(data stored in ACNUC25087 zone)

HOVERGEN: RFA2_HUMAN

ID   RFA2_HUMAN              Reviewed;         270 AA.
AC   P15927; Q52II0; Q5TEI9; Q5TEJ5;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-NOV-2009, entry version 108.
DE   RecName: Full=Replication protein A 32 kDa subunit;
DE            Short=RP-A p32;
DE   AltName: Full=RP-A p34;
DE   AltName: Full=Replication factor A protein 2;
DE            Short=RF-A protein 2;
GN   Name=RPA2; Synonyms=REPA2, RPA32, RPA34;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=90153966; PubMed=2406247;
RA   Erdile L.F., Wold M.S., Kelly T.J.;
RT   "The primary structure of the 32-kDa subunit of human replication
RT   protein A.";
RL   J. Biol. Chem. 265:3177-3182(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-14; ARG-15 AND
RP   SER-203.
RG   NIEHS SNPs program;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney, Lung, and Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   ACETYLATION AT MET-1, PHOSPHORYLATION AT THR-21; SER-29 AND SER-33,
RP   MASS SPECTROMETRY, AND MUTAGENESIS OF SER-29.
RX   MEDLINE=97284742; PubMed=9139719; DOI=10.1074/jbc.272.19.12634;
RA   Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P.,
RA   Hurwitz J.;
RT   "Mapping of amino acid residues in the p34 subunit of human single-
RT   stranded DNA-binding protein phosphorylated by DNA-dependent protein
RT   kinase and Cdc2 kinase in vitro.";
RL   J. Biol. Chem. 272:12634-12641(1997).
RN   [7]
RP   INTERACTION WITH SERTAD3.
RX   MEDLINE=20440390; PubMed=10982866; DOI=10.1093/nar/28.18.3478;
RA   Cho J.M., Song D.J., Bergeron J., Benlimame N., Wold M.S.,
RA   Alaoui-Jamali M.A.;
RT   "RBT1, a novel transcriptional co-activator, binds the second subunit
RT   of replication protein A.";
RL   Nucleic Acids Res. 28:3478-3485(2000).
RN   [8]
RP   PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=22698999; PubMed=12814551; DOI=10.1016/S0960-9822(03)00376-2;
RA   Barr S.M., Leung C.G., Chang E.E., Cimprich K.A.;
RT   "ATR kinase activity regulates the intranuclear translocation of ATR
RT   and RPA following ionizing radiation.";
RL   Curr. Biol. 13:1047-1051(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=15205463; DOI=10.1074/jbc.M403825200;
RA   Weisshart K., Pestryakov P., Smith R.W.P., Hartmann H., Kremmer E.,
RA   Lavrik O., Nasheuer H.-P.;
RT   "Coordinated regulation of replication protein A activities by its
RT   subunits p14 and p32.";
RL   J. Biol. Chem. 279:35368-35376(2004).
RN   [10]
RP   INTERACTION WITH TIPIN.
RX   PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097;
RA   Gotter A.L., Suppa C., Emanuel B.S.;
RT   "Mammalian TIMELESS and Tipin are evolutionarily conserved replication
RT   fork-associated factors.";
RL   J. Mol. Biol. 366:36-52(2007).
RN   [11]
RP   INTERACTION WITH TIPIN.
RX   PubMed=17296725; DOI=10.1128/MCB.02190-06;
RA   Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P.,
RA   Cordeiro-Stone M., Sancar A., Kaufmann W.K.;
RT   "The human Tim/Tipin complex coordinates an Intra-S checkpoint
RT   response to UV that slows replication fork displacement.";
RL   Mol. Cell. Biol. 27:3131-3142(2007).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-171 IN COMPLEX WITH RPA1
RP   AND RPA3.
RX   PubMed=10449415; DOI=10.1093/emboj/18.16.4498;
RA   Bochkarev A., Bochkareva E., Frappier L., Edwards A.M.;
RT   "The crystal structure of the complex of replication protein A
RT   subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA
RT   binding.";
RL   EMBO J. 18:4498-4504(1999).
RN   [13]
RP   STRUCTURE BY NMR OF 172-270.
RX   MEDLINE=20531881; PubMed=11081631; DOI=10.1016/S0092-8674(00)00136-7;
RA   Mer G., Bochkarev A., Gupta R., Bochkareva E., Frappier L.,
RA   Ingles C.J., Edwards A.M., Chazin W.J.;
RT   "Structural basis for the recognition of DNA repair proteins UNG2,
RT   XPA, and RAD52 by replication factor RPA.";
RL   Cell 103:449-456(2000).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-171.
RX   PubMed=11927569; DOI=10.1093/emboj/21.7.1855;
RA   Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.;
RT   "Structure of the RPA trimerization core and its role in the multistep
RT   DNA-binding mechanism of RPA.";
RL   EMBO J. 21:1855-1863(2002).
CC   -!- FUNCTION: Required for DNA recombination, repair and replication.
CC       The activity of RP-A is mediated by single-stranded DNA binding
CC       and protein interactions.
CC   -!- SUBUNIT: Heterotrimer of 70, 32 and 14 kDa chains. The DNA-binding
CC       activity may reside exclusively on the 70 kDa subunit. Binds to
CC       SERTAD3/RBT1. Interacts with TIPIN.
CC   -!- INTERACTION:
CC       Q92793:CREBBP; NbExp=1; IntAct=EBI-621404, EBI-81215;
CC       P04406:GAPDH; NbExp=1; IntAct=EBI-621404, EBI-354056;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Also present in PML nuclear
CC       bodies. Redistributes to discrete nuclear foci upon DNA damage.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P15927-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15927-2; Sequence=VSP_017201;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=P15927-3; Sequence=VSP_017202;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated in a cell-cycle-dependent manner (from the S
CC       phase until mitosis). Phosphorylated by ATR upon DNA damage, which
CC       promotes its translocation to nuclear foci. Can be phosphorylated
CC       in vitro by PRKDC/DNA-PK in the presence of Ku and DNA, and by
CC       CDC2.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/rpa2/";
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CC   -!- GENE_FAMILY: HBG000086 [ FAMILY / ALN / TREE ]
DR   EMBL; J05249; AAA36560.1; -; mRNA.
DR   EMBL; CR450348; CAG29344.1; -; mRNA.
DR   EMBL; DQ001128; AAX84514.1; -; Genomic_DNA.
DR   EMBL; AL109927; CAI21777.1; -; Genomic_DNA.
DR   EMBL; AL109927; CAI21778.1; -; Genomic_DNA.
DR   EMBL; AL109927; CAI21775.1; -; Genomic_DNA.
DR   EMBL; BC001630; AAH01630.1; -; mRNA.
DR   EMBL; BC012157; AAH12157.1; -; mRNA.
DR   EMBL; BC021257; AAH21257.1; -; mRNA.
DR   IPI; IPI00013939; -.
DR   IPI; IPI00646500; -.
DR   IPI; IPI00647667; -.
DR   PIR; A43711; A43711.
DR   RefSeq; NP_002937.1; -.
DR   UniGene; Hs.513261; -.
DR   UniGene; Hs.703070; -.
DR   UniGene; Hs.79411; -.
DR   PDB; 1DPU; NMR; -; A=172-270.
DR   PDB; 1L1O; X-ray; 2.80 A; B/E=44-171.
DR   PDB; 1QUQ; X-ray; 2.50 A; A/C=43-171.
DR   PDB; 1Z1D; NMR; -; A=172-270.
DR   PDB; 2PI2; X-ray; 2.00 A; A/B/C/D=1-270.
DR   PDB; 2PQA; X-ray; 2.50 A; A/C=42-172.
DR   PDB; 2Z6K; X-ray; 3.00 A; A/B=1-270.
DR   PDBsum; 1DPU; -.
DR   PDBsum; 1L1O; -.
DR   PDBsum; 1QUQ; -.
DR   PDBsum; 1Z1D; -.
DR   PDBsum; 2PI2; -.
DR   PDBsum; 2PQA; -.
DR   PDBsum; 2Z6K; -.
DR   DIP; DIP:24187N; -.
DR   IntAct; P15927; 23.
DR   STRING; P15927; -.
DR   PhosphoSite; P15927; -.
DR   PRIDE; P15927; -.
DR   Ensembl; ENST00000313433; ENSP00000363015; ENSG00000117748; Homo sapiens.
DR   Ensembl; ENST00000373909; ENSP00000363017; ENSG00000117748; Homo sapiens.
DR   Ensembl; ENST00000373912; ENSP00000363021; ENSG00000117748; Homo sapiens.
DR   Ensembl; ENST00000419958; ENSP00000413541; ENSG00000117748; Homo sapiens.
DR   Ensembl; ENST00000444045; ENSP00000387649; ENSG00000117748; Homo sapiens.
DR   GeneID; 6118; -.
DR   KEGG; hsa:6118; -.
DR   UCSC; uc001bpd.1; human.
DR   UCSC; uc001bpe.1; human.
DR   CTD; 6118; -.
DR   GeneCards; GC01M028090; -.
DR   H-InvDB; HIX0000302; -.
DR   HGNC; HGNC:10290; RPA2.
DR   HPA; CAB016538; -.
DR   MIM; 179836; gene.
DR   PharmGKB; PA34652; -.
DR   HOVERGEN; P15927; -.
DR   OMA; WVDTDDT; -.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_216; DNA Repair.
DR   Reactome; REACT_383; DNA Replication.
DR   Reactome; REACT_7970; Telomere Maintenance.
DR   NextBio; 23759; -.
DR   ArrayExpress; P15927; -.
DR   Bgee; P15927; -.
DR   CleanEx; HS_RPA2; -.
DR   Genevestigator; P15927; -.
DR   GermOnline; ENSG00000117748; Homo sapiens.
DR   GO; GO:0005662; C:DNA replication factor A complex; IPI:MGI.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; TAS:ProtInc.
DR   GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; EXP:Reactome.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; EXP:Reactome.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA_bd_OB_tRNA-helicase.
DR   InterPro; IPR014646; RPA32.
DR   InterPro; IPR014892; RPA_C.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF08784; RPA_C; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PIRSF; PIRSF036949; RPA32; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P15927.
DR   SWISS-2DPAGE; P15927.
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; DNA replication; Nucleus; Phosphoprotein;
KW   Polymorphism.
FT   DOMAIN       21     46       PRODOM:2005.1:PD718451  4
FT   DOMAIN       51    171       PRODOM:2005.1:PD336970  34
FT   DOMAIN      189    268       PRODOM:2005.1:PD987856  12
FT   CHAIN         1    270       Replication protein A 32 kDa subunit.
FT                                /FTId=PRO_0000097270.
FT   REGION      187    270       Interaction with TIPIN (By similarity).
FT   COMPBIAS      1     29       Gly/Ser-rich.
FT   COMPBIAS     37     45       Arg/Lys-rich (basic).
FT   COMPBIAS     95    123       Asp/Glu-rich (acidic).
FT   COMPBIAS    127    145       Arg/Lys-rich (basic).
FT   COMPBIAS    247    270       Asp/Glu-rich (acidic).
FT   SITE         23     23       Not phosphorylated (Probable).
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES      21     21       Phosphothreonine; by PRKDC; in vitro.
FT   MOD_RES      29     29       Phosphoserine; by CDC2; in vitro.
FT   MOD_RES      33     33       Phosphoserine; by PRKDC; in vitro.
FT   VAR_SEQ       1      4       MWNS -> MGRGDRNKRSIR (in isoform 2).
FT                                /FTId=VSP_017201.
FT   VAR_SEQ       1      4       MWNS -> MWNSNDGGAGWRRKRIAGGFSKRASLGSERRVV
FT                                AGEEGRERSWGVWGSPAGRRRGRLGRLGQCLKGRSLREPAG
FT                                FSEAWDVAQALILLFKTG (in isoform 3).
FT                                /FTId=VSP_017202.
FT   VARIANT      14     14       Y -> S (in dbSNP:rs28988896).
FT                                /FTId=VAR_023300.
FT   VARIANT      15     15       G -> R (in dbSNP:rs28988897).
FT                                /FTId=VAR_023301.
FT   VARIANT     203    203       N -> S (in dbSNP:rs28904899).
FT                                /FTId=VAR_023302.
FT   MUTAGEN      29     29       S->A: Reduces phosphorylation by CDC2.
FT   HELIX        51     56
FT   STRAND       58     60
FT   STRAND       63     66
FT   STRAND       69     85
FT   STRAND       87     95
FT   STRAND       97    100
FT   STRAND      102    107
FT   STRAND      125    135
FT   STRAND      138    148
FT   HELIX       153    172
FT   HELIX       207    218
FT   TURN        222    224
FT   HELIX       227    233
FT   HELIX       239    251
FT   STRAND      254    257
FT   STRAND      263    268
SQ   SEQUENCE   270 AA;  29247 MW;  61A563EA7B34A9B1 CRC64;
     MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV
     DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV
     PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR
     APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS
     SIKQAVDFLS NEGHIYSTVD DDHFKSTDAE
//

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