ID SNF1_YEAST Reviewed; 633 AA. AC P06782; D6VTA0; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 09-DEC-2015, entry version 179. DE RecName: Full=Carbon catabolite-derepressing protein kinase; DE EC=2.7.11.1; GN Name=SNF1; Synonyms=CAT1, CCR1, GLC2, PAS14; GN OrderedLocusNames=YDR477W; ORFNames=D8035.20; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3526554; DOI=10.1126/science.3526554; RA Celenza J.L., Carlson M.; RT "A yeast gene that is essential for release from glucose repression RT encodes a protein kinase."; RL Science 233:1175-1180(1986). 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., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP PROTEIN SEQUENCE OF 274-284; 528-539 AND 622-630, AND PHOSPHORYLATION RP AT THR-210. RX PubMed=7905477; RA Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., RA Katsis F., Witters L.A., Kemp B.E.; RT "Mammalian AMP-activated protein kinase shares structural and RT functional homology with the catalytic domain of yeast Snf1 protein RT kinase."; RL J. Biol. Chem. 269:2361-2364(1994). RN [5] RP PHOSPHORYLATION AT THR-210, AND INTERACTION WITH SAK1. RX PubMed=12748292; DOI=10.1128/MCB.23.11.3909-3917.2003; RA Nath N., McCartney R.R., Schmidt M.C.; RT "Yeast Pak1 kinase associates with and activates Snf1."; RL Mol. Cell. Biol. 23:3909-3917(2003). 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., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3. RX PubMed=15719021; DOI=10.1038/sj.emboj.7600577; RA Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.; RT "Histone H3 phosphorylation can promote TBP recruitment through RT distinct promoter-specific mechanisms."; RL EMBO J. 24:997-1008(2005). RN [8] RP INTERACTION WITH CTK1. RX PubMed=16182287; DOI=10.1016/j.febslet.2005.08.057; RA Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J.; RT "Glucose deprivation mediates interaction between CTDK-I and Snf1 in RT Saccharomyces cerevisiae."; RL FEBS Lett. 579:5318-5324(2005). RN [9] RP PHOSPHORYLATION, AND INTERACTION WITH SAK1. RX PubMed=16847059; DOI=10.1074/jbc.M603811200; RA Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C.; RT "Subunits of the Snf1 kinase heterotrimer show interdependence for RT association and activity."; RL J. Biol. Chem. 281:26170-26180(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION RP BY MASS 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-487, AND 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-632, 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 RT insights into evolution."; RL Science 325:1682-1686(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). CC -!- FUNCTION: Essential for release from glucose repression. It CC interacts and has functional relationship to the regulatory CC protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 CC to form H3S10ph, which promotes H3K14ac formation, and which is CC required for transcriptional activation through TBP recruitment to CC the promoters. {ECO:0000269|PubMed:15719021}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with CTK1, GAL83, SAK1, SIP1, SIP2 and SNF4. CC {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:16182287, CC ECO:0000269|PubMed:16847059}. CC -!- INTERACTION: CC Q00684:CDC14; NbExp=2; IntAct=EBI-17516, EBI-4192; CC Q04739:GAL83; NbExp=5; IntAct=EBI-17516, EBI-7244; CC P22211:NPR1; NbExp=2; IntAct=EBI-17516, EBI-12207; CC Q00816:REG1; NbExp=3; IntAct=EBI-17516, EBI-8270; CC P34164:SIP2; NbExp=9; IntAct=EBI-17516, EBI-17187; CC P12904:SNF4; NbExp=16; IntAct=EBI-17516, EBI-17537; CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane CC protein. CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13971; AAA35058.1; -; Genomic_DNA. DR EMBL; U33050; AAB64904.1; -; Genomic_DNA. DR EMBL; BK006938; DAA12310.1; -; Genomic_DNA. DR PIR; A26030; A26030. DR RefSeq; NP_010765.3; NM_001180785.3. DR PDB; 2FH9; X-ray; 2.80 A; A=46-319. DR PDB; 2QLV; X-ray; 2.60 A; A/D=460-630. DR PDB; 3DAE; X-ray; 2.90 A; A/B=41-315. DR PDB; 3HYH; X-ray; 2.20 A; A/B=41-315. DR PDB; 3MN3; X-ray; 2.38 A; A=50-320. DR PDB; 3T4N; X-ray; 2.30 A; A=457-633. DR PDB; 3TDH; X-ray; 2.30 A; A=457-633. DR PDB; 3TE5; X-ray; 2.50 A; A=457-633. DR PDBsum; 2FH9; -. DR PDBsum; 2QLV; -. DR PDBsum; 3DAE; -. DR PDBsum; 3HYH; -. DR PDBsum; 3MN3; -. DR PDBsum; 3T4N; -. DR PDBsum; 3TDH; -. DR PDBsum; 3TE5; -. DR ProteinModelPortal; P06782; -. DR SMR; P06782; 18-630. DR BioGrid; 32529; 449. DR DIP; DIP-18N; -. DR IntAct; P06782; 25. DR MINT; MINT-364314; -. DR MaxQB; P06782; -. DR PeptideAtlas; P06782; -. DR EnsemblFungi; YDR477W; YDR477W; YDR477W. DR GeneID; 852088; -. DR KEGG; sce:YDR477W; -. DR EuPathDB; FungiDB:YDR477W; -. DR SGD; S000002885; SNF1. DR GeneTree; ENSGT00790000122947; -. DR HOGENOM; HOG000233016; -. DR InParanoid; P06782; -. DR KO; K12761; -. DR OMA; TMGYDRD; -. DR OrthoDB; EOG793BK1; -. DR BioCyc; YEAST:G3O-30003-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR Reactome; R-SCE-1257604; PIP3 activates AKT signaling. DR Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity. DR Reactome; R-SCE-165158; Activation of AKT2. DR Reactome; R-SCE-199418; Negative regulation of the PI3K/AKT network. DR Reactome; R-SCE-200425; Import of palmitoyl-CoA into the mitochondrial matrix. DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability. DR EvolutionaryTrace; P06782; -. DR NextBio; 970409; -. DR PRO; PR:P06782; -. DR Proteomes; UP000002311; Chromosome IV. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0000324; C:fungal-type vacuole; IPI:SGD. DR GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IMP:SGD. DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IMP:SGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IDA:SGD. DR GO; GO:0071940; P:fungal-type cell wall assembly; IMP:SGD. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD. DR GO; GO:0017148; P:negative regulation of translation; IMP:SGD. DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:SGD. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:SGD. DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:GOC. DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD. DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD. DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD. DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IGI:SGD. DR GO; GO:0001302; P:replicative cell aging; IMP:SGD. DR GO; GO:0006986; P:response to unfolded protein; IMP:SGD. DR GO; GO:0090606; P:single-species surface biofilm formation; IMP:SGD. DR InterPro; IPR032270; AMPK_C. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR013896; Ubiquitin-assoc_dom. DR Pfam; PF16579; AdenylateSensor; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08587; UBA_2; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF103243; SSF103243; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Carbohydrate metabolism; Complete proteome; KW Direct protein sequencing; Kinase; Membrane; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 633 Carbon catabolite-derepressing protein FT kinase. FT /FTId=PRO_0000086670. FT DOMAIN 55 306 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 61 69 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT COMPBIAS 18 32 Poly-His. FT ACT_SITE 177 177 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 84 84 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 210 210 Phosphothreonine; by autocatalysis. FT {ECO:0000269|PubMed:12748292, FT ECO:0000269|PubMed:7905477}. FT MOD_RES 413 413 Phosphoserine. FT {ECO:0000244|PubMed:17330950, FT ECO:0000244|PubMed:18407956, FT ECO:0000244|PubMed:19779198}. FT MOD_RES 487 487 Phosphoserine. FT {ECO:0000244|PubMed:18407956}. FT MOD_RES 632 632 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT STRAND 56 62 {ECO:0000244|PDB:3HYH}. FT HELIX 64 66 {ECO:0000244|PDB:3MN3}. FT STRAND 69 73 {ECO:0000244|PDB:3HYH}. FT TURN 75 77 {ECO:0000244|PDB:3HYH}. FT STRAND 80 87 {ECO:0000244|PDB:3HYH}. FT HELIX 88 91 {ECO:0000244|PDB:3DAE}. FT HELIX 97 109 {ECO:0000244|PDB:3HYH}. FT STRAND 118 123 {ECO:0000244|PDB:3HYH}. FT STRAND 125 133 {ECO:0000244|PDB:3HYH}. FT HELIX 139 145 {ECO:0000244|PDB:3HYH}. FT HELIX 151 170 {ECO:0000244|PDB:3HYH}. FT TURN 180 182 {ECO:0000244|PDB:3HYH}. FT STRAND 183 185 {ECO:0000244|PDB:3HYH}. FT STRAND 191 193 {ECO:0000244|PDB:3HYH}. FT TURN 207 209 {ECO:0000244|PDB:3MN3}. FT HELIX 215 217 {ECO:0000244|PDB:3MN3}. FT HELIX 220 223 {ECO:0000244|PDB:3HYH}. FT STRAND 224 227 {ECO:0000244|PDB:3HYH}. FT HELIX 232 247 {ECO:0000244|PDB:3HYH}. FT HELIX 257 266 {ECO:0000244|PDB:3HYH}. FT HELIX 277 286 {ECO:0000244|PDB:3HYH}. FT HELIX 291 293 {ECO:0000244|PDB:3HYH}. FT HELIX 297 302 {ECO:0000244|PDB:3HYH}. FT HELIX 304 307 {ECO:0000244|PDB:3HYH}. FT HELIX 312 314 {ECO:0000244|PDB:3HYH}. FT TURN 317 319 {ECO:0000244|PDB:3MN3}. FT HELIX 471 473 {ECO:0000244|PDB:3T4N}. FT HELIX 475 485 {ECO:0000244|PDB:3T4N}. FT HELIX 489 492 {ECO:0000244|PDB:3T4N}. FT STRAND 506 511 {ECO:0000244|PDB:3T4N}. FT HELIX 515 529 {ECO:0000244|PDB:3T4N}. FT STRAND 532 534 {ECO:0000244|PDB:3T4N}. FT HELIX 538 540 {ECO:0000244|PDB:3T4N}. FT STRAND 543 548 {ECO:0000244|PDB:3T4N}. FT STRAND 565 576 {ECO:0000244|PDB:3T4N}. FT STRAND 579 590 {ECO:0000244|PDB:3T4N}. FT HELIX 607 610 {ECO:0000244|PDB:2QLV}. FT HELIX 613 628 {ECO:0000244|PDB:3T4N}. SQ SEQUENCE 633 AA; 72045 MW; F5C63565C986C4E3 CRC64; MSSNNNTNTA PANANSSHHH HHHHHHHHHH GHGGSNSTLN NPKSSLADGA HIGNYQIVKT LGEGSFGKVK LAYHTTTGQK VALKIINKKV LAKSDMQGRI EREISYLRLL RHPHIIKLYD VIKSKDEIIM VIEYAGNELF DYIVQRDKMS EQEARRFFQQ IISAVEYCHR HKIVHRDLKP ENLLLDEHLN VKIADFGLSN IMTDGNFLKT SCGSPNYAAP EVISGKLYAG PEVDVWSCGV ILYVMLCRRL PFDDESIPVL FKNISNGVYT LPKFLSPGAA GLIKRMLIVN PLNRISIHEI MQDDWFKVDL PEYLLPPDLK PHPEEENENN DSKKDGSSPD NDEIDDNLVN ILSSTMGYEK DEIYESLESS EDTPAFNEIR DAYMLIKENK SLIKDMKANK SVSDELDTFL SQSPPTFQQQ SKSHQKSQVD HETAKQHARR MASAITQQRT YHQSPFMDQY KEEDSTVSIL PTSLPQIHRA NMLAQGSPAA SKISPLVTKK SKTRWHFGIR SRSYPLDVMG EIYIALKNLG AEWAKPSEED LWTIKLRWKY DIGNKTNTNE KIPDLMKMVI QLFQIETNNY LVDFKFDGWE SSYGDDTTVS NISEDEMSTF SAYPFLHLTT KLIMELAVNS QSN //