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RPA2

Protein FULL name:

Replication protein A 32 kDa subunit, Replication protein A 34 kDa subunit, Replication factor A protein 2,


Protein SHORT name:

RP-A p32 RP-A p34 RF-A 2.


RPA2 (Homo sapiens) is product of expression of RPA2 gene.






FUNCTION: Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions.

SUBUNIT: Heterotrimer of 70, 32 and 14 kDa chains. The DNA-binding activity may reside exclusively on the 70 kDa subunit. Binds to SERTAD3/RBT1. Interacts with TIPIN.

INTERACTION: Q92793:CREBBP; NbExp=1; IntAct=EBI-621404, EBI-81215; P04406:GAPDH; NbExp=1; IntAct=EBI-621404, EBI-354056;

SUBCELLULAR LOCATION: Nucleus. Note=Also present in PML nuclear bodies. Redistributes to discrete nuclear foci upon DNA damage.

PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). Phosphorylated by ATR upon DNA damage, which promotes its translocation to nuclear foci. Can be phosphorylated in vitro by PRKDC/DNA-PK in the presence of Ku and DNA, and by CDK1.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 132474
4506585
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P15927 P15927
PFAM: PF08784
PF01336
PF08784
PF01336
InterPro: IPR012340
IPR016027
IPR004365
IPR014646
IPR014892
IPR011991
IPR012340
IPR016027
IPR004365
IPR014646
IPR014892
IPR011991
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCT
ISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAA
PMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLE
DMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFM
PANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLS
NEGHIYSTVDDDHFKSTDAE

RPA2 (Homo sapiens) is able to recognize following damages:
References:

Title Authors Journal
The primary structure of the 32-kDa subunit of human replication protein A. Erdile LF, Wold MS, Kelly TJ J Biol Chem Jan. 25, 1990
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. Niu H, Erdjument-Bromage H, Pan ZQ, Lee SH, Tempst P, Hurwitz J J Biol Chem May 9, 1997
The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. Bochkarev A, Bochkareva E, Frappier L, Edwards AM EMBO J Aug. 16, 1999
RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A. Cho JM, Song DJ, Bergeron J, Benlimame N, Wold MS, Alaoui-Jamali MA Nucleic Acids Res Sept. 15, 2000
Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA. Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ Cell Oct. 27, 2000
Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A EMBO J April 2, 2002
ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation. Barr SM, Leung CG, Chang EE, Cimprich KA Curr Biol June 17, 2003
Coordinated regulation of replication protein A activities by its subunits p14 and p32. Weisshart K, Pestryakov P, Smith RW, Hartmann H, Kremmer E, Lavrik O, Nasheuer HP J Biol Chem Aug. 20, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
The DNA sequence and biological annotation of human chromosome 1. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E Nature May 18, 2006
Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors. Gotter AL, Suppa C, Emanuel BS J Mol Biol Jan. 9, 2007
The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement. Unsal-Kacmaz K, Chastain PD, Qu PP, Minoo P, Cordeiro-Stone M, Sancar A, Kaufmann WK Mol Cell Biol April 1, 2007
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009


Last modification of this entry: Oct. 6, 2010.

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