SIP1_YEAST
ID SIP1_YEAST Reviewed; 815 AA.
AC P32578; D6VT52;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=SNF1 protein kinase subunit beta-1;
DE AltName: Full=SNF1-interacting protein 1;
GN Name=SIP1; OrderedLocusNames=YDR422C; ORFNames=D9461.11;
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], INTERACTION WITH SNF1, AND
RP PHOSPHORYLATION.
RX PubMed=1496382; DOI=10.1126/science.1496382;
RA Yang X., Hubbard E.J.A., Carlson M.;
RT "A protein kinase substrate identified by the two-hybrid system.";
RL Science 257:680-682(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP INTERACTION WITH SNF1, AND PHOSPHORYLATION.
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 [5]
RP FUNCTION.
RX PubMed=8088514; DOI=10.1093/genetics/137.3.689;
RA Mylin L.M., Bushman V.L., Long R.M., Yu X., Lebo C.M., Blank T.E.,
RA Hopper J.E.;
RT "SIP1 is a catabolite repression-specific negative regulator of GAL gene
RT expression.";
RL Genetics 137:689-700(1994).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=7785324; DOI=10.1002/yea.320110306;
RA Long R.M., Hopper J.E.;
RT "Genetic and carbon source regulation of phosphorylation of Sip1p, a Snf1p-
RT associated protein involved in carbon response in Saccharomyces
RT cerevisiae.";
RL Yeast 11:233-246(1995).
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.
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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 OF INITIATION SITE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-2.
RX PubMed=14966266; DOI=10.1128/mcb.24.5.1836-1843.2004;
RA Hedbacker K., Townley R., Carlson M.;
RT "Cyclic AMP-dependent protein kinase regulates the subcellular localization
RT of Snf1-Sip1 protein kinase.";
RL Mol. Cell. Biol. 24:1836-1843(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-200; SER-220;
RP SER-331; SER-494; SER-497 AND SER-643, AND IDENTIFICATION BY MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-181; SER-198;
RP SER-206; SER-209; SER-220; SER-331; SER-494; SER-497 AND SER-643, 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).
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. Promotes the PKA-regulated relocalization of the SNF1
CC kinase complex to the vacuolar membrane in response to various types of
CC carbon stress. {ECO:0000269|PubMed:10990457,
CC ECO:0000269|PubMed:8088514}.
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:1496382, ECO:0000269|PubMed:7813428,
CC ECO:0000269|PubMed:9121458}.
CC -!- INTERACTION:
CC P32578; P12904: SNF4; NbExp=4; IntAct=EBI-17179, EBI-17537;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331606,
CC ECO:0000269|PubMed:14966266}. Vacuole membrane
CC {ECO:0000269|PubMed:11331606, ECO:0000269|PubMed:14966266}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11331606,
CC ECO:0000269|PubMed:14966266}; Cytoplasmic side
CC {ECO:0000269|PubMed:11331606, ECO:0000269|PubMed:14966266}.
CC Note=Resides in the cytosol during growth in glucose and relocalizes to
CC the vacuolar membrane in response to carbon stress.
CC {ECO:0000269|PubMed:14966266}.
CC -!- PTM: Phosphorylated by SNF1 in vitro. {ECO:0000269|PubMed:1496382,
CC ECO:0000269|PubMed:7785324, ECO:0000269|PubMed:7813428}.
CC -!- MISCELLANEOUS: Present with 623 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35045.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB64887.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M90531; AAA35045.1; ALT_INIT; Genomic_DNA.
DR EMBL; U33007; AAB64887.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA12262.1; -; Genomic_DNA.
DR PIR; S41984; S41984.
DR RefSeq; NP_010710.4; NM_001180730.3.
DR AlphaFoldDB; P32578; -.
DR BioGRID; 32481; 110.
DR ComplexPortal; CPX-232; Snf1 protein kinase complex variant SIP1.
DR DIP; DIP-777N; -.
DR IntAct; P32578; 11.
DR MINT; P32578; -.
DR STRING; 4932.YDR422C; -.
DR iPTMnet; P32578; -.
DR MaxQB; P32578; -.
DR PaxDb; P32578; -.
DR PRIDE; P32578; -.
DR EnsemblFungi; YDR422C_mRNA; YDR422C; YDR422C.
DR GeneID; 852032; -.
DR KEGG; sce:YDR422C; -.
DR SGD; S000002830; SIP1.
DR VEuPathDB; FungiDB:YDR422C; -.
DR eggNOG; KOG1616; Eukaryota.
DR HOGENOM; CLU_011585_0_0_1; -.
DR InParanoid; P32578; -.
DR OMA; VVDCNQD; -.
DR BioCyc; YEAST:G3O-29963-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 PRO; PR:P32578; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32578; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; 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:0005774; C:vacuolar membrane; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IGI:SGD.
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; IPR030073; Sip1.
DR PANTHER; PTHR10343:SF87; PTHR10343:SF87; 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 Cytoplasm; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..815
FT /note="SNF1 protein kinase subunit beta-1"
FT /id="PRO_0000204374"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..716
FT /note="Kinase-interacting sequence (KIS); required for
FT interaction with SNF1"
FT REGION 581..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..804
FT /note="Association with SNF1 kinase complex (ASC) domain;
FT required for interaction with SNF4"
FT /evidence="ECO:0000269|PubMed:9121458"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT MUTAGEN 2
FT /note="G->A: Prevents relocalization to the vacuolar
FT membrane."
FT /evidence="ECO:0000269|PubMed:14966266"
SQ SEQUENCE 815 AA; 91071 MW; E198E6DD57B74FD5 CRC64;
MGNSPSTQDP SHSTKKEHGH HFHDAFNKDR QGSITSQLFN NRKSTHKRRA SHTSEHNGAI
PPRMQLLASH DPSTDCDGRM SSDTTIDKGP SHLFKKDYSL SSAADVNDTT LANLTLSDDH
DVGAPEEQVK SPSFLSPGPS MATVKRTKSD LDDLSTLNYT MVDETTENER NDKPHHERHR
SSIIALKKNL LESSATASPS PTRSSSVHSA SLPALTKTDS IDIPVRQPYS KKPSIHAYQY
QYLNNDETFS ENSQMDKEGN SDSVDAEAGV LQSEDMVLNQ SLLQNALKKD MQRLSRVNSS
NSMYTAERIS HANNNGNIEN NTRNKGNAGG SNDDFTAPIS ATAKMMMKLY GDKTLMERDL
NKHHNKTKKA QNKKIRSVSN SRRSSFASLH SLQSRKSILT NGLNLQPLHP LHPIINDNES
QYSAPQHREI SHHSNSMSSM SSISSTNSTE NTLVVLKWKD DGTVAATTEV FIVSTDIASA
LKEQRELTLD ENASLDSEKQ LNPRIRMVYD DVHKEWFVPD LFLPAGIYRL QFSINGILTH
SNFLPTATDS EGNFVNWFEV LPGYHTIEPF RNEADIDSQV EPTLDEELPK RPELKRFPSS
SRKSSYYSAK GVERPSTPFS DYRGLSRSSS INMRDSFVRL KASSLDLMAE VKPERLVYSN
EIPNLFNIGD GSTISVKGDS DDVHPQEPPS FTHRVVDCNQ DDLFATLQQG GNIDAETAEA
VFLSRYPVPD LPIYLNSSYL NRILNQSNQN SESHERDEGA INHIIPHVNL NHLLTSSIRD
EIISVACTTR YEGKFITQVV YAPCYYKTQK SQISN
