RPA2
Apariencia
Subunidad de 32 kDa de la proteína A de replicación | ||||
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![]() Estructura tridimensional de la proteína RPA2. | ||||
Estructuras disponibles | ||||
PDB |
Lista de códigos PDB 1dpu
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Identificadores | ||||
Símbolos | RPA2 (HGNC: 10290) REPA2; RPA32 | |||
Identificadores externos | ||||
Locus | Cr. 1 p35.3 | |||
Ortólogos | ||||
Especies |
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Entrez |
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UniProt |
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RefSeq (ARNm) |
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La subunidad de 32 kDa de la proteína A de replicación (RPA2) es una proteína codificada en humanos por el gen rpa2.[1][2]
Interacciones
[editar]La proteína RPA2 ha demostrado ser capaz de interaccionar con:
- Ku70[3]
- Proteína de replicación A1[3][4]
- RPA3[5][4]
- DNA-PKcs[3]
- STAT3[6]
- Ciclina O[7]
- MEN1[8]
- TP53BP1[9]
- Uracil-ADN glicosilasa[10]
Referencias
[editar]- ↑ Umbricht CB, Erdile LF, Jabs EW, Kelly TJ (Apr de 1993). «Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A». J Biol Chem 268 (9): 6131-8. PMID 8454588.
- ↑ «Entrez Gene: RPA2 Replication protein A2, 32kDa».
- ↑ a b c Shao, R G; Cao C X, Zhang H, Kohn K W, Wold M S, Pommier Y (Mar. de 1999). «Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes». EMBO J. (ENGLAND) 18 (5): 1397-406. ISSN 0261-4189. PMID 10064605. doi:10.1093/emboj/18.5.1397.
- ↑ a b Bochkareva, Elena; Korolev Sergey, Lees-Miller Susan P, Bochkarev Alexey (Apr. de 2002). «Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA». EMBO J. (England) 21 (7): 1855-63. ISSN 0261-4189. PMID 11927569. doi:10.1093/emboj/21.7.1855.
- ↑ Bochkareva, E; Frappier L, Edwards A M, Bochkarev A (Feb. de 1998). «The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain». J. Biol. Chem. (UNITED STATES) 273 (7): 3932-6. ISSN 0021-9258. 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 Biol. Int. (ENGLAND) 24 (7): 467-73. ISSN 1065-6995. PMID 10875894. doi:10.1006/cbir.2000.0525.
- ↑ Otterlei, M; Warbrick E, Nagelhus T A, Haug T, Slupphaug G, Akbari M, Aas P A, Steinsbekk K, Bakke O, Krokan H E (Jul. de 1999). «Post-replicative base excision repair in replication foci». EMBO J. (ENGLAND) 18 (13): 3834-44. ISSN 0261-4189. PMID 10393198. doi:10.1093/emboj/18.13.3834.
- ↑ Sukhodolets, Karen E; Hickman Alison B, Agarwal Sunita K, Sukhodolets Maxim V, Obungu Victor H, Novotny Elizabeth A, Crabtree Judy S, Chandrasekharappa Settara C, Collins Francis S, Spiegel Allen M, Burns A Lee, Marx Stephen J (Jan. de 2003). «The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene». Mol. Cell. Biol. (United States) 23 (2): 493-509. ISSN 0270-7306. PMID 12509449.
- ↑ Yoo, Eunjae; Kim Byung U, Lee Seung Youn, Cho Chae Hyun, Chung Jay H, Lee Chang-Hun (Aug. de 2005). «53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damage». Oncogene (England) 24 (35): 5423-30. ISSN 0950-9232. PMID 15856006. doi:10.1038/sj.onc.1208710.
- ↑ Nagelhus, T A; Haug T, Singh K K, Keshav K F, Skorpen F, Otterlei M, Bharati S, Lindmo T, Benichou S, Benarous R, Krokan H E (Mar. de 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». J. Biol. Chem. (UNITED STATES) 272 (10): 6561-6. ISSN 0021-9258. PMID 9045683.