ID SNF1_YEAST STANDARD; PRT; 633 AA. AC P06782; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Carbon catabolite derepressing protein kinase (EC 2.7.1.-). GN Name=SNF1; Synonyms=CAT1, CCR1, GLC2, PAS14; GN OrderedLocusNames=YDR477W; ORFNames=D8035.20; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE. 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]. 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 SITE 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). CC -!- FUNCTION: Essential for release from glucose repression. It CC interacts and has functional relationship to the regulatory CC protein SNF4. Interacts also with SIP1, SIP2 and GAL83. Could CC phosphorylates CAT8. CC -!- INTERACTION: CC Q04739:gal83; NbExp=2; IntAct=EBI-17516, EBI-7244; CC -!- SUBCELLULAR LOCATION: Associated with the nuclear membrane. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. SNF1 CC subfamily. 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; -. DR EMBL; U33050; AAB64904.1; -. DR PIR; A26030; A26030. DR HSSP; P24941; 1H0U. DR IntAct; P06782; -. DR GermOnline; 140969; -. DR SGD; S000002885; SNF1. DR GO; GO:0005739; C:mitochondrion; IDA. DR GO; GO:0005634; C:nucleus; IPI. DR GO; GO:0000324; C:vacuole (sensu Fungi); IPI. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IDA. DR GO; GO:0007155; P:cell adhesion; IMP. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IDA. DR GO; GO:0030447; P:filamentous growth; IMP. DR GO; GO:0006006; P:glucose metabolism; TAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA. DR GO; GO:0006109; P:regulation of carbohydrate metabolism; IGI. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 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. KW ATP-binding; Carbohydrate metabolism; Complete proteome; KW Direct protein sequencing; Kinase; Nuclear protein; Phosphorylation; KW Serine/threonine-protein kinase; Transferase. FT DOMAIN 18 32 Poly-His. FT DOMAIN 55 306 Protein kinase. FT NP_BIND 61 69 ATP (By similarity). FT BINDING 84 84 ATP (By similarity). FT ACT_SITE 177 177 Proton acceptor (By similarity). FT MOD_RES 210 210 Phosphothreonine (by autocatalysis). 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 //