UniProtKB - P27694 (RFA1_HUMAN)
Replication protein A 70 kDa DNA-binding subunit
RPA1
Functioni
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 197 – 281 | OBAdd BLAST | 85 | |
Zinc fingeri | 481 – 503 | C4-typeSequence analysisAdd BLAST | 23 |
GO - Molecular functioni
- damaged DNA binding Source: UniProtKB
- G-rich strand telomeric DNA binding Source: BHF-UCL
- metal ion binding Source: UniProtKB-KW
- sequence-specific DNA binding Source: GO_Central
- single-stranded DNA binding Source: UniProtKB
- single-stranded telomeric DNA binding Source: GO_Central
GO - Biological processi
- base-excision repair Source: UniProtKB
- cellular response to DNA damage stimulus Source: UniProtKB
- DNA damage response, detection of DNA damage Source: Reactome
- DNA-dependent DNA replication Source: GO_Central
- DNA recombination Source: ProtInc
- DNA repair Source: CACAO
- DNA replication Source: UniProtKB
- DNA unwinding involved in DNA replication Source: GO_Central
- double-strand break repair via homologous recombination Source: UniProtKB
- error-free translesion synthesis Source: Reactome
- error-prone translesion synthesis Source: Reactome
- G1/S transition of mitotic cell cycle Source: Reactome
- interstrand cross-link repair Source: Reactome
- meiotic cell cycle Source: GO_Central
- mismatch repair Source: UniProtKB
- nucleotide-excision repair Source: UniProtKB
- nucleotide-excision repair, DNA gap filling Source: Reactome
- nucleotide-excision repair, DNA incision Source: Reactome
- nucleotide-excision repair, DNA incision, 3'-to lesion Source: Reactome
- nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
- nucleotide-excision repair, preincision complex assembly Source: Reactome
- nucleotide-excision repair, preincision complex stabilization Source: Reactome
- protein localization to chromosome Source: UniProtKB
- regulation of cellular response to heat Source: Reactome
- regulation of signal transduction by p53 class mediator Source: Reactome
- telomere maintenance Source: UniProtKB
- telomere maintenance via semi-conservative replication Source: Reactome
- telomere maintenance via telomerase Source: GO_Central
- transcription-coupled nucleotide-excision repair Source: Reactome
- translesion synthesis Source: Reactome
Keywordsi
Molecular function | DNA-binding |
Biological process | DNA damage, DNA recombination, DNA repair, DNA replication |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
PathwayCommonsi | P27694 |
Reactomei | R-HSA-110312, Translesion synthesis by REV1 R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex R-HSA-110320, Translesion Synthesis by POLH R-HSA-174437, Removal of the Flap Intermediate from the C-strand R-HSA-176187, Activation of ATR in response to replication stress R-HSA-3108214, SUMOylation of DNA damage response and repair proteins R-HSA-3371453, Regulation of HSF1-mediated heat shock response R-HSA-3371511, HSF1 activation R-HSA-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-HSA-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) R-HSA-5651801, PCNA-Dependent Long Patch Base Excision Repair R-HSA-5655862, Translesion synthesis by POLK R-HSA-5656121, Translesion synthesis by POLI R-HSA-5656169, Termination of translesion DNA synthesis R-HSA-5685938, HDR through Single Strand Annealing (SSA) R-HSA-5685942, HDR through Homologous Recombination (HRR) R-HSA-5693607, Processing of DNA double-strand break ends R-HSA-5693616, Presynaptic phase of homologous DNA pairing and strand exchange R-HSA-5696395, Formation of Incision Complex in GG-NER R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER R-HSA-5696400, Dual Incision in GG-NER R-HSA-6782135, Dual incision in TC-NER R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-6783310, Fanconi Anemia Pathway R-HSA-6804756, Regulation of TP53 Activity through Phosphorylation R-HSA-68962, Activation of the pre-replicative complex R-HSA-69166, Removal of the Flap Intermediate R-HSA-69473, G2/M DNA damage checkpoint R-HSA-912446, Meiotic recombination |
SIGNORi | P27694 |
Names & Taxonomyi
Protein namesi | Recommended name: Replication protein A 70 kDa DNA-binding subunitShort 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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000132383.11 |
HGNCi | HGNC:10289, RPA1 |
MIMi | 179835, gene |
neXtProti | NX_P27694 |
Subcellular locationi
Nucleus
- DNA replication factor A complex Source: UniProtKB
- nuclear chromosome, telomeric region Source: BHF-UCL
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
- PML body Source: MGI
Other locations
- site of DNA damage Source: UniProtKB
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 41 | R → E: Loss of HELB-binding; when associated with E-43. 1 Publication | 1 | |
Mutagenesisi | 43 | R → E: Loss of HELB-binding; when associated with E-41. 1 Publication | 1 | |
Mutagenesisi | 449 | K → R: Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577. 1 Publication | 1 | |
Mutagenesisi | 500 | C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-503. 1 Publication | 1 | |
Mutagenesisi | 503 | C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-500. 1 Publication | 1 | |
Mutagenesisi | 577 | K → R: Slight sumoylation decrease. Loss of sumoylation; when associated with R-449. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 6117 |
OpenTargetsi | ENSG00000132383 |
PharmGKBi | PA34651 |
Miscellaneous databases
Pharosi | P27694, Tchem |
Chemistry databases
ChEMBLi | CHEMBL1764940 |
Polymorphism and mutation databases
BioMutai | RPA1 |
DMDMi | 1350579 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000423231 | 1 – 616 | Replication protein A 70 kDa DNA-binding subunitAdd BLAST | 616 | |
Initiator methioninei | Removed; alternate1 Publication | |||
ChainiPRO_0000097260 | 2 – 616 | Replication protein A 70 kDa DNA-binding subunit, N-terminally processedAdd BLAST | 615 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineCombined sources | 1 | |
Cross-linki | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 88 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Modified residuei | 163 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 163 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication | ||
Modified residuei | 167 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 167 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication | ||
Modified residuei | 180 | PhosphothreonineCombined sources | 1 | |
Cross-linki | 183 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Modified residuei | 191 | PhosphothreonineCombined sources | 1 | |
Cross-linki | 220 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 244 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Modified residuei | 259 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 259 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication | ||
Cross-linki | 267 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 331 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Modified residuei | 384 | PhosphoserineCombined sources | 1 | |
Cross-linki | 410 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 431 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 449 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication | ||
Cross-linki | 458 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 553 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 577 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P27694 |
jPOSTi | P27694 |
MassIVEi | P27694 |
MaxQBi | P27694 |
PaxDbi | P27694 |
PeptideAtlasi | P27694 |
PRIDEi | P27694 |
ProteomicsDBi | 54405 |
PTM databases
iPTMneti | P27694 |
MetOSitei | P27694 |
PhosphoSitePlusi | P27694 |
SwissPalmi | P27694 |
Expressioni
Gene expression databases
Bgeei | ENSG00000132383, Expressed in secondary oocyte and 247 other tissues |
ExpressionAtlasi | P27694, baseline and differential |
Genevisiblei | P27694, HS |
Organism-specific databases
HPAi | ENSG00000132383, Low tissue specificity |
Interactioni
Subunit structurei
Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3 (PubMed:27723720, PubMed:27723717). 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 (PubMed:7760808, PubMed:19116208). 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) (PubMed:24332808).
Interacts with RIPK1 (PubMed:16135809).
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 (PubMed:9214288).
Interacts with RAD51 and SENP6 to regulate DNA repair (PubMed:20705237).
Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage (PubMed:22194613, PubMed:26774285).
Interacts with PRIMPOL; leading to recruit PRIMPOL on chromatin and stimulate its DNA primase activity (PubMed:24126761, PubMed:25550423, PubMed:28534480).
Interacts with XPA; the interaction is direct and associates XPA with the RPA complex (PubMed:7700386, PubMed:9699634, PubMed:10563794).
Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks (PubMed:27601467, PubMed:27723720, PubMed:27723717).
Interacts with RPA1; this interaction associates HROB with the RPA complex (By similarity).
By similarity17 PublicationsBinary interactionsi
Hide detailsP27694
Protein-protein interaction databases
BioGRIDi | 112037, 547 interactors |
CORUMi | P27694 |
DIPi | DIP-24189N |
IntActi | P27694, 87 interactors |
MINTi | P27694 |
STRINGi | 9606.ENSP00000254719 |
Chemistry databases
BindingDBi | P27694 |
Miscellaneous databases
RNActi | P27694, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P27694 |
SASBDBi | P27694 |
SMRi | P27694 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P27694 |
Family & Domainsi
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 481 – 503 | C4-typeSequence analysisAdd BLAST | 23 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG0851, Eukaryota |
GeneTreei | ENSGT00390000012403 |
HOGENOMi | CLU_012393_2_1_1 |
InParanoidi | P27694 |
OMAi | YRLLINM |
OrthoDBi | 1189265at2759 |
PhylomeDBi | P27694 |
TreeFami | TF105241 |
Family and domain databases
CDDi | cd04476, RPA1_DBD_C, 1 hit cd04477, RPA1N, 1 hit |
DisProti | DP00061 |
IDEALi | IID00036 |
InterProi | View protein in InterPro IPR012340, NA-bd_OB-fold IPR004365, NA-bd_OB_tRNA IPR013955, Rep_factor-A_C IPR007199, Rep_factor-A_N IPR031657, REPA_OB_2 IPR004591, Rfa1 |
Pfami | View protein in Pfam PF04057, Rep-A_N, 1 hit PF08646, Rep_fac-A_C, 1 hit PF16900, REPA_OB_2, 1 hit PF01336, tRNA_anti-codon, 1 hit |
SUPFAMi | SSF50249, SSF50249, 4 hits |
TIGRFAMsi | TIGR00617, rpa1, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketI3L2M5 | I3L2M5_HUMAN | Replication protein A 70 kDa DNA-bi... | RPA1 | 153 | Annotation score: | ||
I3L524 | I3L524_HUMAN | Replication protein A 70 kDa DNA-bi... | RPA1 | 124 | Annotation score: | ||
I3L4R8 | I3L4R8_HUMAN | Replication protein A 70 kDa DNA-bi... | RPA1 | 313 | Annotation score: |
Sequence cautioni
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_019236 | 351 | T → A2 PublicationsCorresponds to variant dbSNP:rs5030755Ensembl. | 1 |
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 |
CCDSi | CCDS11014.1 |
PIRi | A40457 |
RefSeqi | NP_002936.1, NM_002945.3 |
Genome annotation databases
Ensembli | ENST00000254719; ENSP00000254719; ENSG00000132383 |
GeneIDi | 6117 |
KEGGi | hsa:6117 |
UCSCi | uc002fto.3, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
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 |
CCDSi | CCDS11014.1 |
PIRi | A40457 |
RefSeqi | NP_002936.1, NM_002945.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EWI | NMR | - | A | 1-114 | [»] | |
1FGU | X-ray | 2.50 | A/B | 182-432 | [»] | |
1JMC | X-ray | 2.40 | A | 181-422 | [»] | |
1L1O | X-ray | 2.80 | C/F | 436-616 | [»] | |
2B29 | X-ray | 1.60 | A | 1-120 | [»] | |
2B3G | X-ray | 1.60 | A | 1-120 | [»] | |
4IJH | X-ray | 1.50 | A | 1-120 | [»] | |
4IJL | X-ray | 1.70 | A | 1-120 | [»] | |
4IPC | X-ray | 1.22 | A | 1-120 | [»] | |
4IPD | X-ray | 1.51 | A | 1-120 | [»] | |
4IPG | X-ray | 1.58 | A | 1-120 | [»] | |
4IPH | X-ray | 1.94 | A | 1-120 | [»] | |
4LUO | X-ray | 1.54 | A | 1-120 | [»] | |
4LUV | X-ray | 1.40 | A | 1-120 | [»] | |
4LUZ | X-ray | 1.90 | A | 1-120 | [»] | |
4LW1 | X-ray | 1.63 | A | 1-120 | [»] | |
4LWC | X-ray | 1.61 | A | 1-120 | [»] | |
4NB3 | X-ray | 1.35 | A/B | 1-120 | [»] | |
4O0A | X-ray | 1.20 | A | 1-120 | [»] | |
4R4C | X-ray | 1.40 | A | 1-120 | [»] | |
4R4I | X-ray | 1.40 | A | 1-120 | [»] | |
4R4O | X-ray | 1.33 | A | 1-120 | [»] | |
4R4Q | X-ray | 1.35 | A | 1-120 | [»] | |
4R4T | X-ray | 1.28 | A | 1-120 | [»] | |
5E7N | X-ray | 1.21 | A | 1-120 | [»] | |
5EAY | X-ray | 1.55 | A/B/C/D | 3-120 | [»] | |
5N85 | X-ray | 2.00 | A | 1-120 | [»] | |
5N8A | X-ray | 1.28 | A | 1-120 | [»] | |
BMRBi | P27694 | |||||
SASBDBi | P27694 | |||||
SMRi | P27694 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 112037, 547 interactors |
CORUMi | P27694 |
DIPi | DIP-24189N |
IntActi | P27694, 87 interactors |
MINTi | P27694 |
STRINGi | 9606.ENSP00000254719 |
Chemistry databases
BindingDBi | P27694 |
ChEMBLi | CHEMBL1764940 |
PTM databases
iPTMneti | P27694 |
MetOSitei | P27694 |
PhosphoSitePlusi | P27694 |
SwissPalmi | P27694 |
Polymorphism and mutation databases
BioMutai | RPA1 |
DMDMi | 1350579 |
Proteomic databases
EPDi | P27694 |
jPOSTi | P27694 |
MassIVEi | P27694 |
MaxQBi | P27694 |
PaxDbi | P27694 |
PeptideAtlasi | P27694 |
PRIDEi | P27694 |
ProteomicsDBi | 54405 |
Protocols and materials databases
Antibodypediai | 1868, 465 antibodies |
DNASUi | 6117 |
Genome annotation databases
Ensembli | ENST00000254719; ENSP00000254719; ENSG00000132383 |
GeneIDi | 6117 |
KEGGi | hsa:6117 |
UCSCi | uc002fto.3, human |
Organism-specific databases
CTDi | 6117 |
DisGeNETi | 6117 |
EuPathDBi | HostDB:ENSG00000132383.11 |
GeneCardsi | RPA1 |
HGNCi | HGNC:10289, RPA1 |
HPAi | ENSG00000132383, Low tissue specificity |
MIMi | 179835, gene |
neXtProti | NX_P27694 |
OpenTargetsi | ENSG00000132383 |
PharmGKBi | PA34651 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0851, Eukaryota |
GeneTreei | ENSGT00390000012403 |
HOGENOMi | CLU_012393_2_1_1 |
InParanoidi | P27694 |
OMAi | YRLLINM |
OrthoDBi | 1189265at2759 |
PhylomeDBi | P27694 |
TreeFami | TF105241 |
Enzyme and pathway databases
PathwayCommonsi | P27694 |
Reactomei | R-HSA-110312, Translesion synthesis by REV1 R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex R-HSA-110320, Translesion Synthesis by POLH R-HSA-174437, Removal of the Flap Intermediate from the C-strand R-HSA-176187, Activation of ATR in response to replication stress R-HSA-3108214, SUMOylation of DNA damage response and repair proteins R-HSA-3371453, Regulation of HSF1-mediated heat shock response R-HSA-3371511, HSF1 activation R-HSA-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-HSA-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) R-HSA-5651801, PCNA-Dependent Long Patch Base Excision Repair R-HSA-5655862, Translesion synthesis by POLK R-HSA-5656121, Translesion synthesis by POLI R-HSA-5656169, Termination of translesion DNA synthesis R-HSA-5685938, HDR through Single Strand Annealing (SSA) R-HSA-5685942, HDR through Homologous Recombination (HRR) R-HSA-5693607, Processing of DNA double-strand break ends R-HSA-5693616, Presynaptic phase of homologous DNA pairing and strand exchange R-HSA-5696395, Formation of Incision Complex in GG-NER R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER R-HSA-5696400, Dual Incision in GG-NER R-HSA-6782135, Dual incision in TC-NER R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-6783310, Fanconi Anemia Pathway R-HSA-6804756, Regulation of TP53 Activity through Phosphorylation R-HSA-68962, Activation of the pre-replicative complex R-HSA-69166, Removal of the Flap Intermediate R-HSA-69473, G2/M DNA damage checkpoint R-HSA-912446, Meiotic recombination |
SIGNORi | P27694 |
Miscellaneous databases
BioGRID-ORCSi | 6117, 767 hits in 849 CRISPR screens |
ChiTaRSi | RPA1, human |
EvolutionaryTracei | P27694 |
GeneWikii | Replication_protein_A1 |
GenomeRNAii | 6117 |
Pharosi | P27694, Tchem |
PROi | PR:P27694 |
RNActi | P27694, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000132383, Expressed in secondary oocyte and 247 other tissues |
ExpressionAtlasi | P27694, baseline and differential |
Genevisiblei | P27694, HS |
Family and domain databases
CDDi | cd04476, RPA1_DBD_C, 1 hit cd04477, RPA1N, 1 hit |
DisProti | DP00061 |
IDEALi | IID00036 |
InterProi | View protein in InterPro IPR012340, NA-bd_OB-fold IPR004365, NA-bd_OB_tRNA IPR013955, Rep_factor-A_C IPR007199, Rep_factor-A_N IPR031657, REPA_OB_2 IPR004591, Rfa1 |
Pfami | View protein in Pfam PF04057, Rep-A_N, 1 hit PF08646, Rep_fac-A_C, 1 hit PF16900, REPA_OB_2, 1 hit PF01336, tRNA_anti-codon, 1 hit |
SUPFAMi | SSF50249, SSF50249, 4 hits |
TIGRFAMsi | TIGR00617, rpa1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RFA1_HUMAN | |
Accessioni | P27694Primary (citable) accession number: P27694 Secondary accession number(s): A8K0Y9, Q59ES9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | February 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 219 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations