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P38827

- SET1_YEAST

UniProt

P38827 - SET1_YEAST

Protein

Histone-lysine N-methyltransferase, H3 lysine-4 specific

Gene

SET1

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 135 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.12 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    2. histone methyltransferase activity Source: SGD
    3. protein binding Source: IntAct
    4. protein-lysine N-methyltransferase activity Source: SGD
    5. RNA binding Source: SGD

    GO - Biological processi

    1. ascospore formation Source: SGD
    2. chromatin silencing at rDNA Source: SGD
    3. chromatin silencing at silent mating-type cassette Source: SGD
    4. chromatin silencing at telomere Source: SGD
    5. histone H3-K4 methylation Source: SGD
    6. peptidyl-lysine dimethylation Source: SGD
    7. positive regulation of histone acetylation Source: SGD
    8. regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
    9. telomere maintenance Source: SGD

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31161-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-4 specific (EC:2.1.1.43)
    Alternative name(s):
    COMPASS component SET1
    Lysine N-methyltransferase 2
    SET domain-containing protein 1
    Gene namesi
    Name:SET1
    Synonyms:KMT2, YTX1
    Ordered Locus Names:YHR119W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR119w.
    SGDiS000001161. SET1.

    Subcellular locationi

    Nucleus Curated. Chromosome Curated

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. Set1C/COMPASS complex Source: SGD

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10801080Histone-lysine N-methyltransferase, H3 lysine-4 specificPRO_0000186086Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei625 – 6251Phosphoserine2 Publications
    Modified residuei875 – 8751Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38827.
    PaxDbiP38827.
    PRIDEiP38827.

    Expressioni

    Gene expression databases

    GenevestigatoriP38827.

    Interactioni

    Subunit structurei

    Component of the COMPASS (Set1C) complex which consists of SET12, BRE22, SPP12, SDC11, SHG11, SWD11, SWD21, and SWD31. Interacts with MEC3.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRE2P431326EBI-16977,EBI-27115
    MEC3Q025743EBI-16977,EBI-10658
    SHG1P383375EBI-16977,EBI-21106
    SWD2P361046EBI-16977,EBI-26608

    Protein-protein interaction databases

    BioGridi36552. 132 interactions.
    DIPiDIP-4616N.
    IntActiP38827. 30 interactions.
    MINTiMINT-552558.
    STRINGi4932.YHR119W.

    Structurei

    Secondary structure

    1
    1080
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi249 – 25810
    Helixi265 – 2739
    Beta strandi279 – 2857
    Turni287 – 2893
    Beta strandi292 – 2998
    Helixi310 – 32011
    Turni321 – 3244
    Beta strandi326 – 3283
    Beta strandi331 – 3377
    Helixi342 – 36423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J8AX-ray3.00A247-375[»]
    ProteinModelPortaliP38827.
    SMRiP38827. Positions 247-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38827.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini938 – 1055118SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1064 – 108017Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00740000115089.
    HOGENOMiHOG000066111.
    KOiK11422.
    OMAiERLPCLC.
    OrthoDBiEOG7P8PH3.

    Family and domain databases

    InterProiIPR024657. COMPASS_Set1_N-SET.
    IPR017111. Hist_H3-K4_MeTrfase_1_fun.
    IPR003616. Post-SET_dom.
    IPR024636. SET_assoc.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF11764. N-SET. 1 hit.
    PF00856. SET. 1 hit.
    PF11767. SET_assoc. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037104. Histone_H3-K4_mtfrase_Set1_fun. 1 hit.
    SMARTiSM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    PROSITEiPS50868. POST_SET. 1 hit.
    PS51572. SAM_MT43_1. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38827-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNYYRRAHA SSGSYRQPQE QPQYSRSGHY QYSNGHSHQQ YSSQYNQRRR     50
    YNHNDGTRRR YNDDRPHSSN NASTRQYYAT NNSQSGPYVN KKSDISSRRG 100
    MSQSRYSNSN VHNTLASSSG SLPTESALLL QQRPPSVLRY NTDNLKSKFH 150
    YFDPIKGEFF NKDKMLSWKA TDKEFSETGY YVVKELQDGQ FKFKIKHRHP 200
    EIKASDPRNE NGIMTSGKVA THRKCRNSLI LLPRISYDRY SLGPPPSCEI 250
    VVYPAQDSTT TNIQDISIKN YFKKYGEISH FEAFNDPNSA LPLHVYLIKY 300
    ASSDGKINDA AKAAFSAVRK HESSGCFIMG FKFEVILNKH SILNNIISKF 350
    VEINVKKLQK LQENLKKAKE KEAENEKAKE LQGKDITLPK EPKVDTLSHS 400
    SGSEKRIPYD LLGVVNNRPV LHVSKIFVAK HRFCVEDFKY KLRGYRCAKF 450
    IDHPTGIYII FNDIAHAQTC SNAESGNLTI MSRSRRIPIL IKFHLILPRF 500
    QNRTRFNKSS SSSNSTNVPI KYESKEEFIE ATAKQILKDL EKTLHVDIKK 550
    RLIGPTVFDA LDHANFPELL AKRELKEKEK RQQIASKIAE DELKRKEEAK 600
    RDFDLFGLYG GYAKSNKRNL KRHNSLALDH TSLKRKKLSN GIKPMAHLLN 650
    EETDSKETTP LNDEGITRVS KEHDEEDENM TSSSSEEEEE EAPDKKFKSE 700
    SEPTTPESDH LHGIKPLVPD QNGSSDVLDA SSMYKPTATE IPEPVYPPEE 750
    YDLKYSQTLS SMDLQNAIKD EEDMLILKQL LSTYTPTVTP ETSAALEYKI 800
    WQSRRKVLEE EKASDWQIEL NGTLFDSELQ PGSSFKAEGF RKIADKLKIN 850
    YLPHRRRVHQ PLNTVNIHNE RNEYTPELCQ REESSNKEPS DSVPQEVSSS 900
    RDNRASNRRF QQDIEAQKAA IGTESELLSL NQLNKRKKPV MFARSAIHNW 950
    GLYALDSIAA KEMIIEYVGE RIRQPVAEMR EKRYLKNGIG SSYLFRVDEN 1000
    TVIDATKKGG IARFINHCCD PNCTAKIIKV GGRRRIVIYA LRDIAASEEL 1050
    TYDYKFEREK DDEERLPCLC GAPNCKGFLN 1080
    Length:1,080
    Mass (Da):123,912
    Last modified:February 1, 1995 - v1
    Checksum:iB7FA5D60F71063FD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00059 Genomic DNA. Translation: AAB68867.1.
    BK006934 Genomic DNA. Translation: DAA06813.1.
    PIRiS48961.
    RefSeqiNP_011987.1. NM_001179249.1.

    Genome annotation databases

    EnsemblFungiiYHR119W; YHR119W; YHR119W.
    GeneIDi856519.
    KEGGisce:YHR119W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00059 Genomic DNA. Translation: AAB68867.1 .
    BK006934 Genomic DNA. Translation: DAA06813.1 .
    PIRi S48961.
    RefSeqi NP_011987.1. NM_001179249.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J8A X-ray 3.00 A 247-375 [» ]
    ProteinModelPortali P38827.
    SMRi P38827. Positions 247-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36552. 132 interactions.
    DIPi DIP-4616N.
    IntActi P38827. 30 interactions.
    MINTi MINT-552558.
    STRINGi 4932.YHR119W.

    Proteomic databases

    MaxQBi P38827.
    PaxDbi P38827.
    PRIDEi P38827.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR119W ; YHR119W ; YHR119W .
    GeneIDi 856519.
    KEGGi sce:YHR119W.

    Organism-specific databases

    CYGDi YHR119w.
    SGDi S000001161. SET1.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00740000115089.
    HOGENOMi HOG000066111.
    KOi K11422.
    OMAi ERLPCLC.
    OrthoDBi EOG7P8PH3.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31161-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P38827.
    NextBioi 982275.
    PROi P38827.

    Gene expression databases

    Genevestigatori P38827.

    Family and domain databases

    InterProi IPR024657. COMPASS_Set1_N-SET.
    IPR017111. Hist_H3-K4_MeTrfase_1_fun.
    IPR003616. Post-SET_dom.
    IPR024636. SET_assoc.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF11764. N-SET. 1 hit.
    PF00856. SET. 1 hit.
    PF11767. SET_assoc. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037104. Histone_H3-K4_mtfrase_Set1_fun. 1 hit.
    SMARTi SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    PROSITEi PS50868. POST_SET. 1 hit.
    PS51572. SAM_MT43_1. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "SET1, a yeast member of the Trithorax family, functions in transcriptional silencing and diverse cellular processes."
      Nislow C., Ray E., Pillus L.
      Mol. Biol. Cell 8:2421-2436(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Interaction between Set1p and checkpoint protein Mec3p in DNA repair and telomere functions."
      Corda Y., Schramke V., Longhese M.P., Smokvina T., Paciotti V., Brevet V., Gilson E., Geli V.
      Nat. Genet. 21:204-208(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MEC3.
    5. "The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4."
      Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M., Aasland R., Stewart A.F.
      EMBO J. 20:7137-7148(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SET1 COMPLEX, FUNCTION OF THE SET1 COMPLEX.
    6. "Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae."
      Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y.R., Winston F., Allis C.D.
      Genes Dev. 15:3286-3295(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: SUBUNIT.
    8. "Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism."
      Bryk M., Briggs S.D., Strahl B.D., Curcio M.J., Allis C.D., Winston F.
      Curr. Biol. 12:165-170(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression."
      Krogan N.J., Dover J., Khorrami S., Greenblatt J.F., Schneider J., Johnston M., Shilatifard A.
      J. Biol. Chem. 277:10753-10755(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, FUNCTION.
    10. Cited for: FUNCTION.
    11. "A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3."
      Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SET1 COMPLEX, FUNCTION OF THE SET1 COMPLEX.
    12. Cited for: FUNCTION.
    13. "Methylation of histone H3 K4 mediates association of the Isw1p ATPase with chromatin."
      Santos-Rosa H., Schneider R., Bernstein B.E., Karabetsou N., Morillon A., Weise C., Schreiber S.L., Mellor J., Kouzarides T.
      Mol. Cell 12:1325-1332(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    15. "Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression."
      Boa S., Coert C., Patterton H.-G.
      Yeast 20:827-835(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription."
      Morillon A., Karabetsou N., Nair A., Mellor J.
      Mol. Cell 18:723-734(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE COMPASS COMPLEX.
    17. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    18. "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-625 AND THR-875, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSET1_YEAST
    AccessioniPrimary (citable) accession number: P38827
    Secondary accession number(s): D3DL69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 135 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 172 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 VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3