SKO1_YEAST
ID SKO1_YEAST Reviewed; 647 AA.
AC Q02100; D6W115;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=CRE-binding bZIP protein SKO1;
GN Name=SKO1; Synonyms=ACR1; OrderedLocusNames=YNL167C; ORFNames=N1702;
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=ATCC 208353 / W303-1A;
RX PubMed=1437546; DOI=10.1093/nar/20.20.5271;
RA Nehlin J.O., Carlberg M., Ronne H.;
RT "Yeast SKO1 gene encodes a bZIP protein that binds to the CRE motif and
RT acts as a repressor of transcription.";
RL Nucleic Acids Res. 20:5271-5278(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1448073; DOI=10.1128/mcb.12.12.5394-5405.1992;
RA Vincent A.C., Struhl K.;
RT "ACR1, a yeast ATF/CREB repressor.";
RL Mol. Cell. Biol. 12:5394-5405(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; THR-113; SER-399 AND
RP SER-558, AND 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).
CC -!- FUNCTION: Binds to the CRE motif 5'-TGACGTCA-3' and acts as a repressor
CC of transcription of the SUC2 gene and most probably other genes.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; X67875; CAA48074.1; -; Genomic_DNA.
DR EMBL; S49588; AAB24288.1; -; Genomic_DNA.
DR EMBL; X92517; CAA63272.1; -; Genomic_DNA.
DR EMBL; Z71443; CAA96054.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10381.1; -; Genomic_DNA.
DR PIR; S26386; S26386.
DR RefSeq; NP_014232.1; NM_001183005.1.
DR AlphaFoldDB; Q02100; -.
DR SMR; Q02100; -.
DR BioGRID; 35661; 75.
DR DIP; DIP-700N; -.
DR IntAct; Q02100; 3.
DR MINT; Q02100; -.
DR STRING; 4932.YNL167C; -.
DR iPTMnet; Q02100; -.
DR MaxQB; Q02100; -.
DR PaxDb; Q02100; -.
DR PRIDE; Q02100; -.
DR EnsemblFungi; YNL167C_mRNA; YNL167C; YNL167C.
DR GeneID; 855554; -.
DR KEGG; sce:YNL167C; -.
DR SGD; S000005111; SKO1.
DR VEuPathDB; FungiDB:YNL167C; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000176028; -.
DR HOGENOM; CLU_027901_0_0_1; -.
DR InParanoid; Q02100; -.
DR OMA; HGAFMSQ; -.
DR BioCyc; YEAST:G3O-33183-MON; -.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-450341; Activation of the AP-1 family of transcription factors.
DR PRO; PR:Q02100; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; Q02100; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR020956; TF_Aft1_OSM.
DR Pfam; PF11785; Aft1_OSA; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..647
FT /note="CRE-binding bZIP protein SKO1"
FT /id="PRO_0000076517"
FT DOMAIN 429..492
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..451
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 454..461
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 647 AA; 70192 MW; 3E0B8C72A6CE14AB CRC64;
MSSEERSRQP STVSTFDLEP NPFEQSFASS KKALSLPGTI SHPSLPKELS RNNSTSTITQ
HSQRSTHSLN SIPEENGNST VTDNSNHNDV KKDSPSFLPG QQRPTIISPP ILTPGGSKRL
PPLLLSPSIL YQANSTTNPS QNSHSVSVSN SNPSAIGVSS TSGSLYPNSS SPSGTSLIRQ
PRNSNVTTSN SGNGFPTNDS QMPGFLLNLS KSGLTPNESN IRTGLTPGIL TQSYNYPVLP
SINKNTITGS KNVNKSVTVN GSIENHPHVN IMHPTVNGTP LTPGLSSLLN LPSTGVLANP
VFKSTPTTNT TDGTVNNSIS NSNFSPNTST KAAVKMDNPA EFNAIEHSAH NHKENENLTT
QIENNDQFNN KTRKRKRRMS STSSTSKASR KNSISRKNSA VTTAPAQKDD VENNKISNNV
TLDENEEQER KRKEFLERNR VAASKFRKRK KEYIKKIEND LQFYESEYDD LTQVIGKLCG
IIPSSSSNSQ FNVNVSTPSS SSPPSTSLIA LLESSISRSD YSSAMSVLSN MKQLICETNF
YRRGGKNPRD DMDGQEDSFN KDTNVVKSEN AGYPSVNSRP IILDKKYSLN SGANISKSNT
TTNNVGNSAQ NIINSCYSVT NPLVINANSD THDTNKHDVL STLPHNN
