位置:首页 > 蛋白库 > MSN4_YEAST
MSN4_YEAST
ID   MSN4_YEAST              Reviewed;         630 AA.
AC   P33749; D6VXM5; P35726;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 195.
DE   RecName: Full=Zinc finger protein MSN4;
DE   AltName: Full=Multicopy suppressor of SNF1 protein 4;
GN   Name=MSN4; OrderedLocusNames=YKL062W;
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 204508 / S288c;
RX   PubMed=8321194; DOI=10.1128/mcb.13.7.3872-3881.1993;
RA   Estruch F., Carlson M.;
RT   "Two homologous zinc finger genes identified by multicopy suppression in a
RT   SNF1 protein kinase mutant of Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 13:3872-3881(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091862; DOI=10.1002/yea.320100008;
RA   Rasmussen S.W.;
RT   "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT   TOA2 genes, an open reading frame (ORF) similar to a translationally
RT   controlled tumour protein, one ORF containing motifs also found in plant
RT   storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL   Yeast 10:S63-S68(1994).
RN   [3]
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   [4]
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   [5]
RP   CHARACTERIZATION.
RX   PubMed=8641288; DOI=10.1002/j.1460-2075.1996.tb00576.x;
RA   Martinez-Pastor M.T., Marchler G., Schueller C., Marchler-Bauer A.,
RA   Ruis H., Estruch F.;
RT   "The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are
RT   required for transcriptional induction through the stress response element
RT   (STRE).";
RL   EMBO J. 15:2227-2235(1996).
RN   [6]
RP   NUCLEOCYTOPLASMIC SHUTTLING.
RX   PubMed=12732613; DOI=10.1083/jcb.200303030;
RA   Jacquet M., Renault G., Lallet S., De Mey J., Goldbeter A.;
RT   "Oscillatory nucleocytoplasmic shuttling of the general stress response
RT   transcriptional activators Msn2 and Msn4 in Saccharomyces cerevisiae.";
RL   J. Cell Biol. 161:497-505(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-319 AND SER-558, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-263; SER-316 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).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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).
RN   [13]
RP   DOMAIN.
RX   PubMed=27618436; DOI=10.1371/journal.pone.0162842;
RA   Piskacek M., Havelka M., Rezacova M., Knight A.;
RT   "The 9aaTAD transactivation domains: From Gal4 to p53.";
RL   PLoS ONE 11:E0162842-E0162842(2016).
CC   -!- FUNCTION: Positive transcriptional factor that acts as a component of
CC       the stress responsive system. Recognizes and binds to the stress
CC       response element (STRE) which is involved in the response to various
CC       forms of stress (heat, oxidative, osmotic, etc.). Involved in the
CC       regulation of the CTT1, DDR2, HSP12 genes.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- DOMAIN: the 9aaTAD motif (residues 237 to 245) is a transactivation
CC       domain present in a large number of yeast and animal transcription
CC       factors. {ECO:0000305|PubMed:27618436}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L08839; AAA34807.1; -; Genomic_DNA.
DR   EMBL; X75781; CAA53421.1; -; Genomic_DNA.
DR   EMBL; Z28062; CAA81899.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09095.1; -; Genomic_DNA.
DR   PIR; S37884; S37884.
DR   RefSeq; NP_012861.1; NM_001179628.1.
DR   AlphaFoldDB; P33749; -.
DR   SMR; P33749; -.
DR   BioGRID; 34071; 158.
DR   DIP; DIP-6574N; -.
DR   IntAct; P33749; 59.
DR   MINT; P33749; -.
DR   STRING; 4932.YKL062W; -.
DR   iPTMnet; P33749; -.
DR   MaxQB; P33749; -.
DR   PaxDb; P33749; -.
DR   PRIDE; P33749; -.
DR   EnsemblFungi; YKL062W_mRNA; YKL062W; YKL062W.
DR   GeneID; 853803; -.
DR   KEGG; sce:YKL062W; -.
DR   SGD; S000001545; MSN4.
DR   VEuPathDB; FungiDB:YKL062W; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000174779; -.
DR   HOGENOM; CLU_024342_0_0_1; -.
DR   InParanoid; P33749; -.
DR   OMA; ISHSIEF; -.
DR   BioCyc; YEAST:G3O-31860-MON; -.
DR   PRO; PR:P33749; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P33749; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IGI:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..630
FT                   /note="Zinc finger protein MSN4"
FT                   /id="PRO_0000046811"
FT   ZN_FING         573..596
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         602..624
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          37..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           237..245
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000269|PubMed:27618436"
FT   COMPBIAS        502..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         479
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   630 AA;  69723 MW;  3A264FB37C82C385 CRC64;
     MLVFGPNSSF VRHANKKQED SSIMNEPNGL MDPVLSTTNV SATSSNDNSA NNSISSPEYT
     FGQFSMDSPH RTDATNTPIL TATTNTTANN SLMNLKDTAS LATNWKWKNS NNAQFVNDGE
     KQSSNANGKK NGGDKIYSSV ATPQALNDEL KNLEQLEKVF SPMNPINDSH FNENIELSPH
     QHATSPKTNL LEAEPSIYSN LFLDARLPNN ANSTTGLNDN DYNLDDTNND NTNSMQSILE
     DFVSSEEALK FMPDAGRDAR RYSEVVTSSF PSMTDSRNSI SHSIEFWNLN HKNSSNSKPT
     QQIIPEGTAT TERRGSTISP TTTINNSNPN FKLLDHDVSQ ALSGYSMDFS KDSGITKPKS
     ISSSLNRISH SSSTTRQQRA SLPLIHDIES FANDSVMANP LSDSASFLSE ENEDDAFGAL
     NYNSLDATTM SAFDNNVDPF NILKSSPAQD QQFIKPSMML SDNASAAAKL ATSGVDNITP
     TPAFQRRSYD ISMNSSFKIL PTSQAHHAAQ HHQQQPTKQA TVSPNTRRRK SSSVTLSPTI
     SHNNNNGKVP VQPRKRKSIT TIDPNNYDKN KPFKCKDCEK AFRRSEHLKR HIRSVHSTER
     PFACMFCEKK FSRSDNLSQH LKTHKKHGDF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024