CSK22_YEAST
ID CSK22_YEAST Reviewed; 339 AA.
AC P19454; D6W2C4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Casein kinase II subunit alpha';
DE Short=CK II;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P68400};
GN Name=CKA2 {ECO:0000303|PubMed:2196445}; OrderedLocusNames=YOR061W;
GN ORFNames=YOR29-12;
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].
RX PubMed=2196445; DOI=10.1128/mcb.10.8.4089-4099.1990;
RA Padmanabha R., Chen-Wu J.L.-P., Hanna D.E., Glover C.V.C.;
RT "Isolation, sequencing, and disruption of the yeast CKA2 gene: casein
RT kinase II is essential for viability in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 10:4089-4099(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 PROTEIN SEQUENCE OF 2-38.
RX PubMed=3468112; DOI=10.1016/s0021-9258(19)75714-7;
RA Padmanabha R., Glover C.V.C.;
RT "Casein kinase II of yeast contains two distinct alpha polypeptides and an
RT unusually large beta subunit.";
RL J. Biol. Chem. 262:1829-1835(1987).
RN [7]
RP INTERACTION WITH POB3 AND SPT16.
RX PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA Shilatifard A., Buratowski S., Greenblatt J.F.;
RT "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT targeted proteomics approach.";
RL Mol. Cell. Biol. 22:6979-6992(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 INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH YTA7.
RX PubMed=22156209; DOI=10.1101/gad.173427.111;
RA Kurat C.F., Lambert J.P., van Dyk D., Tsui K., van Bakel H.,
RA Kaluarachchi S., Friesen H., Kainth P., Nislow C., Figeys D.,
RA Fillingham J., Andrews B.J.;
RT "Restriction of histone gene transcription to S phase by phosphorylation of
RT a chromatin boundary protein.";
RL Genes Dev. 25:2489-2501(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Catalytic subunit of a constitutively active
CC serine/threonine-protein kinase complex that phosphorylates a large
CC number of substrates containing acidic residues C-terminal to the
CC phosphorylated serine or threonine (By similarity). Phosphorylates YTA7
CC during S-phase to promote transcription of histones (PubMed:22156209).
CC {ECO:0000250|UniProtKB:P68400, ECO:0000269|PubMed:22156209}.
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 Evidence={ECO:0000250|UniProtKB:P68400};
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; Evidence={ECO:0000250|UniProtKB:P68400};
CC -!- SUBUNIT: Tetramer composed of an alpha chain, an alpha', one beta chain
CC and one beta' chain (PubMed:12242279). Interacts with FACT subunits
CC POB3 and SPT16 (PubMed:12242279). Interacts with NAP1
CC (PubMed:18086883). Interacts with YTA7 (PubMed:22156209).
CC {ECO:0000269|PubMed:12242279, ECO:0000269|PubMed:18086883,
CC ECO:0000269|PubMed:22156209}.
CC -!- INTERACTION:
CC P19454; Q00684: CDC14; NbExp=3; IntAct=EBI-9548, EBI-4192;
CC P19454; P15790: CKA1; NbExp=12; IntAct=EBI-9548, EBI-9533;
CC P19454; P43639: CKB1; NbExp=11; IntAct=EBI-9548, EBI-9563;
CC P19454; P38930: CKB2; NbExp=10; IntAct=EBI-9548, EBI-9578;
CC -!- MISCELLANEOUS: Present with 4540 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M33759; AAA34500.1; -; Genomic_DNA.
DR EMBL; Z74969; CAA99254.1; -; Genomic_DNA.
DR EMBL; Z70678; CAA94546.1; -; Genomic_DNA.
DR EMBL; AY723867; AAU09784.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10840.1; -; Genomic_DNA.
DR PIR; S11192; TVBY2A.
DR RefSeq; NP_014704.1; NM_001183480.1.
DR AlphaFoldDB; P19454; -.
DR SMR; P19454; -.
DR BioGRID; 34460; 415.
DR ComplexPortal; CPX-581; Protein kinase CK2 variant 1.
DR ComplexPortal; CPX-770; Protein kinase CK2 variant 3.
DR ComplexPortal; CPX-772; UTP-C complex variant 1.
DR ComplexPortal; CPX-773; UTP-C complex variant 3.
DR ComplexPortal; CPX-774; CURI complex variant 1.
DR ComplexPortal; CPX-776; CURI complex variant 3.
DR DIP; DIP-1038N; -.
DR IntAct; P19454; 113.
DR MINT; P19454; -.
DR STRING; 4932.YOR061W; -.
DR iPTMnet; P19454; -.
DR MaxQB; P19454; -.
DR PaxDb; P19454; -.
DR PRIDE; P19454; -.
DR EnsemblFungi; YOR061W_mRNA; YOR061W; YOR061W.
DR GeneID; 854227; -.
DR KEGG; sce:YOR061W; -.
DR SGD; S000005587; CKA2.
DR VEuPathDB; FungiDB:YOR061W; -.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR HOGENOM; CLU_000288_70_4_1; -.
DR OMA; ACEKRPQ; -.
DR BioCyc; YEAST:G3O-33601-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-SCE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SCE-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:P19454; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P19454; protein.
DR GO; GO:0032545; C:CURI complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0034456; C:UTP-C complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006974; P:cellular response to DNA damage stimulus; IDA:SGD.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:SGD.
DR GO; GO:0007535; P:donor selection; IGI:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:ComplexPortal.
DR GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IDA:SGD.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IC:ComplexPortal.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR InterPro; IPR045216; CK2_alpha.
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 PANTHER; PTHR24054; PTHR24054; 1.
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 ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3468112"
FT CHAIN 2..339
FT /note="Casein kinase II subunit alpha'"
FT /id="PRO_0000085896"
FT DOMAIN 50..334
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 56..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 339 AA; 39404 MW; 30E214BD852824D0 CRC64;
MPLPPSTLNQ KSNRVYSVAR VYKNACEERP QEYWDYEQGV TIDWGKISNY EIINKIGRGK
YSEVFSGRCI VNNQKCVIKV LKPVKMKKIY RELKILTNLT GGPNVVGLYD IVQDADSKIP
ALIFEEIKNV DFRTLYPTFK LPDIQYYFTQ LLIALDYCHS MGIMHRDVKP QNVMIDPTER
KLRLIDWGLA EFYHPGVDYN VRVASRYHKG PELLVNLNQY DYSLDLWSVG CMLAAIVFKK
EPFFKGSSNP DQLVKIATVL GTKELLGYLG KYGLHLPSEY DNIMRDFTKK SWTHFITSET
KLAVPEVVDL IDNLLRYDHQ ERLTAKEAMD HKFFKTKFE
