DUN1_YEAST
ID DUN1_YEAST Reviewed; 513 AA.
AC P39009; D6VRP9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=DNA damage response protein kinase DUN1;
DE EC=2.7.11.1;
GN Name=DUN1; OrderedLocusNames=YDL101C; ORFNames=D2370;
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, AND MUTAGENESIS OF LYS-229 AND ASP-328.
RX PubMed=8261511; DOI=10.1016/0092-8674(93)90321-g;
RA Zhou Z., Elledge S.J.;
RT "DUN1 encodes a protein kinase that controls the DNA damage response in
RT yeast.";
RL Cell 75:1119-1127(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896274;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1077::aid-yea8>3.0.co;2-z;
RA Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.;
RT "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces
RT cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1
RT genes, and six new open reading frames.";
RL Yeast 12:1077-1084(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH PAN3.
RX PubMed=11953437; DOI=10.1074/jbc.m202473200;
RA Hammet A., Pike B.L., Heierhorst J.;
RT "Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1
RT kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival
RT of replication blocks.";
RL J. Biol. Chem. 277:22469-22474(2002).
RN [7]
RP FUNCTION IN PHOSPHORYLATION OF SML1.
RX PubMed=11904430; DOI=10.1073/pnas.062502299;
RA Zhao X., Rothstein R.;
RT "The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide
RT reductase inhibitor Sml1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3746-3751(2002).
RN [8]
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 [9]
RP IDENTIFICATION BY 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-139 AND THR-380, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Transducer of the DNA damage signal. Phosphorylates SML1 on
CC serine residues. Cooperates with the PAN deadenylation complex in the
CC regulation of RAD5 mRNA levels and cell survival in response to
CC replicational stress. {ECO:0000269|PubMed:11904430,
CC ECO:0000269|PubMed:11953437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with the PAB-dependent poly(A)-nuclease (PAN)
CC complex regulatory subunit PAN3 via its forkhead-associated (FHA)
CC domain. {ECO:0000269|PubMed:11953437}.
CC -!- INTERACTION:
CC P39009; Q12449: AHA1; NbExp=2; IntAct=EBI-6194, EBI-37072;
CC P39009; P26188: MGT1; NbExp=2; IntAct=EBI-6194, EBI-10873;
CC P39009; P32641: RAD24; NbExp=2; IntAct=EBI-6194, EBI-14675;
CC P39009; Q12021: RAD28; NbExp=2; IntAct=EBI-6194, EBI-29718;
CC P39009; P12753: RAD50; NbExp=2; IntAct=EBI-6194, EBI-14700;
CC P39009; P22216: RAD53; NbExp=3; IntAct=EBI-6194, EBI-17843;
CC P39009; P12954: SRS2; NbExp=3; IntAct=EBI-6194, EBI-18110;
CC P39009; Q05016: YMR226C; NbExp=2; IntAct=EBI-6194, EBI-27486;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Autophosphorylation increases in response to DNA damage.
CC -!- MISCELLANEOUS: Present with 3480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily. {ECO:0000305}.
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DR EMBL; L25548; AAA16324.1; -; Unassigned_DNA.
DR EMBL; X95644; CAA64912.1; -; Genomic_DNA.
DR EMBL; Z74149; CAA98668.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11759.1; -; Genomic_DNA.
DR PIR; S43941; S43941.
DR RefSeq; NP_010182.1; NM_001180160.1.
DR PDB; 2JQJ; NMR; -; A=19-159.
DR PDB; 2JQL; NMR; -; A=19-159.
DR PDBsum; 2JQJ; -.
DR PDBsum; 2JQL; -.
DR AlphaFoldDB; P39009; -.
DR SMR; P39009; -.
DR BioGRID; 31961; 491.
DR DIP; DIP-1772N; -.
DR IntAct; P39009; 57.
DR MINT; P39009; -.
DR STRING; 4932.YDL101C; -.
DR iPTMnet; P39009; -.
DR MaxQB; P39009; -.
DR PaxDb; P39009; -.
DR PRIDE; P39009; -.
DR EnsemblFungi; YDL101C_mRNA; YDL101C; YDL101C.
DR GeneID; 851457; -.
DR KEGG; sce:YDL101C; -.
DR SGD; S000002259; DUN1.
DR VEuPathDB; FungiDB:YDL101C; -.
DR eggNOG; KOG0615; Eukaryota.
DR GeneTree; ENSGT00800000124190; -.
DR HOGENOM; CLU_000288_63_47_1; -.
DR InParanoid; P39009; -.
DR OMA; NETRAIF; -.
DR BioCyc; YEAST:G3O-29504-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-69473; G2/M DNA damage checkpoint.
DR Reactome; R-SCE-69541; Stabilization of p53.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR EvolutionaryTrace; P39009; -.
DR PRO; PR:P39009; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39009; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:SGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0048478; P:replication fork protection; IGI:SGD.
DR CDD; cd00060; FHA; 1.
DR IDEAL; IID50174; -.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..513
FT /note="DNA damage response protein kinase DUN1"
FT /id="PRO_0000085930"
FT DOMAIN 56..112
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 200..480
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT BINDING 206..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 229
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:8261511"
FT MUTAGEN 328
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:8261511"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2JQL"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:2JQJ"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:2JQJ"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2JQL"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2JQJ"
SQ SEQUENCE 513 AA; 58633 MW; 4990F24F024702D7 CRC64;
MSLSTKREHS GDVTDSSFKR QQRSNKPSSE YTCLGHLVNL IPGKEQKVEI TNRNVTTIGR
SRSCDVILSE PDISTFHAEF HLLQMDVDNF QRNLINVIDK SRNGTFINGN RLVKKDYILK
NGDRIVFGKS CSFLFKYASS SSTDIENDDE KVSSESRSYK NDDEVFKKPQ ISATSSQNAT
TSAAIRKLNK TRPVSFFDKY LLGKELGAGH YALVKEAKNK KTGQQVAVKI FHAQQNDDQK
KNKQFREETN ILMRVQHPNI VNLLDSFVEP ISKSQIQKYL VLEKIDDGEL FERIVRKTCL
RQDESKALFK QLLTGLKYLH EQNIIHRDIK PENILLNITR RENPSQVQLG PWDEDEIDIQ
VKIADFGLAK FTGEMQFTNT LCGTPSYVAP EVLTKKGYTS KVDLWSAGVI LYVCLCGFPP
FSDQLGPPSL KEQILQAKYA FYSPYWDKID DSVLHLISNL LVLNPDERYN IDEALNHPWF
NDIQQQSSVS LELQRLQITD NKIPKTYSEL SCL
