CSK21_YEAST
ID CSK21_YEAST Reviewed; 372 AA.
AC P15790; D6VVP7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II subunit alpha;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P68400};
GN Name=CKA1 {ECO:0000303|PubMed:3062376}; OrderedLocusNames=YIL035C;
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=3062376; DOI=10.1128/mcb.8.11.4981-4990.1988;
RA Chen-Wu J.L.-P., Padmanabha R., Glover C.V.C.;
RT "Isolation, sequencing, and disruption of the CKA1 gene encoding the alpha
RT subunit of yeast casein kinase II.";
RL Mol. Cell. Biol. 8:4981-4990(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
RX PubMed=1315784; DOI=10.1083/jcb.117.5.1067;
RA Amatruda J.F., Cooper J.A.;
RT "Purification, characterization, and immunofluorescence localization of
RT Saccharomyces cerevisiae capping protein.";
RL J. Cell Biol. 117:1067-1076(1992).
RN [6]
RP PROTEIN SEQUENCE OF 1-45.
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 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).
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 YTA7
CC (PubMed:22156209). {ECO:0000269|PubMed:12242279,
CC ECO:0000269|PubMed:22156209}.
CC -!- INTERACTION:
CC P15790; P40458: ATG32; NbExp=2; IntAct=EBI-9533, EBI-25256;
CC P15790; Q00684: CDC14; NbExp=3; IntAct=EBI-9533, EBI-4192;
CC P15790; P19454: CKA2; NbExp=12; IntAct=EBI-9533, EBI-9548;
CC P15790; P43639: CKB1; NbExp=11; IntAct=EBI-9533, EBI-9563;
CC P15790; P38930: CKB2; NbExp=8; IntAct=EBI-9533, EBI-9578;
CC P15790; P20448: HCA4; NbExp=2; IntAct=EBI-9533, EBI-5612;
CC P15790; P53335: PXR1; NbExp=2; IntAct=EBI-9533, EBI-23652;
CC P15790; Q12481: RRP36; NbExp=3; IntAct=EBI-9533, EBI-31770;
CC P15790; P40362: UTP18; NbExp=3; IntAct=EBI-9533, EBI-4534;
CC P15790; P53254: UTP22; NbExp=4; IntAct=EBI-9533, EBI-1878;
CC -!- MISCELLANEOUS: Present with 7180 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; M22473; AAA34534.1; -; Genomic_DNA.
DR EMBL; Z46861; CAA86916.1; -; Genomic_DNA.
DR EMBL; AY558299; AAS56625.1; -; Genomic_DNA.
DR EMBL; X62630; CAA44498.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08513.1; -; Genomic_DNA.
DR PIR; A31564; A31564.
DR RefSeq; NP_012229.1; NM_001179385.1.
DR PDB; 4FI1; X-ray; 2.09 A; A=1-372.
DR PDB; 4JQE; X-ray; 1.77 A; A=1-372.
DR PDB; 4JR7; X-ray; 1.48 A; A=1-372.
DR PDB; 4LFI; X-ray; 1.85 A; A/B=1-372.
DR PDB; 4MWH; X-ray; 2.09 A; A=1-372.
DR PDBsum; 4FI1; -.
DR PDBsum; 4JQE; -.
DR PDBsum; 4JR7; -.
DR PDBsum; 4LFI; -.
DR PDBsum; 4MWH; -.
DR AlphaFoldDB; P15790; -.
DR SMR; P15790; -.
DR BioGRID; 34955; 388.
DR ComplexPortal; CPX-581; Protein kinase CK2 variant 1.
DR ComplexPortal; CPX-769; Protein kinase CK2 variant 2.
DR ComplexPortal; CPX-771; UTP-C complex variant 2.
DR ComplexPortal; CPX-772; UTP-C complex variant 1.
DR ComplexPortal; CPX-774; CURI complex variant 1.
DR ComplexPortal; CPX-775; CURI complex variant 2.
DR DIP; DIP-48N; -.
DR IntAct; P15790; 136.
DR MINT; P15790; -.
DR STRING; 4932.YIL035C; -.
DR iPTMnet; P15790; -.
DR MaxQB; P15790; -.
DR PaxDb; P15790; -.
DR PRIDE; P15790; -.
DR EnsemblFungi; YIL035C_mRNA; YIL035C; YIL035C.
DR GeneID; 854776; -.
DR KEGG; sce:YIL035C; -.
DR SGD; S000001297; CKA1.
DR VEuPathDB; FungiDB:YIL035C; -.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; P15790; -.
DR OMA; RAYWDYD; -.
DR BioCyc; YEAST:G3O-31307-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:P15790; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P15790; 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: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:0006974; P:cellular response to DNA damage stimulus; IDA: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; IBA:GO_Central.
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 3D-structure; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..372
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085889"
FT DOMAIN 40..363
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4FI1"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:4JR7"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4JR7"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4JR7"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:4JR7"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4JR7"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4JR7"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 169..188
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4JR7"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4JR7"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 251..266
FT /evidence="ECO:0007829|PDB:4JR7"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4LFI"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:4JR7"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:4JR7"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:4JR7"
SQ SEQUENCE 372 AA; 44668 MW; 6A1A7F1BF47250C9 CRC64;
MKCRVWSEAR VYTNINKQRT EEYWDYENTV IDWSTNTKDY EIENKVGRGK YSEVFQGVKL
DSKVKIVIKM LKPVKKKKIK REIKILTDLS NEKVPPTTLP FQKDQYYTNQ KEDVLKFIRP
YIFDQPHNGH ANIIHLFDII KDPISKTPAL VFEYVDNVDF RILYPKLTDL EIRFYMFELL
KALDYCHSMG IMHRDVKPHN VMIDHKNKKL RLIDWGLAEF YHVNMEYNVR VASRFFKGPE
LLVDYRMYDY SLDLWSFGTM LASMIFKREP FFHGTSNTDQ LVKIVKVLGT SDFEKYLLKY
EITLPREFYD MDQYIRKPWH RFINDGNKHL SGNDEIIDLI DNLLRYDHQE RLTAKEAMGH
PWFAPIREQI EK
