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DDC1_YEAST
ID   DDC1_YEAST              Reviewed;         612 AA.
AC   Q08949; D6W3H4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=DNA damage checkpoint protein 1;
GN   Name=DDC1; OrderedLocusNames=YPL194W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, AND PHOSPHORYLATION.
RX   PubMed=9311982; DOI=10.1093/emboj/16.17.5216;
RA   Longhese M.P., Paciotti V., Fraschini R., Zaccarini R., Plevani P.,
RA   Lucchini G.;
RT   "The novel DNA damage checkpoint protein ddc1p is phosphorylated
RT   periodically during the cell cycle and in response to DNA damage in budding
RT   yeast.";
RL   EMBO J. 16:5216-5226(1997).
RN   [4]
RP   FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH MEC3.
RX   PubMed=9670034; DOI=10.1093/emboj/17.14.4199;
RA   Paciotti V., Lucchini G., Plevani P., Longhese M.P.;
RT   "Mec1p is essential for phosphorylation of the yeast DNA damage checkpoint
RT   protein Ddc1p, which physically interacts with Mec3p.";
RL   EMBO J. 17:4199-4209(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=10562568; DOI=10.1093/emboj/18.22.6561;
RA   Pellicioli A., Lucca C., Liberi G., Marini F., Lopes M., Plevani P.,
RA   Romano A., Di Fiore P.P., Foiani M.;
RT   "Activation of Rad53 kinase in response to DNA damage and its effect in
RT   modulating phosphorylation of the lagging strand DNA polymerase.";
RL   EMBO J. 18:6561-6572(1999).
RN   [6]
RP   IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP   CHECKPOINT CLAMP COMPLEX.
RX   PubMed=9891048; DOI=10.1128/mcb.19.2.1136;
RA   Kondo T., Matsumoto K., Sugimoto K.;
RT   "Role of a complex containing Rad17, Mec3, and Ddc1 in the yeast DNA damage
RT   checkpoint pathway.";
RL   Mol. Cell. Biol. 19:1136-1143(1999).
RN   [7]
RP   FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=11825877; DOI=10.1101/gad.938102;
RA   Hong E.-J.E., Roeder G.S.;
RT   "A role for Ddc1 in signaling meiotic double-strand breaks at the pachytene
RT   checkpoint.";
RL   Genes Dev. 16:363-376(2002).
RN   [8]
RP   INTERACTION WITH DPB11.
RX   PubMed=11973288; DOI=10.1093/genetics/160.4.1295;
RA   Wang H., Elledge S.J.;
RT   "Genetic and physical interactions between DPB11 and DDC1 in the yeast DNA
RT   damage response pathway.";
RL   Genetics 160:1295-1304(2002).
RN   [9]
RP   FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX   PubMed=12271137; DOI=10.1073/pnas.202463999;
RA   Giannattasio M., Sommariva E., Vercillo R., Lippi-Boncambi F., Liberi G.,
RA   Foiani M., Plevani P., Muzi-Falconi M.;
RT   "A dominant-negative MEC3 mutant uncovers new functions for the Rad17
RT   complex and Tel1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12997-13002(2002).
RN   [10]
RP   IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP   CHECKPOINT CLAMP COMPLEX.
RX   PubMed=12672803; DOI=10.1074/jbc.m301260200;
RA   Giannattasio M., Sabbioneda S., Minuzzo M., Plevani P., Muzi-Falconi M.;
RT   "Correlation between checkpoint activation and in vivo assembly of the
RT   yeast checkpoint complex Rad17-Mec3-Ddc1.";
RL   J. Biol. Chem. 278:22303-22308(2003).
RN   [11]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [12]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [13]
RP   PHOSPHORYLATION BY CDC28.
RX   PubMed=14574415; DOI=10.1038/nature02062;
RA   Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA   Shokat K.M., Morgan D.O.;
RT   "Targets of the cyclin-dependent kinase Cdk1.";
RL   Nature 425:859-864(2003).
RN   [14]
RP   INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT
RP   CLAMP LOADER COMPLEX, AND FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX   PubMed=12604797; DOI=10.1073/pnas.0437148100;
RA   Majka J., Burgers P.M.J.;
RT   "Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2249-2254(2003).
RN   [15]
RP   INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT
RP   CLAMP LOADER COMPLEX.
RX   PubMed=15014082; DOI=10.1074/jbc.m400898200;
RA   Majka J., Chung B.Y., Burgers P.M.J.;
RT   "Requirement for ATP by the DNA damage checkpoint clamp loader.";
RL   J. Biol. Chem. 279:20921-20926(2004).
RN   [16]
RP   IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP   CHECKPOINT CLAMP COMPLEX.
RX   PubMed=16137930; DOI=10.1016/j.dnarep.2005.07.008;
RA   Majka J., Burgers P.M.J.;
RT   "Function of Rad17/Mec3/Ddc1 and its partial complexes in the DNA damage
RT   checkpoint.";
RL   DNA Repair 4:1189-1194(2005).
RN   [17]
RP   INTERACTION WITH REV7, AND FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX   PubMed=16169844; DOI=10.1074/jbc.m507638200;
RA   Sabbioneda S., Minesinger B.K., Giannattasio M., Plevani P.,
RA   Muzi-Falconi M., Jinks-Robertson S.;
RT   "The 9-1-1 checkpoint clamp physically interacts with polzeta and is
RT   partially required for spontaneous polzeta-dependent mutagenesis in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 280:38657-38665(2005).
RN   [18]
RP   INTERACTION WITH MEC3 AND RAD17.
RX   PubMed=16202664; DOI=10.1016/j.dnarep.2005.08.018;
RA   Cardone J.M., Revers L.F., Machado R.M., Bonatto D., Brendel M.,
RA   Henriques J.A.P.;
RT   "Psoralen-sensitive mutant pso9-1 of Saccharomyces cerevisiae contains a
RT   mutant allele of the DNA damage checkpoint gene MEC3.";
RL   DNA Repair 5:163-171(2006).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC   -!- FUNCTION: Component of the checkpoint clamp complex involved in the
CC       surveillance mechanism that allows the DNA repair pathways to act to
CC       restore the integrity of the DNA prior to DNA synthesis or separation
CC       of the replicated chromosomes. Associates with sites of DNA damage and
CC       modulates the MEC1 signaling pathway and the activation of RAD53 in
CC       response to DNA damage at phase G1. The complex also physically
CC       regulates DNA polymerase zeta-dependent mutagenesis by controlling the
CC       access of polymerase zeta to damaged DNA. {ECO:0000269|PubMed:10562568,
CC       ECO:0000269|PubMed:11825877, ECO:0000269|PubMed:12271137,
CC       ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12672803,
CC       ECO:0000269|PubMed:16137930, ECO:0000269|PubMed:16169844,
CC       ECO:0000269|PubMed:9311982, ECO:0000269|PubMed:9670034,
CC       ECO:0000269|PubMed:9891048}.
CC   -!- SUBUNIT: Component of the checkpoint clamp complex composed of DDC1,
CC       MEC3 and RAD17. The interaction with MEC3 is performed in a RAD17-
CC       dependent manner. The checkpoint clamp complex loads onto DNA in an
CC       ATP-dependent manner through its interaction with the RFC-RAD4
CC       checkpoint clamp loader complex. Interacts with the DNA polymerase zeta
CC       subunit REV7 and DPB11. {ECO:0000269|PubMed:11973288,
CC       ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12672803,
CC       ECO:0000269|PubMed:15014082, ECO:0000269|PubMed:16137930,
CC       ECO:0000269|PubMed:16169844, ECO:0000269|PubMed:16202664,
CC       ECO:0000269|PubMed:9670034, ECO:0000269|PubMed:9891048}.
CC   -!- INTERACTION:
CC       Q08949; Q02574: MEC3; NbExp=5; IntAct=EBI-30769, EBI-10658;
CC       Q08949; P48581: RAD17; NbExp=4; IntAct=EBI-30769, EBI-14652;
CC       Q08949; P38927: REV7; NbExp=3; IntAct=EBI-30769, EBI-14960;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- PTM: Phosphorylated during cell cycle S-phase and in response to DNA
CC       damage. This phosphorylation is MEC14 dependent. Also hosphorylated by
CC       CDC28. {ECO:0000269|PubMed:11825877, ECO:0000269|PubMed:14574415,
CC       ECO:0000269|PubMed:9311982, ECO:0000269|PubMed:9670034}.
CC   -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DDC1 family. {ECO:0000305}.
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DR   EMBL; Z73550; CAA97907.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11240.1; -; Genomic_DNA.
DR   PIR; S65213; S65213.
DR   RefSeq; NP_015130.1; NM_001184008.1.
DR   PDB; 7SH2; EM; 3.23 A; H=1-612.
DR   PDB; 7ST9; EM; 2.20 A; G=1-612.
DR   PDB; 7STB; EM; 2.72 A; G=1-612.
DR   PDBsum; 7SH2; -.
DR   PDBsum; 7ST9; -.
DR   PDBsum; 7STB; -.
DR   AlphaFoldDB; Q08949; -.
DR   BioGRID; 35989; 223.
DR   ComplexPortal; CPX-1806; Rad17-Mec3-Ddc1 checkpoint clamp complex.
DR   DIP; DIP-2323N; -.
DR   IntAct; Q08949; 13.
DR   MINT; Q08949; -.
DR   STRING; 4932.YPL194W; -.
DR   iPTMnet; Q08949; -.
DR   MaxQB; Q08949; -.
DR   PaxDb; Q08949; -.
DR   PRIDE; Q08949; -.
DR   EnsemblFungi; YPL194W_mRNA; YPL194W; YPL194W.
DR   GeneID; 855907; -.
DR   KEGG; sce:YPL194W; -.
DR   SGD; S000006115; DDC1.
DR   VEuPathDB; FungiDB:YPL194W; -.
DR   eggNOG; ENOG502QT39; Eukaryota.
DR   HOGENOM; CLU_490204_0_0_1; -.
DR   InParanoid; Q08949; -.
DR   OMA; TTLCQVR; -.
DR   BioCyc; YEAST:G3O-34087-MON; -.
DR   Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR   PRO; PR:Q08949; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q08949; protein.
DR   GO; GO:0030896; C:checkpoint clamp complex; IDA:SGD.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:SGD.
DR   GO; GO:0032147; P:activation of protein kinase activity; IDA:SGD.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IBA:GO_Central.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IDA:ComplexPortal.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR   GO; GO:0051598; P:meiotic recombination checkpoint signaling; IMP:SGD.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0000725; P:recombinational repair; IDA:SGD.
DR   InterPro; IPR026217; Ddc1.
DR   InterPro; IPR007268; Rad9/Ddc1.
DR   PANTHER; PTHR15237; PTHR15237; 1.
DR   Pfam; PF04139; Rad9; 2.
DR   PRINTS; PR02063; DNADAMAGECP1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..612
FT                   /note="DNA damage checkpoint protein 1"
FT                   /id="PRO_0000239638"
FT   REGION          576..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
SQ   SEQUENCE   612 AA;  69694 MW;  F9933697C61021D3 CRC64;
     MSFKATITES GKQNIWFRAI YVLSTIQDDI KITVTTNELI AWSMNETDTT LCQVRFQKSF
     FEEYEFKPHE IVFGENGVQV IEDTYGNSHK LYSFRVNGRH LTTISRKPDG DGIKSFTIAV
     NNTSTCPESL ANRLIVVIEM DSLIVKEYCP QFQPIKYDPI IINLKYKRRF LDVFGTAASD
     RNPQEPLDPK LLDVFTNTER ELTSALFNEE VESDIRKRNQ LTAADEINYI CCNSTLLKNF
     LDNCNVNVTD EVKLEINVHR LSITAFTKAV YGKNNDLLRN ALSMSNTIST LDLEHYCLFT
     TIEDEKQDKR SHSKRREHMK SIIFKLKDFK NFITIGPSWK TTQDGNDNIS LWFCHPGDPI
     LMQMQKPGVK LELVEVTDSN INDDILEGKF IKTAISGSKE EAGLKDNKES CESPLKSKTA
     LKRENLPHSV AGTRNSPLKV SYLTPDNGST VAKTYRNNTA RKLFVEEQSQ STNYEQDKRF
     RQASSVHMNM NREQSFDIGT THEVACPRNE SNSLKRSIAD ICNETEDPTQ QSTFAKRADT
     TVTWGKALPA ADDEVSCSNI DRKGMLKKEK LKHMQGLLNS QNDTSNHKKQ DNKEMEDGLG
     LTQVEKPRGI FD
 
 
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