KC11_YEAST
ID KC11_YEAST Reviewed; 538 AA.
AC P23291; D3DL84; E9P958;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Casein kinase I homolog 1;
DE EC=2.7.11.1;
GN Name=YCK1; Synonyms=CKI2; OrderedLocusNames=YHR135C;
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 [GENOMIC DNA].
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RC STRAIN=Sigma 1278B;
RX PubMed=9491083; DOI=10.1007/s004380050644;
RA Iraqui I., Vissers S., Cartiaux M., Urrestarazu A.;
RT "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding
RT aromatic aminotransferases I and II reveals a new aminotransferase
RT subfamily.";
RL Mol. Gen. Genet. 257:238-248(1998).
RN [7]
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 [8]
RP PALMITOYLATION.
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 [9]
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 [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-523 AND SER-527, AND
RP IDENTIFICATION BY 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-523 AND SER-527, AND
RP IDENTIFICATION BY 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).
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 P23291; P00445: SOD1; NbExp=2; IntAct=EBI-4718, EBI-17635;
CC P23291; P19812: UBR1; NbExp=2; IntAct=EBI-4718, EBI-19909;
CC P23291; P23292: YCK2; NbExp=4; IntAct=EBI-4718, EBI-4729;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10866691};
CC Lipid-anchor {ECO:0000269|PubMed:10866691}. Mitochondrion membrane
CC {ECO:0000269|PubMed:16823961}.
CC -!- PTM: Palmitoylated by AKR1. {ECO:0000269|PubMed:12370247}.
CC -!- MISCELLANEOUS: Present with 1630 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; M74552; AAA35229.1; -; Genomic_DNA.
DR EMBL; X60327; CAA42897.1; -; Genomic_DNA.
DR EMBL; U10398; AAB68417.1; -; Genomic_DNA.
DR EMBL; Y13625; CAA73948.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06828.1; -; Genomic_DNA.
DR EMBL; AY723826; AAU09743.1; -; Genomic_DNA.
DR PIR; S29521; S29521.
DR RefSeq; NP_012003.1; NM_001179265.1.
DR PDB; 5X18; X-ray; 1.80 A; A/B=62-355.
DR PDBsum; 5X18; -.
DR AlphaFoldDB; P23291; -.
DR SMR; P23291; -.
DR BioGRID; 36568; 493.
DR DIP; DIP-719N; -.
DR IntAct; P23291; 86.
DR MINT; P23291; -.
DR STRING; 4932.YHR135C; -.
DR ChEMBL; CHEMBL3497; -.
DR iPTMnet; P23291; -.
DR SwissPalm; P23291; -.
DR MaxQB; P23291; -.
DR PaxDb; P23291; -.
DR PRIDE; P23291; -.
DR EnsemblFungi; YHR135C_mRNA; YHR135C; YHR135C.
DR GeneID; 856537; -.
DR KEGG; sce:YHR135C; -.
DR SGD; S000001177; YCK1.
DR VEuPathDB; FungiDB:YHR135C; -.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000176388; -.
DR HOGENOM; CLU_019279_1_0_1; -.
DR InParanoid; P23291; -.
DR OMA; NIPYAYY; -.
DR BioCyc; YEAST:YHR135C-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P23291; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P23291; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA: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; IMP: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 3D-structure; ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane;
KW Mitochondrion; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..538
FT /note="Casein kinase I homolog 1"
FT /id="PRO_0000192856"
FT DOMAIN 69..353
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 75..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT LIPID 537
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 538
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 201
FT /note="Q -> H (in Ref. 5; AAU09743)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="K -> E (in Ref. 2; CAA42897)"
FT /evidence="ECO:0000305"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5X18"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:5X18"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5X18"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5X18"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:5X18"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:5X18"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5X18"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:5X18"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:5X18"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5X18"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 254..270
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:5X18"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 328..342
FT /evidence="ECO:0007829|PDB:5X18"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:5X18"
SQ SEQUENCE 538 AA; 61715 MW; 77344717818C2D17 CRC64;
MSMPIASTTL AVNNLTNING NANFNVQANK QLHHQAVDSP ARSSMTATTA ANSNSNSSRD
DSTIVGLHYK IGKKIGEGSF GVLFEGTNMI NGVPVAIKFE PRKTEAPQLR DEYKTYKILN
GTPNIPYAYY FGQEGLHNIL VIDLLGPSLE DLFDWCGRKF SVKTVVQVAV QMITLIEDLH
AHDLIYRDIK PDNFLIGRPG QPDANNIHLI DFGMAKQYRD PKTKQHIPYR EKKSLSGTAR
YMSINTHLGR EQSRRDDMEA LGHVFFYFLR GHLPWQGLKA PNNKQKYEKI GEKKRSTNVY
DLAQGLPVQF GRYLEIVRSL SFEECPDYEG YRKLLLSVLD DLGETADGQY DWMKLNDGRG
WDLNINKKPN LHGYGHPNPP NEKSRKHRNK QLQMQQLQMQ QLQQQQQQQQ YAQKTEADMR
NSQYKPKLDP TSYEAYQHQT QQKYLQEQQK RQQQQKLQEQ QLQEQQLQQQ QQQQQQLRAT
GQPPSQPQAQ TQSQQFGARY QPQQQPSAAL RTPEQHPNDD NSSLAASHKG FFQKLGCC
