ID CBK1_YEAST Reviewed; 756 AA. AC P53894; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-OCT-2007, entry version 66. DE Serine/threonine-protein kinase CBK1 (EC 2.7.11.1) (Cell wall DE biosynthesis kinase). GN Name=CBK1; OrderedLocusNames=YNL161W; ORFNames=N1727; 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]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=96287653; PubMed=8686380; RX DOI=10.1002/(SICI)1097-0061(199602)12:2<169::AID-YEA894>3.0.CO;2-B; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313269; PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., RA Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV RT and its evolutionary implications."; RL Nature 387:93-98(1997). RN [3] 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 [4] 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). RN [5] 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-66 AND SER-187, RP AND MASS 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: Protein kinase that seems to play a role in the 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 -!- INTERACTION: CC P40484:MOB1; NbExp=1; IntAct=EBI-4110, EBI-11119; CC P40468:TAO3; NbExp=1; IntAct=EBI-4110, EBI-18961; CC P40572:YIR016W; NbExp=1; IntAct=EBI-4110, EBI-25414; CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. COT1 subfamily. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. 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; X92517; CAA63278.1; -; Genomic_DNA. DR EMBL; Z71437; CAA96048.1; -; Genomic_DNA. DR PIR; S60966; S60966. DR RefSeq; NP_014238.1; -. DR HSSP; P31751; 1GZK. DR DIP; DIP:5656N; -. DR IntAct; P53894; -. DR Ensembl; YNL161W; Saccharomyces cerevisiae. DR GeneID; 855561; -. DR GenomeReviews; Y13139_GR; YNL161W. DR KEGG; sce:YNL161W; -. DR CYGD; YNL161w; -. DR SGD; S000005105; CBK1. DR LinkHub; P53894; -. DR GermOnline; YNL161W; Saccharomyces cerevisiae. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0043332; C:mating projection tip; TAS:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0000753; P:cellular morphogenesis during conjugation w...; IDA:SGD. DR GO; GO:0000903; P:cellular morphogenesis during vegetative gr...; IGI:SGD. DR GO; GO:0030467; P:establishment and/or maintenance of cell po...; IMP:SGD. DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 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 ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Phosphorylation; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 756 Serine/threonine-protein kinase CBK1. FT /FTId=PRO_0000085697. FT DOMAIN 352 672 Protein kinase. FT DOMAIN 673 754 AGC-kinase C-terminal. FT NP_BIND 358 366 ATP (By similarity). FT COMPBIAS 23 34 Poly-Gln. FT COMPBIAS 160 164 Poly-Ser. FT COMPBIAS 214 232 Poly-Gln. FT COMPBIAS 235 250 Poly-Gln. FT ACT_SITE 475 475 Proton acceptor (By similarity). FT BINDING 381 381 ATP (By similarity). FT MOD_RES 63 63 Phosphoserine. FT MOD_RES 66 66 Phosphoserine. FT MOD_RES 187 187 Phosphoserine. 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 //