SET2_SCHPO
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 03-AUG-2022, entry version 135.
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; 36.
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 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 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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:PomBase.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; IMP: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 CDD; cd19172; SET_SETD2; 1.
DR Gene3D; 2.170.270.10; -; 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 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 SUPFAM; SSF82199; SSF82199; 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
