LID2_SCHPO
ID LID2_SCHPO Reviewed; 1513 AA.
AC Q9HDV4; Q9P7E6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Lid2 complex component lid2;
DE Short=Lid2C component lid2;
GN Name=lid2; ORFNames=SPBP19A11.06, SPBP4H10.01;
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:CAC19756.1}
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, AND IDENTIFICATION BY
RP 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 -!- 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 -!- INTERACTION:
CC Q9HDV4; O74910: raf1; NbExp=2; IntAct=EBI-2105919, EBI-904913;
CC Q9HDV4; Q9Y7R4: set1; NbExp=2; IntAct=EBI-2105919, EBI-2106005;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CU329671; CAC19756.1; -; Genomic_DNA.
DR PIR; T50313; T50313.
DR RefSeq; NP_596174.1; NM_001022094.2.
DR AlphaFoldDB; Q9HDV4; -.
DR SMR; Q9HDV4; -.
DR BioGRID; 277811; 7.
DR IntAct; Q9HDV4; 7.
DR STRING; 4896.SPBP19A11.06.1; -.
DR iPTMnet; Q9HDV4; -.
DR MaxQB; Q9HDV4; -.
DR PaxDb; Q9HDV4; -.
DR PRIDE; Q9HDV4; -.
DR EnsemblFungi; SPBP19A11.06.1; SPBP19A11.06.1:pep; SPBP19A11.06.
DR GeneID; 2541299; -.
DR KEGG; spo:SPBP19A11.06; -.
DR PomBase; SPBP19A11.06; lid2.
DR VEuPathDB; FungiDB:SPBP19A11.06; -.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_0_0_1; -.
DR InParanoid; Q9HDV4; -.
DR OMA; DGISYME; -.
DR PhylomeDB; Q9HDV4; -.
DR PRO; PR:Q9HDV4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0048189; C:Lid2 complex; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; EXP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 3.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1513
FT /note="Lid2 complex component lid2"
FT /id="PRO_0000200599"
FT DOMAIN 56..97
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 121..212
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 408..574
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 268..318
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1093..1145
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1096..1143
FT /note="RING-type 1; degenerate"
FT /evidence="ECO:0000255"
FT ZN_FING 1352..1403
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1354..1401
FT /note="RING-type 2; degenerate"
FT /evidence="ECO:0000255"
FT REGION 211..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1513 AA; 172259 MW; B8787624F9E7DFAD CRC64;
MICQLLWHEH NSMGSGREKK IRKLGDNFSL PYLKFDCDHN DKNYRASNRP FGLSTGLSVQ
LNASNMTDPF KFLLDNWHTI FKNGAIKLLP PEGWQIPVVL DQGAFEFQSK RQCLNKGCLN
YEKNYDYFKK LKAFHESRGL YFYHPPIIGN RPVDFLRLRN AISKFTNSGS SLNNEILHKV
IIYLRLEDTK EVRQVLTRCY DRYIKPFERD SSPSFKSKRS ESSTRKIRNT RSSAQQESPI
PETSAQSPVQ TIQVNGSTSL KRPLIERGEQ CEYCGLDKNP ETILLCDGCE AAYHTSCLDP
PLTSIPKEDW YCDACKFNIS DYDPRKGFKW KLSSLKERSA EIFNTLGERN SSSKLTNLTE
DDIELFYWSS LAESNSGFAP LELEGLSQAY TSTIQSSLPS KEVFPLEKYS SEPWNLHNLP
FENPCLFNYS FSDLSSLTIT RLSIGMVFYT HGWTKSSLST GLLHHHRFGD TVTWYVLPPD
ESDAFERYLI SSYPQYTMED LNRSNGLPVI VSPSSLIENG FHPIAIDLRP NEFLVVSPNS
YHMGFHQGFS SFESVNFATV NWIKDGLLNS SISVLKSMRI PSSVSYEAVI ISMVLSKNPC
FSSEWLIKCF EDMIANESAS KNEIMKLVPN IQALKLESSV PLEIRCSNCK QPCFLSFMQC
HEPKKFICLG DCVKEVSLNA TSWMLFYRWD VHELSNLAER FVSLIRGPEE WTNRLRSVLS
TSPKPQLKVL KSLLVDAEKA MLTTPETVNL RDFVQNANSW IDSVNECLKV ASLKRKKDKK
PPLFKAHDHW NNTSNLKDSA VLFKVLQTSR SMAFTCQEIE NMKQKAFDLL EFRNRLINSF
SGPLDKNTCQ RLLTEAELLG FTIPELGIIQ KYLIQFEWLD MFYSFETTRT TDSDLERLIT
YGVSAGIPED NDYMIFAKAM KGRAEIWENQ VYDTLSKSNI SYDKLSLLRD EAMNLCVNKE
LFSKVVGILN NAEEIKNKIA TLCERSQEKD FALRPSIDEV KEALASAEKL PILSESTVTL
QKMYDVVLEW IRRGKRLFGK ANAPLEILGQ HLDYVEKRNS ASLSLNDRPG PPMEPASRET
SPDSEGRLTI RKKKGCIFCF CRLPESGVMI ECEICHEWYH AKCLKMSKKK LRQDEKFTCP
ICDYRVEIPR LSNRPKLEDL QSLYKDVKLL PFQPKETETL RKVVDLASKF RQEMQALAHN
PFGLTMAEVP LARFYLRKME GAEILLVDET NLFRQKLHEC VPIAPNPPPI IGESKSTRKP
RPTKRQRQIM KQVAEGLLPA SAIAPPKSSN EKKSSNNVKA VEAETKSKSE KSPKKNGTNI
SDANNKNESH VSLMKNWKLG SPAFVTLVKE KNSSCLCGEE FSPRDSFIDC TICERRFHYD
CVGLNNEIAD SVSKFTCPIC MEQSGGIYPW QLRPRNGMHP DHISGFSKEV ETDPKLGSSG
YTLNNSKFDK AAVSKTLSAQ DVSRLQKVSC GEHLYFGTDV FTPLGDMATS ASMFSLDDSS
EKTDAFTENF LNV
