LYS14_YEAST
ID LYS14_YEAST Reviewed; 790 AA.
AC P40971; D6VS18;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Lysine biosynthesis regulatory protein LYS14;
GN Name=LYS14; OrderedLocusNames=YDR034C; ORFNames=YD9673.04C;
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=1278B;
RX PubMed=7935367; DOI=10.1128/mcb.14.10.6411-6418.1994;
RA Feller A., Dubois E., Ramos F., Pierard A.;
RT "Repression of the genes for lysine biosynthesis in Saccharomyces
RT cerevisiae is caused by limitation of Lys14-dependent transcriptional
RT activation.";
RL Mol. Cell. Biol. 14:6411-6418(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [6]
RP IDENTIFICATION BY 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 [7]
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).
CC -!- FUNCTION: Activates the transcription of lysine biosynthesis genes.
CC This activation is dependent on the inducer alpha-aminoadipate
CC semialdehyde and repressed by lysine.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X77361; CAA54550.1; -; Genomic_DNA.
DR EMBL; Z68196; CAA92371.1; -; Genomic_DNA.
DR EMBL; Z74330; CAA98856.1; -; Genomic_DNA.
DR EMBL; AY723768; AAU09685.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11878.1; -; Genomic_DNA.
DR PIR; S61587; S61587.
DR RefSeq; NP_010317.3; NM_001180342.3.
DR AlphaFoldDB; P40971; -.
DR BioGRID; 32083; 26.
DR DIP; DIP-5178N; -.
DR IntAct; P40971; 62.
DR MINT; P40971; -.
DR STRING; 4932.YDR034C; -.
DR iPTMnet; P40971; -.
DR MaxQB; P40971; -.
DR PaxDb; P40971; -.
DR PRIDE; P40971; -.
DR EnsemblFungi; YDR034C_mRNA; YDR034C; YDR034C.
DR GeneID; 851598; -.
DR KEGG; sce:YDR034C; -.
DR SGD; S000002441; LYS14.
DR VEuPathDB; FungiDB:YDR034C; -.
DR eggNOG; ENOG502QW5G; Eukaryota.
DR HOGENOM; CLU_014489_1_0_1; -.
DR InParanoid; P40971; -.
DR OMA; SWYDISH; -.
DR BioCyc; YEAST:G3O-29649-MON; -.
DR PRO; PR:P40971; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40971; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001196; P:positive regulation of lysine biosynthetic process via alpha-aminoadipate and saccharopine; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR021858; Fun_TF.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF11951; Fungal_trans_2; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Amino-acid biosynthesis; DNA-binding; Lysine biosynthesis;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..790
FT /note="Lysine biosynthesis regulatory protein LYS14"
FT /id="PRO_0000114955"
FT DNA_BIND 159..186
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 121
FT /note="I -> F (in Ref. 1; CAA54550)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="K -> R (in Ref. 1; CAA54550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 89397 MW; 713966BE6B327F46 CRC64;
MFESVNLDEN SPEDRELAKV LSPPGSYLSP ASLDSGSSFT NSGTSTSCFE PKNNLPSLSF
LNARAGSLGG IFNHKQMTSP SNSNIGGENV ESTTSSNDGS NENAGHPTTS EQDQNADHPT
ISQADDNGHS SLTPNPAVTS TVTDKKGNTV KRKYSRNGCS ECKRRRMKCD ETKPTCWQCA
RLNRQCVYVL NPKNKKRRTS NAQRVKEFRK HSTSLDNDHN NARKRQHSSC KAEKKKKVRQ
NLSEDTTDPK PITDNGKNVP LDEIESLEIP NLDLTTTMNG YDVNLLMQNL NDMVNMKLHD
SYLLNEELKG LDLPDLDIPE LLPASNVNSS VPISFLVNNV ITFNTKLSSF KLGGIHDKYL
KIFYYDCLDS IAPFFQNQGN PLRDILLSFA KNEAYLLSSI LATGASIAYR KSNNLEDERN
YCAYLSHCLS LLGEQFKNES NVLNRIEPII LTVIMLAWDC IYSMNSQWRS HLKGVTDLFK
KINAGNSSKV LNVAKCWFKV METFASISTV FGGSLIDNND LDAIFDPYDY QYVDSLKFLN
IMTPLNEFNL LRGHKEDFDL VIKEVFKSLN TIRSTEKNYF SKEEGLFTKK LDYLLLSSQT
SSEKSKDQIS YFNTQKILVE IDKQLDYEFI DKSGIIPSDN QSHPRISNIH DNAIDMVTLK
NGEEVAISWY DISHQTQVLS FLLIVLLKLL GMPKESSTIQ QVVKKIMSFF KFLDSDSPPQ
NSRTCYSNFA VLIAGLNAMD EETRAIVKRY YKINGGKFQK LTEHNLNRLE KVWYGKNQNY
RLEEQDVLTW
