi J, et al. (2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. PMID 10801818.
Smolenski A, Poller W, Walter U, Lohmann SM (2000). "Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I". J. Biol. Chem. 275 (33): 25723–32. doi:10.1074/jbc.M909632199. PMID 10851246.
Harbeck B, Hüttelmaier S, Schluter K, et al. (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
Burkhardt M, Glazova M, Gambaryan S, et al. (2000). "KT5823 inhibits cGMP-dependent protein kinase activity in vitro but not in intact human platelets and rat mesangial cells". J. Biol. Chem. 275 (43): 33536–41. doi:10.1074/jbc.M005670200. PMID 10922374.
Ball LJ, Kühne R, Hoffmann B, et al. (2000). "Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity". EMBO J. 19 (18): 4903–14. doi:10.1093/emboj/19.18.4903. PMC 314220. PMID 10990454.
Bearer EL, Prakash JM, Manchester RD, Allen PG (2001). "VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations". Cell Motil. Cytoskeleton. 47 (4): 351–64. doi:10.1002/1097-0169(200012)47:4<351::AID-CM8>3.0.CO;2-8. PMC 3376085. PMID 11093254.
Lawrence DW, Pryzwansky KB (2001). "The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading". J. Immunol. 166 (9): 5550–6. doi:10.4049/jimmunol.166.9.5550. PMID 11313394.
Castellano F, Le Clainche C, Patin D, et al. (2001). "A WASp-VASP complex regulates actin polymerization at the plasma membrane". EMBO J. 20 (20): 5603–14. doi:10.1093/emboj/20.20.5603. PMC 125672. PMID 11598004.

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

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리즈 89: ENSG00000125753 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리즈 89: ENSMUSG000030403 - 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.

[pmid8812448-5] Zimmer M, Fink T, Fischer L, Hauser W, Scherer K, Lichter P, Walter U (January 1997). "Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization". Genomics. 36 (2): 227–33. doi:10.1006/geno.1996.0457. PMID 8812448.

[entrez-6] "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".

[pmid10882740-7] Harbeck, B; Hüttelmaier S; Schluter K; Jockusch B M; Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.

[pmid10801818-8] Drees, B; Friederich E; Fradelizi J; Louvard D; Beckerle M C; Golsteyn R M (July 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. ISSN 0021-9258. PMID 10801818.

[pmid7737110-9] Reinhard, M; Giehl K; Abel K; Haffner C; Jarchau T; Hoppe V; Jockusch B M; Walter U (April 1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. ISSN 0261-4189. PMC 398250. PMID 7737110.

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혈관확장제 자극인단백질

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레퍼런스

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