CBK1_YEAST
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 03-AUG-2022, entry version 197.
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; P21192: ACE2; NbExp=3; IntAct=EBI-4110, EBI-2073;
CC P53894; P53894: CBK1; NbExp=3; IntAct=EBI-4110, EBI-4110;
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}.
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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 AlphaFoldDB; P53894; -.
DR SMR; P53894; -.
DR BioGRID; 35668; 132.
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 SGD; S000005105; CBK1.
DR VEuPathDB; FungiDB:YNL161W; -.
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000153544; -.
DR HOGENOM; CLU_000288_67_2_1; -.
DR InParanoid; P53894; -.
DR OMA; PERYSEN; -.
DR BioCyc; YEAST:G3O-33177-MON; -.
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; HDA: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:1902554; C:serine/threonine protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; IDA:ComplexPortal.
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:ComplexPortal.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:SGD.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IDA:ComplexPortal.
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 358..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 278..316
FT /evidence="ECO:0007829|PDB:5NCM"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 322..344
FT /evidence="ECO:0007829|PDB:5NCM"
FT STRAND 351..360
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:5NCL"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:4LQS"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:5NCL"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 449..468
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:4LQS"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 554..565
FT /evidence="ECO:0007829|PDB:5NCL"
FT TURN 566..570
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 592..606
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 616..624
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 626..629
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 642..649
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:4LQS"
FT TURN 665..668
FT /evidence="ECO:0007829|PDB:5NCL"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 679..682
FT /evidence="ECO:0007829|PDB:5NCL"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 746..753
FT /evidence="ECO:0007829|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
