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Database: UniProt
Entry: Q10362
LinkDB: Q10362
Original site: Q10362 
ID   SET3_SCHPO              Reviewed;         859 AA.
AC   Q10362; Q9USE1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JAN-2019, entry version 122.
DE   RecName: Full=SET domain-containing protein 3;
GN   Name=set3; ORFNames=SPAC22E12.11c;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 14-152, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496; SER-533; SER-575;
RP   SER-714 AND SER-716, AND IDENTIFICATION 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: Transcriptional regulator that acts via the formation of
CC       large multiprotein complexes that modify and/or remodel the
CC       chromatin. Required for both gene activation and repression. Part
CC       of the Set3C complex, which is required to repress early/middle
CC       sporulation genes during meiosis. Required for the transcriptional
CC       activation of genes with high activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET3 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
DR   EMBL; CU329670; CAA93898.1; -; Genomic_DNA.
DR   EMBL; AB027830; BAA87134.1; -; Genomic_DNA.
DR   PIR; T38168; T38168.
DR   RefSeq; NP_594837.1; NM_001020266.2.
DR   ProteinModelPortal; Q10362; -.
DR   SMR; Q10362; -.
DR   BioGrid; 278389; 123.
DR   STRING; 4896.SPAC22E12.11c.1; -.
DR   iPTMnet; Q10362; -.
DR   MaxQB; Q10362; -.
DR   PaxDb; Q10362; -.
DR   PRIDE; Q10362; -.
DR   EnsemblFungi; SPAC22E12.11c.1; SPAC22E12.11c.1:pep; SPAC22E12.11c.
DR   GeneID; 2541899; -.
DR   KEGG; spo:SPAC22E12.11c; -.
DR   EuPathDB; FungiDB:SPAC22E12.11c; -.
DR   PomBase; SPAC22E12.11c; set3.
DR   InParanoid; Q10362; -.
DR   KO; K07117; -.
DR   Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q10362; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IDA:PomBase.
DR   GO; GO:0034967; C:Set3 complex; IDA:PomBase.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061659; F:ubiquitin-like protein ligase activity; ISM:PomBase.
DR   GO; GO:0006338; P:chromatin remodeling; IPI:PomBase.
DR   GO; GO:0070869; P:heterochromatin assembly involved in chromatin silencing; IC:PomBase.
DR   GO; GO:0034968; P:histone lysine methylation; IC:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Complete proteome; Meiosis;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    859       SET domain-containing protein 3.
FT                                /FTId=PRO_0000076313.
FT   DOMAIN      210    337       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING       5     51       PHD-type.
FT   MOD_RES     496    496       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     533    533       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     575    575       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     714    714       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     716    716       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
SQ   SEQUENCE   859 AA;  94887 MW;  B4865BF40FD2C5D8 CRC64;
     MWKIRCVCPF EDDDGFTIQC ESCEVWQHAV CVNIDANNVP EKYFCEQCQP RPIDADKAHK
     IQLARLQREE EQSRILSRSR SSNNKRRTSF GKNGASPTHS ASPRQGNNTG ANGALFSQST
     NSSNSGSYRN SVTGATLPNA HAPHSQNRRR RSNHLNNPPE APITEASNEY VYSFHLEYVP
     LESNTFSASA LEYSKNLDLK NLDESEVLMD GCQVVPISSS KFCCSRFGLV STCEIPPNTP
     IMEVKGRVCT QNEYKSDPKN QYNILGAPKP HVFFDSNSQL VVDSRVAGSK ARFARKGCQS
     NSVVSSVYMN GSNSVPRFIL YSTTHIAPET EIIGDWTLDI SHPFRQFAPG MSRPSFNMEE
     LELLSEVLST FLSFNECASQ DKKNCVFSRV TKYIKAARRA STANRVSVAK DRLSLTPSST
     PSTPSPAESL PQPSNPTSVY AKSLKEFWLD KYRLSILQKW PAVKSLPTES VGIDVVMEPK
     LQPSVKEKKP TKDLQSPLPS VEEDSSNRDK KTDIADLHTD SKVGIADVLS PISPDAALQS
     DGPLKKAKEP EESSITPTTP PSFNVGESLS RRSASPLQHP RTSPDMLDKT SPCKRGLGTI
     TTVHKKHGSV DHLPSVKRRR SIANDFHGKP DYNKRSLSIE RKPEAFKTKG DRPHKVHPSF
     HRNSDSKLKL EPSSKEKSGS MFFNTLRTVK DKSHVHDTQR SSDVNFSRQN GTRSHSPSVS
     PVGFSFDKSP VTTPPLPTAP APVITSRHAL VNNQFPTNNP NILDHKANNG DDISNALNTS
     RSENKPNSNL VQGSVVKPSN TSASALPTSA PKKLSLSEYR QRRQQNILHQ QSKDNQAHGD
     TARPHTVPAA TVSNPSFTR
//
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