Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32849

- RAD5_YEAST

UniProt

P32849 - RAD5_YEAST

Protein

DNA repair protein RAD5

Gene

RAD5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA repair.8 Publications

    Cofactori

    Magnesium, manganese or calcium.

    Kineticsi

    1. KM=525 µM for ATP

    pH dependencei

    Optimum pH is 7.0. for ATPase activity.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi532 – 5398ATPPROSITE-ProRule annotation
    Zinc fingeri914 – 96148RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA-dependent ATPase activity Source: SGD
    3. four-way junction DNA binding Source: SGD
    4. four-way junction helicase activity Source: SGD
    5. Y-form DNA binding Source: SGD
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA duplex unwinding Source: GOC
    3. double-strand break repair Source: SGD
    4. error-prone translesion synthesis Source: SGD
    5. free ubiquitin chain polymerization Source: SGD
    6. postreplication repair Source: SGD
    7. protein polyubiquitination Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32191-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein RAD5 (EC:3.6.4.-)
    Alternative name(s):
    Radiation sensitivity protein 5
    Revertibility protein 2
    Gene namesi
    Name:RAD5
    Synonyms:REV2, SNM2
    Ordered Locus Names:YLR032W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR032w.
    SGDiS000004022. RAD5.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome, telomeric region Source: SGD
    2. cytoplasm Source: UniProtKB-SubCell
    3. nuclear chromatin Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi538 – 5392KT → AA: Increased sensitivity toward ionizing radiation. 1 Publication
    Mutagenesisi914 – 9141C → S: Abolishes interaction with UBC13. 3 Publications
    Mutagenesisi916 – 9161I → A: Abolishes interaction with UBC13. 2 Publications
    Mutagenesisi944 – 9441Y → A: Abolishes interaction with UBC13. 2 Publications
    Mutagenesisi959 – 9591N → A: Abolishes interaction with UBC13. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 11691168DNA repair protein RAD5PRO_0000056130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei20 – 201Phosphoserine1 Publication
    Modified residuei23 – 231Phosphoserine1 Publication
    Modified residuei129 – 1291Phosphoserine1 Publication
    Modified residuei130 – 1301Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP32849.
    PaxDbiP32849.
    PeptideAtlasiP32849.

    Expressioni

    Gene expression databases

    GenevestigatoriP32849.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13.4 Publications

    Protein-protein interaction databases

    BioGridi31306. 158 interactions.
    DIPiDIP-5830N.
    IntActiP32849. 3 interactions.
    MINTiMINT-2784640.
    STRINGi4932.YLR032W.

    Structurei

    3D structure databases

    ProteinModelPortaliP32849.
    SMRiP32849. Positions 527-900, 911-966, 993-1168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini519 – 730212Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini995 – 1165171Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi681 – 6844DEGH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi42 – 6019Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi303 – 31513Arg/Lys-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri914 – 96148RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00740000115627.
    HOGENOMiHOG000040492.
    KOiK15505.
    OMAiKHGLSWM.
    OrthoDBiEOG7PCJR9.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.40.50.300. 4 hits.
    InterProiIPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014905. HIRAN.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF08797. HIRAN. 1 hit.
    PF00176. SNF2_N. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00910. HIRAN. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P32849-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHIEQEERK RFFNDDLDTS ETSLNFKSEN KESFLFANSH NDDDDDVVVS     50
    VSDTTEGEGD RSIVPVRREI EEEGQNQFIT ELLRIIPEMP KDLVMELNEK 100
    FGSQEEGLSL ALSHYFDHNS GTSISKIPSS PNQLNTLSDT SNSTLSPSSF 150
    HPKRRRIYGF RNQTRLEDKV TWKRFIGALQ VTGMATRPTV RPLKYGSQMK 200
    LKRSSEEISA TKVYDSRGRK KASMASLVRI FDIQYDREIG RVSEDIAQIL 250
    YPLLSSHEIS FEVTLIFCDN KRLSIGDSFI LQLDCFLTSL IFEERNDGES 300
    LMKRRRTEGG NKREKDNGNF GRTLTETDEE LESRSKRLAL LKLFDKLRLK 350
    PILDEQKALE KHKIELNSDP EIIDLDNDEI CSNQVTEVHN NLRDTQHEEE 400
    TMNLNQLKTF YKAAQSSESL KSLPETEPSR DVFKLELRNY QKQGLTWMLR 450
    REQEFAKAAS DGEASETGAN MINPLWKQFK WPNDMSWAAQ NLQQDHVNVE 500
    DGIFFYANLH SGEFSLAKPI LKTMIKGGIL SDEMGLGKTV AAYSLVLSCP 550
    HDSDVVDKKL FDIENTAVSD NLPSTWQDNK KPYASKTTLI VVPMSLLTQW 600
    SNEFTKANNS PDMYHEVYYG GNVSSLKTLL TKTKTPPTVV LTTYGIVQNE 650
    WTKHSKGRMT DEDVNISSGL FSVNFYRIII DEGHNIRNRT TVTSKAVMAL 700
    QGKCKWVLTG TPIINRLDDL YSLVKFLELD PWRQINYWKT FVSTPFESKN 750
    YKQAFDVVNA ILEPVLLRRT KQMKDKDGKP LVELPPKEVV IKRLPFSKSQ 800
    DLLYKFLLDK AEVSVKSGIA RGDLLKKYST ILVHILRLRQ VCCHPGLIGS 850
    QDENDEDLSK NNKLVTEQTV ELDSLMRVVS ERFDNSFSKE ELDAMIQRLK 900
    VKYPDNKSFQ SLECSICTTE PMDLDKALFT ECGHSFCEKC LFEYIEFQNS 950
    KNLGLKCPNC RNQIDACRLL ALVQTNSNSK NLEFKPYSPA SKSSKITALL 1000
    KELQLLQDSS AGEQVVIFSQ FSTYLDILEK ELTHTFSKDV AKIYKFDGRL 1050
    SLKERTSVLA DFAVKDYSRQ KILLLSLKAG GVGLNLTCAS HAYMMDPWWS 1100
    PSMEDQAIDR LHRIGQTNSV KVMRFIIQDS IEEKMLRIQE KKRTIGEAMD 1150
    TDEDERRKRR IEEIQMLFE 1169
    Length:1,169
    Mass (Da):134,002
    Last modified:October 1, 1993 - v1
    Checksum:i226B720097433EE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti478 – 4781Q → R in AAB23590. (PubMed:1394508)Curated
    Sequence conflicti635 – 6351T → N in AAB23590. (PubMed:1394508)Curated
    Sequence conflicti846 – 8461G → S in AAB23590. (PubMed:1394508)Curated
    Sequence conflicti898 – 8981R → S in AAB23590. (PubMed:1394508)Curated
    Sequence conflicti973 – 9731V → A in AAB23590. (PubMed:1394508)Curated
    Sequence conflicti1063 – 10631A → R in AAB23590. (PubMed:1394508)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96644 Genomic DNA. Translation: AAA34951.1.
    Z73204 Genomic DNA. Translation: CAA97556.1.
    S46103 Genomic DNA. Translation: AAB23590.1.
    BK006945 Genomic DNA. Translation: DAA09350.1.
    PIRiS64859.
    RefSeqiNP_013132.1. NM_001181919.1.

    Genome annotation databases

    EnsemblFungiiYLR032W; YLR032W; YLR032W.
    GeneIDi850719.
    KEGGisce:YLR032W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96644 Genomic DNA. Translation: AAA34951.1 .
    Z73204 Genomic DNA. Translation: CAA97556.1 .
    S46103 Genomic DNA. Translation: AAB23590.1 .
    BK006945 Genomic DNA. Translation: DAA09350.1 .
    PIRi S64859.
    RefSeqi NP_013132.1. NM_001181919.1.

    3D structure databases

    ProteinModelPortali P32849.
    SMRi P32849. Positions 527-900, 911-966, 993-1168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31306. 158 interactions.
    DIPi DIP-5830N.
    IntActi P32849. 3 interactions.
    MINTi MINT-2784640.
    STRINGi 4932.YLR032W.

    Proteomic databases

    MaxQBi P32849.
    PaxDbi P32849.
    PeptideAtlasi P32849.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR032W ; YLR032W ; YLR032W .
    GeneIDi 850719.
    KEGGi sce:YLR032W.

    Organism-specific databases

    CYGDi YLR032w.
    SGDi S000004022. RAD5.

    Phylogenomic databases

    eggNOGi COG0553.
    GeneTreei ENSGT00740000115627.
    HOGENOMi HOG000040492.
    KOi K15505.
    OMAi KHGLSWM.
    OrthoDBi EOG7PCJR9.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32191-MONOMER.

    Miscellaneous databases

    NextBioi 966793.

    Gene expression databases

    Genevestigatori P32849.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.40.50.300. 4 hits.
    InterProi IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014905. HIRAN.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF08797. HIRAN. 1 hit.
    PF00176. SNF2_N. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00910. HIRAN. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA helicase and zinc-binding sequence motifs and affects the stability of simple repetitive sequences in the genome."
      Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M., Prakash L.
      Mol. Cell. Biol. 12:3807-3818(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The REV2 gene of Saccharomyces cerevisiae: cloning and DNA sequence."
      Ahne F., Baur M., Eckardt-Schupp F.
      Curr. Genet. 22:277-282(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-1063.
    5. "Yeast DNA repair protein RAD5 that promotes instability of simple repetitive sequences is a DNA-dependent ATPase."
      Johnson R.E., Prakash S., Prakash L.
      J. Biol. Chem. 269:28259-28262(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "The RAD5 gene product is involved in the avoidance of non-homologous end-joining of DNA double strand breaks in the yeast Saccharomyces cerevisiae."
      Ahne F., Ja B., Eckardt-Schupp F.
      Nucleic Acids Res. 25:743-749(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair."
      Ulrich H.D., Jentsch S.
      EMBO J. 19:3388-3397(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-914, SUBUNIT, INTERACTION WITH RAD18 AND UBC13.
    8. "The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways."
      Xiao W., Chow B.L., Broomfield S., Hanna M.
      Genetics 155:1633-1641(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae."
      Torres-Ramos C.A., Prakash S., Prakash L.
      Mol. Cell. Biol. 22:2419-2426(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO."
      Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.
      Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH POL30 AND UBC9.
    11. "Protein-protein interactions within an E2-RING finger complex. Implications for ubiquitin-dependent DNA damage repair."
      Ulrich H.D.
      J. Biol. Chem. 278:7051-7058(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH UBC13, MUTAGENESIS OF CYS-914; ILE-916; TYR-944 AND ASN-959.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner."
      Chen S., Davies A.A., Sagan D., Ulrich H.D.
      Nucleic Acids Res. 33:5878-5886(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH POL30; RAD18 AND UBC13, MUTAGENESIS OF 538-LYS-THR-539.
    15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-129 AND SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRAD5_YEAST
    AccessioniPrimary (citable) accession number: P32849
    Secondary accession number(s): D6VY34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1520 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3