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 07-NOV-2018, entry version 177. 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; OC Saccharomycetes; 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 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 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., 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 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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 RT required for cell morphogenesis and proliferation in Saccharomyces RT 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 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 [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., 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND IDENTIFICATION RP BY 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). 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 {ECO:0000269|PubMed:11854408, ECO:0000269|PubMed:12196508}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-4110, EBI-4110; CC P21192:ACE2; NbExp=3; IntAct=EBI-4110, EBI-2073; CC Q00684:CDC14; NbExp=5; IntAct=EBI-4110, EBI-4192; CC P43563:MOB2; NbExp=7; IntAct=EBI-4110, EBI-11125; CC P24276:SSD1; NbExp=3; IntAct=EBI-4110, EBI-18153; CC P40468:TAO3; NbExp=8; IntAct=EBI-4110, EBI-18961; CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD CC medium. {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 ProteinModelPortal; P53894; -. 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; YNL161W; YNL161W. DR GeneID; 855561; -. DR KEGG; sce:YNL161W; -. DR SGD; S000005105; CBK1. DR GeneTree; ENSGT00760000118994; -. DR HOGENOM; HOG000233033; -. DR InParanoid; P53894; -. DR KO; K08286; -. DR OMA; FFYGVDW; -. DR OrthoDB; EOG092C0HH3; -. DR BioCyc; YEAST:G3O-33177-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR Reactome; R-SCE-2028269; Signaling by Hippo. DR Reactome; R-SCE-3928662; EPHB-mediated forward signaling. DR Reactome; R-SCE-416482; G alpha (12/13) signalling events. DR Reactome; R-SCE-416572; Sema4D induced cell migration and growth-cone collapse. DR Reactome; R-SCE-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-SCE-5625900; RHO GTPases activate CIT. DR Reactome; R-SCE-5627117; RHO GTPases Activate ROCKs. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR PRO; PR:P53894; -. DR Proteomes; UP000002311; Chromosome XIV. 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: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; Complete proteome; Kinase; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 756 Serine/threonine-protein kinase CBK1. FT /FTId=PRO_0000085697. FT DOMAIN 352 672 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 673 754 AGC-kinase C-terminal. FT NP_BIND 358 366 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. 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. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 381 381 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 109 109 Phosphothreonine. FT {ECO:0000244|PubMed:18407956}. FT HELIX 278 316 {ECO:0000244|PDB:5NCM}. FT TURN 317 319 {ECO:0000244|PDB:5NCM}. FT HELIX 322 344 {ECO:0000244|PDB:5NCM}. FT STRAND 351 360 {ECO:0000244|PDB:5NCL}. FT STRAND 365 370 {ECO:0000244|PDB:5NCL}. FT TURN 372 374 {ECO:0000244|PDB:4LQS}. FT STRAND 378 384 {ECO:0000244|PDB:5NCL}. FT TURN 385 387 {ECO:0000244|PDB:5NCL}. FT STRAND 415 420 {ECO:0000244|PDB:5NCL}. FT STRAND 422 430 {ECO:0000244|PDB:5NCL}. FT HELIX 437 444 {ECO:0000244|PDB:5NCL}. FT HELIX 449 468 {ECO:0000244|PDB:5NCL}. FT STRAND 478 480 {ECO:0000244|PDB:4LQS}. FT STRAND 481 483 {ECO:0000244|PDB:5NCL}. FT STRAND 489 491 {ECO:0000244|PDB:5NCL}. FT STRAND 495 498 {ECO:0000244|PDB:5NCL}. FT HELIX 554 565 {ECO:0000244|PDB:5NCL}. FT TURN 566 570 {ECO:0000244|PDB:5NCL}. FT HELIX 580 582 {ECO:0000244|PDB:5NCL}. FT STRAND 584 586 {ECO:0000244|PDB:5NCL}. FT HELIX 592 606 {ECO:0000244|PDB:5NCL}. FT HELIX 616 624 {ECO:0000244|PDB:5NCL}. FT HELIX 626 629 {ECO:0000244|PDB:5NCL}. FT HELIX 642 649 {ECO:0000244|PDB:5NCL}. FT HELIX 653 655 {ECO:0000244|PDB:5NCL}. FT STRAND 656 658 {ECO:0000244|PDB:4LQS}. FT TURN 665 668 {ECO:0000244|PDB:5NCL}. FT TURN 670 672 {ECO:0000244|PDB:5NCL}. FT HELIX 679 682 {ECO:0000244|PDB:5NCL}. FT STRAND 692 695 {ECO:0000244|PDB:5NCL}. FT HELIX 697 699 {ECO:0000244|PDB:5NCL}. FT HELIX 746 753 {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 //