ID CBK1_YEAST Reviewed; 756 AA. AC P53894; D6W122; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 22-APR-2020, entry version 186. DE RecName: Full=Serine/threonine-protein kinase CBK1; DE EC=2.7.11.1; DE AltName: Full=Cell wall biosynthesis kinase; GN Name=CBK1; OrderedLocusNames=YNL161W; ORFNames=N1727; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX 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 24 RT complete open reading frames: 18 correspond to new genes, one of which RT encodes a protein similar to the human myotonic dystrophy kinase."; RL Yeast 12:169-175(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX 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., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP INTERACTION WITH PAG1/TAO3. RX 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 required RT for cell morphogenesis and proliferation in Saccharomyces cerevisiae."; RL Mol. Biol. Cell 13:503-514(2002). RN [5] 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 polarized RT growth and acts with the mitotic exit network to facilitate daughter cell- RT specific localization of Ace2p transcription factor."; RL J. Cell Biol. 158:885-900(2002). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Protein kinase that seems to play a role in the regulation of CC cell morphogenesis and proliferation. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- SUBUNIT: Associates with PAG1/TAO3 and interacts with MOB2. CC {ECO:0000269|PubMed:11854408, ECO:0000269|PubMed:12196508}. CC -!- INTERACTION: CC P53894; P53894; NbExp=3; IntAct=EBI-4110, EBI-4110; CC P53894; P21192: ACE2; NbExp=3; IntAct=EBI-4110, EBI-2073; CC P53894; Q00684: CDC14; NbExp=5; IntAct=EBI-4110, EBI-4192; CC P53894; P43563: MOB2; NbExp=7; IntAct=EBI-4110, EBI-11125; CC P53894; P24276: SSD1; NbExp=3; IntAct=EBI-4110, EBI-18153; CC P53894; P40468: TAO3; NbExp=8; IntAct=EBI-4110, EBI-18961; CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. COT1 subfamily. {ECO:0000305}. 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 EMBL; BK006947; DAA10388.1; -; Genomic_DNA. DR PIR; S60966; S60966. DR RefSeq; NP_014238.3; NM_001182999.3. DR PDB; 4LQP; X-ray; 4.50 A; A=251-756. DR PDB; 4LQQ; X-ray; 3.60 A; A/D=251-756. DR PDB; 4LQS; X-ray; 3.30 A; A=251-756. DR PDB; 5NCL; X-ray; 3.15 A; A=251-756. DR PDB; 5NCM; X-ray; 2.80 A; B=251-351. DR PDBsum; 4LQP; -. DR PDBsum; 4LQQ; -. DR PDBsum; 4LQS; -. DR PDBsum; 5NCL; -. DR PDBsum; 5NCM; -. DR SMR; P53894; -. DR BioGrid; 35668; 130. DR ComplexPortal; CPX-1684; CBK1-MOB2 kinase complex. DR DIP; DIP-5656N; -. DR ELM; P53894; -. DR IntAct; P53894; 56. DR MINT; P53894; -. DR STRING; 4932.YNL161W; -. DR iPTMnet; P53894; -. DR MaxQB; P53894; -. DR PaxDb; P53894; -. DR PRIDE; P53894; -. DR EnsemblFungi; YNL161W_mRNA; YNL161W; YNL161W. DR GeneID; 855561; -. DR KEGG; sce:YNL161W; -. DR EuPathDB; FungiDB:YNL161W; -. DR SGD; S000005105; CBK1. DR HOGENOM; CLU_000288_67_2_1; -. DR InParanoid; P53894; -. DR KO; K08286; -. DR OMA; GYTFDCD; -. DR BioCyc; YEAST:G3O-33177-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR PRO; PR:P53894; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P53894; protein. DR GO; GO:0005938; C:cell cortex; IDA:SGD. DR GO; GO:0005933; C:cellular bud; IDA:SGD. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0005934; C:cellular bud tip; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD. DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD. DR GO; GO:0043332; C:mating projection tip; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005628; C:prospore membrane; HDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD. DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD. DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:SGD. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD. DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IGI:SGD. DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..756 FT /note="Serine/threonine-protein kinase CBK1" FT /id="PRO_0000085697" FT DOMAIN 352..672 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 673..754 FT /note="AGC-kinase C-terminal" FT NP_BIND 358..366 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT COMPBIAS 23..34 FT /note="Poly-Gln" FT COMPBIAS 160..164 FT /note="Poly-Ser" FT COMPBIAS 214..232 FT /note="Poly-Gln" FT COMPBIAS 235..250 FT /note="Poly-Gln" FT ACT_SITE 475 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 381 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 109 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:18407956" FT HELIX 278..316 FT /evidence="ECO:0000244|PDB:5NCM" FT TURN 317..319 FT /evidence="ECO:0000244|PDB:5NCM" FT HELIX 322..344 FT /evidence="ECO:0000244|PDB:5NCM" FT STRAND 351..360 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 365..370 FT /evidence="ECO:0000244|PDB:5NCL" FT TURN 372..374 FT /evidence="ECO:0000244|PDB:4LQS" FT STRAND 378..384 FT /evidence="ECO:0000244|PDB:5NCL" FT TURN 385..387 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 415..420 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 422..430 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 437..444 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 449..468 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 478..480 FT /evidence="ECO:0000244|PDB:4LQS" FT STRAND 481..483 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 489..491 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 495..498 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 554..565 FT /evidence="ECO:0000244|PDB:5NCL" FT TURN 566..570 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 580..582 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 584..586 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 592..606 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 616..624 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 626..629 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 642..649 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 653..655 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 656..658 FT /evidence="ECO:0000244|PDB:4LQS" FT TURN 665..668 FT /evidence="ECO:0000244|PDB:5NCL" FT TURN 670..672 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 679..682 FT /evidence="ECO:0000244|PDB:5NCL" FT STRAND 692..695 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 697..699 FT /evidence="ECO:0000244|PDB:5NCL" FT HELIX 746..753 FT /evidence="ECO:0000244|PDB:5NCL" 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 //