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P14737

- RAD9_YEAST

UniProt

P14737 - RAD9_YEAST

Protein

DNA repair protein RAD9

Gene

RAD9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Essential for cell cycle arrest at the G2 stage following DNA damage by X-irradiation or inactivation of DNA ligase.

    GO - Molecular functioni

    1. double-stranded DNA binding Source: SGD
    2. enzyme activator activity Source: SGD
    3. histone binding Source: SGD
    4. protein binding Source: IntAct

    GO - Biological processi

    1. DNA damage checkpoint Source: SGD
    2. DNA repair Source: SGD
    3. G1 DNA damage checkpoint Source: SGD
    4. intra-S DNA damage checkpoint Source: SGD
    5. mitotic G1 DNA damage checkpoint Source: SGD
    6. negative regulation of DNA replication Source: UniProtKB-KW
    7. nucleotide-excision repair Source: SGD
    8. positive regulation of catalytic activity Source: GOC
    9. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    10. regulation of cell cycle Source: SGD

    Keywords - Molecular functioni

    DNA replication inhibitor

    Keywords - Biological processi

    Cell cycle, DNA damage

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29798-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein RAD9
    Gene namesi
    Name:RAD9
    Ordered Locus Names:YDR217C
    ORF Names:YD9934.02C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002625. RAD9.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13091309DNA repair protein RAD9PRO_0000097158Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261Phosphoserine3 Publications
    Modified residuei56 – 561Phosphoserine3 Publications
    Modified residuei205 – 2051Phosphoserine2 Publications
    Modified residuei218 – 2181Phosphothreonine2 Publications
    Modified residuei248 – 2481Phosphoserine2 Publications
    Modified residuei312 – 3121Phosphoserine2 Publications
    Modified residuei315 – 3151Phosphoserine3 Publications
    Modified residuei462 – 4621Phosphoserine3 Publications
    Modified residuei471 – 4711Phosphothreonine2 Publications
    Modified residuei474 – 4741Phosphothreonine2 Publications
    Modified residuei568 – 5681Phosphoserine2 Publications
    Modified residuei729 – 7291Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14737.
    PaxDbiP14737.

    Expressioni

    Gene expression databases

    GenevestigatoriP14737.

    Interactioni

    Subunit structurei

    Physically associates with RAD53.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DPB11P470279EBI-14788,EBI-25984
    RAD53P222163EBI-14788,EBI-17843

    Protein-protein interaction databases

    BioGridi32270. 356 interactions.
    DIPiDIP-2516N.
    IntActiP14737. 8 interactions.
    MINTiMINT-375284.
    STRINGi4932.YDR217C.

    Structurei

    Secondary structure

    1
    1309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi190 – 1923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FHRNMR-P826-832[»]
    1J4KNMR-P826-832[»]
    1J4LNMR-P599-607[»]
    1J4PNMR-B149-161[»]
    1J4QNMR-B188-200[»]
    1K2MNMR-P826-832[»]
    1K2NNMR-P599-607[»]
    1K3NNMR-B149-161[»]
    1K3QNMR-B188-200[»]
    2FF4X-ray1.90E/F188-195[»]
    ProteinModelPortaliP14737.
    SMRiP14737. Positions 998-1132.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14737.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini994 – 1122129BRCTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BRCT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG323789.
    KOiK06661.
    OrthoDBiEOG75J0WC.

    Family and domain databases

    Gene3Di3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR013914. Rad9_Rad53-bd_dom_fun.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    PF08605. Rad9_Rad53_bind. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 1 hit.
    [Graphical view]
    SUPFAMiSSF52113. SSF52113. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14737-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGQLVQWKS SPDRVTQSAI KEALHSPLAD GDMNEMNVPV DPLENKVNST     50
    NIIEGSPKAN PNPVKFMNTS EIFQKSLGLL DESPRHDDEL NIEVGDNDRP 100
    NANILHNERT PDLDRIANFF KSNRTPGKEN LLTKYQSSDL EDTPLMLRKK 150
    MTFQTPTDPL EQKTFKKLKS DTGFCYYGEQ NDGEENASLE VTEADATFVQ 200
    MAERSADNYD CALEGIVTPK RYKDELSKSG GMQDERVQKT QIMISAESPN 250
    SISSYDKNKI TGNGRTTRNV NKVFNNNEDN IGAIEEKNPV KKKSENYSSD 300
    DLRERNNQII QSNESEEINE LEKNLNVSGR ENDVNNLDID INSAVSGTPS 350
    RNNAEEEMYS SESVNNREPS KKWIFRYSKD KTENNSNRST QIVNNPRTQE 400
    MPLDSISIDT QPLSKSFNTE TNNELETQII VSSLSQGISA QKGPVFHSTG 450
    QTEEIKTQII NSPEQNALNA TFETPVTLSR INFEPILEVP ETSSPSKNTM 500
    SKPSNSSPIP KEKDTFNIHE REVETNNVFS NDIQNSSNAA TRDDIIIAGS 550
    SDFNEQKEIT DRIYLQLSGK QISDSGSDET ERMSPNELDT KKESTIMSEV 600
    ELTQELPEVE EQQDLQTSPK KLVVEEETLM EIKKSKGNSL QLHDDNKECN 650
    SDKQDGTESL DVALIEHESK GQSSELQKNL MQLFPSESQE IIQNRRTIKR 700
    RQKDTIEIGE EEENRSTKTS PTKHLKRNSD LDAASIKREP SCSITIQTGE 750
    TGSGKDSKEQ SYVFPEGIRT ADNSFLSKDD IIFGNAVWCQ YTWNYKFYPG 800
    ILLEVDTNQD GCWIYFETGR SLTKDEDIYY LDIRIGDAVT FDGNEYVVVG 850
    LECRSHDLNI IRCIRGYDTV HLKKKNASGL LGKRTLIKAL SSISLDLSEW 900
    AKRAKIILED NEKNKGDAYR YLRHPIRGRK SMTNVLSPKK HTDDEKDINT 950
    HTEVYNNEIE SSSEKKEIVK KDSRDALAEH AGAPSLLFSS GEIRTGNVFD 1000
    KCIFVLTSLF ENREELRQTI ESQGGTVIES GFSTLFNFTH PLAKSLVNKG 1050
    NTDNIRELAL KLAWKPHSLF ADCRFACLIT KRHLRSLKYL ETLALGWPTL 1100
    HWKFISACIE KKRIVPHLIY QYLLPSGESF RLSLDSPSKG GIIKSNNIFS 1150
    FYTQFLRGSN LRDQICGVKK MLNDYIVIVW GRSELDSFVK FAFACLSAGR 1200
    MLTIDLPNID VDDTEPLLNA LDSLVPRIGS ELSNRKLKFL IYANENNGKS 1250
    QMKLLERLRS QISLKFKKFN YIFHTESKEW LIQTIINEDT GFHDDITDND 1300
    IYNTISEVR 1309
    Length:1,309
    Mass (Da):148,398
    Last modified:October 5, 2010 - v2
    Checksum:iFCDAC16694484D8D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti433 – 4331S → C in AAA34954. (PubMed:2664461)Curated
    Sequence conflicti433 – 4331S → C no nucleotide entry (PubMed:2247073)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26049 Genomic DNA. Translation: AAA34954.1.
    Z48612 Genomic DNA. Translation: CAA88497.1.
    BK006938 Genomic DNA. Translation: DAA12060.1.
    PIRiS59424. BVBYD9.
    RefSeqiNP_010503.1. NM_001180525.1.

    Genome annotation databases

    EnsemblFungiiYDR217C; YDR217C; YDR217C.
    GeneIDi851803.
    KEGGisce:YDR217C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26049 Genomic DNA. Translation: AAA34954.1 .
    Z48612 Genomic DNA. Translation: CAA88497.1 .
    BK006938 Genomic DNA. Translation: DAA12060.1 .
    PIRi S59424. BVBYD9.
    RefSeqi NP_010503.1. NM_001180525.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FHR NMR - P 826-832 [» ]
    1J4K NMR - P 826-832 [» ]
    1J4L NMR - P 599-607 [» ]
    1J4P NMR - B 149-161 [» ]
    1J4Q NMR - B 188-200 [» ]
    1K2M NMR - P 826-832 [» ]
    1K2N NMR - P 599-607 [» ]
    1K3N NMR - B 149-161 [» ]
    1K3Q NMR - B 188-200 [» ]
    2FF4 X-ray 1.90 E/F 188-195 [» ]
    ProteinModelPortali P14737.
    SMRi P14737. Positions 998-1132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32270. 356 interactions.
    DIPi DIP-2516N.
    IntActi P14737. 8 interactions.
    MINTi MINT-375284.
    STRINGi 4932.YDR217C.

    Proteomic databases

    MaxQBi P14737.
    PaxDbi P14737.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR217C ; YDR217C ; YDR217C .
    GeneIDi 851803.
    KEGGi sce:YDR217C.

    Organism-specific databases

    SGDi S000002625. RAD9.

    Phylogenomic databases

    eggNOGi NOG323789.
    KOi K06661.
    OrthoDBi EOG75J0WC.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29798-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14737.
    NextBioi 969644.

    Gene expression databases

    Genevestigatori P14737.

    Family and domain databases

    Gene3Di 3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR013914. Rad9_Rad53-bd_dom_fun.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    PF08605. Rad9_Rad53_bind. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52113. SSF52113. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of the Saccharomyces cerevisiae RAD9 gene and further evidence that its product is required for cell cycle arrest induced by DNA damage."
      Schiestl R.H., Reynolds P., Prakash S., Prakash L.
      Mol. Cell. Biol. 9:1882-1896(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Characterization of RAD9 of Saccharomyces cerevisiae and evidence that its function acts posttranslationally in cell cycle arrest after DNA damage."
      Weinert T.A., Hartwell L.H.
      Mol. Cell. Biol. 10:6554-6564(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-dependent hyperphosphorylation and interacts with Rad53 after DNA damage."
      Vialard J.E., Gilbert C.S., Green C.M., Lowndes N.F.
      EMBO J. 17:5679-5688(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH RAD53.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-56; SER-205; THR-218; SER-248; SER-312; SER-315; SER-462; SER-568 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-26; SER-56; SER-315; SER-462; THR-471; THR-474 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRAD9_YEAST
    AccessioniPrimary (citable) accession number: P14737
    Secondary accession number(s): D6VSK0, Q04920
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 400 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3