UniProtKB - P27694 (RFA1_HUMAN)
Protein
Replication protein A 70 kDa DNA-binding subunit
Gene
RPA1
Organism
Homo sapiens (Human)
Status
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 (PubMed:27723720, PubMed:27723717). 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). 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).12 Publications
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
- single-stranded DNA binding Source: UniProtKB
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: ProtInc
- DNA recombination Source: ProtInc
- DNA repair Source: CACAO
- DNA replication Source: UniProtKB
- 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
- 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, 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
- telomere maintenance Source: UniProtKB
- telomere maintenance via semi-conservative replication Source: Reactome
- 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
| 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 |
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 |
Pathology & 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 |
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
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 (PubMed:24332808). Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination (PubMed:26474068).2 Publications
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 conjugationProteomic databases
| EPDi | P27694 |
| MaxQBi | P27694 |
| PaxDbi | P27694 |
| PeptideAtlasi | P27694 |
| PRIDEi | P27694 |
| ProteomicsDBi | 54405 |
PTM databases
| iPTMneti | P27694 |
| PhosphoSitePlusi | P27694 |
| SwissPalmi | P27694 |
Expressioni
Gene expression databases
| Bgeei | ENSG00000132383 Expressed in 235 organ(s), highest expression level in secondary oocyte |
| CleanExi | HS_RPA1 |
| ExpressionAtlasi | P27694 baseline and differential |
| Genevisiblei | P27694 HS |
Organism-specific databases
| HPAi | CAB004563 HPA006914 HPA046497 |
Interactioni
Subunit structurei
Component of the canonical replication protein A complex (RPA), an 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 (PubMed:24126761). 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).15 Publications
Binary interactionsi
Protein-protein interaction databases
| BioGridi | 112037, 484 interactors |
| CORUMi | P27694 |
| DIPi | DIP-24189N |
| IntActi | P27694, 77 interactors |
| MINTi | P27694 |
| STRINGi | 9606.ENSP00000254719 |
Chemistry databases
| BindingDBi | P27694 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
| DisProti | DP00061 |
| ProteinModelPortali | P27694 |
| SMRi | P27694 |
| ModBasei | Search... |
| MobiDBi | Search... |
Miscellaneous databases
| EvolutionaryTracei | P27694 |
Family & Domainsi
Sequence similaritiesi
Belongs to the replication factor A protein 1 family.Curated
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 COG1599 LUCA |
| GeneTreei | ENSGT00390000012403 |
| HOGENOMi | HOG000162322 |
| HOVERGENi | HBG010502 |
| InParanoidi | P27694 |
| KOi | K07466 |
| OMAi | DMTRNKL |
| OrthoDBi | EOG091G02VJ |
| PhylomeDBi | P27694 |
| TreeFami | TF105241 |
Family and domain databases
| CDDi | cd04476 RPA1_DBD_C, 1 hit cd04477 RPA1N, 1 hit |
| 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 |
Sequence (1+)i
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
P27694-1 [UniParc]FASTAAdd to basket
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 basket| I3L2M5 | 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
The sequence BAD92969 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
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 |
| UniGenei | Hs.461925 Hs.595562 |
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 |
| UniGenei | Hs.461925 Hs.595562 |
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 | [»] | |
| DisProti | DP00061 | |||||
| ProteinModelPortali | P27694 | |||||
| SMRi | P27694 | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Protein-protein interaction databases
| BioGridi | 112037, 484 interactors |
| CORUMi | P27694 |
| DIPi | DIP-24189N |
| IntActi | P27694, 77 interactors |
| MINTi | P27694 |
| STRINGi | 9606.ENSP00000254719 |
Chemistry databases
| BindingDBi | P27694 |
| ChEMBLi | CHEMBL1764940 |
PTM databases
| iPTMneti | P27694 |
| PhosphoSitePlusi | P27694 |
| SwissPalmi | P27694 |
Polymorphism and mutation databases
| BioMutai | RPA1 |
| DMDMi | 1350579 |
Proteomic databases
| EPDi | P27694 |
| MaxQBi | P27694 |
| PaxDbi | P27694 |
| PeptideAtlasi | P27694 |
| PRIDEi | P27694 |
| ProteomicsDBi | 54405 |
Protocols and materials databases
| DNASUi | 6117 |
| Structural Biology Knowledgebase | Search... |
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 | CAB004563 HPA006914 HPA046497 |
| MIMi | 179835 gene |
| neXtProti | NX_P27694 |
| OpenTargetsi | ENSG00000132383 |
| PharmGKBi | PA34651 |
| GenAtlasi | Search... |
Phylogenomic databases
| eggNOGi | KOG0851 Eukaryota COG1599 LUCA |
| GeneTreei | ENSGT00390000012403 |
| HOGENOMi | HOG000162322 |
| HOVERGENi | HBG010502 |
| InParanoidi | P27694 |
| KOi | K07466 |
| OMAi | DMTRNKL |
| OrthoDBi | EOG091G02VJ |
| PhylomeDBi | P27694 |
| TreeFami | TF105241 |
Enzyme and pathway databases
| 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 |
Miscellaneous databases
| ChiTaRSi | RPA1 human |
| EvolutionaryTracei | P27694 |
| GeneWikii | Replication_protein_A1 |
| GenomeRNAii | 6117 |
| PROi | PR:P27694 |
| SOURCEi | Search... |
Gene expression databases
| Bgeei | ENSG00000132383 Expressed in 235 organ(s), highest expression level in secondary oocyte |
| CleanExi | HS_RPA1 |
| ExpressionAtlasi | P27694 baseline and differential |
| Genevisiblei | P27694 HS |
Family and domain databases
| CDDi | cd04476 RPA1_DBD_C, 1 hit cd04477 RPA1N, 1 hit |
| 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... |
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: | October 10, 2018 | |
| This is version 201 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, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - SIMILARITY comments
Index of protein domains and families - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM - 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
