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Database: UniProt
Entry: O14026
LinkDB: O14026
Original site: O14026 
ID   SET2_SCHPO              Reviewed;         798 AA.
AC   O14026;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   13-FEB-2019, entry version 119.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 3;
DE   AltName: Full=SET domain-containing protein 2;
GN   Name=set2; Synonyms=kmt3; ORFNames=SPAC29B12.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION.
RX   PubMed=16087749; DOI=10.1128/EC.4.8.1446-1454.2005;
RA   Morris S.A., Shibata Y., Noma K., Tsukamoto Y., Warren E., Temple B.,
RA   Grewal S.I.S., Strahl B.D.;
RT   "Histone H3 K36 methylation is associated with transcription
RT   elongation in Schizosaccharomyces pombe.";
RL   Eukaryot. Cell 4:1446-1454(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-545; SER-594;
RP   SER-596; THR-783; THR-785; SER-787; SER-789 AND SER-793, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Histone methyltransferase that methylates histone H3 to
CC       form H3K36me. Involved in transcription elongation as well as in
CC       transcription repression. {ECO:0000269|PubMed:16087749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00901};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- DOMAIN: The AWS and SET domains are necessary for transcription
CC       repression. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00901}.
DR   EMBL; CU329670; CAB16247.1; -; Genomic_DNA.
DR   PIR; T38490; T38490.
DR   RefSeq; NP_594980.1; NM_001020411.2.
DR   ProteinModelPortal; O14026; -.
DR   SMR; O14026; -.
DR   BioGrid; 278547; 31.
DR   STRING; 4896.SPAC29B12.02c.1; -.
DR   iPTMnet; O14026; -.
DR   MaxQB; O14026; -.
DR   PaxDb; O14026; -.
DR   PRIDE; O14026; -.
DR   EnsemblFungi; SPAC29B12.02c.1; SPAC29B12.02c.1:pep; SPAC29B12.02c.
DR   GeneID; 2542070; -.
DR   KEGG; spo:SPAC29B12.02c; -.
DR   EuPathDB; FungiDB:SPAC29B12.02c; -.
DR   PomBase; SPAC29B12.02c; set2.
DR   InParanoid; O14026; -.
DR   KO; K11423; -.
DR   OMA; MTSIECT; -.
DR   PhylomeDB; O14026; -.
DR   Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   PRO; PR:O14026; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0000790; C:nuclear chromatin; IC:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:PomBase.
DR   GO; GO:0034401; P:chromatin organization involved in regulation of transcription; IC:GOC-OWL.
DR   GO; GO:0097676; P:histone H3-K36 dimethylation; IMP:PomBase.
DR   GO; GO:0010452; P:histone H3-K36 methylation; IDA:PomBase.
DR   GO; GO:0097198; P:histone H3-K36 trimethylation; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:PomBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:PomBase.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR025788; Hist-Lys_N-MeTrfase_SET2_fun.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR013257; SRI.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF08236; SRI; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF47676; SSF47676; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51568; SAM_MT43_SET2_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Coiled coil; Complete proteome; Methyltransferase;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    798       Histone-lysine N-methyltransferase, H3
FT                                lysine-36 specific.
FT                                /FTId=PRO_0000269792.
FT   DOMAIN      124    178       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN      180    297       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      304    320       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   COILED      627    674       {ECO:0000255}.
FT   COMPBIAS     22     78       Ser-rich.
FT   MOD_RES      67     67       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     545    545       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     594    594       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     596    596       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     783    783       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     785    785       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     787    787       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     789    789       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     793    793       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
SQ   SEQUENCE   798 AA;  90679 MW;  4ACEE9D1705A639E CRC64;
     MQTASSLSVL TPLNEENVDR KSSWSKDTIA VQAVGSSPSS SSSHDFESKE DAEGMNKDES
     APSPSTSSPS SASSRSQSKY VRKEALPPQL FHHLDSAKDK ALTTFEEIQE CQYASANIGK
     PPENEAMICD CRPHWVDGVN VACGHGSNCI NRMTSIECTD EDNVCGPSCQ NQRFQRHEFA
     KVDVFLTEKK GFGLRADANL PKDTFVYEYI GEVIPEQKFR KRMRQYDSEG IKHFYFMMLQ
     KGEYIDATKR GSLARFCNHS CRPNCYVDKW MVGDKLRMGI FCKRDIIRGE ELTFDYNVDR
     YGAQAQPCYC GEPCCVGYIG GKTQTEAQSK LPENVREALG IEDEEDSWEN ITARRQRRKK
     GIDETSKIIE EVQPTPLTSE SATKVIGVLL QTKDDLLTRK LMERIFLTSD PSVCRSIIAL
     RGYNIFGLML KKFSIDIEFI LRSIKTMLSW PRLTRNKIQD SNIEPVVQEF CDHENEEVKD
     HAKTLLKEWE SLEIAYRIPR RKPGQVAPQS TNAEPSNNQS NPPLRDQEPQ RGDKGDIKSA
     INNSTEDLSK KHPALHSSRP SDSRSRSKFG NDYQSHSKHN LFRKNSFPKR RRLSNSDTPS
     ETTTPNNEQE QVSNQANKVD LNKIISAAME SVNQKNVLKA QKEEEERIAQ QKREEKRRLA
     YEESLKRHAK KLHEKKTKSS QDATIDHHLT SHSPESIAFK AVLAKFFANK TARYQEKLGK
     AEFKLRVKKM TEIILKKHIQ LVLSKKEKAL PDELSDSQQR KLRVWAFRYL DTVVSRSGTA
     TTTPTDSPSI GESPKKAA
//
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