CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004394
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Replication protein A 32 kDa subunit 
Protein Synonyms/Alias
 RP-A p32; Replication factor A protein 2; RF-A protein 2; Replication protein A 34 kDa subunit; RP-A p34 
Gene Name
 RPA2 
Gene Synonyms/Alias
 REPA2; RPA32; RPA34 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
85GIIRHAEKAPTNIVYubiquitination[1, 2, 3]
93APTNIVYKIDDMTAAubiquitination[1, 2, 4]
127VPPETYVKVAGHLRSubiquitination[1, 2, 3, 4, 5, 6]
171NAHMVLSKANSQPSAubiquitination[1]
231GLNFQDLKNQLKHMSacetylation[3]
231GLNFQDLKNQLKHMSubiquitination[3]
243HMSVSSIKQAVDFLSubiquitination[7]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
 Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage. 
Sequence Annotation
 REGION 187 270 Interaction with TIPIN (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 21 21 Phosphothreonine; by PRKDC; in vitro.
 MOD_RES 23 23 Phosphoserine.
 MOD_RES 29 29 Phosphoserine; by CDK1; in vitro.
 MOD_RES 33 33 Phosphoserine; by PRKDC; in vitro.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA replication; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 270 AA 
Protein Sequence
MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV 60
DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV 120
PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR 180
APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS 240
SIKQAVDFLS NEGHIYSTVD DDHFKSTDAE 270 
Gene Ontology
 GO:0005662; C:DNA replication factor A complex; IPI:MGI.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
 GO:0000730; P:DNA recombinase assembly; TAS:Reactome.
 GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0000718; P:nucleotide-excision repair, DNA damage removal; TAS:Reactome.
 GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
 GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
 GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
 GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase.
 IPR014646; RPA32.
 IPR014892; RPA_C.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF08784; RPA_C
 PF01336; tRNA_anti 
SMART
  
PROSITE
  
PRINTS