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UniProtKB/Swiss-Prot entry P27694


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

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Entry information
Entry name RFA1_HUMAN
Primary accession number P27694
Secondary accession number Q59ES9
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on February 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 93)
Name and origin of the protein
Protein name Replication protein A 70 kDa DNA-binding subunit
Synonyms RP-A p70
Replication factor A protein 1
RF-A protein 1
Single-stranded DNA-binding protein
Gene name
Name: RPA1
Synonyms: REPA1, RPA70
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], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2050703 [NCBI, ExPASy, EBI, Israel, Japan]
Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.;
"Characterization of a cDNA encoding the 70-kDa single-stranded DNA-binding subunit of human replication protein A and the role of the protein in DNA replication.";
J. Biol. Chem. 266:12090-12098(1991).
[2]
SEQUENCE REVISION TO 217.
PubMed=8420996 [NCBI, ExPASy, EBI, Israel, Japan]
Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.;
"Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing.";
J. Biol. Chem. 268:2268-2268(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-351.
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-351.
Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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]
PROTEIN SEQUENCE OF 2-41; 82-88; 93-103; 168-196; 221-259; 314-324; 345-379; 390-410; 413-472; 490-499; 503-511; 552-568; 576-586 AND 589-600, CLEAVAGE OF INITIATOR METHIONINE, AND MASS SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[7]
INTERACTION WITH XPA.
DOI=10.1038/1400; PubMed=9699634 [NCBI, ExPASy, EBI, Israel, Japan]
Ikegami T., Kuraoka I., Saijo M., Kodo N., Kyogoku Y., Morikawa K., Tanaka K., Shirakawa M.;
"Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.";
Nat. Struct. Biol. 5:701-706(1998).
[8]
INTERACTION WITH XPA.
DOI=10.1021/bi991755p; PubMed=10563794 [NCBI, ExPASy, EBI, Israel, Japan]
Buchko G.W., Daughdrill G.W., de Lorimier R., Sudha Rao B.K., Isern N.G., Lingbeck J.M., Taylor J.-S., Wold M.S., Gochin M., Spicer L.D., Lowry D.F., Kennedy M.A.;
"Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.";
Biochemistry 38:15116-15128(1999).
[9]
INTERACTION WITH RIP.
DOI=10.1128/MCB.25.18.8202-8214.2005; PubMed=16135809 [NCBI, ExPASy, EBI, Israel, Japan]
Park J., Seo T., Kim H., Choe J.;
"Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies.";
Mol. Cell. Biol. 25:8202-8214(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 183-420.
DOI=10.1038/385176a0; PubMed=8990123 [NCBI, ExPASy, EBI, Israel, Japan]
Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L.;
"Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA.";
Nature 385:176-181(1997).
Comments
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
M63488; AAA36584.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209732; BAD92969.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY599563; AAS94324.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018126; AAH18126.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40457; A40457.
RefSeq NP_002936.1; -.
UniGene Hs.461925
3D structure databases
PDB
1EWI; NMR; -; A=1-114.[ExPASy / RCSB / EBI]
1FGU; X-ray; 2.50 A; A/B=182-432.[ExPASy / RCSB / EBI]
1JMC; X-ray; 2.40 A; A=181-422.[ExPASy / RCSB / EBI]
1L1O; X-ray; 2.80 A; C/F=436-616.[ExPASy / RCSB / EBI]
2B29; X-ray; 1.60 A; A=1-120.[ExPASy / RCSB / EBI]
2B3G; X-ray; 1.60 A; A=1-120.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EWI; -.
1FGU; -.
1JMC; -.
1L1O; -.
2B29; -.
2B3G; -.
DisProt DP00061; -.
ModBase P27694.
Protein-protein interaction databases
DIP DIP:24189N; -.
IntAct P27694; -.
PTM databases
PhosphoSite P27694; -.
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.
Polymorphism databases
NIEHS-SNPs RPA1.
Organism-specific databases
H-InvDB HIX0017624; -.
HGNC HGNC:10289; RPA1.
GenAtlas RPA1.
HPA CAB004563; -.
HPA006914; -.
MIM 179835; gene. [NCBI / EBI]
PharmGKB PA29353; -.
GeneCards P27694.
Gene expression databases
ArrayExpress P27694; -.
CleanEx HS_RPA1; -.
GermOnline ENSG00000132383; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005856; Cellular component: cytoskeleton (inferred from direct assay from HPA).
GO:0005662; Cellular component: DNA replication factor A complex (inferred from physical interaction from MGI).
GO:0016605; Cellular component: PML body (inferred from direct assay from MGI).
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:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006310; Biological process: DNA recombination (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.
IPR007199; Rep-A_N.
IPR013955; Rep_factor-A_C.
IPR004591; Rpa1.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 4.
Pfam PF04057; Rep-A_N; 1.
PF08646; Rep_fac-A_C; 1.
PF01336; tRNA_anti; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00617; rpa1; 1.
BLOCKS P27694.
ProtoNet P27694.
Proteomic databases
PeptideAtlas P27694; -.
Genome annotation databases
Ensembl ENSG00000132383; Homo sapiens. [Contig view]
GeneID 6117; -.
KEGG hsa:6117; -.
Phylogenomic databases
HOGENOM P27694; -.
HOVERGEN P27694; -.
Other
LinkHub P27694; -.
NextBio 23755; -.
SOURCE RPA1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; DNA replication; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   616  615     Replication protein A 70 kDa DNA-binding subunit. PRO_0000097260
ZN_FING   481   503  23     C4-type (Potential). 
MOD_RES   180   180        Phosphothreonine. 
VARIANT   351   351  1     T -> A (in dbSNP:rs5030755 [NCBI]). VAR_019236 [3D]
HELIX   9    16  8      
STRAND   24    33  10      
STRAND   41    47  7      
STRAND   49    58  10      
HELIX   60    62  3      
HELIX   63    67  5      
STRAND   76    86  11      
STRAND   88    90  3      
STRAND   92   103  12      
HELIX   445   451  7      
TURN   452   454  3      
STRAND   455   458  4      
STRAND   460   471  12      
STRAND   477   480  4      
STRAND   491   493  3      
TURN   494   496  3      
STRAND   497   500  4      
TURN   501   504  4      
STRAND   505   509  5      
STRAND   512   521  10      
STRAND   526   532  7      
HELIX   533   540  8      
HELIX   544   550  7      
HELIX   555   564  10      
TURN   565   567  3      
STRAND   569   577  9      
STRAND   588   596  9      
HELIX   599   615  17      
Sequence information
Length: 616 AA [This is the length of the unprocessed precursor] Molecular weight: 68138 Da [This is the MW of the unprocessed precursor] CRC64: FE038F40F5886CD1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVGQLSEGAI AAIMQKGDTN IKPILQVINI RPITTGNSPP RYRLLMSDGL NTLSSFMLAT 

        70         80         90        100        110        120 
QLNPLVEEEQ LSSNCVCQIH RFIVNTLKDG RRVVILMELE VLKSAEAVGV KIGNPVPYNE 

       130        140        150        160        170        180 
GLGQPQVAPP APAASPAASS RPQPQNGSSG MGSTVSKAYG ASKTFGKAAG PSLSHTSGGT 

       190        200        210        220        230        240 
QSKVVPIASL TPYQSKWTIC ARVTNKSQIR TWSNSRGEGK LFSLELVDES GEIRATAFNE 

       250        260        270        280        290        300 
QVDKFFPLIE VNKVYYFSKG TLKIANKQFT AVKNDYEMTF NNETSVMPCE DDHHLPTVQF 

       310        320        330        340        350        360 
DFTGIDDLEN KSKDSLVDII GICKSYEDAT KITVRSNNRE VAKRNIYLMD TSGKVVTATL 

       370        380        390        400        410        420 
WGEDADKFDG SRQPVLAIKG ARVSDFGGRS LSVLSSSTII ANPDIPEAYK LRGWFDAEGQ 

       430        440        450        460        470        480 
ALDGVSISDL KSGGVGGSNT NWKTLYEVKS ENLGQGDKPD YFSSVATVVY LRKENCMYQA 

       490        500        510        520        530        540 
CPTQDCNKKV IDQQNGLYRC EKCDTEFPNF KYRMILSVNI ADFQENQWVT CFQESAEAIL 

       550        560        570        580        590        600 
GQNAAYLGEL KDKNEQAFEE VFQNANFRSF IFRVRVKVET YNDESRIKAT VMDVKPVDYR 

       610 
EYGRRLVMSI RRSALM 

P27694 in FASTA format

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