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Protein

DNA damage response protein kinase DUN1

Gene

DUN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transducer of the DNA damage signal. Phosphorylates SML1 on serine residues. Cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei229 – 2291ATP
Active sitei328 – 3281Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2149ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • DNA damage checkpoint Source: SGD
  • peptidyl-serine phosphorylation Source: SGD
  • peptidyl-threonine phosphorylation Source: SGD
  • protein phosphorylation Source: SGD
  • replication fork protection Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29504-MONOMER.
BRENDAi2.7.11.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA damage response protein kinase DUN1 (EC:2.7.11.1)
Gene namesi
Name:DUN1
Ordered Locus Names:YDL101C
ORF Names:D2370
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL101C.
SGDiS000002259. DUN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi229 – 2291K → R: Loss of kinase activity. 1 Publication
Mutagenesisi328 – 3281D → A: Loss of kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513DNA damage response protein kinase DUN1PRO_0000085930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei139 – 1391PhosphoserineCombined sources
Modified residuei380 – 3801PhosphothreonineCombined sources

Post-translational modificationi

Autophosphorylation increases in response to DNA damage.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39009.

PTM databases

iPTMnetiP39009.

Interactioni

Subunit structurei

Interacts with the PAB-dependent poly(A)-nuclease (PAN) complex regulatory subunit PAN3 via its forkhead-associated (FHA) domain.1 Publication

Protein-protein interaction databases

BioGridi31961. 408 interactions.
DIPiDIP-1772N.
IntActiP39009. 16 interactions.
MINTiMINT-410328.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 303Combined sources
Beta strandi33 – 419Combined sources
Beta strandi44 – 518Combined sources
Beta strandi56 – 616Combined sources
Beta strandi64 – 674Combined sources
Beta strandi77 – 8711Combined sources
Beta strandi90 – 9910Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi121 – 1277Combined sources
Turni128 – 1303Combined sources
Beta strandi131 – 1377Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi154 – 1574Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQJNMR-A19-159[»]
2JQLNMR-A19-159[»]
ProteinModelPortaliP39009.
SMRiP39009. Positions 19-511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 11257FHAPROSITE-ProRule annotationAdd
BLAST
Domaini200 – 480281Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00840000129794.
HOGENOMiHOG000233016.
InParanoidiP39009.
KOiK06641.
OMAiLGPWDED.
OrthoDBiEOG793BK1.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR000253. FHA_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 3 hits.
PfamiPF00498. FHA. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSTKREHS GDVTDSSFKR QQRSNKPSSE YTCLGHLVNL IPGKEQKVEI
60 70 80 90 100
TNRNVTTIGR SRSCDVILSE PDISTFHAEF HLLQMDVDNF QRNLINVIDK
110 120 130 140 150
SRNGTFINGN RLVKKDYILK NGDRIVFGKS CSFLFKYASS SSTDIENDDE
160 170 180 190 200
KVSSESRSYK NDDEVFKKPQ ISATSSQNAT TSAAIRKLNK TRPVSFFDKY
210 220 230 240 250
LLGKELGAGH YALVKEAKNK KTGQQVAVKI FHAQQNDDQK KNKQFREETN
260 270 280 290 300
ILMRVQHPNI VNLLDSFVEP ISKSQIQKYL VLEKIDDGEL FERIVRKTCL
310 320 330 340 350
RQDESKALFK QLLTGLKYLH EQNIIHRDIK PENILLNITR RENPSQVQLG
360 370 380 390 400
PWDEDEIDIQ VKIADFGLAK FTGEMQFTNT LCGTPSYVAP EVLTKKGYTS
410 420 430 440 450
KVDLWSAGVI LYVCLCGFPP FSDQLGPPSL KEQILQAKYA FYSPYWDKID
460 470 480 490 500
DSVLHLISNL LVLNPDERYN IDEALNHPWF NDIQQQSSVS LELQRLQITD
510
NKIPKTYSEL SCL
Length:513
Mass (Da):58,633
Last modified:February 1, 1995 - v1
Checksum:i4990F24F024702D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25548 Unassigned DNA. Translation: AAA16324.1.
X95644 Genomic DNA. Translation: CAA64912.1.
Z74149 Genomic DNA. Translation: CAA98668.1.
BK006938 Genomic DNA. Translation: DAA11759.1.
PIRiS43941.
RefSeqiNP_010182.1. NM_001180160.1.

Genome annotation databases

EnsemblFungiiYDL101C; YDL101C; YDL101C.
GeneIDi851457.
KEGGisce:YDL101C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25548 Unassigned DNA. Translation: AAA16324.1.
X95644 Genomic DNA. Translation: CAA64912.1.
Z74149 Genomic DNA. Translation: CAA98668.1.
BK006938 Genomic DNA. Translation: DAA11759.1.
PIRiS43941.
RefSeqiNP_010182.1. NM_001180160.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQJNMR-A19-159[»]
2JQLNMR-A19-159[»]
ProteinModelPortaliP39009.
SMRiP39009. Positions 19-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31961. 408 interactions.
DIPiDIP-1772N.
IntActiP39009. 16 interactions.
MINTiMINT-410328.

PTM databases

iPTMnetiP39009.

Proteomic databases

MaxQBiP39009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL101C; YDL101C; YDL101C.
GeneIDi851457.
KEGGisce:YDL101C.

Organism-specific databases

EuPathDBiFungiDB:YDL101C.
SGDiS000002259. DUN1.

Phylogenomic databases

GeneTreeiENSGT00840000129794.
HOGENOMiHOG000233016.
InParanoidiP39009.
KOiK06641.
OMAiLGPWDED.
OrthoDBiEOG793BK1.

Enzyme and pathway databases

BioCyciYEAST:G3O-29504-MONOMER.
BRENDAi2.7.11.1. 984.

Miscellaneous databases

EvolutionaryTraceiP39009.
PROiP39009.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR000253. FHA_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 3 hits.
PfamiPF00498. FHA. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DUN1 encodes a protein kinase that controls the DNA damage response in yeast."
    Zhou Z., Elledge S.J.
    Cell 75:1119-1127(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, MUTAGENESIS OF LYS-229 AND ASP-328.
  2. "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1 genes, and six new open reading frames."
    Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.
    Yeast 12:1077-1084(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames."
    Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
    Yeast 12:1377-1384(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks."
    Hammet A., Pike B.L., Heierhorst J.
    J. Biol. Chem. 277:22469-22474(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAN3.
  7. "The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1."
    Zhao X., Rothstein R.
    Proc. Natl. Acad. Sci. U.S.A. 99:3746-3751(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SML1.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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].
  10. "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-10; SER-139 AND THR-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDUN1_YEAST
AccessioniPrimary (citable) accession number: P39009
Secondary accession number(s): D6VRP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 163 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 3480 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.