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Q04089

- DOT1_YEAST

UniProt

Q04089 - DOT1_YEAST

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Protein
Histone-lysine N-methyltransferase, H3 lysine-79 specific
Gene
DOT1, KMT4, PCH1, YDR440W, D9461.26
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro).8 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].3 Publications

Enzyme regulationi

Ubiquitination of histone H2B by the RAD6/UBC2-BRE1 complex to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3. Interaction with DNA is required for optimal histone methyltransferase activity.2 Publications

pH dependencei

Optimum pH is 8 to 9.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei422 – 4221S-adenosyl-L-methionine

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. histone methyltransferase activity (H3-K79 specific) Source: SGD
  3. nucleosomal histone binding Source: SGD

GO - Biological processi

  1. DNA damage checkpoint Source: SGD
  2. G1 DNA damage checkpoint Source: SGD
  3. chromatin silencing at telomere Source: SGD
  4. global genome nucleotide-excision repair Source: SGD
  5. histone H3-K79 methylation Source: SGD
  6. intra-S DNA damage checkpoint Source: SGD
  7. meiotic recombination checkpoint Source: SGD
  8. nucleotide-excision repair Source: SGD
  9. postreplication repair Source: SGD
  10. recombinational repair Source: SGD
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29974-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC:2.1.1.43)
Alternative name(s):
Disrupter of telomere silencing protein 1
Histone H3-K79 methyltransferase
Short name:
H3-K79-HMTase
Lysine N-methyltransferase 4
Gene namesi
Name:DOT1
Synonyms:KMT4, PCH1
Ordered Locus Names:YDR440W
ORF Names:D9461.26
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR440w.
SGDiS000002848. DOT1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi301 – 3011D → A or N: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi350 – 3501Y → F: Reduces methyltransferase activity. 1 Publication
Mutagenesisi372 – 3721Y → F: Reduces methyltransferase activity. 1 Publication
Mutagenesisi374 – 3741E → A or Q: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi399 – 3991G → R: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi401 – 4033Missing: Abolishes methyltransferase activity. 2 Publications
Mutagenesisi401 – 4011G → A or R: Abolishes silencing function. 1 Publication
Mutagenesisi422 – 4221E → A: Abolishes S-adenosyl-L-methionine binding and methyltransferase activity. 1 Publication
Mutagenesisi422 – 4221E → D: No effect. 1 Publication
Mutagenesisi543 – 5431W → A: Abolishes methyltransferase activity, but not S-adenosyl-L-methionine binding. 1 Publication
Mutagenesisi550 – 5501Y → A: Abolishes methyltransferase activity, but not S-adenosyl-L-methionine binding. 1 Publication
Mutagenesisi550 – 5501Y → F: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582Histone-lysine N-methyltransferase, H3 lysine-79 specific
PRO_0000186091Add
BLAST

Proteomic databases

MaxQBiQ04089.
PaxDbiQ04089.

Expressioni

Gene expression databases

GenevestigatoriQ04089.

Interactioni

Protein-protein interaction databases

BioGridi32496. 163 interactions.
DIPiDIP-2560N.
IntActiQ04089. 4 interactions.
MINTiMINT-426373.
STRINGi4932.YDR440W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi178 – 1803
Beta strandi186 – 1883
Helixi196 – 2016
Helixi212 – 2143
Beta strandi236 – 2405
Beta strandi248 – 2525
Beta strandi255 – 2573
Beta strandi260 – 2623
Helixi264 – 27714
Helixi284 – 2918
Helixi293 – 3019
Helixi305 – 31915
Helixi324 – 3318
Beta strandi336 – 3383
Helixi340 – 35314
Helixi355 – 3617
Helixi368 – 3703
Helixi377 – 38610
Beta strandi394 – 3996
Helixi404 – 41310
Beta strandi416 – 4227
Helixi425 – 44420
Beta strandi452 – 4587
Helixi464 – 4696
Helixi470 – 4723
Beta strandi474 – 4785
Helixi485 – 49511
Beta strandi503 – 5086
Beta strandi519 – 5213
Helixi525 – 5284
Beta strandi529 – 5357
Beta strandi544 – 5463
Beta strandi549 – 5557
Helixi561 – 5633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M0Rmodel-A392-511[»]
1U2ZX-ray2.20A/B/C158-582[»]
ProteinModelPortaliQ04089.
SMRiQ04089. Positions 176-567.

Miscellaneous databases

EvolutionaryTraceiQ04089.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini254 – 568315DOT1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 17215Required for interaction with nucleosomes and DNA
Add
BLAST
Regioni372 – 3754S-adenosyl-L-methionine binding
Regioni395 – 40410S-adenosyl-L-methionine binding
Regioni459 – 4602S-adenosyl-L-methionine binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi106 – 16964Lys-rich
Add
BLAST

Sequence similaritiesi

Contains 1 DOT1 domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG294902.
GeneTreeiENSGT00390000013515.
HOGENOMiHOG000112251.
KOiK11427.
OMAiYTRSIHP.
OrthoDBiEOG7KH9VN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR013110. DOT1.
IPR025789. Histone_H3-K79_MeTrfase.
IPR021162. Histone_H3-K79_MeTrfase_fungi.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF08123. DOT1. 1 hit.
[Graphical view]
PIRSFiPIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51569. DOT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04089-1 [UniParc]FASTAAdd to Basket

« Hide

MGGQESISNN NSDSFIMSSP NLDSQESSIS PIDEKKGTDM QTKSLSSYSK    50
GTLLSKQVQN LLEEANKYDP IYGSSLPRGF LRDRNTKGKD NGLVPLVEKV 100
IPPIHKKTNN RNTRKKSSTT TKKDVKKPKA AKVKGKNGRT NHKHTPISKQ 150
EIDTAREKKP LKKGRANKKN DRDSPSSTFV DWNGPCLRLQ YPLFDIEYLR 200
SHEIYSGTPI QSISLRTNSP QPTSLTSDND TSSVTTAKLQ SILFSNYMEE 250
YKVDFKRSTA IYNPMSEIGK LIEYSCLVFL PSPYAEQLKE TILPDLNASF 300
DNSDTKGFVN AINLYNKMIR EIPRQRIIDH LETIDKIPRS FIHDFLHIVY 350
TRSIHPQANK LKHYKAFSNY VYGELLPNFL SDVYQQCQLK KGDTFMDLGS 400
GVGNCVVQAA LECGCALSFG CEIMDDASDL TILQYEELKK RCKLYGMRLN 450
NVEFSLKKSF VDNNRVAELI PQCDVILVNN FLFDEDLNKK VEKILQTAKV 500
GCKIISLKSL RSLTYQINFY NVENIFNRLK VQRYDLKEDS VSWTHSGGEY 550
YISTVMEDVD ESLFSPAARG RRNRGTPVKY TR 582
Length:582
Mass (Da):66,201
Last modified:November 1, 1996 - v1
Checksum:i05CAA6A8F8CBAB9A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33007 Genomic DNA. Translation: AAB64868.1.
BK006938 Genomic DNA. Translation: DAA12277.1.
PIRiS69720.
RefSeqiNP_010728.1. NM_001180748.1.

Genome annotation databases

EnsemblFungiiYDR440W; YDR440W; YDR440W.
GeneIDi852050.
KEGGisce:YDR440W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33007 Genomic DNA. Translation: AAB64868.1 .
BK006938 Genomic DNA. Translation: DAA12277.1 .
PIRi S69720.
RefSeqi NP_010728.1. NM_001180748.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M0R model - A 392-511 [» ]
1U2Z X-ray 2.20 A/B/C 158-582 [» ]
ProteinModelPortali Q04089.
SMRi Q04089. Positions 176-567.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32496. 163 interactions.
DIPi DIP-2560N.
IntActi Q04089. 4 interactions.
MINTi MINT-426373.
STRINGi 4932.YDR440W.

Proteomic databases

MaxQBi Q04089.
PaxDbi Q04089.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR440W ; YDR440W ; YDR440W .
GeneIDi 852050.
KEGGi sce:YDR440W.

Organism-specific databases

CYGDi YDR440w.
SGDi S000002848. DOT1.

Phylogenomic databases

eggNOGi NOG294902.
GeneTreei ENSGT00390000013515.
HOGENOMi HOG000112251.
KOi K11427.
OMAi YTRSIHP.
OrthoDBi EOG7KH9VN.

Enzyme and pathway databases

BioCyci YEAST:G3O-29974-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q04089.
NextBioi 970311.
PROi Q04089.

Gene expression databases

Genevestigatori Q04089.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR013110. DOT1.
IPR025789. Histone_H3-K79_MeTrfase.
IPR021162. Histone_H3-K79_MeTrfase_fungi.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF08123. DOT1. 1 hit.
[Graphical view ]
PIRSFi PIRSF017570. Histone_H3-K79_MeTrfase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51569. DOT1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae."
    Singer M.S., Kahana A., Wolf A.J., Meisinger L.L., Peterson S.E., Goggin C., Mahowald M., Gottschling D.E.
    Genetics 150:613-632(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Role for the silencing protein Dot1 in meiotic checkpoint control."
    San-Segundo P.A., Roeder G.S.
    Mol. Biol. Cell 11:3601-3615(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Dot1p modulates silencing in yeast by methylation of the nucleosome core."
    van Leeuwen F., Gafken P.R., Gottschling D.E.
    Cell 109:745-756(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, MUTAGENESIS OF GLY-401.
  6. "Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association."
    Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K.
    Genes Dev. 16:1518-1527(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, MUTAGENESIS OF GLY-399 AND 401-GLY--GLY-403.
  7. "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase."
    Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.
    J. Biol. Chem. 277:30421-30424(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79."
    Ng H.H., Xu R.-M., Zhang Y., Struhl K.
    J. Biol. Chem. 277:34655-34657(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. Cited for: FUNCTION.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation."
    Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.
    Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1."
    Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.
    J. Biol. Chem. 280:9879-9886(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9."
    Wysocki R., Javaheri A., Allard S., Sha F., Cote J., Kron S.J.
    Mol. Cell. Biol. 25:8430-8443(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "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].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase."
    Sawada K., Yang Z., Horton J.R., Collins R.E., Zhang X., Cheng X.
    J. Biol. Chem. 279:43296-43306(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 158-582 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, DNA-BINDING, MUTAGENESIS OF ASP-301; TYR-350; TYR-372; GLU-374; GLU-422; TRP-543 AND TYR-550.

Entry informationi

Entry nameiDOT1_YEAST
AccessioniPrimary (citable) accession number: Q04089
Secondary accession number(s): D6VT67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Present with 2160 molecules/cell in log phase SD medium.

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

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