Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Replication protein A 70 kDa DNA-binding subunit

Gene

RPA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Plays also a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance (PubMed:17959650). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105).10 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi197 – 28185OBAdd
BLAST
Zinc fingeri481 – 50323C4-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. damaged DNA binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. cellular response to heat Source: Reactome
  3. DNA-dependent DNA replication Source: ProtInc
  4. DNA recombinase assembly Source: Reactome
  5. DNA recombination Source: ProtInc
  6. DNA repair Source: Reactome
  7. DNA replication Source: UniProtKB
  8. DNA strand elongation involved in DNA replication Source: Reactome
  9. double-strand break repair Source: Reactome
  10. double-strand break repair via homologous recombination Source: UniProtKB
  11. G1/S transition of mitotic cell cycle Source: Reactome
  12. hemopoiesis Source: Ensembl
  13. homeostasis of number of cells within a tissue Source: Ensembl
  14. in utero embryonic development Source: Ensembl
  15. meiotic nuclear division Source: Ensembl
  16. mismatch repair Source: UniProtKB
  17. mitotic cell cycle Source: Reactome
  18. nucleotide-excision repair Source: UniProtKB
  19. nucleotide-excision repair, DNA damage removal Source: Reactome
  20. nucleotide-excision repair, DNA gap filling Source: Reactome
  21. positive regulation of cell proliferation Source: Ensembl
  22. regulation of cellular response to heat Source: Reactome
  23. telomere maintenance Source: UniProtKB
  24. telomere maintenance via recombination Source: Reactome
  25. telomere maintenance via semi-conservative replication Source: Reactome
  26. transcription-coupled nucleotide-excision repair Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2055. Processing of DNA double-strand break ends.
REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_257. Formation of incision complex in GG-NER.
REACT_264071. HSF1 activation.
REACT_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264487. Regulation of HSF1-mediated heat shock response.
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_27271. Meiotic recombination.
REACT_311. Dual incision reaction in GG-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_6769. Activation of ATR in response to replication stress.
REACT_70. Removal of the Flap Intermediate.
REACT_7999. Removal of the Flap Intermediate from the C-strand.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication protein A 70 kDa DNA-binding subunit
Short name:
RP-A p70
Alternative name(s):
Replication factor A protein 1
Short name:
RF-A protein 1
Single-stranded DNA-binding protein
Cleaved into the following chain:
Gene namesi
Name:RPA1
Synonyms:REPA1, RPA70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10289. RPA1.

Subcellular locationi

Nucleus 1 Publication. NucleusPML body 1 Publication
Note: Enriched in PML bodies in cells displaying alternative lengthening of their telomeres.1 Publication

GO - Cellular componenti

  1. DNA replication factor A complex Source: UniProtKB
  2. lateral element Source: Ensembl
  3. male germ cell nucleus Source: Ensembl
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
  6. PML body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411R → E: Loss of HELB-binding; when associated with E-43. 1 Publication
Mutagenesisi43 – 431R → E: Loss of HELB-binding; when associated with E-41. 1 Publication
Mutagenesisi449 – 4491K → R: Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577. 1 Publication
Mutagenesisi500 – 5001C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-503. 1 Publication
Mutagenesisi503 – 5031C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-500. 1 Publication
Mutagenesisi577 – 5771K → R: Slight sumoylation decrease. Loss of sumoylation; when associated with R-449. 1 Publication

Organism-specific databases

PharmGKBiPA34651.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 616616Replication protein A 70 kDa DNA-binding subunitPRO_0000423231Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 616615Replication protein A 70 kDa DNA-binding subunit, N-terminally processedPRO_0000097260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei163 – 1631N6-acetyllysine1 Publication
Modified residuei167 – 1671N6-acetyllysine1 Publication
Modified residuei180 – 1801Phosphothreonine2 Publications
Modified residuei191 – 1911Phosphothreonine1 Publication
Modified residuei259 – 2591N6-acetyllysine1 Publication
Modified residuei384 – 3841Phosphoserine1 Publication
Cross-linki449 – 449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki577 – 577Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR.1 Publication
Sumoylated on lysine residues Lys-449 and Lys-577, with Lys-449 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP27694.
PaxDbiP27694.
PeptideAtlasiP27694.
PRIDEiP27694.

PTM databases

PhosphoSiteiP27694.

Expressioni

Gene expression databases

BgeeiP27694.
CleanExiHS_RPA1.
ExpressionAtlasiP27694. baseline and differential.
GenevestigatoriP27694.

Organism-specific databases

HPAiCAB004563.
HPA006914.
HPA046497.

Interactioni

Subunit structurei

Component of the canonical replication protein A complex (RPA), an heterotrimer composed of RPA1, RPA2 and RPA3. Also component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2. The DNA-binding activity may reside exclusively on the RPA1 subunit. Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA). Interacts with RIPK1. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with PRIMPOL. Interacts with XPA; the interaction is direct and associates XPA with the RPA complex.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030703EBI-621389,EBI-617698From a different organism.
BLMP541323EBI-621389,EBI-621372
POLA1P098842EBI-621389,EBI-850026
RPA2P159274EBI-621389,EBI-621404
RPA3P352444EBI-621389,EBI-621428
WRNQ141918EBI-621389,EBI-368417

Protein-protein interaction databases

BioGridi112037. 450 interactions.
DIPiDIP-24189N.
IntActiP27694. 44 interactions.
MINTiMINT-91488.
STRINGi9606.ENSP00000254719.

Structurei

Secondary structure

1
616
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi9 – 146Combined sources
Turni15 – 173Combined sources
Beta strandi18 – 203Combined sources
Beta strandi24 – 329Combined sources
Beta strandi36 – 383Combined sources
Beta strandi42 – 476Combined sources
Beta strandi49 – 5810Combined sources
Helixi60 – 623Combined sources
Helixi63 – 675Combined sources
Beta strandi70 – 745Combined sources
Beta strandi76 – 8611Combined sources
Beta strandi88 – 903Combined sources
Beta strandi92 – 10312Combined sources
Helixi105 – 1084Combined sources
Helixi187 – 1893Combined sources
Beta strandi198 – 2069Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi218 – 22710Combined sources
Beta strandi232 – 2387Combined sources
Helixi239 – 2457Combined sources
Helixi246 – 2483Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi261 – 2644Combined sources
Helixi267 – 2693Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi285 – 2884Combined sources
Helixi305 – 3106Combined sources
Beta strandi316 – 32611Combined sources
Beta strandi330 – 3345Combined sources
Turni335 – 3384Combined sources
Beta strandi339 – 34911Combined sources
Beta strandi355 – 3617Combined sources
Helixi362 – 3676Combined sources
Beta strandi375 – 38410Combined sources
Beta strandi388 – 3925Combined sources
Beta strandi398 – 4025Combined sources
Helixi406 – 41611Combined sources
Turni417 – 4193Combined sources
Helixi445 – 4517Combined sources
Turni452 – 4543Combined sources
Beta strandi455 – 4584Combined sources
Beta strandi460 – 47112Combined sources
Beta strandi477 – 4804Combined sources
Beta strandi491 – 4933Combined sources
Turni494 – 4963Combined sources
Beta strandi497 – 5004Combined sources
Turni501 – 5044Combined sources
Beta strandi505 – 5095Combined sources
Beta strandi512 – 52110Combined sources
Beta strandi526 – 5327Combined sources
Helixi533 – 5408Combined sources
Helixi544 – 5507Combined sources
Helixi555 – 56410Combined sources
Turni565 – 5673Combined sources
Beta strandi569 – 5779Combined sources
Beta strandi588 – 5969Combined sources
Helixi599 – 61517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EWINMR-A1-114[»]
1FGUX-ray2.50A/B182-432[»]
1JMCX-ray2.40A181-422[»]
1L1OX-ray2.80C/F436-616[»]
2B29X-ray1.60A1-120[»]
2B3GX-ray1.60A1-120[»]
4IJHX-ray1.50A1-120[»]
4IJLX-ray1.70A1-120[»]
4IPCX-ray1.22A1-120[»]
4IPDX-ray1.51A1-120[»]
4IPGX-ray1.58A1-120[»]
4IPHX-ray1.94A1-120[»]
4LUOX-ray1.54A1-120[»]
4LUVX-ray1.40A1-120[»]
4LUZX-ray1.90A1-120[»]
4LW1X-ray1.63A1-120[»]
4LWCX-ray1.61A1-120[»]
4NB3X-ray1.35A/B1-120[»]
4O0AX-ray1.20A1-120[»]
4R4CX-ray1.40A1-120[»]
4R4IX-ray1.40A1-120[»]
4R4OX-ray1.33A1-120[»]
4R4QX-ray1.35A1-120[»]
4R4TX-ray1.28A1-120[»]
DisProtiDP00061.
ProteinModelPortaliP27694.
SMRiP27694. Positions 3-120, 183-616.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27694.

Family & Domainsi

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri481 – 50323C4-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1599.
GeneTreeiENSGT00390000012403.
HOGENOMiHOG000162322.
HOVERGENiHBG010502.
InParanoidiP27694.
KOiK07466.
OMAiVIAFKGC.
OrthoDBiEOG7GXPBM.
PhylomeDBiP27694.
TreeFamiTF105241.

Family and domain databases

Gene3Di2.40.50.140. 4 hits.
InterProiIPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
IPR013955. Rep_factor-A_C.
IPR007199. Rep_factor-A_N.
IPR004591. Rfa1.
[Graphical view]
PfamiPF04057. Rep-A_N. 1 hit.
PF08646. Rep_fac-A_C. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
TIGRFAMsiTIGR00617. rpa1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27694-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGQLSEGAI AAIMQKGDTN IKPILQVINI RPITTGNSPP RYRLLMSDGL
60 70 80 90 100
NTLSSFMLAT QLNPLVEEEQ LSSNCVCQIH RFIVNTLKDG RRVVILMELE
110 120 130 140 150
VLKSAEAVGV KIGNPVPYNE GLGQPQVAPP APAASPAASS RPQPQNGSSG
160 170 180 190 200
MGSTVSKAYG ASKTFGKAAG PSLSHTSGGT QSKVVPIASL TPYQSKWTIC
210 220 230 240 250
ARVTNKSQIR TWSNSRGEGK LFSLELVDES GEIRATAFNE QVDKFFPLIE
260 270 280 290 300
VNKVYYFSKG TLKIANKQFT AVKNDYEMTF NNETSVMPCE DDHHLPTVQF
310 320 330 340 350
DFTGIDDLEN KSKDSLVDII GICKSYEDAT KITVRSNNRE VAKRNIYLMD
360 370 380 390 400
TSGKVVTATL WGEDADKFDG SRQPVLAIKG ARVSDFGGRS LSVLSSSTII
410 420 430 440 450
ANPDIPEAYK LRGWFDAEGQ ALDGVSISDL KSGGVGGSNT NWKTLYEVKS
460 470 480 490 500
ENLGQGDKPD YFSSVATVVY LRKENCMYQA CPTQDCNKKV IDQQNGLYRC
510 520 530 540 550
EKCDTEFPNF KYRMILSVNI ADFQENQWVT CFQESAEAIL GQNAAYLGEL
560 570 580 590 600
KDKNEQAFEE VFQNANFRSF IFRVRVKVET YNDESRIKAT VMDVKPVDYR
610
EYGRRLVMSI RRSALM
Length:616
Mass (Da):68,138
Last modified:January 31, 1996 - v2
Checksum:iFE038F40F5886CD1
GO

Sequence cautioni

The sequence BAD92969.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti351 – 3511T → A.2 Publications
Corresponds to variant rs5030755 [ dbSNP | Ensembl ].
VAR_019236

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63488 mRNA. Translation: AAA36584.1.
AK289704 mRNA. Translation: BAF82393.1.
AB209732 mRNA. Translation: BAD92969.1. Different initiation.
AY599563 Genomic DNA. Translation: AAS94324.1.
CH471108 Genomic DNA. Translation: EAW90574.1.
BC018126 mRNA. Translation: AAH18126.1.
CCDSiCCDS11014.1.
PIRiA40457.
RefSeqiNP_002936.1. NM_002945.3.
UniGeneiHs.461925.

Genome annotation databases

EnsembliENST00000254719; ENSP00000254719; ENSG00000132383.
GeneIDi6117.
KEGGihsa:6117.
UCSCiuc002fto.2. human.

Polymorphism databases

DMDMi1350579.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63488 mRNA. Translation: AAA36584.1.
AK289704 mRNA. Translation: BAF82393.1.
AB209732 mRNA. Translation: BAD92969.1. Different initiation.
AY599563 Genomic DNA. Translation: AAS94324.1.
CH471108 Genomic DNA. Translation: EAW90574.1.
BC018126 mRNA. Translation: AAH18126.1.
CCDSiCCDS11014.1.
PIRiA40457.
RefSeqiNP_002936.1. NM_002945.3.
UniGeneiHs.461925.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EWINMR-A1-114[»]
1FGUX-ray2.50A/B182-432[»]
1JMCX-ray2.40A181-422[»]
1L1OX-ray2.80C/F436-616[»]
2B29X-ray1.60A1-120[»]
2B3GX-ray1.60A1-120[»]
4IJHX-ray1.50A1-120[»]
4IJLX-ray1.70A1-120[»]
4IPCX-ray1.22A1-120[»]
4IPDX-ray1.51A1-120[»]
4IPGX-ray1.58A1-120[»]
4IPHX-ray1.94A1-120[»]
4LUOX-ray1.54A1-120[»]
4LUVX-ray1.40A1-120[»]
4LUZX-ray1.90A1-120[»]
4LW1X-ray1.63A1-120[»]
4LWCX-ray1.61A1-120[»]
4NB3X-ray1.35A/B1-120[»]
4O0AX-ray1.20A1-120[»]
4R4CX-ray1.40A1-120[»]
4R4IX-ray1.40A1-120[»]
4R4OX-ray1.33A1-120[»]
4R4QX-ray1.35A1-120[»]
4R4TX-ray1.28A1-120[»]
DisProtiDP00061.
ProteinModelPortaliP27694.
SMRiP27694. Positions 3-120, 183-616.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112037. 450 interactions.
DIPiDIP-24189N.
IntActiP27694. 44 interactions.
MINTiMINT-91488.
STRINGi9606.ENSP00000254719.

Chemistry

BindingDBiP27694.
ChEMBLiCHEMBL1764940.

PTM databases

PhosphoSiteiP27694.

Polymorphism databases

DMDMi1350579.

Proteomic databases

MaxQBiP27694.
PaxDbiP27694.
PeptideAtlasiP27694.
PRIDEiP27694.

Protocols and materials databases

DNASUi6117.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254719; ENSP00000254719; ENSG00000132383.
GeneIDi6117.
KEGGihsa:6117.
UCSCiuc002fto.2. human.

Organism-specific databases

CTDi6117.
GeneCardsiGC17P001680.
HGNCiHGNC:10289. RPA1.
HPAiCAB004563.
HPA006914.
HPA046497.
MIMi179835. gene.
neXtProtiNX_P27694.
PharmGKBiPA34651.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1599.
GeneTreeiENSGT00390000012403.
HOGENOMiHOG000162322.
HOVERGENiHBG010502.
InParanoidiP27694.
KOiK07466.
OMAiVIAFKGC.
OrthoDBiEOG7GXPBM.
PhylomeDBiP27694.
TreeFamiTF105241.

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_2055. Processing of DNA double-strand break ends.
REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_257. Formation of incision complex in GG-NER.
REACT_264071. HSF1 activation.
REACT_264347. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_264487. Regulation of HSF1-mediated heat shock response.
REACT_264501. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_27271. Meiotic recombination.
REACT_311. Dual incision reaction in GG-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_6769. Activation of ATR in response to replication stress.
REACT_70. Removal of the Flap Intermediate.
REACT_7999. Removal of the Flap Intermediate from the C-strand.

Miscellaneous databases

ChiTaRSiRPA1. human.
EvolutionaryTraceiP27694.
GeneWikiiReplication_protein_A1.
GenomeRNAii6117.
NextBioi23755.
PROiP27694.
SOURCEiSearch...

Gene expression databases

BgeeiP27694.
CleanExiHS_RPA1.
ExpressionAtlasiP27694. baseline and differential.
GenevestigatoriP27694.

Family and domain databases

Gene3Di2.40.50.140. 4 hits.
InterProiIPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
IPR013955. Rep_factor-A_C.
IPR007199. Rep_factor-A_N.
IPR004591. Rfa1.
[Graphical view]
PfamiPF04057. Rep-A_N. 1 hit.
PF08646. Rep_fac-A_C. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
TIGRFAMsiTIGR00617. rpa1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.
    J. Biol. Chem. 266:12090-12098(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing."
    Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.
    J. Biol. Chem. 268:2268-2268(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 217.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-351.
    Tissue: Aortic endothelium.
  5. NIEHS SNPs program
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-351.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  8. Bienvenut W.V., Vousden K.H., Lukashchuk N.
    Submitted (FEB-2008) to UniProtKB
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  9. "Mammalian DNA nucleotide excision repair reconstituted with purified protein components."
    Aboussekhra A., Biggerstaff M., Shivji M.K., Vilpo J.A., Moncollin V., Podust V.N., Protic M., Huebscher U., Egly J.M., Wood R.D.
    Cell 80:859-868(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
  10. "RPA involvement in the damage-recognition and incision steps of nucleotide excision repair."
    He Z., Henricksen L.A., Wold M.S., Ingles C.J.
    Nature 374:566-569(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEOTIDE EXCISION REPAIR, INTERACTION WITH XPA.
  11. "Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex."
    Keshav K.F., Chen C., Dutta A.
    Mol. Cell. Biol. 15:3119-3128(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPA4.
  12. "Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms."
    Braun K.A., Lao Y., He Z., Ingles C.J., Wold M.S.
    Biochemistry 36:8443-8454(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLA1.
  13. "The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair."
    Lin Y.L., Shivji M.K., Chen C., Kolodner R., Wood R.D., Dutta A.
    J. Biol. Chem. 273:1453-1461(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPLICATION, FUNCTION IN DNA MISMATCH REPAIR, FUNCTION IN NUCLEOTIDE EXCISION REPAIR, MUTAGENESIS OF CYS-500 AND CYS-503.
  14. "Replication protein A stimulates long patch DNA base excision repair."
    DeMott M.S., Zigman S., Bambara R.A.
    J. Biol. Chem. 273:27492-27498(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BASE EXCISION REPAIR.
  15. "Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA."
    Ikegami T., Kuraoka I., Saijo M., Kodo N., Kyogoku Y., Morikawa K., Tanaka K., Shirakawa M.
    Nat. Struct. Biol. 5:701-706(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XPA.
  16. "Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies."
    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.
    Biochemistry 38:15116-15128(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XPA.
  17. "Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes."
    Zou L., Elledge S.J.
    Science 300:1542-1548(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CHEK1 SIGNALING.
  18. "Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies."
    Park J., Seo T., Kim H., Choe J.
    Mol. Cell. Biol. 25:8202-8214(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIPK1.
  19. "RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells."
    Sleeth K.M., Sorensen C.S., Issaeva N., Dziegielewski J., Bartek J., Helleday T.
    J. Mol. Biol. 373:38-47(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR.
  20. "Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres."
    Grudic A., Jul-Larsen A., Haring S.J., Wold M.S., Loenning P.E., Bjerkvig R., Boee S.O.
    Nucleic Acids Res. 35:7267-7278(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TELOMERE MAINTENANCE, SUBCELLULAR LOCATION.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "An alternative form of replication protein a prevents viral replication in vitro."
    Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F., Wold M.S.
    J. Biol. Chem. 284:5324-5331(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ARPA COMPLEX, FUNCTION OF THE ARPA COMPLEX.
  25. "Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA."
    Salas T.R., Petruseva I., Lavrik O., Saintome C.
    Nucleic Acids Res. 37:38-46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SINGLE-STRANDED DNA-BINDING.
  26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-167 AND LYS-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "An alternative form of replication protein a expressed in normal human tissues supports DNA repair."
    Kemp M.G., Mason A.C., Carreira A., Reardon J.T., Haring S.J., Borgstahl G.E., Kowalczykowski S.C., Sancar A., Wold M.S.
    J. Biol. Chem. 285:4788-4797(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ARPA COMPLEX.
  28. "Regulation of DNA repair through desumoylation and sumoylation of replication protein A complex."
    Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.
    Mol. Cell 39:333-345(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-449 AND LYS-577, DESUMOYLATION BY SENP6, MUTAGENESIS OF LYS-449 AND LYS-577, INTERACTION WITH SENP6 AND RAD51.
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180; THR-191 AND SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Human DNA helicase B (HDHB) binds to replication protein A and facilitates cellular recovery from replication stress."
    Guler G.D., Liu H., Vaithiyalingam S., Arnett D.R., Kremmer E., Chazin W.J., Fanning E.
    J. Biol. Chem. 287:6469-6481(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HELB, MUTAGENESIS OF ARG-41 AND ARG-43.
  32. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity."
    Wan L., Lou J., Xia Y., Su B., Liu T., Cui J., Sun Y., Lou H., Huang J.
    EMBO Rep. 14:1104-1112(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRIMPOL.
  34. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  35. "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry."
    Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S., Jimenez A.E., Jin J., Zou L.
    Mol. Cell 53:235-246(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRPF19, UBIQUITINATION BY PRPF19.
  36. "Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA."
    Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L.
    Nature 385:176-181(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 183-420.

Entry informationi

Entry nameiRFA1_HUMAN
AccessioniPrimary (citable) accession number: P27694
Secondary accession number(s): A8K0Y9, Q59ES9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: January 31, 1996
Last modified: March 31, 2015
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.