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UniProtKB/Swiss-Prot entry P15927


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RFA2_HUMAN
Primary accession number P15927
Secondary accession numbers Q52II0 Q5TEI9 Q5TEJ5
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on April 1, 1990 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 103)
Name and origin of the protein
Protein name Replication protein A 32 kDa subunit
Synonyms RP-A p32
RP-A p34
Replication factor A protein 2
RF-A protein 2
Gene name
Name: RPA2
Synonyms: REPA2, RPA32, RPA34
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2406247 [NCBI, ExPASy, EBI, Israel, Japan]
Erdile L.F., Wold M.S., Kelly T.J.;
"The primary structure of the 32-kDa subunit of human replication protein A.";
J. Biol. Chem. 265:3177-3182(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-14; ARG-15 AND SER-203.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney, Lung, and Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
ACETYLATION AT MET-1, PHOSPHORYLATION AT THR-21; SER-29 AND SER-33, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-29.
DOI=10.1074/jbc.272.19.12634; PubMed=9139719 [NCBI, ExPASy, EBI, Israel, Japan]
Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P., Hurwitz J.;
"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. 272:12634-12641(1997).
[7]
INTERACTION WITH SERTAD3.
DOI=10.1093/nar/28.18.3478; PubMed=10982866 [NCBI, ExPASy, EBI, Israel, Japan]
Cho J.M., Song D.J., Bergeron J., Benlimame N., Wold M.S., Alaoui-Jamali M.A.;
"RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A.";
Nucleic Acids Res. 28:3478-3485(2000).
[8]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
DOI=10.1016/S0960-9822(03)00376-2; PubMed=12814551 [NCBI, ExPASy, EBI, Israel, Japan]
Barr S.M., Leung C.G., Chang E.E., Cimprich K.A.;
"ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation.";
Curr. Biol. 13:1047-1051(2003).
[9]
FUNCTION.
DOI=10.1074/jbc.M403825200; PubMed=15205463 [NCBI, ExPASy, EBI, Israel, Japan]
Weisshart K., Pestryakov P., Smith R.W.P., Hartmann H., Kremmer E., Lavrik O., Nasheuer H.-P.;
"Coordinated regulation of replication protein A activities by its subunits p14 and p32.";
J. Biol. Chem. 279:35368-35376(2004).
[10]
INTERACTION WITH TIPIN.
DOI=10.1016/j.jmb.2006.10.097; PubMed=17141802 [NCBI, ExPASy, EBI, Israel, Japan]
Gotter A.L., Suppa C., Emanuel B.S.;
"Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors.";
J. Mol. Biol. 366:36-52(2007).
[11]
INTERACTION WITH TIPIN.
DOI=10.1128/MCB.02190-06; PubMed=17296725 [NCBI, ExPASy, EBI, Israel, Japan]
Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P., Cordeiro-Stone M., Sancar A., Kaufmann W.K.;
"The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement.";
Mol. Cell. Biol. 27:3131-3142(2007).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-171 IN COMPLEX WITH RPA1 AND RPA3.
DOI=10.1093/emboj/18.16.4498; PubMed=10449415 [NCBI, ExPASy, EBI, Israel, Japan]
Bochkarev A., Bochkareva E., Frappier L., Edwards A.M.;
"The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding.";
EMBO J. 18:4498-4504(1999).
[13]
STRUCTURE BY NMR OF 172-270.
DOI=10.1016/S0092-8674(00)00136-7; PubMed=11081631 [NCBI, ExPASy, EBI, Israel, Japan]
Mer G., Bochkarev A., Gupta R., Bochkareva E., Frappier L., Ingles C.J., Edwards A.M., Chazin W.J.;
"Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA.";
Cell 103:449-456(2000).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-171.
DOI=10.1093/emboj/21.7.1855; PubMed=11927569 [NCBI, ExPASy, EBI, Israel, Japan]
Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.;
"Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA.";
EMBO J. 21:1855-1863(2002).
Comments
  • 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.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDP15927-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDP15927-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_017201.
    Name3
    Isoform IDP15927-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_017202.
  • 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 CDC2.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rpa2/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J05249; AAA36560.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450348; CAG29344.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ001128; AAX84514.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109927; CAI21777.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109927; CAI21778.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109927; CAI21775.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001630; AAH01630.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012157; AAH12157.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021257; AAH21257.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00013939; -.
IPI00646500; -.
IPI00647667; -.
PIR A43711; A43711.
RefSeq NP_002937.1; -.
UniGene Hs.513261
3D structure databases
PDB
1DPU; NMR; -; A=172-270.[ExPASy / RCSB / EBI]
1L1O; X-ray; 2.80 A; B/E=44-171.[ExPASy / RCSB / EBI]
1QUQ; X-ray; 2.50 A; A/C=43-171.[ExPASy / RCSB / EBI]
1Z1D; NMR; -; A=172-270.[ExPASy / RCSB / EBI]
2PI2; X-ray; 2.00 A; A/B/C/D=1-270.[ExPASy / RCSB / EBI]
2PQA; X-ray; 2.50 A; A/C=42-172.[ExPASy / RCSB / EBI]
2Z6K; X-ray; 3.00 A; A/B=1-270.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DPU; -.
1L1O; -.
1QUQ; -.
1Z1D; -.
2PI2; -.
2PQA; -.
2Z6K; -.
ModBase P15927.
Protein-protein interaction databases
DIP DIP:24187N; -.
IntAct P15927; 23.
PTM databases
PhosphoSite P15927; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_216; DNA Repair.
REACT_383; DNA Replication.
REACT_7970; Telomere Maintenance.
Organism-specific databases
GeneCards GC01M028090; -.
H-InvDB HIX0000302; -.
HGNC HGNC:10290; RPA2.
GenAtlas RPA2.
HPA CAB016538; -.
MIM 179836; gene. [NCBI / EBI]
PharmGKB PA34652; -.
Gene expression databases
ArrayExpress P15927; -.
Bgee P15927; -.
CleanEx HS_RPA2; -.
GermOnline ENSG00000117748; Homo sapiens.
Ontologies
GO
GO:0005662; Cellular component: DNA replication factor A complex (inferred from physical interaction from MGI).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003697; Molecular function: single-stranded DNA binding (traceable author statement from ProtInc).
GO:0006261; Biological process: DNA-dependent DNA replication (traceable author statement from ProtInc).
GO:0000718; Biological process: nucleotide-excision repair, DNA damage removal (inferred from experiment from Reactome).
GO:0006297; Biological process: nucleotide-excision repair, DNA gap filling (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR012340; NA-bd_OB-fold.
IPR004365; NA_bd_OB_tRNA-helicase.
IPR014646; RPA32.
IPR014892; RPA_C.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF08784; RPA_C; 1.
PF01336; tRNA_anti; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036949; RPA32; 1.
Proteomic databases
PRIDE P15927; -.
Genome annotation databases
Ensembl ENSG00000117748; Homo sapiens. [Contig view]
GeneID 6118; -.
KEGG hsa:6118; -.
Phylogenomic databases
HOVERGEN P15927; -.
OMA P15927; WVDTDDT.
Other
NextBio 23759; -.
SOURCE RPA2; Homo sapiens.
ProtoNet P15927.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; DNA replication; Nucleus; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   270  270     Replication protein A 32 kDa subunit. PRO_0000097270
REGION   187   270  84     Interaction with TIPIN (By similarity). 
COMPBIAS   1    29  29     Gly/Ser-rich. 
COMPBIAS   37    45  9     Arg/Lys-rich (basic). 
COMPBIAS   95   123  29     Asp/Glu-rich (acidic). 
COMPBIAS   127   145  19     Arg/Lys-rich (basic). 
COMPBIAS   247   270  24     Asp/Glu-rich (acidic). 
SITE   23    23  1     Not phosphorylated (Probable). 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   21    21        Phosphothreonine; by PRKDC; in vitro. 
MOD_RES   29    29        Phosphoserine; by CDC2; in vitro. 
MOD_RES   33    33        Phosphoserine; by PRKDC; in vitro. 
VAR_SEQ   1     4        MWNS -> MGRGDRNKRSIR (in isoform 2). VSP_017201
VAR_SEQ   1     4        MWNS -> MWNSNDGGAGWRRKRIAGGFSKRASLGSERRVVAGEEGRE RSWGVWGSPAGRRRGRLGRLGQCLKGRSLREPAGFSEAWD VAQALILLFKTG (in isoform 3). VSP_017202
VARIANT   14    14  1     Y -> S (in dbSNP:rs28988896 [NCBI]). VAR_023300 
VARIANT   15    15  1     G -> R (in dbSNP:rs28988897 [NCBI]). VAR_023301 
VARIANT   203   203  1     N -> S (in dbSNP:rs28904899 [NCBI]). VAR_023302 
MUTAGEN   29    29        S->A: Reduces phosphorylation by CDC2. 
HELIX   51    56  6      
STRAND   58    60  3      
STRAND   63    66  4      
STRAND   69    85  17      
STRAND   87    95  9      
STRAND   97   100  4      
STRAND   102   107  6      
STRAND   125   135  11      
STRAND   138   148  11      
HELIX   153   172  20      
HELIX   207   218  12      
TURN   222   224  3      
HELIX   227   233  7      
HELIX   239   251  13      
STRAND   254   257  4      
STRAND   263   268  6      
Sequence information
Length: 270 AA [This is the length of the unprocessed precursor] Molecular weight: 29247 Da [This is the MW of the unprocessed precursor] CRC64: 61A563EA7B34A9B1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV 

        70         80         90        100        110        120 
DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV 

       130        140        150        160        170        180 
PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR 

       190        200        210        220        230        240 
APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS 

       250        260        270 
SIKQAVDFLS NEGHIYSTVD DDHFKSTDAE 

P15927 in FASTA format

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