RPA2

From Wikipedia, the free encyclopedia

Replication protein A2, 32kDa

PDB rendering based on 1dpu.

Available structures: 1dpu, 1l1o, 1quq, 1z1d

Identifiers

Symbol(s)

RPA2; REPA2; RPA32

External IDs

OMIM: 179836 MGI: 1339939 HomoloGene: 37712

Gene ontology
Molecular Function:	• nucleic acid binding • single-stranded DNA binding • DNA-directed DNA polymerase activity • protein binding • transferase activity
Cellular Component:	• nucleus • DNA replication factor A complex
Biological Process:	• DNA replication • DNA-dependent DNA replication

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002946 (mRNA)
NP_002937 (protein)

NM_011284 (mRNA)
NP_035414 (protein)

Location

Chr 1: 28.09 - 28.11 Mb

Chr 4: 132.04 - 132.05 Mb

Pubmed search

[1]

[2]

Replication protein A2, 32kDa, also known as RPA2, is a human gene.^[1]

[edit] References

^ Entrez Gene: RPA2 Replication protein A2, 32kDa.

[edit] Further reading

Dutta A, Stillman B (1992). "cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication.". EMBO J. 11 (6): 2189-99. PMID 1318195.
Erdile LF, Wold MS, Kelly TJ (1990). "The primary structure of the 32-kDa subunit of human replication protein A.". J. Biol. Chem. 265 (6): 3177-82. PMID 2406247.
Li L, Lu X, Peterson CA, Legerski RJ (1995). "An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair.". Mol. Cell. Biol. 15 (10): 5396-402. PMID 7565690.
Umbricht CB, Griffin CA, Hawkins AL, et al. (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.
Umbricht CB, Erdile LF, Jabs EW, Kelly TJ (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.
Nagelhus TA, Haug T, Singh KK, et al. (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. 272 (10): 6561-6. PMID 9045683.
Amacker M, Hottiger M, Mossi R, Hübscher U (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, et al. (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.". J. Biol. Chem. 272 (19): 12634-41. PMID 9139719.
Zernik-Kobak M, Vasunia K, Connelly M, et al. (1997). "Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells.". J. Biol. Chem. 272 (38): 23896-904. PMID 9295339.
Bochkareva E, Frappier L, Edwards AM, Bochkarev A (1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain.". J. Biol. Chem. 273 (7): 3932-6. PMID 9461578.
Shao RG, Cao CX, Zhang H, et al. (1999). "Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes.". EMBO J. 18 (5): 1397-406. doi:10.1093/emboj/18.5.1397. PMID 10064605.
Otterlei M, Warbrick E, Nagelhus TA, et al. (1999). "Post-replicative base excision repair in replication foci.". EMBO J. 18 (13): 3834-44. doi:10.1093/emboj/18.13.3834. PMID 10393198.
Bochkarev A, Bochkareva E, Frappier L, Edwards AM (1999). "The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding.". EMBO J. 18 (16): 4498-504. doi:10.1093/emboj/18.16.4498. PMID 10449415.
Lao Y, Gomes XV, Ren Y, et al. (2000). "Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA.". Biochemistry 39 (5): 850-9. PMID 10653628.
Costello JF, Frühwald MC, Smiraglia DJ, et al. (2000). "Aberrant CpG-island methylation has non-random and tumour-type-specific patterns.". Nat. Genet. 24 (2): 132-8. doi:10.1038/72785. PMID 10655057.
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. 24 (7): 467-73. doi:10.1006/cbir.2000.0525. PMID 10875894.
Cho JM, Song DJ, Bergeron J, et al. (2000). "RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A.". Nucleic Acids Res. 28 (18): 3478-85. PMID 10982866.
Brush GS, Kelly TJ (2000). "Phosphorylation of the replication protein A large subunit in the Saccharomyces cerevisiae checkpoint response.". Nucleic Acids Res. 28 (19): 3725-32. PMID 11000264.
Mer G, Bochkarev A, Gupta R, et al. (2000). "Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA.". Cell 103 (3): 449-56. PMID 11081631.
Habel JE, Ohren JF, Borgstahl GE (2001). "Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association.". Acta Crystallogr. D Biol. Crystallogr. 57 (Pt 2): 254-9. PMID 11173472.