SNT2_SCHPO
ID SNT2_SCHPO Reviewed; 1131 AA.
AC Q10077;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Lid2 complex component snt2;
DE Short=Lid2C component snt2;
GN Name=snt2; ORFNames=SPAC3H1.12c;
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]
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]
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]
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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CU329670; CAA92265.1; -; Genomic_DNA.
DR PIR; T38744; T38744.
DR RefSeq; NP_593554.1; NM_001018987.2.
DR AlphaFoldDB; Q10077; -.
DR SMR; Q10077; -.
DR BioGRID; 279863; 118.
DR STRING; 4896.SPAC3H1.12c.1; -.
DR iPTMnet; Q10077; -.
DR MaxQB; Q10077; -.
DR PaxDb; Q10077; -.
DR PRIDE; Q10077; -.
DR EnsemblFungi; SPAC3H1.12c.1; SPAC3H1.12c.1:pep; SPAC3H1.12c.
DR GeneID; 2543443; -.
DR KEGG; spo:SPAC3H1.12c; -.
DR PomBase; SPAC3H1.12c; snt2.
DR VEuPathDB; FungiDB:SPAC3H1.12c; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_001514_0_0_1; -.
DR InParanoid; Q10077; -.
DR OMA; LSWRKYA; -.
DR PhylomeDB; Q10077; -.
DR PRO; PR:Q10077; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0048189; C:Lid2 complex; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IC:PomBase.
DR GO; GO:0036205; P:histone catabolic process; IBA:GO_Central.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IBA:GO_Central.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR029617; Snt2.
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 PANTHER; PTHR47672; PTHR47672; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1131
FT /note="Lid2 complex component snt2"
FT /id="PRO_0000072032"
FT DOMAIN 103..222
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT ZN_FING 241..296
FT /note="Phorbol-ester/DAG-type"
FT ZN_FING 259..311
FT /note="PHD-type 1"
FT ZN_FING 812..896
FT /note="PHD-type 2"
FT ZN_FING 904..939
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 962..1016
FT /note="PHD-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 128839 MW; 44612482C32AF777 CRC64;
MLVIEADSNL LFTAMFDLDK NTNIESNHVK IGNKNTTRRL IIKSSKNSVR IAYAPPEKHF
VDVTDRFLLP ETETQNLKTR LGIFELEPLP PNGLVCCVLP NGELIQPNDF VLVNSPFPGE
PFQIARIISF EKSRPCVSTN LYDSVRLNWY FRPRDIQRHL TDTRLLFASM HSDIYNIGSV
QEKCTVKHRS QIENLDEYKS QAKSYYFDRL FDQNINKVFD VVPVTQVKNA PDDVLEDLFK
NYDFIVTEYG KGRALLNEPS NCKVCKKWCA FDFSVQCADC KKYYHMDCVV PPLLKKPPHG
FGWTCATCSF ATQRKKSTFQ KENANVDANH ATENNLEGQA TQKSVSILKG HNKALSNVSL
QEDHGKRRNL KSLRSSRNLH QQSRKSLDEN KPNSFSNVSK LKRLPWNMRY LDLKSDLTVE
KKSDIYPSRA RISISPMLPT SSEDNLHPLQ PLTTADEEMD LDLKSDERFK VDIPTFFERW
PFLKDLPLKG YLFPLCEPNL QSAMLLVPIT YSDALLDDYL CSCWNLWKKL RLPVSAFVFL
ELTITALYET KLSPAAAFEK LKSWMPGFGD PKNCTGKRVD EHKINSLVKE FGVSLQCFVE
KLKFEYSLKE IFFSFLSWAS SPKGLNTFKK LSDSSLSTTT TDSHGLPTCC YDIGMYDLQK
ILKLKKTPIC RWCHSKRSSE WFVAPPIEES SPKDKSKIVA LCQRCGYVWR YYGYPLQQAT
PSDLRNCDFE PVKKRKADWD HLSNHDNEVK KENNRIRNAS SLMENPRVST KTFDNFTLTH
DSTINVKADT VKRARQNNIK NKDDVNFSED RKKCCALCGI VGTEGLLVCF KCGTCVHERC
YVCDDYAENE QMLVSASHLS GRTTRNSASP GIVSGKKSYA KKDQVLSWAC LSCRSNDNLG
QNNDNHCVLC LQSASHSLMK KTVEGNWVHL ICASWTPDVY VPAEESEPVC GIAQLPPNRW
EKKCEVCGNS FGVCVSSPNS GLTSHVTCAE KANWYLGFEF VKQDQSPFSM LSNLKSLSFF
GNVTEINTNK CMINSWTSLR PVLFGPSEQL PRNFLLRNDI VPNTNNSAWS EYIRNLYPKA
YIYLLQYTIA VCKPTIAPTN VACCCSKCNS TMSPFWWPGN ICQACHCLRV E
