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Histone-lysine N-methyltransferase, H3 lysine-4 specific (EC 2.1.1.43) (COMPASS component set1) (Lysine N-methyltransferase 2) (SET domain-containing protein 1) (Set1 complex component set1) (Set1C component set1) (Spset1)

 SET1_SCHPO              Reviewed;         920 AA.
Q9Y7R4;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
18-JUL-2018, entry version 133.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
EC=2.1.1.43;
AltName: Full=COMPASS component set1;
AltName: Full=Lysine N-methyltransferase 2;
AltName: Full=SET domain-containing protein 1;
AltName: Full=Set1 complex component set1;
Short=Set1C component set1;
AltName: Full=Spset1;
Name=set1 {ECO:0000312|EMBL:CAB41652.1}; Synonyms=kmt2;
ORFNames=SPCC306.04c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1] {ECO:0000312|EMBL:CAB41652.1}
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] {ECO:0000305}
FUNCTION.
PubMed=12193658; DOI=10.1073/pnas.182436399;
Noma K., Grewal S.I.S.;
"Histone H3 lysine 4 methylation is mediated by Set1 and promotes
maintenance of active chromatin states in fission yeast.";
Proc. Natl. Acad. Sci. U.S.A. 99:16438-16445(2002).
[3] {ECO:0000305}
FUNCTION, AND IDENTIFICATION IN THE SET1 COMPLEX.
PubMed=12488447; DOI=10.1074/jbc.M209562200;
Roguev A., Schaft D., Shevchenko A., Aasland R., Shevchenko A.,
Stewart A.F.;
"High conservation of the Set1/Rad6 axis of histone 3 lysine 4
methylation in budding and fission yeasts.";
J. Biol. Chem. 278:8487-8493(2003).
[4] {ECO:0000305}
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12589755; DOI=10.1016/S0022-2836(03)00030-5;
Kanoh J., Francesconi S., Collura A., Schramke V., Ishikawa F.,
Baldacci G., Geli V.;
"The fission yeast spSet1p is a histone H3-K4 methyltransferase that
functions in telomere maintenance and DNA repair in an ATM kinase
Rad3-dependent pathway.";
J. Mol. Biol. 326:1081-1094(2003).
[5] {ECO:0000305}
IDENTIFICATION IN THE SET1 COMPLEX.
PubMed=14617822; DOI=10.1074/mcp.M300081-MCP200;
Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
Shevchenko A.;
"A comparative analysis of an orthologous proteomic environment in the
yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
Mol. Cell. Proteomics 3:125-132(2004).
-!- FUNCTION: Catalytic component of the Set1 complex that
specifically mono-, di- and trimethylates histone H3 to form
H3K4me1/2/3. Methylation promotes maintenance of active chromatin
states at euchromatic chromosomal domains and is present
throughout the cell cycle. Plays a role in telomere maintenance
and DNA repair in an ATM kinase rad3-dependent pathway. Required
for efficient telomeric and centromeric silencing.
{ECO:0000269|PubMed:12193658, ECO:0000269|PubMed:12488447,
ECO:0000269|PubMed:12589755}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:12589755}.
-!- SUBUNIT: Component of the Set1 complex composed of ash2, sdc1,
set1, shg1, spp1, swd1, swd2 and swd3.
{ECO:0000269|PubMed:12488447, ECO:0000269|PubMed:14617822}.
-!- INTERACTION:
Q9HDV4:lid2; NbExp=2; IntAct=EBI-2106005, EBI-2105919;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome
{ECO:0000305}.
-!- DOMAIN: A construct containing set1 C-terminal fragment of 692-920
is able to form H3K4me.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-----------------------------------------------------------------------
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EMBL; CU329672; CAB41652.1; -; Genomic_DNA.
PIR; T41282; T41282.
RefSeq; NP_587812.1; NM_001022805.2.
ProteinModelPortal; Q9Y7R4; -.
SMR; Q9Y7R4; -.
BioGrid; 275345; 361.
ELM; Q9Y7R4; -.
IntAct; Q9Y7R4; 1.
STRING; 4896.SPCC306.04c.1; -.
iPTMnet; Q9Y7R4; -.
MaxQB; Q9Y7R4; -.
PaxDb; Q9Y7R4; -.
PRIDE; Q9Y7R4; -.
EnsemblFungi; SPCC306.04c.1; SPCC306.04c.1:pep; SPCC306.04c.
GeneID; 2538762; -.
KEGG; spo:SPCC306.04c; -.
EuPathDB; FungiDB:SPCC306.04c; -.
PomBase; SPCC306.04c; set1.
InParanoid; Q9Y7R4; -.
KO; K11422; -.
OMA; PSCTAKI; -.
OrthoDB; EOG092C3T9B; -.
PhylomeDB; Q9Y7R4; -.
Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
PRO; PR:Q9Y7R4; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0005737; C:cytoplasm; HDA:PomBase.
GO; GO:0000790; C:nuclear chromatin; NAS:PomBase.
GO; GO:0048188; C:Set1C/COMPASS complex; IDA:PomBase.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:PomBase.
GO; GO:0003723; F:RNA binding; ISM:PomBase.
GO; GO:0070869; P:heterochromatin assembly involved in chromatin silencing; IC:PomBase.
GO; GO:0051568; P:histone H3-K4 methylation; IMP:PomBase.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR024657; COMPASS_Set1_N-SET.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR017111; Set1.
InterPro; IPR024636; SET_assoc.
InterPro; IPR001214; SET_dom.
PANTHER; PTHR22884:SF462; PTHR22884:SF462; 2.
Pfam; PF11764; N-SET; 1.
Pfam; PF00076; RRM_1; 1.
Pfam; PF00856; SET; 1.
Pfam; PF11767; SET_assoc; 1.
PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
SMART; SM01291; N-SET; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00360; RRM; 2.
SMART; SM00317; SET; 1.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50102; RRM; 1.
PROSITE; PS51572; SAM_MT43_1; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Chromatin regulator; Chromosome; Complete proteome; Methyltransferase;
Nucleus; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 920 Histone-lysine N-methyltransferase, H3
lysine-4 specific.
/FTId=PRO_0000186085.
DOMAIN 94 179 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 781 898 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 904 920 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
COMPBIAS 469 474 Poly-Arg. {ECO:0000255}.
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


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