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Entry: SET2_SCHPO
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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   24-JAN-2024, entry version 142.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE            EC=2.1.1.359 {ECO:0000250|UniProtKB:P46995};
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; Schizosaccharomycetaceae;
OC   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., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   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 elongation in
RT   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 IDENTIFICATION
RP   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 trimethylates histone H3 'Lys-
CC       36' forming H3K36me3 (By similarity). Involved in transcription
CC       elongation as well as in transcription repression (PubMed:16087749).
CC       {ECO:0000250|UniProtKB:P46995, ECO:0000269|PubMed:16087749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC         Evidence={ECO:0000250|UniProtKB:P46995, ECO:0000255|PROSITE-
CC         ProRule:PRU00901};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {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 methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00901}.
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DR   EMBL; CU329670; CAB16247.1; -; Genomic_DNA.
DR   PIR; T38490; T38490.
DR   RefSeq; NP_594980.1; NM_001020411.2.
DR   AlphaFoldDB; O14026; -.
DR   SMR; O14026; -.
DR   BioGRID; 278547; 38.
DR   STRING; 284812.O14026; -.
DR   iPTMnet; O14026; -.
DR   MaxQB; O14026; -.
DR   PaxDb; 4896-SPAC29B12-02c-1; -.
DR   EnsemblFungi; SPAC29B12.02c.1; SPAC29B12.02c.1:pep; SPAC29B12.02c.
DR   GeneID; 2542070; -.
DR   KEGG; spo:SPAC29B12.02c; -.
DR   PomBase; SPAC29B12.02c; set2.
DR   VEuPathDB; FungiDB:SPAC29B12.02c; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   HOGENOM; CLU_008492_1_1_1; -.
DR   InParanoid; O14026; -.
DR   OMA; MTSIECT; -.
DR   PhylomeDB; O14026; -.
DR   PRO; PR:O14026; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0046975; F:histone H3K36 methyltransferase activity; IDA:PomBase.
DR   GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; EXP:PomBase.
DR   CDD; cd19172; SET_SETD2; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR025788; Set2_fungi.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044437; SETD2/Set2_SET.
DR   InterPro; IPR013257; SRI.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
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; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   SUPFAM; SSF82199; SET domain; 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; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..798
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT                   specific"
FT                   /id="PRO_0000269792"
FT   DOMAIN          124..178
FT                   /note="AWS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT   DOMAIN          180..297
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          304..320
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          627..674
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         545
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         596
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         783
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         785
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         787
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         789
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         793
FT                   /note="Phosphoserine"
FT                   /evidence="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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