JMJ3_SCHPO
ID JMJ3_SCHPO Reviewed; 752 AA.
AC O94691;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Lid2 complex component jmj3;
DE Short=Lid2C component jmj3;
GN Name=jmj3 {ECO:0000312|PomBase:SPBC83.07};
GN Synonyms=ecm5 {ECO:0000303|PubMed:12488447}; ORFNames=SPBC83.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB36869.1}
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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP COMPOSITION OF THE LID2 COMPLEX.
RX PubMed=12488447; DOI=10.1074/jbc.m209562200;
RA Roguev A., Schaft D., Shevchenko A., Aasland R., Shevchenko A.,
RA Stewart A.F.;
RT "High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation
RT in budding and fission yeasts.";
RL J. Biol. Chem. 278:8487-8493(2003).
RN [3] {ECO:0000305}
RP COMPOSITION OF THE LID2 COMPLEX.
RX PubMed=14617822; DOI=10.1074/mcp.m300081-mcp200;
RA Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
RA Shevchenko A.;
RT "A comparative analysis of an orthologous proteomic environment in the
RT yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL Mol. Cell. Proteomics 3:125-132(2004).
CC -!- SUBUNIT: Component of the Lid2 complex composed of ash2, jmj3, lid2,
CC sdc1 and snt2. {ECO:0000269|PubMed:12488447,
CC ECO:0000269|PubMed:14617822}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CU329671; CAB36869.1; -; Genomic_DNA.
DR PIR; T40696; T40696.
DR RefSeq; NP_595639.1; NM_001021533.2.
DR AlphaFoldDB; O94691; -.
DR SMR; O94691; -.
DR BioGRID; 277299; 13.
DR STRING; 4896.SPBC83.07.1; -.
DR iPTMnet; O94691; -.
DR MaxQB; O94691; -.
DR PaxDb; O94691; -.
DR PRIDE; O94691; -.
DR EnsemblFungi; SPBC83.07.1; SPBC83.07.1:pep; SPBC83.07.
DR GeneID; 2540780; -.
DR KEGG; spo:SPBC83.07; -.
DR PomBase; SPBC83.07; jmj3.
DR VEuPathDB; FungiDB:SPBC83.07; -.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_378624_0_0_1; -.
DR InParanoid; O94691; -.
DR OMA; YECILTS; -.
DR Reactome; R-SPO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O94691; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0048189; C:Lid2 complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISO:PomBase.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:PomBase.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 4: Predicted;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..752
FT /note="Lid2 complex component jmj3"
FT /id="PRO_0000084288"
FT DOMAIN 34..75
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 162..333
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 391..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 84930 MW; E15995F33AB94B66 CRC64;
MQQNVKEKHA GKSDTSVSSL ECEIDYHIEG SDGIPVVEPK ISEFVDMESF IRRVERLGKK
YGAIKVVRPS SVLNPWNEDT MKPSDVKMDL WLERMVRRKG EYFEIQSDID HGSAGPKKPT
DMNVDDRFPS NAGSSNDFEN NVAKAIAYYW RSLTHDSLWY GYTNRPSIPF YFIPSISAAQ
KDRVHLRSNT LINTWPNVGH LFAGKWKTTL PWRVESPELH AVQVHLGGSS LQWYVIPSAH
SESFKKLAGK LAQDEHWRCS DFLLHQNILF PPSTLVQNGI VTYSTVLKQD ELLITFPGTH
HSAFCLGDAV LRRFVFRSPR SASNYEFSNL RRLMVSESLY SSKSLWPHSH KPQRACSQKF
LDEFYLHDLP ESNIHDSGNF HPIHSSVDNN SFSQRDFDSP NSINPPSPLM SNHESASTEH
FNSTTTTEKE LSSLHVGEER KNRSLPLSLI WNSKAREEYI KKQKEENGDN IEFSHFDPLY
TRPSSHPLHP PPILGLPVPA QFARGELFLG RILEDRVSEH MLLLECEKSD VVEVPYECIL
TSSSAAGRRE SSYYNPALKA PNIVYDDGVP INWNEYSELP SLDRFVLPKL LPGKPIEFTP
PISVEPTSIK TIAAEESSEP TSSVDVAPTP VEDVNVNLES ISNTNESVVD LSDPLVSKNG
FEDVERSSVA DLEEDVLETR SSIFETSDID DRLTVIDRSQ SVVPSESEFS IAGANLTRRN
AVDFSVSLDT YELYVSDEVE NVDDFSLFPS LE
