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SNF1 protein kinase subunit beta-3 (Glucose repression protein GAL83) (Protein SPM1)

 GAL83_YEAST             Reviewed;         417 AA.
Q04739; D3DLS6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
22-NOV-2017, entry version 143.
RecName: Full=SNF1 protein kinase subunit beta-3;
AltName: Full=Glucose repression protein GAL83;
AltName: Full=Protein SPM1;
Name=GAL83; Synonyms=SPM1; OrderedLocusNames=YER027C;
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 204511 / S288c / AB972;
PubMed=8293971;
Erickson J.R., Johnston M.;
"Genetic and molecular characterization of GAL83: its interaction and
similarities with other genes involved in glucose repression in
Saccharomyces cerevisiae.";
Genetics 135:655-664(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Drebot M.A., Jansma D., Himmelfarb H.J., Friesen J.D.;
"Dominant, pleiotropic gain-of-function suppressors of temperature-
sensitive alleles of the Saccharomyces cerevisiae RPO21 gene.";
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(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]
INTERACTION WITH SNF1, AND PHOSPHORYLATION.
PubMed=7813428;
Yang X., Jiang R., Carlson M.;
"A family of proteins containing a conserved domain that mediates
interaction with the yeast SNF1 protein kinase complex.";
EMBO J. 13:5878-5886(1994).
[7]
INTERACTION WITH SNF1 AND SNF4.
PubMed=9121458; DOI=10.1128/MCB.17.4.2099;
Jiang R., Carlson M.;
"The Snf1 protein kinase and its activating subunit, Snf4, interact
with distinct domains of the Sip1/Sip2/Gal83 component in the kinase
complex.";
Mol. Cell. Biol. 17:2099-2106(1997).
[8]
FUNCTION.
PubMed=10990457; DOI=10.1093/emboj/19.18.4936;
Schmidt M.C., McCartney R.R.;
"beta-subunits of Snf1 kinase are required for kinase function and
substrate definition.";
EMBO J. 19:4936-4943(2000).
[9]
SUBCELLULAR LOCATION.
PubMed=11331606; DOI=10.1101/gad.879301;
Vincent O., Townley R., Kuchin S., Carlson M.;
"Subcellular localization of the Snf1 kinase is regulated by specific
beta subunits and a novel glucose signaling mechanism.";
Genes Dev. 15:1104-1114(2001).
[10]
IDENTIFICATION IN SNF1 KINASE COMPLEX.
PubMed=12393914; DOI=10.1074/jbc.M207058200;
Nath N., McCartney R.R., Schmidt M.C.;
"Purification and characterization of Snf1 kinase complexes containing
a defined beta subunit composition.";
J. Biol. Chem. 277:50403-50408(2002).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-279, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[14]
INTERACTION WITH REE1.
PubMed=18851946; DOI=10.1016/j.bbrc.2008.09.146;
Choi I.D., Jeong M.Y., Ham M.S., Sung H.C., Yun C.W.;
"Novel Ree1 regulates the expression of ENO1 via the Snf1 complex
pathway in Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 377:395-399(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-44, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-21 AND SER-135,
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: Beta subunit of the SNF1 kinase complex, which is
required for transcriptional, metabolic, and developmental
adaptations in response to glucose limitation. Has a structural
role, mediating heterotrimer formation, and a regulatory role,
defining carbon source-regulated subcellular location and
substrate specificity of the SNF1 kinase complex. Promotes the
relocalization of the SNF1 kinase complex to the nucleus upon
shift to nonfermentable carbon sources.
{ECO:0000269|PubMed:10990457}.
-!- SUBUNIT: Component of the SNF1 kinase complex, a heterotrimeric
complex composed of the catalytic alpha subunit SNF1, one of the
three related beta subunits SIP1, SIP2 or GAL83, and the
regulatory gamma subunit SNF4. The beta subunit serves as a bridge
between the catalytic and the regulatory subunit. Interacts (via
KIS domain) with SNF1. Interacts (via ASC domain) with SNF4.
Interacts with REE1. {ECO:0000269|PubMed:12393914,
ECO:0000269|PubMed:18851946, ECO:0000269|PubMed:7813428,
ECO:0000269|PubMed:9121458}.
-!- INTERACTION:
P06782:SNF1; NbExp=5; IntAct=EBI-7244, EBI-17516;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331606}.
Nucleus {ECO:0000269|PubMed:11331606}. Note=Resides in the cytosol
during growth on fermentable carbon sources and relocalizes
rapidly to the nucleus in response to carbon stress.
{ECO:0000269|PubMed:11331606}.
-!- PTM: Phosphorylated by SNF1 in vitro.
{ECO:0000269|PubMed:7813428}.
-!- MISCELLANEOUS: Present with 3590 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta
subunit family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X72893; CAA51411.1; -; Genomic_DNA.
EMBL; L13599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z14127; CAA78501.1; -; Genomic_DNA.
EMBL; U18778; AAB64560.1; -; Genomic_DNA.
EMBL; AY692771; AAT92790.1; -; Genomic_DNA.
EMBL; BK006939; DAA07680.1; -; Genomic_DNA.
PIR; S52591; S52591.
RefSeq; NP_010944.1; NM_001178918.1.
ProteinModelPortal; Q04739; -.
SMR; Q04739; -.
BioGrid; 36762; 71.
DIP; DIP-1298N; -.
IntAct; Q04739; 9.
MINT; MINT-394443; -.
STRING; 4932.YER027C; -.
CAZy; CBM48; Carbohydrate-Binding Module Family 48.
iPTMnet; Q04739; -.
MaxQB; Q04739; -.
PRIDE; Q04739; -.
EnsemblFungi; YER027C; YER027C; YER027C.
GeneID; 856749; -.
KEGG; sce:YER027C; -.
EuPathDB; FungiDB:YER027C; -.
SGD; S000000829; GAL83.
GeneTree; ENSGT00390000001416; -.
HOGENOM; HOG000093748; -.
InParanoid; Q04739; -.
OMA; WGLTNDD; -.
OrthoDB; EOG092C4NLT; -.
BioCyc; YEAST:G3O-30208-MONOMER; -.
Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-SCE-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
PRO; PR:Q04739; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0007155; P:cell adhesion; IMP:SGD.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
GO; GO:2000222; P:positive regulation of pseudohyphal growth; IGI:SGD.
GO; GO:0006468; P:protein phosphorylation; IMP:SGD.
GO; GO:0043254; P:regulation of protein complex assembly; IGI:SGD.
GO; GO:0045859; P:regulation of protein kinase activity; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IGI:SGD.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR032640; AMPK1_CBM.
InterPro; IPR006828; ASC_dom.
InterPro; IPR037256; ASC_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR030077; SIP2/GAL83.
PANTHER; PTHR10343:SF45; PTHR10343:SF45; 1.
Pfam; PF16561; AMPK1_CBM; 1.
Pfam; PF04739; AMPKBI; 1.
SMART; SM01010; AMPKBI; 1.
SUPFAM; SSF160219; SSF160219; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 417 SNF1 protein kinase subunit beta-3.
/FTId=PRO_0000204373.
REGION 152 342 Kinase-interacting sequence (KIS);
required for interaction with SNF1.
REGION 343 417 Association with SNF1 kinase complex
(ASC) domain; required for interaction
with SNF4. {ECO:0000269|PubMed:9121458}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
SEQUENCE 417 AA; 46648 MW; E7BDAC821C1E049A CRC64;
MAGDNPENKD ASMLDVSDAA SNTTINGKHS ADSTNEASLA YTFSQMNVDN PNELEPQHPL
RHKSSLIFND DDDDEIPPYS NHAENGSGET FDSDDDIDAS SSSSIDSNEG DIHDADMTGN
TLQKMDYQPS QQPDSLQNQG FQQQQEQQQG TVEGKKGRAM MFPVDITWQQ GGNKVYVTGS
FTGWRKMIGL VPVPGQPGLM HVKLQLPPGT HRFRFIVDNE LRFSDYLPTA TDQMGNFVNY
MEVSAPPDWG NEPQQHLAEK KANHVDDSKL SKRPMSARSR IALEIEKEPD DMGDGYTRFH
DETPAKPNLE YTQDIPAVFT DPNVMEQYYL TLDQQQNNHQ NMAWLTPPQL PPHLENVILN
SYSNAQTDNT SGALPIPNHV ILNHLATSSI KHNTLCVASI VRYKQKYVTQ ILYTPLQ


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