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BAS1_YEAST
ID   BAS1_YEAST              Reviewed;         811 AA.
AC   P22035; D6VXG0;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 191.
DE   RecName: Full=Myb-like DNA-binding protein BAS1;
GN   Name=BAS1; OrderedLocusNames=YKR099W;
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].
RX   PubMed=2683089; DOI=10.1126/science.2683089;
RA   Tice-Baldwin K., Fink G.R., Arndt K.T.;
RT   "BAS1 has a Myb motif and activates HIS4 transcription only in combination
RT   with BAS2.";
RL   Science 246:931-935(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   DNA-BINDING REGION.
RX   PubMed=8021277; DOI=10.1016/s0021-9258(17)32492-4;
RA   Hoevring P.I., Bostad A., Ording E., Myrset A.H., Gabrielsen O.S.;
RT   "DNA-binding domain and recognition sequence of the yeast BAS1 protein, a
RT   divergent member of the Myb family of transcription factors.";
RL   J. Biol. Chem. 269:17663-17669(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=9822821; DOI=10.1046/j.1365-2958.1998.01087.x;
RA   Denis V., Boucherie H., Monribot C., Daignan-Fornier B.;
RT   "Role of the myb-like protein bas1p in Saccharomyces cerevisiae: a proteome
RT   analysis.";
RL   Mol. Microbiol. 30:557-566(1998).
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   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: Activates HIS4 transcription only in combination with
CC       PHO2/BAS2. BAS1 is also involved in the regulation of the purine
CC       biosynthesis pathway. {ECO:0000269|PubMed:9822821}.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; M58057; AAB04030.1; -; Genomic_DNA.
DR   EMBL; Z28324; CAA82179.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09250.1; -; Genomic_DNA.
DR   PIR; A40083; A40083.
DR   RefSeq; NP_013025.3; NM_001179889.3.
DR   AlphaFoldDB; P22035; -.
DR   SMR; P22035; -.
DR   BioGRID; 34230; 289.
DR   DIP; DIP-142N; -.
DR   IntAct; P22035; 8.
DR   MINT; P22035; -.
DR   STRING; 4932.YKR099W; -.
DR   iPTMnet; P22035; -.
DR   MaxQB; P22035; -.
DR   PaxDb; P22035; -.
DR   PRIDE; P22035; -.
DR   EnsemblFungi; YKR099W_mRNA; YKR099W; YKR099W.
DR   GeneID; 853974; -.
DR   KEGG; sce:YKR099W; -.
DR   SGD; S000001807; BAS1.
DR   VEuPathDB; FungiDB:YKR099W; -.
DR   eggNOG; KOG0048; Eukaryota.
DR   HOGENOM; CLU_021117_0_0_1; -.
DR   InParanoid; P22035; -.
DR   OMA; IHQHIHN; -.
DR   BioCyc; YEAST:G3O-32061-MON; -.
DR   PRO; PR:P22035; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P22035; protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd00167; SANT; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00717; SANT; 3.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..811
FT                   /note="Myb-like DNA-binding protein BAS1"
FT                   /id="PRO_0000197085"
FT   DOMAIN          34..110
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DOMAIN          111..165
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          166..218
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        138..161
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        191..214
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          237..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  89604 MW;  E874E72A3B7BDDE5 CRC64;
     MSNISTKDIR KSKPKRGSGF DLLEVTESLG YQTHRKNGRN SWSKDDDNML RSLVNESAKE
     LGYENGLEDV KTIQQSNHLS KCIAWDVLAT RFKHTVRTSK DVRKRWTGSL DPNLKKGKWT
     QEEDEQLLKA YEEHGPHWLS ISMDIPGRTE DQCAKRYIEV LGPGSKGRLR EWTLEEDLNL
     ISKVKAYGTK WRKISSEMEF RPSLTCRNRW RKIITMVVRG QASEVITKAI KENKNIDMTD
     GKLRQHPIAD SDIRSDSTPN KEEQLQLSQQ NNPSLIKQDI LNVKENESSK LPRLKDNDGP
     ILNDSKPQAL PPLKEISAPP PIRMTQVGQT HTSGSIRSKV SLPIEGLSQM NKQSPGGISD
     SPQTSLPPAF NPASLDEHMM NSNSISDSPK HAYSTVKTRE PNSSSTQWKF TLKDGQGLSI
     SNGTIDSTKL VKELVDQAKK YSLKISIHQH IHNHYVTSTD HPVSSNTGLS NIGNINGNPL
     LMDSFPHMGR QLGNGLPGLN SNSDTFNPEY RTSLDNMDSD FLSRTPNYNA FSLEATSHNP
     ADNANELGSQ SNRETNSPSV FYPQANTLIP TNSTATNNEI IQGNVSANSM SPNFNGTNGK
     APSSTASYTT SGSEMPPDVG PNRIAHFNYL PPTIRPHLGS SDATRGADLN KLLNPSPNSV
     RSNGSKTKKK EKRKSESSQH HSSSSVTTNK FNHIDQSEIS RTTSRSDTPL RDEDGLDFWE
     TLRSLATTNP NPPVEKSAEN DGAKPQVVHQ GIGSHTEDSS LGSHSGGYDF FNELLDKKAD
     TLHNEAKKTS EHDMTSGGST DNGSVLPLNP S
 
 
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