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Q8VEE4 - RFA1_MOUSE

UniProt

Q8VEE4 - RFA1_MOUSE

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Protein

Replication protein A 70 kDa DNA-binding subunit

Gene

Rpa1

Organism
Mus musculus (Mouse)
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. 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. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. 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. Plays also a role in base excision repair (BER) probably through interaction with UNG. 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.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi206 – 29085OBAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. chromosome organization Source: MGI
  3. DNA replication Source: UniProtKB
  4. double-strand break repair via homologous recombination Source: MGI
  5. hemopoiesis Source: MGI
  6. homeostasis of number of cells within a tissue Source: MGI
  7. in utero embryonic development Source: MGI
  8. meiotic nuclear division Source: MGI
  9. mismatch repair Source: UniProtKB
  10. nucleotide-excision repair Source: UniProtKB
  11. positive regulation of cell proliferation Source: MGI
  12. telomere maintenance Source: MGI
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_198629. Meiotic recombination.
REACT_209299. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_216529. Removal of the Flap Intermediate from the C-strand.
REACT_219381. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_222185. Regulation of HSF1-mediated heat shock response.
REACT_232236. Activation of ATR in response to replication stress.
REACT_235085. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_240368. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_240507. Dual incision reaction in GG-NER.
REACT_245362. Processing of DNA double-strand break ends.
REACT_246095. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_251075. Removal of the Flap Intermediate.
REACT_252106. Formation of incision complex in GG-NER.
REACT_254983. Activation of the pre-replicative complex.
REACT_261855. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_27235. Meiotic Recombination.

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
Cleaved into the following chain:
Replication protein A 70 kDa DNA-binding subunit, N-terminally processed
Gene namesi
Name:Rpa1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1915525. Rpa1.

Subcellular locationi

Nucleus By similarity. Nucleus › PML body By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. condensed chromosome Source: MGI
  3. condensed nuclear chromosome Source: MGI
  4. cytoplasm Source: MGI
  5. DNA replication factor A complex Source: UniProtKB
  6. lateral element Source: MGI
  7. male germ cell nucleus Source: MGI
  8. nucleoplasm Source: Reactome
  9. nucleus Source: MGI
  10. PML body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623Replication protein A 70 kDa DNA-binding subunitPRO_0000097261Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 623622Replication protein A 70 kDa DNA-binding subunit, N-terminally processedPRO_0000423232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei176 – 1761N6-acetyllysine1 Publication
Modified residuei189 – 1891PhosphothreonineBy similarity
Modified residuei200 – 2001PhosphothreonineBy similarity
Modified residuei268 – 2681N6-acetyllysineBy similarity
Modified residuei393 – 3931PhosphoserineBy similarity
Cross-linki458 – 458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki586 – 586Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

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.By similarity
Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8VEE4.
PaxDbiQ8VEE4.
PRIDEiQ8VEE4.

Expressioni

Gene expression databases

BgeeiQ8VEE4.
CleanExiMM_RPA1.
ExpressionAtlasiQ8VEE4. baseline and differential.
GenevestigatoriQ8VEE4.

Interactioni

Subunit structurei

Component of the canonical replication protein A complex (RPA), an heterotrimer composed of RPA1, RPA2 and RPA3. 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.By similarity

Protein-protein interaction databases

BioGridi212778. 6 interactions.
IntActiQ8VEE4. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8VEE4.
SMRiQ8VEE4. Positions 1-120, 192-623.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the replication factor A protein 1 family.Curated
Contains 1 OB DNA-binding domain.Curated

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1599.
GeneTreeiENSGT00390000012403.
HOGENOMiHOG000162322.
HOVERGENiHBG010502.
InParanoidiQ8VEE4.
KOiK07466.
OrthoDBiEOG7GXPBM.
PhylomeDBiQ8VEE4.

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.

Q8VEE4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVGHLSEGAI EVMIQQENTS IKPILQVINI RPISTGNRSP RYRLLMSDGL 
        60         70         80         90        100
NTLSSFMLAT QLNTLVEGGQ LASNCVCQVH KFIVNTLKDG RKVVVLMDLE 
       110        120        130        140        150
VMKSAEDVGL KIGNPVPYNE GYGQQQQQQQ QQQQQAVPSP ASAATPPASK 
       160        170        180        190        200
PQPQNGSLGM GSTAAKAYGA SKPFGKPAGT GLLQPSGGTQ SKVVPIASLT 
       210        220        230        240        250
PYQSKWTICA RVTNKSQIRT WSNSRGEGKL FSLELVDESG EIRATAFNEQ 
       260        270        280        290        300
VDKFFPLIEV NKVYYFSKGA LKIANKQFSA VKNDYEMTFN NETSVLPCED 
       310        320        330        340        350
GHHLPTVQFD FTGIGDLESK AKDALVDIIG ICKSYEDSIK ITVKSNNREV 
       360        370        380        390        400
AKRNIYLMDM SGKVVTTTLW GEDADKFDGS RQPVMAIKGA RVSDFGGRSL 
       410        420        430        440        450
SVLSSSTVIV NPDIPEAYKL RGWFDSEGQA LDGVSISDHR SGGAGGGNTN 
       460        470        480        490        500
WKTLHEAKSE NLGQGDKADY FSTVAAVVFL RKENCMYQAC PTQDCNKKVI 
       510        520        530        540        550
DQQNGLYRCE KCDREFPNFK YRMILSANIA DFQENQWVTC FQESAEAILG 
       560        570        580        590        600
QNTMYLGELK EKNEQAFEEV FQNANFRSFT FRIRVKLETY NDESRIKATV 
       610        620 
MDVKPVDFRD YGRRLIANIR KNM
Length:623
Mass (Da):69,037
Last modified:March 1, 2002 - v1
Checksum:i2317F69F1E51B657
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti134 – 1352Missing.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK148035 mRNA. Translation: BAE28302.1.
AK150785 mRNA. Translation: BAE29849.1.
AK151590 mRNA. Translation: BAE30530.1.
AK153144 mRNA. Translation: BAE31755.1.
AK165316 mRNA. Translation: BAE38134.1.
AK165944 mRNA. Translation: BAE38476.1.
AK167598 mRNA. Translation: BAE39655.1.
AK169599 mRNA. Translation: BAE41250.1.
AL603834 Genomic DNA. Translation: CAI23976.1.
BC019119 mRNA. Translation: AAH19119.1.
CCDSiCCDS25044.1.
RefSeqiNP_001157695.1. NM_001164223.1.
NP_080929.1. NM_026653.2.
UniGeneiMm.180734.
Mm.472099.

Genome annotation databases

EnsembliENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751.
GeneIDi68275.
KEGGimmu:68275.
UCSCiuc007kdi.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK148035 mRNA. Translation: BAE28302.1.
AK150785 mRNA. Translation: BAE29849.1.
AK151590 mRNA. Translation: BAE30530.1.
AK153144 mRNA. Translation: BAE31755.1.
AK165316 mRNA. Translation: BAE38134.1.
AK165944 mRNA. Translation: BAE38476.1.
AK167598 mRNA. Translation: BAE39655.1.
AK169599 mRNA. Translation: BAE41250.1.
AL603834 Genomic DNA. Translation: CAI23976.1.
BC019119 mRNA. Translation: AAH19119.1.
CCDSiCCDS25044.1.
RefSeqiNP_001157695.1. NM_001164223.1.
NP_080929.1. NM_026653.2.
UniGeneiMm.180734.
Mm.472099.

3D structure databases

ProteinModelPortaliQ8VEE4.
SMRiQ8VEE4. Positions 1-120, 192-623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212778. 6 interactions.
IntActiQ8VEE4. 2 interactions.

Proteomic databases

MaxQBiQ8VEE4.
PaxDbiQ8VEE4.
PRIDEiQ8VEE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751.
GeneIDi68275.
KEGGimmu:68275.
UCSCiuc007kdi.2. mouse.

Organism-specific databases

CTDi6117.
MGIiMGI:1915525. Rpa1.

Phylogenomic databases

eggNOGiCOG1599.
GeneTreeiENSGT00390000012403.
HOGENOMiHOG000162322.
HOVERGENiHBG010502.
InParanoidiQ8VEE4.
KOiK07466.
OrthoDBiEOG7GXPBM.
PhylomeDBiQ8VEE4.

Enzyme and pathway databases

ReactomeiREACT_198629. Meiotic recombination.
REACT_209299. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_216529. Removal of the Flap Intermediate from the C-strand.
REACT_219381. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_222185. Regulation of HSF1-mediated heat shock response.
REACT_232236. Activation of ATR in response to replication stress.
REACT_235085. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_240368. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_240507. Dual incision reaction in GG-NER.
REACT_245362. Processing of DNA double-strand break ends.
REACT_246095. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
REACT_251075. Removal of the Flap Intermediate.
REACT_252106. Formation of incision complex in GG-NER.
REACT_254983. Activation of the pre-replicative complex.
REACT_261855. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_27235. Meiotic Recombination.

Miscellaneous databases

ChiTaRSiRpa1. mouse.
NextBioi326898.
PROiQ8VEE4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VEE4.
CleanExiMM_RPA1.
ExpressionAtlasiQ8VEE4. baseline and differential.
GenevestigatoriQ8VEE4.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT 134-GLN-GLN-135 DEL.
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Liver, Lung, Spleen and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Entry informationi

Entry nameiRFA1_MOUSE
AccessioniPrimary (citable) accession number: Q8VEE4
Secondary accession number(s): Q3TEJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2002
Last modified: February 4, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.