MSN1_YEAST
ID MSN1_YEAST Reviewed; 382 AA.
AC P22148; D6W1V1; Q12227; Q9URF6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein MSN1;
DE AltName: Full=Multicopy suppressor of SNF1 protein 1;
GN Name=MSN1; Synonyms=FUP1, PHD2; OrderedLocusNames=YOL116W; ORFNames=HRB382;
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=2263457; DOI=10.1093/nar/18.23.6959;
RA Estruch F., Carlson M.;
RT "Increased dosage of the MSN1 gene restores invertase expression in yeast
RT mutants defective in the SNF1 protein kinase.";
RL Nucleic Acids Res. 18:6959-6964(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1564445; DOI=10.1099/00221287-138-2-347;
RA Eide D., Guarente L.;
RT "Increased dosage of a transcriptional activator gene enhances iron-limited
RT growth of Saccharomyces cerevisiae.";
RL J. Gen. Microbiol. 138:347-354(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [8]
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: May function as a transcriptional activator. Increased dosage
CC of MSN1 restores invertase expression in yeast mutants defective in the
CC SNF1 protein kinase, and msn1 disruption reduced derepression of
CC invertase in the wild-type. May affect SUC2 expression. Expression of
CC MSN1 enhances growth in iron-limiting conditions.
CC {ECO:0000269|PubMed:1564445}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 491 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X54324; CAA38222.1; -; Genomic_DNA.
DR EMBL; Z48149; CAA88144.1; -; Genomic_DNA.
DR EMBL; Z74858; CAA99135.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10667.1; -; Genomic_DNA.
DR PIR; S51881; S51881.
DR RefSeq; NP_014525.1; NM_001183370.1.
DR AlphaFoldDB; P22148; -.
DR SMR; P22148; -.
DR BioGRID; 34284; 315.
DR DIP; DIP-5660N; -.
DR IntAct; P22148; 6.
DR MINT; P22148; -.
DR STRING; 4932.YOL116W; -.
DR iPTMnet; P22148; -.
DR MaxQB; P22148; -.
DR PaxDb; P22148; -.
DR PRIDE; P22148; -.
DR EnsemblFungi; YOL116W_mRNA; YOL116W; YOL116W.
DR GeneID; 854033; -.
DR KEGG; sce:YOL116W; -.
DR SGD; S000005476; MSN1.
DR VEuPathDB; FungiDB:YOL116W; -.
DR eggNOG; ENOG502RNWJ; Eukaryota.
DR HOGENOM; CLU_030906_0_0_1; -.
DR InParanoid; P22148; -.
DR OMA; QPIGWLC; -.
DR BioCyc; YEAST:G3O-33513-MON; -.
DR PRO; PR:P22148; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22148; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR InterPro; IPR022210; TF_GCR1-like.
DR Pfam; PF12550; GCR1_C; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..382
FT /note="Protein MSN1"
FT /id="PRO_0000096598"
FT REGION 12..26
FT /note="Leucine-zipper"
FT REGION 104..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 266..271
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 155..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 360
FT /note="D -> Y (in Ref. 1; CAA38222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 43060 MW; 2E09FD17A3A5B715 CRC64;
MASNQHIGAS NLNENEAILT NRVAELERRM SMFEGIFHAL SNRLDLHFKK YDVVVNSQQQ
QINELTAFLS TLLNDQQRHA EILSEKLSGT LHGVSATSIS LSQTLDPQGF TDGTTAPGAP
RNYTSVPMNN DQTAHPQNEG AVSNETLFED ILNGNSQEND KSQQQTNSSN SISQENNSTN
PSVDTRFNKP QNYNSNLVPS LEEYSANPPN NDGGQSQGLY ISSNSSQSRQ SPNLQKVSPN
HENAVESNAQ ESVPTFEEEQ YETKTGLKRK RIVCTRPFEF IKSPHSVMEV WKEYTEGVNG
QPSIRKMEAL YQTAWRRDPA VNKRYSRRKV LWKAIQTGLN RGYSLNYVVE ILENSRYVND
KQKVKQPIGW LCHSSHIPET LK
