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LEE1_YEAST
ID   LEE1_YEAST              Reviewed;         301 AA.
AC   Q02799; D6W3W0; Q06701;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Zinc finger protein LEE1;
GN   Name=LEE1; OrderedLocusNames=YPL054W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YNN 259;
RA   Jamieson L., Orr E.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-30 AND SER-282, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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DR   EMBL; X86735; CAA60414.1; -; Genomic_DNA.
DR   EMBL; U39205; AAB68311.1; -; Genomic_DNA.
DR   EMBL; AY693073; AAT93092.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11376.1; -; Genomic_DNA.
DR   PIR; S60936; S60936.
DR   RefSeq; NP_015271.1; NM_001183868.1.
DR   AlphaFoldDB; Q02799; -.
DR   BioGRID; 36126; 72.
DR   STRING; 4932.YPL054W; -.
DR   iPTMnet; Q02799; -.
DR   PaxDb; Q02799; -.
DR   PRIDE; Q02799; -.
DR   EnsemblFungi; YPL054W_mRNA; YPL054W; YPL054W.
DR   GeneID; 856053; -.
DR   KEGG; sce:YPL054W; -.
DR   SGD; S000005975; LEE1.
DR   VEuPathDB; FungiDB:YPL054W; -.
DR   eggNOG; KOG1039; Eukaryota.
DR   GeneTree; ENSGT00950000183077; -.
DR   HOGENOM; CLU_080788_0_0_1; -.
DR   InParanoid; Q02799; -.
DR   OMA; NSRYCHE; -.
DR   BioCyc; YEAST:G3O-33966-MON; -.
DR   PRO; PR:Q02799; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q02799; protein.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR11224; PTHR11224; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   1: Evidence at protein level;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..301
FT                   /note="Zinc finger protein LEE1"
FT                   /id="PRO_0000213909"
FT   ZN_FING         87..114
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         123..145
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        198
FT                   /note="Y -> F (in Ref. 1; CAA60414)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  33596 MW;  9FAC35F9C91950A6 CRC64;
     MDAFENMSVS NHPGGNARRN SQSANEMLAS QIQDFQNIPR SFNDSNANVN LSKNCTVGNQ
     LPFSSRQQKI IMEHLLITKN NSQQQKDYSH VPCKFFKMGN CQAGSSCPFS HSPDIISSAN
     NLPCKYFAKG NCKFGNKCVN AHVLPNGFKM NSKEPIDITP PSQNNYLSHA RSASFSTYTS
     PPLSAQTEFS HSASNANYFS SQYLMYSPQK SPEALYTEFF SPPSSSSSYI NYSYNNSNIN
     AYSPVSSSSS NIWQEQGQTT LSNPSVNQNL RYRTGPAIQE ESDNEIEDLL IHNFNSRYCH
     E
 
 
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