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Q8VEE4

- RFA1_MOUSE

UniProt

Q8VEE4 - RFA1_MOUSE

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
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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.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

    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

    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

    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

    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.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

    Contains 1 OB DNA-binding domain.Curated

    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.1 Publication

    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: October 1, 2014
    This is version 108 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