KC12_YEAST
ID KC12_YEAST Reviewed; 546 AA.
AC P23292; D6W129;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Casein kinase I homolog 2;
DE EC=2.7.11.1;
GN Name=YCK2; Synonyms=CKI1; OrderedLocusNames=YNL154C; ORFNames=N1755;
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 204508 / S288c;
RX PubMed=1729698; DOI=10.1073/pnas.89.1.28;
RA Robinson L.C., Hubbard E.J.A., Graves P.R., dePaoli-Roach A.A., Roach P.J.,
RA Kung C., Haas D.W., Hagedorn C.H., Goebl M., Culbertson M.R., Carlson M.;
RT "Yeast casein kinase I homologues: an essential gene pair.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:28-32(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1627830; DOI=10.1091/mbc.3.3.275;
RA Wang P.-C., Vancura A., Mitcheson T.G.M., Kuret J.;
RT "Two genes in Saccharomyces cerevisiae encode a membrane-bound form of
RT casein kinase-1.";
RL Mol. Biol. Cell 3:275-286(1992).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10866691; DOI=10.1128/mcb.20.14.5350-5359.2000;
RA Feng Y., Davis N.G.;
RT "Akr1p and the type I casein kinases act prior to the ubiquitination step
RT of yeast endocytosis: Akr1p is required for kinase localization to the
RT plasma membrane.";
RL Mol. Cell. Biol. 20:5350-5359(2000).
RN [7]
RP PALMITOYLATION AT CYS-545 AND CYS-546.
RX PubMed=12370247; DOI=10.1083/jcb.200206120;
RA Roth A.F., Feng Y., Chen L., Davis N.G.;
RT "The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl
RT transferase.";
RL J. Cell Biol. 159:23-28(2002).
RN [8]
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 [9]
RP PALMITOYLATION AT CYS-545 AND CYS-546, AND MUTAGENESIS OF CYS-545 AND
RP CYS-546.
RX PubMed=15105419; DOI=10.1074/jbc.m403071200;
RA Babu P., Deschenes R.J., Robinson L.C.;
RT "Akr1p-dependent palmitoylation of Yck2p yeast casein kinase 1 is necessary
RT and sufficient for plasma membrane targeting.";
RL J. Biol. Chem. 279:27138-27147(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP IDENTIFICATION 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. {ECO:0000269|PubMed:10866691}.
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 -!- INTERACTION:
CC P23292; P23291: YCK1; NbExp=4; IntAct=EBI-4729, EBI-4718;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10866691};
CC Lipid-anchor {ECO:0000269|PubMed:10866691}.
CC -!- PTM: Palmitoylated by AKR1, which is required for proper plasma
CC membrane localization of YCK2. {ECO:0000269|PubMed:12370247,
CC ECO:0000269|PubMed:15105419}.
CC -!- MISCELLANEOUS: Present with 6160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; M74453; AAA35230.1; -; Genomic_DNA.
DR EMBL; X60326; CAA42896.1; -; mRNA.
DR EMBL; X92517; CAA63285.1; -; Genomic_DNA.
DR EMBL; Z71430; CAA96041.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10395.1; -; Genomic_DNA.
DR PIR; S29522; S29522.
DR RefSeq; NP_014245.1; NM_001182992.1.
DR AlphaFoldDB; P23292; -.
DR SMR; P23292; -.
DR BioGRID; 35675; 489.
DR DIP; DIP-720N; -.
DR IntAct; P23292; 12.
DR MINT; P23292; -.
DR STRING; 4932.YNL154C; -.
DR iPTMnet; P23292; -.
DR SwissPalm; P23292; -.
DR MaxQB; P23292; -.
DR PaxDb; P23292; -.
DR PRIDE; P23292; -.
DR EnsemblFungi; YNL154C_mRNA; YNL154C; YNL154C.
DR GeneID; 855568; -.
DR KEGG; sce:YNL154C; -.
DR SGD; S000005098; YCK2.
DR VEuPathDB; FungiDB:YNL154C; -.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000176388; -.
DR HOGENOM; CLU_019279_1_0_1; -.
DR InParanoid; P23292; -.
DR OMA; DWMHLNG; -.
DR BioCyc; YEAST:YNL154C-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P23292; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P23292; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005937; C:mating projection; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
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:0000902; P:cell morphogenesis; IGI:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IGI:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Acetylation; ATP-binding; Cell membrane; Isopeptide bond; Kinase;
KW Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..546
FT /note="Casein kinase I homolog 2"
FT /id="PRO_0000192857"
FT DOMAIN 76..360
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 82..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT LIPID 545
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12370247,
FT ECO:0000269|PubMed:15105419"
FT LIPID 546
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12370247,
FT ECO:0000269|PubMed:15105419"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 545
FT /note="C->S: Impaired palmitoylation and plasma membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:15105419"
FT MUTAGEN 546
FT /note="C->S: Impaired palmitoylation and plasma membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:15105419"
SQ SEQUENCE 546 AA; 62079 MW; A88D99BC265BF4FA CRC64;
MSQVQSPLTA TNSGLAVNNN TMNSQMPNRS NVRLVNGTLP PSLHVSSNLN HNTGNSSASY
SGSQSRDDST IVGLHYKIGK KIGEGSFGVL FEGTNMINGL PVAIKFEPRK TEAPQLKDEY
RTYKILAGTP GIPQEYYFGQ EGLHNILVID LLGPSLEDLF DWCGRRFSVK TVVQVAVQMI
TLIEDLHAHD LIYRDIKPDN FLIGRPGQPD ANKVHLIDFG MAKQYRDPKT KQHIPYREKK
SLSGTARYMS INTHLGREQS RRDDMEAMGH VFFYFLRGQL PWQGLKAPNN KQKYEKIGEK
KRLTNVYDLA QGLPIQFGRY LEIVRNLSFE ETPDYEGYRM LLLSVLDDLG ETADGQYDWM
KLNGGRGWDL SINKKPNLHG YGHPNPPNEK SKRHRSKNHQ YSSPDHHHHY NQQQQQQQAQ
AQAQAQAQAK VQQQQLQQAQ AQQQANRYQL QPDDSHYDEE REASKLDPTS YEAYQQQTQQ
KYAQQQQKQM QQKSKQFANT GANGQTNKYP YNAQPTANDE QNAKNAAQDR NSNKSSKGFF
SKLGCC
