SIP2_YEAST
ID SIP2_YEAST Reviewed; 415 AA.
AC P34164; D6VTU7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=SNF1 protein kinase subunit beta-2;
DE AltName: Full=Protein SPM2;
DE AltName: Full=SNF1-interacting protein 2;
GN Name=SIP2; Synonyms=SPM2; OrderedLocusNames=YGL208W; ORFNames=G1155;
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].
RA Drebot M.A., Jansma D., Himmelfarb H.J., Friesen J.D.;
RT "Suppressors of yeast RNA polymerase II mutations belong to a family of
RT gene products that interact with a protein kinase.";
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH SNF1, AND
RP PHOSPHORYLATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813428; DOI=10.1002/j.1460-2075.1994.tb06933.x;
RA Yang X., Jiang R., Carlson M.;
RT "A family of proteins containing a conserved domain that mediates
RT interaction with the yeast SNF1 protein kinase complex.";
RL EMBO J. 13:5878-5886(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9153757;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0;
RA Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
RT "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
RT reveals 11 open reading frames: two correspond to new genes.";
RL Yeast 13:475-477(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-284.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8813766;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<799::aid-yea965>3.0.co;2-u;
RA Kail M., Juettner E., Vaux D.;
RT "Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces
RT cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and
RT containing three novel transcribed open reading frames.";
RL Yeast 12:799-807(1996).
RN [7]
RP INTERACTION WITH SNF1 AND SNF4.
RX PubMed=9121458; DOI=10.1128/mcb.17.4.2099;
RA Jiang R., Carlson M.;
RT "The Snf1 protein kinase and its activating subunit, Snf4, interact with
RT distinct domains of the Sip1/Sip2/Gal83 component in the kinase complex.";
RL Mol. Cell. Biol. 17:2099-2106(1997).
RN [8]
RP FUNCTION.
RX PubMed=10990457; DOI=10.1093/emboj/19.18.4936;
RA Schmidt M.C., McCartney R.R.;
RT "beta-subunits of Snf1 kinase are required for kinase function and
RT substrate definition.";
RL EMBO J. 19:4936-4943(2000).
RN [9]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11331606; DOI=10.1101/gad.879301;
RA Vincent O., Townley R., Kuchin S., Carlson M.;
RT "Subcellular localization of the Snf1 kinase is regulated by specific beta
RT subunits and a novel glucose signaling mechanism.";
RL Genes Dev. 15:1104-1114(2001).
RN [10]
RP IDENTIFICATION IN SNF1 KINASE COMPLEX.
RX PubMed=12393914; DOI=10.1074/jbc.m207058200;
RA Nath N., McCartney R.R., Schmidt M.C.;
RT "Purification and characterization of Snf1 kinase complexes containing a
RT defined beta subunit composition.";
RL J. Biol. Chem. 277:50403-50408(2002).
RN [11]
RP FUNCTION, MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-2.
RX PubMed=12562756; DOI=10.1074/jbc.m212818200;
RA Lin S.S., Manchester J.K., Gordon J.I.;
RT "Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in
RT Saccharomyces cerevisiae by affecting cellular histone kinase activity,
RT recombination at rDNA loci, and silencing.";
RL J. Biol. Chem. 278:13390-13397(2003).
RN [12]
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 [13]
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-298, AND
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 161-412 IN COMPLEX WITH SNF1 AND
RP SNF4.
RX PubMed=17851534; DOI=10.1038/nature06127;
RA Amodeo G.A., Rudolph M.J., Tong L.;
RT "Crystal structure of the heterotrimer core of Saccharomyces cerevisiae
RT AMPK homologue SNF1.";
RL Nature 449:492-495(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 304-415 IN COMPLEX WITH SNF1 AND
RP SNF4.
RX PubMed=22019086; DOI=10.1016/j.cmet.2011.09.009;
RA Mayer F.V., Heath R., Underwood E., Sanders M.J., Carmena D.,
RA McCartney R.R., Leiper F.C., Xiao B., Jing C., Walker P.A., Haire L.F.,
RA Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J., Carling D.;
RT "ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-activated
RT protein kinase.";
RL Cell Metab. 14:707-714(2011).
CC -!- FUNCTION: Beta subunit of the SNF1 kinase complex, which is required
CC for transcriptional, metabolic, and developmental adaptations in
CC response to glucose limitation. Has a structural role, mediating
CC heterotrimer formation, and a regulatory role, defining carbon source-
CC regulated subcellular location and substrate specificity of the SNF1
CC kinase complex. Involved in the regulation of aging. Acts as a negative
CC regulator of nuclear SNF1 activity in young cells by sequestering its
CC activating gamma subunit at the plasma membrane.
CC {ECO:0000269|PubMed:10990457, ECO:0000269|PubMed:12562756}.
CC -!- SUBUNIT: Component of the SNF1 kinase complex, a heterotrimeric complex
CC composed of the catalytic alpha subunit SNF1, one of the three related
CC beta subunits SIP1, SIP2 or GAL83, and the regulatory gamma subunit
CC SNF4. The beta subunit serves as a bridge between the catalytic and the
CC regulatory subunit. Interacts (via KIS domain) with SNF1. Interacts
CC (via ASC domain) with SNF4. {ECO:0000269|PubMed:12393914,
CC ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:22019086,
CC ECO:0000269|PubMed:7813428, ECO:0000269|PubMed:9121458}.
CC -!- INTERACTION:
CC P34164; P06782: SNF1; NbExp=11; IntAct=EBI-17187, EBI-17516;
CC P34164; P12904: SNF4; NbExp=9; IntAct=EBI-17187, EBI-17537;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331606}. Cell
CC membrane {ECO:0000269|PubMed:12562756}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12562756}; Cytoplasmic side
CC {ECO:0000269|PubMed:12562756}. Note=Resides in the cytosol during
CC growth in glucose. Excluded from the nucleus. There is an age-
CC associated shift in localization from the plasma membrane to the
CC cytoplasm. {ECO:0000269|PubMed:12562756}.
CC -!- INDUCTION: Induced upon shift to nonfermentable carbon sources.
CC {ECO:0000269|PubMed:11331606}.
CC -!- PTM: Phosphorylated by SNF1 in vitro. {ECO:0000269|PubMed:7813428}.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; Z14128; CAA78503.1; -; Genomic_DNA.
DR EMBL; L31592; AAC37420.1; -; Genomic_DNA.
DR EMBL; Z72730; CAA96922.1; -; Genomic_DNA.
DR EMBL; U33754; AAC49497.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07908.1; -; Genomic_DNA.
DR PIR; S51792; S51792.
DR RefSeq; NP_011307.1; NM_001181073.2.
DR PDB; 2QLV; X-ray; 2.60 A; B/E=161-412.
DR PDB; 3T4N; X-ray; 2.30 A; B=304-415.
DR PDB; 3TDH; X-ray; 2.30 A; B=304-415.
DR PDB; 3TE5; X-ray; 2.50 A; B=304-415.
DR PDBsum; 2QLV; -.
DR PDBsum; 3T4N; -.
DR PDBsum; 3TDH; -.
DR PDBsum; 3TE5; -.
DR AlphaFoldDB; P34164; -.
DR SMR; P34164; -.
DR BioGRID; 33048; 161.
DR ComplexPortal; CPX-2800; Snf1 protein kinase complex variant SIP2.
DR DIP; DIP-865N; -.
DR IntAct; P34164; 39.
DR MINT; P34164; -.
DR STRING; 4932.YGL208W; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; P34164; -.
DR MaxQB; P34164; -.
DR PaxDb; P34164; -.
DR PRIDE; P34164; -.
DR EnsemblFungi; YGL208W_mRNA; YGL208W; YGL208W.
DR GeneID; 852664; -.
DR KEGG; sce:YGL208W; -.
DR SGD; S000003176; SIP2.
DR VEuPathDB; FungiDB:YGL208W; -.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000176367; -.
DR HOGENOM; CLU_033562_1_0_1; -.
DR InParanoid; P34164; -.
DR OMA; TRFHEDL; -.
DR BioCyc; YEAST:G3O-30685-MON; -.
DR BRENDA; 2.7.11.31; 984.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-SCE-200425; Carnitine metabolism.
DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR EvolutionaryTrace; P34164; -.
DR PRO; PR:P34164; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P34164; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR GO; GO:0030447; P:filamentous growth; IMP:ComplexPortal.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IGI:SGD.
DR GO; GO:1904547; P:regulation of cellular response to glucose starvation; EXP:ComplexPortal.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:InterPro.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IGI:SGD.
DR GO; GO:0007165; P:signal transduction; IGI:SGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR030077; SIP2/GAL83.
DR PANTHER; PTHR10343:SF84; PTHR10343:SF84; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF04739; AMPKBI; 1.
DR SMART; SM01010; AMPKBI; 1.
DR SUPFAM; SSF160219; SSF160219; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..415
FT /note="SNF1 protein kinase subunit beta-2"
FT /id="PRO_0000204375"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..335
FT /note="Kinase-interacting sequence (KIS); required for
FT interaction with SNF1"
FT REGION 249..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..415
FT /note="Association with SNF1 kinase complex (ASC) domain;
FT required for interaction with SNF4"
FT /evidence="ECO:0000269|PubMed:9121458"
FT COMPBIAS 55..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12562756"
FT MUTAGEN 2
FT /note="G->A: Changes protein distribution from the plasma
FT membrane to the cytoplasm and nucleus and alters the
FT cellular life span."
FT /evidence="ECO:0000269|PubMed:12562756"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2QLV"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:2QLV"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 349..365
FT /evidence="ECO:0007829|PDB:3T4N"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3T4N"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:3TDH"
FT STRAND 390..399
FT /evidence="ECO:0007829|PDB:3T4N"
FT STRAND 402..411
FT /evidence="ECO:0007829|PDB:3T4N"
SQ SEQUENCE 415 AA; 46405 MW; CBB4FCE0070A563F CRC64;
MGTTTSHPAQ KKQTTKKCRA PIMSDVREKP SNAQGCEPQE MDAVSKKVTE LSLNKCSDSQ
DAGQPSREGS ITKKKSTLLL RDEDEPTMPK LSVMETAVDT DSGSSSTSDD EEGDIIAQTT
EPKQDASPDD DRSGHSSPRE EGQQQIRAKE ASGGPSEIKS SLMVPVEIRW QQGGSKVYVT
GSFTKWRKMI GLIPDSDNNG SFHVKLRLLP GTHRFRFIVD NELRVSDFLP TATDQMGNFV
NYIEVRQPEK NPTNEKIRSK EADSMRPPTS DRSSIALQIG KDPDDFGDGY TRFHEDLSPR
PPLEYTTDIP AVFTDPSVME RYYYTLDRQQ SNTDTSWLTP PQLPPQLENV ILNKYYATQD
QFNENNSGAL PIPNHVVLNH LVTSSIKHNT LCVASIVRYK QKYVTQILYT PIESS
