ID SNF1_YEAST Reviewed; 633 AA. AC P06782; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 02-OCT-2007, entry version 91. DE Carbon catabolite-derepressing protein kinase (EC 2.7.11.1). GN Name=SNF1; Synonyms=CAT1, CCR1, GLC2, PAS14; GN OrderedLocusNames=YDR477W; ORFNames=D8035.20; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86289463; PubMed=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 MEDLINE=97313263; 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 PROTEIN SEQUENCE OF 274-284; 528-539 AND 622-630, AND PHOSPHORYLATION RP AT THR-210. RX MEDLINE=94131988; 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 [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASS RP SPECTROMETRY. RX PubMed=12872131; DOI=10.1038/nbt849; RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., RA Marsischky G., Roelofs J., Finley D., Gygi S.P.; RT "A proteomics approach to understanding protein ubiquitination."; RL Nat. Biotechnol. 21:921-926(2003). RN [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASS RP SPECTROMETRY. 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASS RP SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). 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. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with GAL83, SIP1, SIP2 and SNF4. CC -!- INTERACTION: CC Q04739:GAL83; NbExp=1; IntAct=EBI-17516, EBI-7244; CC P12904:SNF4; NbExp=2; 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. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. SNF1 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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 PIR; A26030; A26030. DR RefSeq; NP_010765.1; -. DR PDB; 2EUE; X-ray; A/B=41-315. DR PDB; 2FH9; X-ray; A=46-319. DR DIP; DIP:18N; -. DR IntAct; P06782; -. DR PeptideAtlas; P06782; -. DR Ensembl; YDR477W; Saccharomyces cerevisiae. DR GeneID; 852088; -. DR GenomeReviews; Z71256_GR; YDR477W. DR KEGG; sce:YDR477W; -. DR CYGD; YDR477w; -. DR SGD; S000002885; SNF1. DR LinkHub; P06782; -. DR GermOnline; YDR477W; Saccharomyces cerevisiae. DR GO; GO:0031588; C:AMP-activated protein kinase complex; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD. DR GO; GO:0000324; C:vacuole, cell cycle-correlated morphology; IPI:SGD. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0042710; P:biofilm formation; IMP:SGD. DR GO; GO:0007155; P:cell adhesion; IMP:SGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IDA:SGD. DR GO; GO:0001403; P:invasive growth (sensu Saccharomyces); IMP:SGD. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:SGD. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA:SGD. DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD. DR GO; GO:0001302; P:replicative cell aging; IGI:SGD. DR GO; GO:0007165; P:signal transduction; TAS:SGD. DR InterPro; IPR015741; AMPK. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR013896; UBA_2. DR PANTHER; PTHR22982:SF61; AMPK; 3. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08587; UBA_2; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 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; Phosphorylation; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1 633 Carbon catabolite-derepressing protein FT kinase. FT /FTId=PRO_0000086670. FT DOMAIN 55 306 Protein kinase. FT NP_BIND 61 69 ATP (By similarity). FT COMPBIAS 18 32 Poly-His. FT ACT_SITE 177 177 Proton acceptor (By similarity). FT BINDING 84 84 ATP (By similarity). FT MOD_RES 210 210 Phosphothreonine; by autocatalysis. FT MOD_RES 413 413 Phosphoserine. FT STRAND 55 64 FT STRAND 67 74 FT TURN 75 77 FT STRAND 80 86 FT HELIX 100 107 FT HELIX 139 145 FT HELIX 151 170 FT HELIX 180 182 FT STRAND 183 185 FT STRAND 191 193 FT HELIX 215 217 FT HELIX 220 223 FT HELIX 232 247 FT HELIX 257 265 FT HELIX 277 286 FT TURN 291 293 FT HELIX 297 302 FT HELIX 304 307 FT HELIX 312 314 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 //