ID   SET1_SCHPO              Reviewed;         920 AA.
AC   Q9Y7R4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=COMPASS component set1;
DE   AltName: Full=Lysine N-methyltransferase 2;
DE   AltName: Full=SET domain-containing protein 1;
DE   AltName: Full=Set1 complex component set1;
DE            Short=Set1C component set1;
DE   AltName: Full=Spset1;
GN   Name=set1; Synonyms=kmt2; ORFNames=SPCC306.04c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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   MEDLINE=22364025; PubMed=12193658; DOI=10.1073/pnas.182436399;
RA   Noma K., Grewal S.I.S.;
RT   "Histone H3 lysine 4 methylation is mediated by Set1 and promotes
RT   maintenance of active chromatin states in fission yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16438-16445(2002).
RN   [3]
RP   FUNCTION AND COMPOSITION OF THE SET1 COMPLEX.
RX   MEDLINE=22499591; PubMed=12488447; DOI=10.1074/jbc.M209562200;
RA   Roguev A., Schaft D., Shevchenko A., Aasland R., Shevchenko A.,
RA   Stewart A.F.;
RT   "High conservation of the Set1/Rad6 axis of histone 3 lysine 4
RT   methylation in budding and fission yeasts.";
RL   J. Biol. Chem. 278:8487-8493(2003).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   MEDLINE=22478158; PubMed=12589755; DOI=10.1016/S0022-2836(03)00030-5;
RA   Kanoh J., Francesconi S., Collura A., Schramke V., Ishikawa F.,
RA   Baldacci G., Geli V.;
RT   "The fission yeast spSet1p is a histone H3-K4 methyltransferase that
RT   functions in telomere maintenance and DNA repair in an ATM kinase
RT   Rad3-dependent pathway.";
RL   J. Mol. Biol. 326:1081-1094(2003).
RN   [5]
RP   COMPOSITION OF THE SET1 COMPLEX.
RX   PubMed=14617822; DOI=10.1074/mcp.M300081-MCP200;
RA   Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
RA   Shevchenko A.;
RT   "A comparative analysis of an orthologous proteomic environment in the
RT   yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL   Mol. Cell. Proteomics 3:125-132(2004).
CC   -!- FUNCTION: Catalytic component of the Set1 complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3. Methylation promotes maintenance of active chromatin
CC       states at euchromatic chromosomal domains and is present
CC       throughout the cell cycle. Plays a role in telomere maintenance
CC       and DNA repair in an ATM kinase rad3-dependent pathway. Required
CC       for efficient telomeric and centromeric silencing.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: Component of the Set1 complex composed of ash2, sdc1,
CC       set1, shg1, spp1, swd1, swd2 and swd3.
CC   -!- INTERACTION:
CC       Q9HDV4:lid2; NbExp=1; IntAct=EBI-2106005, EBI-2105919;
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable). Chromosome (Probable).
CC   -!- DOMAIN: A construct containing set1 C-terminal fragment of 692-920
CC       is able to form H3K4me.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SIMILARITY: Contains 1 SET domain.
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DR   EMBL; CU329672; CAB41652.1; -; Genomic_DNA.
DR   PIR; T41282; T41282.
DR   ProteinModelPortal; Q9Y7R4; -.
DR   SMR; Q9Y7R4; 104-182, 783-920.
DR   IntAct; Q9Y7R4; 2.
DR   STRING; Q9Y7R4; -.
DR   EnsemblFungi; SPCC306.04c-1; SPCC306.04c-1; SPCC306.04c.
DR   GenomeReviews; CU329672_GR; set1.
DR   KEGG; spo:SPCC306.04c; -.
DR   NMPDR; fig|4896.1.peg.150; -.
DR   GeneDB_Spombe; SPCC306.04c; -.
DR   eggNOG; fuNOG05508; -.
DR   GeneTree; EFGT00050000001847; -.
DR   OMA; TIDTISH; -.
DR   OrthoDB; EOG4ZW8K8; -.
DR   PhylomeDB; Q9Y7R4; -.
DR   BRENDA; 2.1.1.43; 653.
DR   ArrayExpress; Q9Y7R4; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB_Spombe.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IDA:GeneDB_Spombe.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); TAS:GeneDB_Spombe.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint; IGI:GeneDB_Spombe.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IMP:GeneDB_Spombe.
DR   InterPro; IPR017111; Hist_H3-K4_MeTrfase_1_fun.
DR   InterPro; IPR015722; Histone-lysine_MeTfrase.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   PANTHER; PTHR22884:SF10; MLL; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Chromosome; Complete proteome; DNA damage;
KW   DNA repair; Methyltransferase; Nucleus; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    920       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000186085.
FT   DOMAIN       94    179       RRM.
FT   DOMAIN      780    902       SET.
FT   DOMAIN      904    920       Post-SET.
FT   COMPBIAS    469    474       Poly-Arg.
SQ   SEQUENCE   920 AA;  105038 MW;  C4AD7E6C3ECFF8BC CRC64;
     MDFNTSTRSK SQPVQRNNYK VLYDPELGIK ENLGRKIIYR FNGVSKPPLV VRDPRLKNPI
     YARGIPKSGR PFLKSLQTIN YDYNENSLGP EPPTQVFVSN ISPLVTSEQL RYHFKSFGEV
     FDLDLKLNPY TGTSLGLCCI SFDKRSSISV AAHSAKIAVQ QANGLRFSGK PLSVVLDRDG
     SLCEEAFKKA LNAVEKQFQE ETLQKQRFER EDESSRQKLS AAMNEDIPPW RQPSKNSQTL
     SNGDLQHSKV QNVDQKSGFL TSSETDVPKN INDYIYLLID DRFVPPDRVY YTDIKHHFRK
     FLYEKIYMNK DGFYITFNNY REASNCYRAL DRTYVQNCRI KLKFHDIPSR TKEDGKKSAV
     RRVVLPPEEA YAEATSVVLR DLEAALLRDV KSKIIGPAIF KYLHSMPKPS VKEELQENLL
     VSSTSVPDVP LKIESTVGKL PSLPKFKKRV DSSKMNLSAG SKTKSKLQRR RRRRHEARPL
     HYQLNQMYNS SASEAESDQE LLLSSGDERV ERGKIGSIKS VKSDEATPVF SDTSDENDKF
     HRFRTKSKIS KKKYEKMEVD YTSSSETESD ASILSPSAAI PKSGSAIKDE LISPKKEIDE
     VLALAPKWRI NEFDETGSVY YGALPYNYPE DDVLLDLDGL QYLVKNDEDY SYLQEALKDE
     PLMDINDPNF WAYERKSCKF KNGDVKYGDT AILPEPKGYF RSNTSGSAKS EGYYIIPTTE
     KSLYLPLRNR STIDTISHST SRITSRMNRV NNRRLAAGVE KSQLPAEADL LRFNALKARK
     KQLHFGPSRI HTLGLFAMEN IDKNDMVIEY IGEIIRQRVA DNREKNYVRE GIGDSYLFRI
     DEDVIVDATK KGNIARFINH SCAPNCIARI IRVEGKRKIV IYADRDIMHG EELTYDYKFP
     EEADKIPCLC GAPTCRGYLN
//