레플리케이션 단백질 A2

RPA2
사용 가능한 구조
PDB	Ortholog 검색: PDBe RCSB
PDB ID 코드 목록
	1DPU, 1L1O, 1QUQ, 1Z1D, 2PI2, 2PQA, 2Z6K, 3KDF, 4MQV, 4OU0
식별자
에일리어스	RPA2, REPA2, RP-A p32, RP-A p34, RPA32, 레플리케이션단백질 A2
외부 ID	OMIM: 179836 MGI: 1339939 HomoloGene: 37712 GenCard: RPA2
유전자 위치(인간)
크르.	1번 염색체(인간)
끝.	27,914,746 bp
유전자 위치(마우스)
크르.	4번 염색체(쥐)
끝.	132,506,063 bp
RNA발현패턴
	상단 표시 위치:
	신경절 융기; ; 위근; ; 아킬레스건; ; 우측 자궁관; ; 정강이뼈전근; ; 림프절; ; 담낭; ; 전전두피질; ; 랑게르한스 섬; ; 우관상 동맥;
	상단 표시 위치:
	소마이트; ; 원시적 특징; ; 심내막 쿠션; ; 복벽; ; 배층; ; 외배엽; ; 광학 플래코드; ; 상악 융기; ; 진피; ; 모룰라;
	추가 참조 표현식 데이터
	추가 참조 표현식 데이터
유전자 존재론
분자 함수	DNA결합; 단백질 N말단결합; 외가닥 DNA결합; 손상 DNA결합; 단백질 결합; 효소결합; 단백질인산가수분해효소결합; 유비퀴틴단백질리가수분해효소결합; G리치스트랜드텔로미어DNA결합; 이중가닥DNA결합; 배열특이적 DNA결합;
셀룰러 컴포넌트	이중 파단부위; PML 본체; 핵소체; 염색체, 텔로미어 영역; DNA복제인자A복합체; 염색질; 핵; 핵체; 축합핵염색체;
생물학적 과정	뉴클레오티드절제복원,DNA갭충전; DNA재조합; 스트랜드간 가교 복구; 상동 재조합에 의한 이중 파단 수리의 조절; 무오차 변환 합성; G1 단계; 오차가 발생하기 쉬운 전이 합성; DNA 손상 자극에 대한 세포 반응; DNA복제; 유사분열성 G1 DNA 손상 체크포인트 시그널링; DNA손상검사점조절; 열에 대한 세포 반응 조절; DNA불일치복구; 전이 합성; 전사가능뉴클레오티드절제수복원; 뉴클레오티드 절제 복구, DNA 절개; 염기 절제 수리; 뉴클레오티드 절제 회복; 뉴클레오티드 절제 복구, 전절제 복합 안정화; p53급 매개자에 의한 신호 전달 조절; DNA복구; 상동 재조합에 의한 이중 파단 수리; 뉴클레오티드-절제복구, 전절제복합체조립체; 뉴클레오티드 절제 복구, DNA 절개, 5'-to 병변; 뉴클레오티드 절제 복구, DNA 절개, 3'-to 병변; 염색체에 대한 단백질 국재화; 텔로미어 유지; Telomere 유지보수, 반보전성 레플리케이션; 유사분열세포주기의 G1/S 전이; 재조합에 의한 텔로미어 유지; DNA토폴로지변화; DNA 복제에 관여하는 DNA 풀림; 유사분열 재조합; 텔로머라아제에 의한 텔로미어 유지; 상호 감수성 재조합; 헤테로듀플렉스 형성; 헬리케이스 활성의 양성 조절;
	출처:아미고 / QuickGO
맞춤법
	6118
	19891
	ENSG00000117748
	ENSMUSG000028884
	P15927
	Q62193
	NM_001286076; NM_001297558; NM_002946; NM_001355128; NM_001355129
	NM_011284
	NP_001273005; NP_001284487; NP_002937; NP_001342057; NP_001342058
	없음
	위키데이터
인간 보기/편집	마우스 표시/편집

복제단백질 A32kDa 서브유닛은 RPA2 유전자에 ^[5]^[6]의해 인체에서 암호화되는 단백질이다.

상호 작용

RPA2는 다음과 상호작용하는 것으로 나타났습니다.

「」를 참조해 주세요.

레퍼런스

^ ^a ^b ^c GRCh38: 앙상블 릴리즈 89: ENSG00000117748 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리즈 89: ENSMUSG000028884 - 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.
^ Umbricht CB, Erdile LF, Jabs EW, Kelly TJ (Mar 1993). "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A". The Journal of Biological Chemistry. 268 (9): 6131–8. doi:10.1016/S0021-9258(18)53229-4. PMID 8454588.
^ "Entrez Gene: RPA2 Replication protein A2, 32kDa".
^ Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE (Jul 1999). "Post-replicative base excision repair in replication foci". The EMBO Journal. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.
^ ^a ^b ^c Shao RG, Cao CX, Zhang H, Kohn KW, Wold MS, Pommier Y (Mar 1999). "Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes". The EMBO Journal. 18 (5): 1397–406. doi:10.1093/emboj/18.5.1397. PMC 1171229. PMID 10064605.
^ Sukhodolets KE, Hickman AB, Agarwal SK, Sukhodolets MV, Obungu VH, Novotny EA, Crabtree JS, Chandrasekharappa SC, Collins FS, Spiegel AM, Burns AL, Marx SJ (Jan 2003). "The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene". Molecular and Cellular Biology. 23 (2): 493–509. doi:10.1128/mcb.23.2.493-509.2003. PMC 151531. PMID 12509449.
^ ^a ^b Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A (Apr 2002). "Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA". The EMBO Journal. 21 (7): 1855–63. doi:10.1093/emboj/21.7.1855. PMC 125950. PMID 11927569.
^ Bochkareva E, Frappier L, Edwards AM, Bochkarev A (Feb 1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain". The Journal of Biological Chemistry. 273 (7): 3932–6. doi:10.1074/jbc.273.7.3932. PMID 9461578.
^ Kim J, Kim D, Chung J (2000). "Replication protein a 32 kDa subunit (RPA p32) binds the SH2 domain of STAT3 and regulates its transcriptional activity". Cell Biology International. 24 (7): 467–73. doi:10.1006/cbir.2000.0525. PMID 10875894. S2CID 23783745.
^ Yoo E, Kim BU, Lee SY, Cho CH, Chung JH, Lee CH (Aug 2005). "53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damage". Oncogene. 24 (35): 5423–30. doi:10.1038/sj.onc.1208710. PMID 15856006.
^ Nagelhus TA, Haug T, Singh KK, Keshav KF, Skorpen F, Otterlei M, Bharati S, Lindmo T, Benichou S, Benarous R, Krokan HE (Mar 1997). "A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A". The Journal of Biological Chemistry. 272 (10): 6561–6. doi:10.1074/jbc.272.10.6561. PMID 9045683.

추가 정보

Dutta A, Stillman B (Jun 1992). "cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication". The EMBO Journal. 11 (6): 2189–99. doi:10.1002/j.1460-2075.1992.tb05278.x. PMC 556686. PMID 1318195.
Erdile LF, Wold MS, Kelly TJ (Feb 1990). "The primary structure of the 32-kDa subunit of human replication protein A". The Journal of Biological Chemistry. 265 (6): 3177–82. doi:10.1016/S0021-9258(19)39750-9. PMID 2406247.
Li L, Lu X, Peterson CA, Legerski RJ (Oct 1995). "An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair". Molecular and Cellular Biology. 15 (10): 5396–402. doi:10.1128/mcb.15.10.5396. PMC 230789. PMID 7565690.
Umbricht CB, Griffin CA, Hawkins AL, Grzeschik KH, O'Connell P, Leach R, Green ED, Kelly TJ (Mar 1994). "High-resolution genomic mapping of the three human replication protein A genes (RPA1, RPA2, and RPA3)". Genomics. 20 (2): 249–57. doi:10.1006/geno.1994.1161. PMID 8020972.
Nagelhus TA, Haug T, Singh KK, Keshav KF, Skorpen F, Otterlei M, Bharati S, Lindmo T, Benichou S, Benarous R, Krokan HE (Mar 1997). "A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A". The Journal of Biological Chemistry. 272 (10): 6561–6. doi:10.1074/jbc.272.10.6561. PMID 9045683.
Amacker M, Hottiger M, Mossi R, Hübscher U (Mar 1997). "HIV-1 nucleocapsid protein and replication protein A influence the strand displacement DNA synthesis of lentiviral reverse transcriptase". AIDS. 11 (4): 534–6. PMID 9084803.
Niu H, Erdjument-Bromage H, Pan ZQ, Lee SH, Tempst P, Hurwitz J (May 1997). "Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro". The Journal of Biological Chemistry. 272 (19): 12634–41. doi:10.1074/jbc.272.19.12634. PMID 9139719.
Zernik-Kobak M, Vasunia K, Connelly M, Anderson CW, Dixon K (Sep 1997). "Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells". The Journal of Biological Chemistry. 272 (38): 23896–904. doi:10.1074/jbc.272.38.23896. PMID 9295339.
Bochkareva E, Frappier L, Edwards AM, Bochkarev A (Feb 1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain". The Journal of Biological Chemistry. 273 (7): 3932–6. doi:10.1074/jbc.273.7.3932. PMID 9461578.
Shao RG, Cao CX, Zhang H, Kohn KW, Wold MS, Pommier Y (Mar 1999). "Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes". The EMBO Journal. 18 (5): 1397–406. doi:10.1093/emboj/18.5.1397. PMC 1171229. PMID 10064605.
Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE (Jul 1999). "Post-replicative base excision repair in replication foci". The EMBO Journal. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.
Bochkarev A, Bochkareva E, Frappier L, Edwards AM (Aug 1999). "The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding". The EMBO Journal. 18 (16): 4498–504. doi:10.1093/emboj/18.16.4498. PMC 1171524. PMID 10449415.
Lao Y, Gomes XV, Ren Y, Taylor JS, Wold MS (Feb 2000). "Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA". Biochemistry. 39 (5): 850–9. doi:10.1021/bi991704s. PMID 10653628.
Costello JF, Frühwald MC, Smiraglia DJ, Rush LJ, Robertson GP, Gao X, Wright FA, Feramisco JD, Peltomäki P, Lang JC, Schuller DE, Yu L, Bloomfield CD, Caligiuri MA, Yates A, Nishikawa R, Su Huang H, Petrelli NJ, Zhang X, O'Dorisio MS, Held WA, Cavenee WK, Plass C (Feb 2000). "Aberrant CpG-island methylation has non-random and tumour-type-specific patterns". Nature Genetics. 24 (2): 132–8. doi:10.1038/72785. PMID 10655057. S2CID 6273676.
Kim J, Kim D, Chung J (2000). "Replication protein a 32 kDa subunit (RPA p32) binds the SH2 domain of STAT3 and regulates its transcriptional activity". Cell Biology International. 24 (7): 467–73. doi:10.1006/cbir.2000.0525. PMID 10875894. S2CID 23783745.
Cho JM, Song DJ, Bergeron J, Benlimame N, Wold MS, Alaoui-Jamali MA (Sep 2000). "RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A". Nucleic Acids Research. 28 (18): 3478–85. doi:10.1093/nar/28.18.3478. PMC 110737. PMID 10982866.
Brush GS, Kelly TJ (Oct 2000). "Phosphorylation of the replication protein A large subunit in the Saccharomyces cerevisiae checkpoint response". Nucleic Acids Research. 28 (19): 3725–32. doi:10.1093/nar/28.19.3725. PMC 110765. PMID 11000264.
Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ (Oct 2000). "Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA". Cell. 103 (3): 449–56. doi:10.1016/S0092-8674(00)00136-7. PMID 11081631. S2CID 16640087.
Habel JE, Ohren JF, Borgstahl GE (Feb 2001). "Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association". Acta Crystallographica Section D. 57 (Pt 2): 254–9. doi:10.1107/S0907444900015225. PMID 11173472.

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리즈 89: ENSG00000117748 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리즈 89: ENSMUSG000028884 - 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.

[pmid8454588-5] Umbricht CB, Erdile LF, Jabs EW, Kelly TJ (Mar 1993). "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A". The Journal of Biological Chemistry. 268 (9): 6131–8. doi:10.1016/S0021-9258(18)53229-4. PMID 8454588.

[6] "Entrez Gene: RPA2 Replication protein A2, 32kDa".

[pmid10393198-7] Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE (Jul 1999). "Post-replicative base excision repair in replication foci". The EMBO Journal. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.

[pmid10064605-8] Shao RG, Cao CX, Zhang H, Kohn KW, Wold MS, Pommier Y (Mar 1999). "Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes". The EMBO Journal. 18 (5): 1397–406. doi:10.1093/emboj/18.5.1397. PMC 1171229. PMID 10064605.

[pmid12509449-9] Sukhodolets KE, Hickman AB, Agarwal SK, Sukhodolets MV, Obungu VH, Novotny EA, Crabtree JS, Chandrasekharappa SC, Collins FS, Spiegel AM, Burns AL, Marx SJ (Jan 2003). "The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene". Molecular and Cellular Biology. 23 (2): 493–509. doi:10.1128/mcb.23.2.493-509.2003. PMC 151531. PMID 12509449.

[pmid11927569-10] Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A (Apr 2002). "Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA". The EMBO Journal. 21 (7): 1855–63. doi:10.1093/emboj/21.7.1855. PMC 125950. PMID 11927569.

[pmid9461578-11] Bochkareva E, Frappier L, Edwards AM, Bochkarev A (Feb 1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain". The Journal of Biological Chemistry. 273 (7): 3932–6. doi:10.1074/jbc.273.7.3932. PMID 9461578.

[pmid10875894-12] Kim J, Kim D, Chung J (2000). "Replication protein a 32 kDa subunit (RPA p32) binds the SH2 domain of STAT3 and regulates its transcriptional activity". Cell Biology International. 24 (7): 467–73. doi:10.1006/cbir.2000.0525. PMID 10875894. S2CID 23783745.

[pmid15856006-13] Yoo E, Kim BU, Lee SY, Cho CH, Chung JH, Lee CH (Aug 2005). "53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damage". Oncogene. 24 (35): 5423–30. doi:10.1038/sj.onc.1208710. PMID 15856006.

[pmid9045683-14] Nagelhus TA, Haug T, Singh KK, Keshav KF, Skorpen F, Otterlei M, Bharati S, Lindmo T, Benichou S, Benarous R, Krokan HE (Mar 1997). "A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A". The Journal of Biological Chemistry. 272 (10): 6561–6. doi:10.1074/jbc.272.10.6561. PMID 9045683.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

Search

레플리케이션 단백질 A2

네임스페이스

더

목차

상호 작용

「」를 참조해 주세요.

레퍼런스

추가 정보

Search

레플리케이션 단백질 A2

상호 작용

「 」를 참조해 주세요.

레퍼런스

추가 정보

「」를 참조해 주세요.