CSK2B_YEAST
ID CSK2B_YEAST Reviewed; 278 AA.
AC P43639; D6VUB8; Q9URG5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Casein kinase II subunit beta;
DE Short=CK II beta;
GN Name=CKB1; OrderedLocusNames=YGL019W;
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=7737972; DOI=10.1074/jbc.270.18.10395;
RA Bidwai A.P., Reed J.C., Glover C.V.C.;
RT "Cloning and disruption of CKB1, the gene encoding the 38-kDa beta subunit
RT of Saccharomyces cerevisiae casein kinase II (CKII). Deletion of CKII
RT regulatory subunits elicits a salt-sensitive phenotype.";
RL J. Biol. Chem. 270:10395-10404(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 PROTEIN SEQUENCE OF 34-52; 182-196 AND 257-270.
RX PubMed=8135547; DOI=10.1006/abbi.1994.1123;
RA Bidwai A.P., Reed J.C., Glover C.V.C.;
RT "Casein kinase II of Saccharomyces cerevisiae contains two distinct
RT regulatory subunits, beta and beta'.";
RL Arch. Biochem. Biophys. 309:348-355(1994).
RN [5]
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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
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).
RN [9]
RP 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 [10]
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).
CC -!- FUNCTION: Regulatory subunit of casein kinase II/CK2 (By similarity).
CC As part of the kinase complex regulates the basal catalytic activity of
CC the alpha subunit a constitutively active serine/threonine-protein
CC kinase that phosphorylates a large number of substrates containing
CC acidic residues C-terminal to the phosphorylated serine or threonine
CC (By similarity). {ECO:0000250|UniProtKB:P67870}.
CC -!- SUBUNIT: Tetramer composed of an alpha subunit, an alpha' subunit, one
CC beta subunit and one beta' subunit (PubMed:12242279). Interacts with
CC FACT subunits POB3 and SPT16 (PubMed:12242279). interacts with YTA7
CC (PubMed:22156209). {ECO:0000269|PubMed:12242279,
CC ECO:0000269|PubMed:22156209}.
CC -!- INTERACTION:
CC P43639; P15790: CKA1; NbExp=11; IntAct=EBI-9563, EBI-9533;
CC P43639; P19454: CKA2; NbExp=11; IntAct=EBI-9563, EBI-9548;
CC P43639; P38930: CKB2; NbExp=6; IntAct=EBI-9563, EBI-9578;
CC P43639; P53254: UTP22; NbExp=3; IntAct=EBI-9563, EBI-1878;
CC -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250|UniProtKB:P67870}.
CC -!- MISCELLANEOUS: Present with 8120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
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DR EMBL; U21283; AAA86829.1; -; Genomic_DNA.
DR EMBL; Z72541; CAA96719.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08079.1; -; Genomic_DNA.
DR PIR; A56421; A56421.
DR RefSeq; NP_011496.3; NM_001180884.3.
DR AlphaFoldDB; P43639; -.
DR SMR; P43639; -.
DR BioGRID; 33227; 553.
DR ComplexPortal; CPX-581; Protein kinase CK2 variant 1.
DR ComplexPortal; CPX-769; Protein kinase CK2 variant 2.
DR ComplexPortal; CPX-770; Protein kinase CK2 variant 3.
DR ComplexPortal; CPX-771; UTP-C complex variant 2.
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-775; CURI complex variant 2.
DR ComplexPortal; CPX-776; CURI complex variant 3.
DR DIP; DIP-282N; -.
DR IntAct; P43639; 79.
DR MINT; P43639; -.
DR STRING; 4932.YGL019W; -.
DR iPTMnet; P43639; -.
DR MaxQB; P43639; -.
DR PaxDb; P43639; -.
DR PRIDE; P43639; -.
DR EnsemblFungi; YGL019W_mRNA; YGL019W; YGL019W.
DR GeneID; 852865; -.
DR KEGG; sce:YGL019W; -.
DR SGD; S000002987; CKB1.
DR VEuPathDB; FungiDB:YGL019W; -.
DR eggNOG; KOG3092; Eukaryota.
DR GeneTree; ENSGT00390000003781; -.
DR HOGENOM; CLU_034027_3_0_1; -.
DR InParanoid; P43639; -.
DR OMA; YTILDYQ; -.
DR BioCyc; YEAST:G3O-30539-MON; -.
DR PRO; PR:P43639; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P43639; protein.
DR GO; GO:0032545; C:CURI complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0019887; F:protein kinase regulator activity; IDA:SGD.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA: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:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:ComplexPortal.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; 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 Gene3D; 1.10.1820.10; -; 1.
DR InterPro; IPR016149; Casein_kin_II_reg-sub_N.
DR InterPro; IPR035991; Casein_kinase_II_beta-like.
DR InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR PANTHER; PTHR11740; PTHR11740; 2.
DR Pfam; PF01214; CK_II_beta; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SMART; SM01085; CK_II_beta; 1.
DR SUPFAM; SSF57798; SSF57798; 1.
DR PROSITE; PS01101; CK2_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..278
FT /note="Casein kinase II subunit beta"
FT /id="PRO_0000068257"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
SQ SEQUENCE 278 AA; 32265 MW; 9ACA8D285E6990AF CRC64;
MSQEFVEDYS RTGSSDDEDS GAYDEWIPSF CSRFGHEYFC QVPTEFIEDD FNMTSLSQEV
PHYRKALDLI LDLEAMSDEE EDEDDVVEED EVDQEMQSND GHDEGKRRNK SPVVNKSIIE
HAAEQLYGLI HARFILTKPG LQAMAEKFDH KEFGTCPRYY CNGMQLLPCG LSDTVGKHTV
RLYCPSCQDL YLPQSSRFLC LEGAFWGTSF PGVFLKHFKE LEEYVERKSK ESYELKVFGF
RINDEAVSGP RMKWLRQYPS TEEDWEEFAK CEFETPAV
