Tag Content
SG ID
SG00000513 
UniProt Accession
Theoretical PI
7.03  
Molecular Weight
68138 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
RPA1 
Gene Synonyms/Alias
REPA1, RPA70 
Protein Name
Replication protein A 70 kDa DNA-binding subunit 
Protein Synonyms/Alias
RP-A p70 Replication factor A protein 1;RF-A protein 1 Single-stranded DNA-binding protein; 
Organism
Homo sapiens (Human) 
NCBI Taxonomy ID
9606 
Chromosome Location
chr:17;1733266-1802848;1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Replication protein A (RPA) has been identified as a component of early recombination nodules. The visualization of post-synaptic RPA foci may indicate the presence of a different role for this protein during homologous recombination. 
The information of related literatures
1. M. Oliver-Bonet, M. Campillo, P. J. Turek, E. Ko and R. H. Martin (2007) Analysis of replication protein A (RPA) in human spermatogenesis. Mol Hum Reprod 13(12): 837-44. 

Abstract
Replication protein A (RPA) has been identified as a component of early recombination nodules. It is thought to stimulate homologous pairing and strand exchange reactions. The expression pattern of RPA in human spermatocytes has been analysed using immunocytogenetic techniques on testicular biopsies from adult male patients. What appears to be connecting RPA-filaments was observed between as yet unsynapsed homologous regions at early stages of zygotene. RPA foci were also observed in synaptic segments at zygotene and early pachytene, in numbers that peak at the end of zygotene. The presence of a localization pattern for RPA was also detected, but statistical analysis of distances between adjacent RPA foci shows that this pattern does not always follow a gamma distribution. Finally, it was determined that RPA is absent from non-centromeric heterochromatin in chromosome 9. The observed bridge-like structure could be the visualization of a proposed pre-synaptic RPA role in the strand invasion that precedes the formation of a Holliday Junction. These observations strengthen the original pre-synaptic model, although the visualization of post-synaptic RPA foci may indicate the presence of a different role for this protein during homologous recombination. PMID: [17981954] 

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Figures for illustrating the function of this protein/gene
Ref: M. Oliver-Bonet, M. Campillo, P. J. Turek, E. Ko and R. H. Martin (2007) Analysis of replication protein A (RPA) in human spermatogenesis. Mol Hum Reprod 13(12): 837-44. PMID: [17981954]
Function
Functions as component of the alternative replicationprotein A complex (aRPA). aRPA binds single-stranded DNA andprobably plays a role in DNA repair; it does not supportchromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNApolymerase alpha but supports DNA polymerase delta synthesis inthe presence of PCNA and replication factor C (RFC), the dualincision/excision reaction of nucleotide excision repair andRAD51-dependent strand exchange. 
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Subcellular Location
Nucleus. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0015629 C:actin cytoskeleton IDA:HPA.
GO:0000794 C:condensed nuclear chromosome IEA:Compara.
GO:0005737 C:cytoplasm IDA:HPA.
GO:0005662 C:DNA replication factor A complex IPI:MGI.
GO:0001673 C:male germ cell nucleus IEA:Compara.
GO:0016605 C:PML body IDA:MGI.
GO:0003682 F:chromatin binding IEA:Compara.
GO:0046872 F:metal ion binding IEA:UniProtKB-KW.
GO:0003697 F:single-stranded DNA binding TAS:ProtInc.
GO:0000075 P:cell cycle checkpoint TAS:Reactome.
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:0030097 P:hemopoiesis IEA:Compara.
GO:0048873 P:homeostasis of number of cells within a tissue IEA:Compara.
GO:0001701 P:in utero embryonic development IEA:Compara.
GO:0000216 P:M/G1 transition of mitotic cell cycle TAS:Reactome.
GO:0007126 P:meiosis IEA:Compara.
GO:0000718 P:nucleotide-excision repair, DNA damage removal TAS:Reactome.
GO:0006297 P:nucleotide-excision repair, DNA gap filling TAS:Reactome.
GO:0008284 P:positive regulation of cell proliferation IEA:Compara.
GO:0000084 P:S phase of mitotic cell cycle TAS:Reactome.
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.
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Interpro
IPR012340;    NA-bd_OB-fold.
IPR016027;    NA-bd_OB-fold-like.
IPR004365;    NA-bd_OB_tRNA-helicase.
IPR013955;    Rep_factor-A_C.
IPR007199;    Rep_factor-A_N.
IPR004591;    Rep_factor_Rpa1.
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Pfam
PF04057;    Rep-A_N;    1.
PF08646;    Rep_fac-A_C;    1.
PF01336;    tRNA_anti;    1.
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SMART
PROSITE
PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
INIT_MET      1      1       Removed.
CHAIN         2    616       Replication protein A 70 kDa DNA-binding
                             subunit.
                             /FTId=PRO_0000097260.
ZN_FING     481    503       C4-type (Potential).
MOD_RES     163    163       N6-acetyllysine.
MOD_RES     167    167       N6-acetyllysine.
MOD_RES     180    180       Phosphothreonine.
MOD_RES     191    191       Phosphothreonine.
MOD_RES     259    259       N6-acetyllysine.
MOD_RES     384    384       Phosphoserine.
CROSSLNK    449    449       Glycyl lysine isopeptide (Lys-Gly)
                             (interchain with G-Cter in SUMO).
CROSSLNK    577    577       Glycyl lysine isopeptide (Lys-Gly)
                             (interchain with G-Cter in SUMO).
VARIANT     351    351       T -> A (in dbSNP:rs5030755).
                             /FTId=VAR_019236.
MUTAGEN      41     41       R->E: Loss of HELB-binding; when
                             associated with E-43.
MUTAGEN      43     43       R->E: Loss of HELB-binding; when
                             associated with E-41.
MUTAGEN     449    449       K->R: Significant reduction of
                             sumoylation. Loss of sumoylation; when
                             associated with R-577.
MUTAGEN     577    577       K->R: Slight sumoylation decrease. Loss
                             of sumoylation; when associated with R-
                             449.
HELIX         2      4
HELIX         9     16
STRAND       18     20
STRAND       24     33
STRAND       36     38
STRAND       41     47
STRAND       49     58
HELIX        60     62
HELIX        63     67
STRAND       70     74
STRAND       76     86
STRAND       88     90
STRAND       92    103
HELIX       105    108
HELIX       187    189
STRAND      198    206
STRAND      210    213
STRAND      218    227
STRAND      232    238
HELIX       239    245
HELIX       246    248
STRAND      254    258
STRAND      261    264
HELIX       267    269
STRAND      275    279
STRAND      285    288
HELIX       305    310
STRAND      316    326
STRAND      330    334
TURN        335    338
STRAND      339    349
STRAND      355    361
HELIX       362    367
STRAND      375    384
STRAND      388    392
STRAND      398    402
HELIX       406    416
TURN        417    419
HELIX       445    451
TURN        452    454
STRAND      455    458
STRAND      460    471
STRAND      477    480
STRAND      491    493
TURN        494    496
STRAND      497    500
TURN        501    504
STRAND      505    509
STRAND      512    521
STRAND      526    532
HELIX       533    540
HELIX       544    550
HELIX       555    564
TURN        565    567
STRAND      569    577
STRAND      588    596
HELIX       599    615
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Nucleotide Sequence
Length: 2393 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 616 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
TOPBP1BioGRID 
RPA3HPRD 
MCM7BioGRID 
HUS1HPRD 
SMARCA4BioGRID 
TOPBP1BioGRID 
ACTBIntAct 
AICDAHPRD 
AKTIPBioGRID 
ARRB2IntAct 
ASCC2BioGRID 
ATG101BioGRID 
ATRIPHPRD 
ATRBioGRID 
RAD51BioGRID 
_BioGRID 
_BioGRID 
_BioGRID 
SMARCA4BioGRID 
_BioGRID 
_BioGRID 
BLMHPRD 
BRCA1BioGRID 
BRCA2HPRD 
CHAF1ABioGRID 
CPEHPRD 
CENPAIntAct 
CHD1LBioGRID 
DMC1HPRD 
POLA1MINT 
POLLHPRD 
_HPRD 
MUTYHBioGRID 
MUTYHBioGRID 
MUTYHBioGRID 
BRCA1BioGRID 
MCPH1BioGRID 
FAM203ABioGRID 
FANCABioGRID 
BRIP1BioGRID 
FANCMBioGRID 
FYCO1BioGRID 
HNRNPUL1BioGRID 
HUS1HPRD 
KINBioGRID 
_MINT 
MCM2BioGRID 
MCM4BioGRID 
MCM6BioGRID 
MCM7HPRD 
MCPH1BioGRID 
MEN1DIP 
MSH4HPRD 
MUTYHHPRD 
ORC2HPRD 
ORC6BioGRID 
TP53HPRD 
PCNABioGRID 
PRIM2MINT 
PRKDCHPRD 
TOPBP1BioGRID 
BRCA1BioGRID 
BRCA1BioGRID 
_HPRD 
AIDHPRD 
_HPRD 
TCEA2BioGRID 
BRCA1BioGRID 
RAD51BioGRID 
dmsBIntAct 
AIDHPRD 
FANCABioGRID 
TCEA2BioGRID 
SMARCA4BioGRID 
RAD1BioGRID 
RAD51BioGRID 
RAD9AHPRD 
RB1CC1BioGRID 
RBM23BioGRID 
RECQLHPRD 
RPA3BioGRID 
MCM7BioGRID 
HUS1BioGRID 
AKTIPHPRD 
ASCC2HPRD 
RAD51HPRD 
BLMBioGRID 
CPEIntAct 
CCNA2BioGRID 
POLA1MINT 
FAM203AHPRD 
HELBHPRD 
HUS1BioGRID 
_MINT 
MCM2HPRD 
MCM4BioGRID 
MCM6BioGRID 
MCM7BioGRID 
ORC2BioGRID 
ORC6BioGRID 
PCNAHPRD 
PRIM1BioGRID 
PRKDCDIP 
RAD52BioGRID 
RAD52BioGRID 
RNPC4IntAct 
TCEA2HPRD 
RAD51HPRD 
TCEA2HPRD 
C8orf30AIntAct 
RAD1BioGRID 
RAD51IntAct 
RAD52BioGRID 
RBM23HPRD 
RPA1HPRD 
RPA1HPRD 
RPA2BioGRID 
RPA3BioGRID 
SELENBP1HPRD 
TCEA2HPRD 
WRNIntAct 
XPADIP 
RPA2HPRD 
RPA3HPRD 
RPA4HPRD 
RMI1IntAct 
SELENBP1BioGRID 
SMARCA4BioGRID 
TCEA2BioGRID 
TIPINBioGRID 
TOPBP1BioGRID 
TP53BP1BioGRID 
E1MINT 
WRNHPRD 
XPAHPRD 
YOL086W-ABioGRID 
Other Protein-Protein interaction resources
String database  
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