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O14026

- SET2_SCHPO

UniProt

O14026 - SET2_SCHPO

Protein

Histone-lysine N-methyltransferase, H3 lysine-36 specific

Gene

set2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that methylates histone H3 to form H3K36me. Involved in transcription elongation as well as in transcription repression.1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. histone methyltransferase activity (H3-K36 specific) Source: PomBase

    GO - Biological processi

    1. histone methylation Source: PomBase
    2. regulation of transcription from RNA polymerase II promoter Source: PomBase
    3. transcription elongation from RNA polymerase II promoter Source: PomBase

    Keywords - Molecular functioni

    Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC:2.1.1.43)
    Alternative name(s):
    Lysine N-methyltransferase 3
    SET domain-containing protein 2
    Gene namesi
    Name:set2
    Synonyms:kmt3
    ORF Names:SPAC29B12.02c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC29B12.02c.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity

    GO - Cellular componenti

    1. DNA-directed RNA polymerase II, holoenzyme Source: PomBase
    2. nuclear chromatin Source: PomBase
    3. nucleus Source: PomBase

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 798798Histone-lysine N-methyltransferase, H3 lysine-36 specificPRO_0000269792Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphoserine1 Publication
    Modified residuei545 – 5451Phosphothreonine1 Publication
    Modified residuei594 – 5941Phosphoserine1 Publication
    Modified residuei596 – 5961Phosphoserine1 Publication
    Modified residuei783 – 7831Phosphothreonine1 Publication
    Modified residuei785 – 7851Phosphothreonine1 Publication
    Modified residuei787 – 7871Phosphoserine1 Publication
    Modified residuei789 – 7891Phosphoserine1 Publication
    Modified residuei793 – 7931Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO14026.

    Interactioni

    Protein-protein interaction databases

    BioGridi278547. 14 interactions.
    MINTiMINT-4669878.
    STRINGi4896.SPAC29B12.02c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO14026.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini124 – 17855AWSPROSITE-ProRule annotationAdd
    BLAST
    Domaini180 – 297118SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini304 – 32017Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili627 – 67448Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 7857Ser-richAdd
    BLAST

    Domaini

    The AWS and SET domains are necessary for transcription repression.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.PROSITE-ProRule annotation
    Contains 1 AWS domain.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG2940.
    KOiK11423.
    OMAiENITARR.
    OrthoDBiEOG7P8PH3.
    PhylomeDBiO14026.

    Family and domain databases

    InterProiIPR006560. AWS.
    IPR025788. Hist-Lys_N-MeTrfase_SET2_fun.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR013257. SRI.
    IPR017923. TFIIS_N.
    [Graphical view]
    PfamiPF00856. SET. 1 hit.
    PF08236. SRI. 1 hit.
    [Graphical view]
    SMARTiSM00570. AWS. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF47676. SSF47676. 1 hit.
    PROSITEiPS51215. AWS. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS51568. SAM_MT43_SET2_1. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O14026-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQTASSLSVL TPLNEENVDR KSSWSKDTIA VQAVGSSPSS SSSHDFESKE    50
    DAEGMNKDES APSPSTSSPS SASSRSQSKY VRKEALPPQL FHHLDSAKDK 100
    ALTTFEEIQE CQYASANIGK PPENEAMICD CRPHWVDGVN VACGHGSNCI 150
    NRMTSIECTD EDNVCGPSCQ NQRFQRHEFA KVDVFLTEKK GFGLRADANL 200
    PKDTFVYEYI GEVIPEQKFR KRMRQYDSEG IKHFYFMMLQ KGEYIDATKR 250
    GSLARFCNHS CRPNCYVDKW MVGDKLRMGI FCKRDIIRGE ELTFDYNVDR 300
    YGAQAQPCYC GEPCCVGYIG GKTQTEAQSK LPENVREALG IEDEEDSWEN 350
    ITARRQRRKK GIDETSKIIE EVQPTPLTSE SATKVIGVLL QTKDDLLTRK 400
    LMERIFLTSD PSVCRSIIAL RGYNIFGLML KKFSIDIEFI LRSIKTMLSW 450
    PRLTRNKIQD SNIEPVVQEF CDHENEEVKD HAKTLLKEWE SLEIAYRIPR 500
    RKPGQVAPQS TNAEPSNNQS NPPLRDQEPQ RGDKGDIKSA INNSTEDLSK 550
    KHPALHSSRP SDSRSRSKFG NDYQSHSKHN LFRKNSFPKR RRLSNSDTPS 600
    ETTTPNNEQE QVSNQANKVD LNKIISAAME SVNQKNVLKA QKEEEERIAQ 650
    QKREEKRRLA YEESLKRHAK KLHEKKTKSS QDATIDHHLT SHSPESIAFK 700
    AVLAKFFANK TARYQEKLGK AEFKLRVKKM TEIILKKHIQ LVLSKKEKAL 750
    PDELSDSQQR KLRVWAFRYL DTVVSRSGTA TTTPTDSPSI GESPKKAA 798
    Length:798
    Mass (Da):90,679
    Last modified:January 1, 1998 - v1
    Checksum:i4ACEE9D1705A639E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB16247.1.
    PIRiT38490.
    RefSeqiNP_594980.1. NM_001020411.2.

    Genome annotation databases

    EnsemblFungiiSPAC29B12.02c.1; SPAC29B12.02c.1:pep; SPAC29B12.02c.
    GeneIDi2542070.
    KEGGispo:SPAC29B12.02c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB16247.1 .
    PIRi T38490.
    RefSeqi NP_594980.1. NM_001020411.2.

    3D structure databases

    ProteinModelPortali O14026.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278547. 14 interactions.
    MINTi MINT-4669878.
    STRINGi 4896.SPAC29B12.02c-1.

    Proteomic databases

    MaxQBi O14026.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC29B12.02c.1 ; SPAC29B12.02c.1:pep ; SPAC29B12.02c .
    GeneIDi 2542070.
    KEGGi spo:SPAC29B12.02c.

    Organism-specific databases

    PomBasei SPAC29B12.02c.

    Phylogenomic databases

    eggNOGi COG2940.
    KOi K11423.
    OMAi ENITARR.
    OrthoDBi EOG7P8PH3.
    PhylomeDBi O14026.

    Miscellaneous databases

    NextBioi 20803143.

    Family and domain databases

    InterProi IPR006560. AWS.
    IPR025788. Hist-Lys_N-MeTrfase_SET2_fun.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR013257. SRI.
    IPR017923. TFIIS_N.
    [Graphical view ]
    Pfami PF00856. SET. 1 hit.
    PF08236. SRI. 1 hit.
    [Graphical view ]
    SMARTi SM00570. AWS. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47676. SSF47676. 1 hit.
    PROSITEi PS51215. AWS. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS51568. SAM_MT43_SET2_1. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "Histone H3 K36 methylation is associated with transcription elongation in Schizosaccharomyces pombe."
      Morris S.A., Shibata Y., Noma K., Tsukamoto Y., Warren E., Temple B., Grewal S.I.S., Strahl B.D.
      Eukaryot. Cell 4:1446-1454(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-545; SER-594; SER-596; THR-783; THR-785; SER-787; SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSET2_SCHPO
    AccessioniPrimary (citable) accession number: O14026
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3