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 15-JUL-1999 (Rel. 38, Last annotation update) DE Carbon catabolite derepressing protein kinase (EC 2.7.1.-). GN SNF1 OR CAT1 OR CCR1 OR PAS14 OR GLC2 OR YDR477W OR 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 SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RA Dietrich F.S., Mulligan J., 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., 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., RA Winant A., Yelton M., Botstein D., Davis R.W.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 274-284; 528-539 AND 622-630, AND PHOSPHORYLATION SITE. 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 -!- SUBCELLULAR LOCATION: ASSOCIATED WITH THE NUCLEAR MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC SNF1 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; 1AQ1. DR SGD; S0002885; SNF1. DR InterPro; IPR000719; Euk_pkinase. DR InterPro; IPR002290; Ser_thr_kin_actsite. DR Pfam; PF00069; pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Phosphorylation; Carbohydrate metabolism; Nuclear protein. 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 BY SIMILARITY. FT MOD_RES 210 210 PHOSPHORYLATION (AUTO-). 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 //