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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: 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. 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. metal ion binding Source: UniProtKB-KW
  3. 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
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_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:
Gene namesi
Name:Rpa1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1915525. Rpa1.

Subcellular locationi

Nucleus By similarity. NucleusPML body By similarity

GO - Cellular componenti

  1. condensed chromosome Source: MGI
  2. condensed nuclear chromosome Source: MGI
  3. DNA replication factor A complex Source: UniProtKB
  4. lateral element Source: MGI
  5. male germ cell nucleus Source: MGI
  6. nucleoplasm Source: Reactome
  7. nucleus 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; alternate By 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-acetylmethionine By similarity
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei176 – 1761N6-acetyllysine1 Publication
Modified residuei189 – 1891Phosphothreonine By similarity
Modified residuei200 – 2001Phosphothreonine By similarity
Modified residuei268 – 2681N6-acetyllysine By similarity
Modified residuei393 – 3931Phosphoserine By 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

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.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8VEE4.
PaxDbiQ8VEE4.
PRIDEiQ8VEE4.

Expressioni

Gene expression databases

ArrayExpressiQ8VEE4.
BgeeiQ8VEE4.
CleanExiMM_RPA1.
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 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.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1599.
GeneTreeiENSGT00390000012403.
HOGENOMiHOG000162322.
HOVERGENiHBG010502.
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. Rep_factor_Rpa1.
[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

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MVGHLSEGAI EVMIQQENTS IKPILQVINI RPISTGNRSP RYRLLMSDGL    50
NTLSSFMLAT QLNTLVEGGQ LASNCVCQVH KFIVNTLKDG RKVVVLMDLE 100
VMKSAEDVGL KIGNPVPYNE GYGQQQQQQQ QQQQQAVPSP ASAATPPASK 150
PQPQNGSLGM GSTAAKAYGA SKPFGKPAGT GLLQPSGGTQ SKVVPIASLT 200
PYQSKWTICA RVTNKSQIRT WSNSRGEGKL FSLELVDESG EIRATAFNEQ 250
VDKFFPLIEV NKVYYFSKGA LKIANKQFSA VKNDYEMTFN NETSVLPCED 300
GHHLPTVQFD FTGIGDLESK AKDALVDIIG ICKSYEDSIK ITVKSNNREV 350
AKRNIYLMDM SGKVVTTTLW GEDADKFDGS RQPVMAIKGA RVSDFGGRSL 400
SVLSSSTVIV NPDIPEAYKL RGWFDSEGQA LDGVSISDHR SGGAGGGNTN 450
WKTLHEAKSE NLGQGDKADY FSTVAAVVFL RKENCMYQAC PTQDCNKKVI 500
DQQNGLYRCE KCDREFPNFK YRMILSANIA DFQENQWVTC FQESAEAILG 550
QNTMYLGELK EKNEQAFEEV FQNANFRSFT FRIRVKLETY NDESRIKATV 600
MDVKPVDFRD YGRRLIANIR KNM 623
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25044.1.
RefSeqi NP_001157695.1. NM_001164223.1.
NP_080929.1. NM_026653.2.
UniGenei Mm.180734.
Mm.472099.

3D structure databases

ProteinModelPortali Q8VEE4.
SMRi Q8VEE4. Positions 1-120, 192-623.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212778. 6 interactions.
IntActi Q8VEE4. 2 interactions.

Proteomic databases

MaxQBi Q8VEE4.
PaxDbi Q8VEE4.
PRIDEi Q8VEE4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000092907 ; ENSMUSP00000090585 ; ENSMUSG00000000751 .
GeneIDi 68275.
KEGGi mmu:68275.
UCSCi uc007kdi.2. mouse.

Organism-specific databases

CTDi 6117.
MGIi MGI:1915525. Rpa1.

Phylogenomic databases

eggNOGi COG1599.
GeneTreei ENSGT00390000012403.
HOGENOMi HOG000162322.
HOVERGENi HBG010502.
KOi K07466.
OrthoDBi EOG7GXPBM.
PhylomeDBi Q8VEE4.

Enzyme and pathway databases

Reactomei REACT_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_27235. Meiotic Recombination.

Miscellaneous databases

ChiTaRSi RPA1. mouse.
NextBioi 326898.
PROi Q8VEE4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8VEE4.
Bgeei Q8VEE4.
CleanExi MM_RPA1.
Genevestigatori Q8VEE4.

Family and domain databases

Gene3Di 2.40.50.140. 4 hits.
InterProi IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
IPR013955. Rep_factor-A_C.
IPR007199. Rep_factor-A_N.
IPR004591. Rep_factor_Rpa1.
[Graphical view ]
Pfami PF04057. Rep-A_N. 1 hit.
PF08646. Rep_fac-A_C. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 4 hits.
TIGRFAMsi TIGR00617. rpa1. 1 hit.
ProtoNeti Search...

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.

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: September 3, 2014
This is version 107 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