GenomeNet

Database: UniProt
Entry: Q9P6L2
LinkDB: Q9P6L2
Original site: Q9P6L2 
ID   RKM4_SCHPO              Reviewed;         468 AA.
AC   Q9P6L2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   16-JAN-2019, entry version 89.
DE   RecName: Full=Ribosomal lysine N-methyltransferase 4 {ECO:0000250|UniProtKB:Q12504};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q12504};
DE   AltName: Full=SET domain-containing protein 13 {ECO:0000303|PubMed:20444689};
GN   Name=set13 {ECO:0000303|PubMed:20444689};
GN   ORFNames=SPAC688.14 {ECO:0000312|PomBase:SPAC688.14};
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
RA   Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
RA   Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
RA   FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
RA   Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
RA   Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
RA   Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
RA   Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
RA   Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20444689; DOI=10.1074/jbc.M110.132274;
RA   Shirai A., Sadaie M., Shinmyozu K., Nakayama J.;
RT   "Methylation of ribosomal protein L42 regulates ribosomal function and
RT   stress-adapted cell growth.";
RL   J. Biol. Chem. 285:22448-22460(2010).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that monomethylates 60S ribosomal protein L42
CC       (rpl42) at 'Lys-55'. {ECO:0000269|PubMed:20444689}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:20444689}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SETD6 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190,
CC       ECO:0000305}.
DR   EMBL; CU329670; CAB90780.2; -; Genomic_DNA.
DR   RefSeq; NP_594072.2; NM_001019496.2.
DR   BioGrid; 279768; 13.
DR   STRING; 4896.SPAC688.14.1; -.
DR   iPTMnet; Q9P6L2; -.
DR   MaxQB; Q9P6L2; -.
DR   PaxDb; Q9P6L2; -.
DR   PRIDE; Q9P6L2; -.
DR   EnsemblFungi; SPAC688.14.1; SPAC688.14.1:pep; SPAC688.14.
DR   GeneID; 2543346; -.
DR   KEGG; spo:SPAC688.14; -.
DR   EuPathDB; FungiDB:SPAC688.14; -.
DR   PomBase; SPAC688.14; set13.
DR   InParanoid; Q9P6L2; -.
DR   KO; K05302; -.
DR   OMA; MFNGDDE; -.
DR   PRO; PR:Q9P6L2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:PomBase.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR   GO; GO:1990497; P:regulation of cytoplasmic translation in response to stress; IMP:PomBase.
DR   InterPro; IPR011383; N-lys_methylase_SETD6.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF011771; RMS1_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    468       Ribosomal lysine N-methyltransferase 4.
FT                                /FTId=PRO_0000303948.
FT   DOMAIN       22    302       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   BINDING     301    301       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   468 AA;  54023 MW;  F2934820771869BC CRC64;
     MLKQAESMLK WAIEKDNYTT SEKIGLNDYR HVHESLGIGF IALEDIKEDE KLVSFKKDSV
     LCLTNSDLAQ LPEVQSLPSW AALLLVMATE NASPNSFWRP YLSIFPTKER ITSPFYWDEN
     KKDALLRGTV LESNEDCNEI TQLWIDRIEP IIKLYPNRFS QVSYEDFLRM SAVMLAYSFD
     IEKTKSPISN ENEKSAAETS IKEDKNGDAA KKNEGSANQD DEKLHSQSLV GNNCEVNSED
     EFSDLESEVD PDELEKAMCP ISDMFNGDDE LCNIRLYDIN GTLTMIATRD IKKGEQLWNT
     YGELDNSELF RKYGFTKKKG TPHDFVLIKK EHWLPEYIEK LGFEEVEARL ELLCREELLY
     NLEGDFTFSK ADLTFKEICL AFVLMEKEKE LISVPSKSDI KPKHYRKLLK IIEKRINMYP
     KISDPKNFDE ENAKTLIEGE IDILQNLSAK VKEALTKNRP KKKQKVDH
//
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