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Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC 2.1.1.43) (Lysine N-methyltransferase 3) (SET domain-containing protein 2)

 SET2_SCHPO              Reviewed;         798 AA.
O14026;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
20-JUN-2018, entry version 114.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
EC=2.1.1.43;
AltName: Full=Lysine N-methyltransferase 3;
AltName: Full=SET domain-containing protein 2;
Name=set2; Synonyms=kmt3; ORFNames=SPAC29B12.02c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
FUNCTION.
PubMed=16087749; DOI=10.1128/EC.4.8.1446-1454.2005;
Morris S.A., Shibata Y., Noma K., Tsukamoto Y., Warren E., Temple B.,
Grewal S.I.S., Strahl B.D.;
"Histone H3 K36 methylation is associated with transcription
elongation in Schizosaccharomyces pombe.";
Eukaryot. Cell 4:1446-1454(2005).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-545; SER-594;
SER-596; THR-783; THR-785; SER-787; SER-789 AND SER-793, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Histone methyltransferase that methylates histone H3 to
form H3K36me. Involved in transcription elongation as well as in
transcription repression. {ECO:0000269|PubMed:16087749}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00901}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
{ECO:0000250}.
-!- DOMAIN: The AWS and SET domains are necessary for transcription
repression. {ECO:0000250}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00901}.
-----------------------------------------------------------------------
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EMBL; CU329670; CAB16247.1; -; Genomic_DNA.
PIR; T38490; T38490.
RefSeq; NP_594980.1; NM_001020411.2.
ProteinModelPortal; O14026; -.
SMR; O14026; -.
BioGrid; 278547; 22.
STRING; 4896.SPAC29B12.02c.1; -.
iPTMnet; O14026; -.
MaxQB; O14026; -.
PaxDb; O14026; -.
PRIDE; O14026; -.
EnsemblFungi; SPAC29B12.02c.1; SPAC29B12.02c.1:pep; SPAC29B12.02c.
GeneID; 2542070; -.
KEGG; spo:SPAC29B12.02c; -.
EuPathDB; FungiDB:SPAC29B12.02c; -.
PomBase; SPAC29B12.02c; set2.
InParanoid; O14026; -.
KO; K11423; -.
OrthoDB; EOG092C3T9B; -.
PhylomeDB; O14026; -.
Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
PRO; PR:O14026; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:PomBase.
GO; GO:0000790; C:nuclear chromatin; IC:PomBase.
GO; GO:0005634; C:nucleus; HDA:PomBase.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:PomBase.
GO; GO:0097676; P:histone H3-K36 dimethylation; IMP:PomBase.
GO; GO:0010452; P:histone H3-K36 methylation; IDA:PomBase.
GO; GO:0097198; P:histone H3-K36 trimethylation; IMP:PomBase.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:PomBase.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:PomBase.
InterPro; IPR006560; AWS_dom.
InterPro; IPR025788; Hist-Lys_N-MeTrfase_SET2_fun.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR013257; SRI.
InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
InterPro; IPR017923; TFIIS_N.
Pfam; PF08711; Med26; 1.
Pfam; PF00856; SET; 1.
Pfam; PF08236; SRI; 1.
SMART; SM00570; AWS; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF47676; SSF47676; 1.
PROSITE; PS51215; AWS; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS51568; SAM_MT43_SET2_1; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Chromosome; Coiled coil; Complete proteome; Methyltransferase;
Nucleus; Phosphoprotein; Reference proteome; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase.
CHAIN 1 798 Histone-lysine N-methyltransferase, H3
lysine-36 specific.
/FTId=PRO_0000269792.
DOMAIN 124 178 AWS. {ECO:0000255|PROSITE-
ProRule:PRU00562}.
DOMAIN 180 297 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 304 320 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
COILED 627 674 {ECO:0000255}.
COMPBIAS 22 78 Ser-rich.
MOD_RES 67 67 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 545 545 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 596 596 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 783 783 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 785 785 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 789 789 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 793 793 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
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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