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Q8VEE4 (RFA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Replication protein A 70 kDa DNA-binding subunit, N-terminally processed
Gene names
Name:Rpa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing By similarity.

Subunit structure

Heterotrimer composed of RPA1, RPA2 and RPA3. The DNA-binding activity may reside exclusively on the RPA1 subunit. Interacts with RIPK1 and XPA. Interacts with RPA4. 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 By similarity. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with PRIMPOL By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

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.

Sequence similarities

Belongs to the replication factor A protein 1 family.

Contains 1 OB DNA-binding domain.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome organization

Inferred from mutant phenotype PubMed 15965476. Source: MGI

double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 15470499. Source: MGI

hemopoiesis

Inferred from mutant phenotype PubMed 15965476. Source: MGI

homeostasis of number of cells within a tissue

Inferred from mutant phenotype PubMed 15965476. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 15470499. Source: MGI

meiotic nuclear division

Inferred from direct assay PubMed 12091911. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15965476. Source: MGI

   Cellular_componentcondensed chromosome

Inferred from direct assay PubMed 12091911. Source: MGI

condensed nuclear chromosome

Inferred from direct assay PubMed 18283110PubMed 18316482PubMed 20551173PubMed 22164254. Source: MGI

lateral element

Inferred from direct assay PubMed 21743440PubMed 22711701. Source: MGI

male germ cell nucleus

Inferred from direct assay PubMed 17696610. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11555636. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from direct assay PubMed 12091911. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 623623Replication protein A 70 kDa DNA-binding subunit
PRO_0000097261
Initiator methionine11Removed; alternate By similarity
Chain2 – 623622Replication protein A 70 kDa DNA-binding subunit, N-terminally processed
PRO_0000423232

Regions

DNA binding206 – 29085OB

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1721N6-acetyllysine Ref.4
Modified residue1761N6-acetyllysine Ref.4
Modified residue1891Phosphothreonine By similarity
Modified residue2001Phosphothreonine By similarity
Modified residue2681N6-acetyllysine By similarity
Modified residue3931Phosphoserine By similarity
Cross-link458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link586Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Natural variant134 – 1352Missing.

Sequences

Sequence LengthMass (Da)Tools
Q8VEE4 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 2317F69F1E51B657

FASTA62369,037
        10         20         30         40         50         60 
MVGHLSEGAI EVMIQQENTS IKPILQVINI RPISTGNRSP RYRLLMSDGL NTLSSFMLAT 

        70         80         90        100        110        120 
QLNTLVEGGQ LASNCVCQVH KFIVNTLKDG RKVVVLMDLE VMKSAEDVGL KIGNPVPYNE 

       130        140        150        160        170        180 
GYGQQQQQQQ QQQQQAVPSP ASAATPPASK PQPQNGSLGM GSTAAKAYGA SKPFGKPAGT 

       190        200        210        220        230        240 
GLLQPSGGTQ SKVVPIASLT PYQSKWTICA RVTNKSQIRT WSNSRGEGKL FSLELVDESG 

       250        260        270        280        290        300 
EIRATAFNEQ VDKFFPLIEV NKVYYFSKGA LKIANKQFSA VKNDYEMTFN NETSVLPCED 

       310        320        330        340        350        360 
GHHLPTVQFD FTGIGDLESK AKDALVDIIG ICKSYEDSIK ITVKSNNREV AKRNIYLMDM 

       370        380        390        400        410        420 
SGKVVTTTLW GEDADKFDGS RQPVMAIKGA RVSDFGGRSL SVLSSSTVIV NPDIPEAYKL 

       430        440        450        460        470        480 
RGWFDSEGQA LDGVSISDHR SGGAGGGNTN WKTLHEAKSE NLGQGDKADY FSTVAAVVFL 

       490        500        510        520        530        540 
RKENCMYQAC PTQDCNKKVI DQQNGLYRCE KCDREFPNFK YRMILSANIA DFQENQWVTC 

       550        560        570        580        590        600 
FQESAEAILG QNTMYLGELK EKNEQAFEEV FQNANFRSFT FRIRVKLETY NDESRIKATV 

       610        620 
MDVKPVDFRD YGRRLIANIR KNM

« Hide

References

[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
CCDSCCDS25044.1.
RefSeqNP_001157695.1. NM_001164223.1.
NP_080929.1. NM_026653.2.
UniGeneMm.180734.
Mm.472099.

3D structure databases

ProteinModelPortalQ8VEE4.
SMRQ8VEE4. Positions 1-120, 192-623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212778. 6 interactions.
IntActQ8VEE4. 2 interactions.

Proteomic databases

MaxQBQ8VEE4.
PaxDbQ8VEE4.
PRIDEQ8VEE4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751.
GeneID68275.
KEGGmmu:68275.
UCSCuc007kdi.2. mouse.

Organism-specific databases

CTD6117.
MGIMGI:1915525. Rpa1.

Phylogenomic databases

eggNOGCOG1599.
GeneTreeENSGT00390000012403.
HOGENOMHOG000162322.
HOVERGENHBG010502.
KOK07466.
OrthoDBEOG7GXPBM.
PhylomeDBQ8VEE4.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressQ8VEE4.
BgeeQ8VEE4.
CleanExMM_RPA1.
GenevestigatorQ8VEE4.

Family and domain databases

Gene3D2.40.50.140. 4 hits.
InterProIPR012340. 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]
PfamPF04057. Rep-A_N. 1 hit.
PF08646. Rep_fac-A_C. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 4 hits.
TIGRFAMsTIGR00617. rpa1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRPA1. mouse.
NextBio326898.
PROQ8VEE4.
SOURCESearch...

Entry information

Entry nameRFA1_MOUSE
AccessionPrimary (citable) accession number: Q8VEE4
Secondary accession number(s): Q3TEJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents