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Regulatory protein MIG1 (Regulatory protein CAT4)

 MIG1_YEAST              Reviewed;         504 AA.
P27705; D6VUA4;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=Regulatory protein MIG1;
AltName: Full=Regulatory protein CAT4;
Name=MIG1; Synonyms=CAT4, SSN1; OrderedLocusNames=YGL035C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 208353 / W303-1A;
PubMed=2167835;
Nehlin J.O., Ronne H.;
"Yeast MIG1 repressor is related to the mammalian early growth
response and Wilms' tumour finger proteins.";
EMBO J. 9:2891-2898(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204510 / AB320;
Huse K., Hohmannn S., Valentin E., Zimmermann F.K.;
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-377, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-310; SER-311
AND SER-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Involved in glucose repression of the SUC, GAL and MAL
genes as well as of the CAT8 gene. Binds to two sites in the
upstream region of SUC2.
-!- INTERACTION:
P02829:HSP82; NbExp=3; IntAct=EBI-10913, EBI-8659;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA39084.1; Type=Frameshift; Positions=381; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X55734; CAA39266.1; -; Genomic_DNA.
EMBL; X55442; CAA39084.1; ALT_FRAME; Genomic_DNA.
EMBL; Z72557; CAA96736.1; -; Genomic_DNA.
EMBL; AY693159; AAT93178.1; -; Genomic_DNA.
EMBL; BK006941; DAA08065.1; -; Genomic_DNA.
PIR; S17248; S17248.
RefSeq; NP_011480.1; NM_001180900.1.
PDB; 1T5W; X-ray; 2.40 A; C/F=455-462.
PDB; 1T5X; X-ray; 2.50 A; C=455-462.
PDBsum; 1T5W; -.
PDBsum; 1T5X; -.
ProteinModelPortal; P27705; -.
SMR; P27705; -.
BioGrid; 33212; 257.
DIP; DIP-665N; -.
IntAct; P27705; 13.
MINT; MINT-400332; -.
STRING; 4932.YGL035C; -.
iPTMnet; P27705; -.
MaxQB; P27705; -.
PRIDE; P27705; -.
EnsemblFungi; YGL035C; YGL035C; YGL035C.
GeneID; 852848; -.
KEGG; sce:YGL035C; -.
EuPathDB; FungiDB:YGL035C; -.
SGD; S000003003; MIG1.
GeneTree; ENSGT00550000074455; -.
HOGENOM; HOG000113589; -.
InParanoid; P27705; -.
KO; K09467; -.
OMA; CDFPGCV; -.
OrthoDB; EOG092C5XWP; -.
BioCyc; YEAST:G3O-30550-MONOMER; -.
EvolutionaryTrace; P27705; -.
PRO; PR:P27705; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:SGD.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:SGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0000433; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IDA:SGD.
GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IGI:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
SMART; SM00355; ZnF_C2H2; 2.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Complete proteome; DNA-binding;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 504 Regulatory protein MIG1.
/FTId=PRO_0000046881.
ZN_FING 38 60 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 66 90 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 253 260 Gln-rich.
COMPBIAS 411 444 Asn/Gln-rich.
MOD_RES 278 278 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
SEQUENCE 504 AA; 55532 MW; 5D3B883D8FA15B7F CRC64;
MQSPYPMTQV SNVDDGSLLK ESKSKSKVAA KSEAPRPHAC PICHRAFHRL EHQTRHMRIH
TGEKPHACDF PGCVKRFSRS DELTRHRRIH TNSHPRGKRG RKKKVVGSPI NSASSSATSI
PDLNTANFSP PLPQQHLSPL IPIAIAPKEN SSRSSTRKGR KTKFEIGESG GNDPYMVSSP
KTMAKIPVSV KPPPSLALNN MNYQTSSAST ALSSLSNSHS GSRLKLNALS SLQMMTPIAS
SAPRTVFIDG PEQKQLQQQQ NSLSPRYSNT VILPRPRSLT DFQGLNNANP NNNGSLRAQT
QSSVQLKRPS SVLSLNDLLV GQRNTNESDS DFTTGGEDEE DGLKDPSNSS IDNLEQDYLQ
EQSRKKSKTS TPTTMLSRST SGTNLHTLGY VMNQNHLHFS SSSPDFQKEL NNRLLNVQQQ
QQEQHTLLQS QNTSNQSQNQ NQNQMMASSS SLSTTPLLLS PRVNMINTAI STQQTPISQS
DSQVQELETL PPIRSLPLPF PHMD


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