ID CBK1_YEAST STANDARD; PRT; 756 AA. AC P53894; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Serine/threonine-protein kinase CBK1 (EC 2.7.1.37) (Cell wall DE biosynthesis kinase). GN Name=CBK1; OrderedLocusNames=YNL161W; ORFNames=N1727; 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. RC STRAIN=S288c / FY1679; RX MEDLINE=96287653; PubMed=8686380; RA Nasr F., Becam A.-M., Herbert C.J.; RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals RT 24 complete open reading frames: 18 correspond to new genes, one of RT which encodes a protein similar to the human myotonic dystrophy RT kinase."; RL Yeast 12:169-175(1996). RN [2] RP INTERACTION WITH PAG1/TAO3. RX MEDLINE=21843681; PubMed=11854408; DOI=10.1091/mbc.01-07-0365; RA Du L.L., Novick P.; RT "Pag1p, a novel protein associated with protein kinase Cbk1p, is RT required for cell morphogenesis and proliferation in Saccharomyces RT cerevisiae."; RL Mol. Biol. Cell 13:503-514(2002). RN [3] RP INTERACTION WITH MOB2. RX PubMed=12196508; DOI=10.1083/jcb.200203094; RA Weiss E.L., Kurischko C., Zhang C., Shokat K., Drubin D.G., Luca F.C.; RT "The Saccharomyces cerevisiae Mob2p-Cbk1p kinase complex promotes RT polarized growth and acts with the mitotic exit network to facilitate RT daughter cell-specific localization of Ace2p transcription factor."; RL J. Cell Biol. 158:885-900(2002). CC -!- FUNCTION: Protein kinase that seems to play a role in thr CC regulation of cell morphogenesis and proliferation. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Associates with PAG1/TAO3 and interacts with MOB2. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. COT1 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; X92517; CAA63278.1; -. DR EMBL; Z71437; CAA96048.1; -. DR PIR; S60966; S60966. DR HSSP; P31751; 1GZK. DR GermOnline; 143167; -. DR SGD; S0005105; CBK1. DR GO; GO:0005935; C:bud neck; IDA. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005634; C:nucleus; IDA. DR GO; GO:0000753; P:cellular morphogenesis during conjugation w...; IDA. DR GO; GO:0030012; P:establishment and/or maintenance of cell po...; IMP. DR GO; GO:0007096; P:regulation of exit from mitosis; IMP. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00133; S_TK_X; 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; Serine/threonine-protein kinase; Transferase. FT DOMAIN 23 34 Poly-Gln. FT DOMAIN 160 164 Poly-Ser. FT DOMAIN 214 232 Poly-Gln. FT DOMAIN 235 250 Poly-Gln. FT DOMAIN 352 672 Protein kinase. FT NP_BIND 358 366 ATP (By similarity). FT BINDING 381 381 ATP (By similarity). FT ACT_SITE 475 475 Proton acceptor (By similarity). SQ SEQUENCE 756 AA; 86946 MW; 87EBCD2C3C96EE11 CRC64; MYNSSTNHHE GAPTSGHGYY MSQQQDQQHQ QQQQYANEMN PYQQIPRPPA AGFSSNYMKE QGSHQSLQEH LQRETGNLGS GFTDVPALNY PATPPPHNNY AASNQMINTP PPSMGGLYRH NNNSQSMVQN GNGSGNAQLP QLSPGQYSIE SEYNQNLNGS SSSSPFHQPQ TLRSNGSYSS GLRSVKSFQR LQQEQENVQV QQQLSQAQQQ NSRQQQQQLQ YQQQQQQQQQ QQHMQIQQQQ QQQQQQQQSQ SPVQSGFNNG TISNYMYFER RPDLLTKGTQ DKAAAVKLKI ENFYQSSVKY AIERNERRVE LETELTSHNW SEERKSRQLS SLGKKESQFL RLRRTRLSLE DFHTVKVIGK GAFGEVRLVQ KKDTGKIYAM KTLLKSEMYK KDQLAHVKAE RDVLAGSDSP WVVSLYYSFQ DAQYLYLIME FLPGGDLMTM LIRWQLFTED VTRFYMAECI LAIETIHKLG FIHRDIKPDN ILIDIRGHIK LSDFGLSTGF HKTHDSNYYK KLLQQDEATN GISKPGTYNA NTTDTANKRQ TMVVDSISLT MSNRQQIQTW RKSRRLMAYS TVGTPDYIAP EIFLYQGYGQ ECDWWSLGAI MYECLIGWPP FCSETPQETY RKIMNFEQTL QFPDDIHISY EAEDLIRRLL THADQRLGRH GGADEIKSHP FFRGVDWNTI RQVEAPYIPK LSSITDTRFF PTDELENVPD SPAMAQAAKQ REQMTKQGGS APVKEDLPFI GYTYSRFDYL TRKNAL //