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Database: UniProt
Entry: Q9USK2
LinkDB: Q9USK2
Original site: Q9USK2 
ID   SET9_SCHPO              Reviewed;         441 AA.
AC   Q9USK2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 110.
DE   RecName: Full=Histone-lysine N-methyltransferase set9;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 5;
DE   AltName: Full=SET domain protein 9;
GN   Name=set9; Synonyms=kmt5; ORFNames=SPCC4B3.12;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; 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.,
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, AND MUTAGENESIS OF TYR-220.
RX   PubMed=15550243; DOI=10.1016/j.cell.2004.11.009;
RA   Sanders S.L., Portoso M., Mata J., Baehler J., Allshire R.C.,
RA   Kouzarides T.;
RT   "Methylation of histone H4 lysine 20 controls recruitment of Crb2 to
RT   sites of DNA damage.";
RL   Cell 119:603-614(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDP1,
RP   HISTONE-BINDING, AND FUNCTION.
RX   PubMed=19250904; DOI=10.1016/j.molcel.2009.02.002;
RA   Wang Y., Reddy B., Thompson J., Wang H., Noma K., Yates J.R. III,
RA   Jia S.;
RT   "Regulation of Set9-mediated H4K20 methylation by a PWWP domain
RT   protein.";
RL   Mol. Cell 33:428-437(2009).
CC   -!- FUNCTION: Histone methyltransferase that specifically methylates
CC       'Lys-20' of histone H4. H4 'Lys-20' methylation is apparently not
CC       involved in the regulation of gene expression or heterochromatin
CC       function but participates in DNA damage response by giving a
CC       'histone mark' required for the recruitment of the checkpoint
CC       protein Crb2 to sites of DNA damage. {ECO:0000269|PubMed:15550243,
CC       ECO:0000269|PubMed:19250904}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00900};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar4-20 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00900}.
DR   EMBL; CU329672; CAB60686.1; -; Genomic_DNA.
DR   PIR; T50436; T50436.
DR   RefSeq; NP_588078.1; NM_001023070.2.
DR   ProteinModelPortal; Q9USK2; -.
DR   SMR; Q9USK2; -.
DR   BioGrid; 276106; 25.
DR   STRING; 4896.SPCC4B3.12.1; -.
DR   MaxQB; Q9USK2; -.
DR   PaxDb; Q9USK2; -.
DR   PRIDE; Q9USK2; -.
DR   EnsemblFungi; SPCC4B3.12.1; SPCC4B3.12.1:pep; SPCC4B3.12.
DR   GeneID; 2539545; -.
DR   KEGG; spo:SPCC4B3.12; -.
DR   EuPathDB; FungiDB:SPCC4B3.12; -.
DR   PomBase; SPCC4B3.12; set9.
DR   InParanoid; Q9USK2; -.
DR   KO; K11429; -.
DR   OMA; ANCRFNT; -.
DR   PhylomeDB; Q9USK2; -.
DR   Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q9USK2; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0000790; C:nuclear chromatin; IC:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IMP:PomBase.
DR   GO; GO:0031491; F:nucleosome binding; IPI:PomBase.
DR   GO; GO:0034613; P:cellular protein localization; IMP:PomBase.
DR   GO; GO:0006342; P:chromatin silencing; IMP:PomBase.
DR   GO; GO:0034770; P:histone H4-K20 methylation; IMP:PomBase.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IMP:PomBase.
DR   InterPro; IPR025783; Hist-Lys_N-MeTrfase_SET9.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51567; SAM_MT43_SUVAR420_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Chromosome; Complete proteome; Methyltransferase;
KW   Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    441       Histone-lysine N-methyltransferase set9.
FT                                /FTId=PRO_0000281807.
FT   DOMAIN      108    221       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   MUTAGEN     220    220       Y->A: Loss of function.
FT                                {ECO:0000269|PubMed:15550243}.
SQ   SEQUENCE   441 AA;  51014 MW;  553FC8E19FFF42B3 CRC64;
     MRQTNTHLET FSLFDDVCTC LLVDKVFYWS QIHKVRKLVD RSIERMESCS IINIITKYII
     EQTDLDQAAK NILQFRELDP LLRRLSSTSL LAFTRHLKYY LSLYLPSCKF EICSTNQYFS
     SSKPEACVIA RESINAGEDI TDLCGTIIKL SPKEERNIGI GKDFSILHSS RLDSMCLFLG
     PARFVNHDCN ANCRFNTSGK RIWLRCVRDI KPGEEITTFY SSNYFGLENC ECLCVSCERM
     GINGFKKLFH TSATSTSCSS KSSSDVSDLS SLPQSNRYVI SEEDRSFLNI WDSGGELSDA
     SSSDLDEEFS LFIPRHKKRV WSREKRLLSE MAITNHSPLL NVDDYRKFRE DLWKKRHGKR
     KVYQCSNCSQ TFINEDIQNS SAFCPKCIRH SKLFSLPWPC RHKVNRELKL EKEKEINTKR
     NLVTSSHSMS LRHKKAVDYQ S
//
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