GenomeNet

Database: UniProt
Entry: O74467
LinkDB: O74467
Original site: O74467 
ID   SET5_SCHPO              Reviewed;         319 AA.
AC   O74467;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JAN-2019, entry version 98.
DE   RecName: Full=SET domain-containing protein 5;
DE            EC=2.1.1.43;
GN   Name=set5; ORFNames=SPCC1739.05;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND THR-318, AND
RP   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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; CU329672; CAA20779.1; -; Genomic_DNA.
DR   PIR; T41113; T41113.
DR   RefSeq; NP_588413.1; NM_001023404.2.
DR   ProteinModelPortal; O74467; -.
DR   SMR; O74467; -.
DR   BioGrid; 275434; 22.
DR   STRING; 4896.SPCC1739.05.1; -.
DR   iPTMnet; O74467; -.
DR   MaxQB; O74467; -.
DR   PaxDb; O74467; -.
DR   PRIDE; O74467; -.
DR   EnsemblFungi; SPCC1739.05.1; SPCC1739.05.1:pep; SPCC1739.05.
DR   GeneID; 2538853; -.
DR   KEGG; spo:SPCC1739.05; -.
DR   EuPathDB; FungiDB:SPCC1739.05; -.
DR   PomBase; SPCC1739.05; set5.
DR   InParanoid; O74467; -.
DR   OMA; PFLAICK; -.
DR   PhylomeDB; O74467; -.
DR   PRO; PR:O74467; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000790; C:nuclear chromatin; IC:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:PomBase.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:PomBase.
DR   GO; GO:0034968; P:histone lysine methylation; IC:PomBase.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    319       SET domain-containing protein 5.
FT                                /FTId=PRO_0000317700.
FT   DOMAIN        4    141       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   MOD_RES     316    316       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     318    318       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18257517}.
SQ   SEQUENCE   319 AA;  36499 MW;  B0A26AF8F546B1CB CRC64;
     MNPYETEIYK VVPIPNKGMG MIAKVKIPVG TRIFAETPLI RTKSDAKEIE EALSTKTKEE
     QEAFHRLFNA HPDTMGPFLG PFYSNALTID ETKGGMFLLG SRMNHDCSPN VKHTWNPRLD
     QVTVHAVRDI EAGEEILTTY IDLHKSHTER QKILLEHFGF KCYCSVCSVE ERKIRKISDL
     RRKQLAYYDR TMAKMCIVNP RGALRALRHR IHIAHEELLF GRLDIIALLD AFRLCVIHGD
     FERASIFAKK GTKAISLYEG TDSEKYLKIS KYVENPRSHA LAEGVPALPL FLEEDDELSD
     LEDNLWGCKL EEDVYSDTD
//
DBGET integrated database retrieval system