CSK2C_YEAST
ID CSK2C_YEAST Reviewed; 258 AA.
AC P38930; D6W2A6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Casein kinase II subunit beta';
DE Short=CK II beta';
GN Name=CKB2 {ECO:0000303|PubMed:8027080}; OrderedLocusNames=YOR039W;
GN ORFNames=OR26.32;
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=8027080; DOI=10.1016/s0021-9258(17)32434-1;
RA Reed J.C., Bidwai A.P., Glover C.V.C.;
RT "Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory
RT beta'-subunit of Saccharomyces cerevisiae casein kinase II.";
RL J. Biol. Chem. 269:18192-18200(1994).
RN [2]
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 [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 172-258.
RC STRAIN=AP3;
RA Haider M., Bito A., Wallner J., Breitenbach M.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
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 [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 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: 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). Interaction with YTA7
CC (PubMed:22156209). {ECO:0000269|PubMed:12242279,
CC ECO:0000269|PubMed:22156209}.
CC -!- INTERACTION:
CC P38930; P15790: CKA1; NbExp=8; IntAct=EBI-9578, EBI-9533;
CC P38930; P19454: CKA2; NbExp=10; IntAct=EBI-9578, EBI-9548;
CC P38930; P43639: CKB1; NbExp=6; IntAct=EBI-9578, EBI-9563;
CC P38930; P39521: FHL1; NbExp=2; IntAct=EBI-9578, EBI-6897;
CC -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250|UniProtKB:P67870}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 7160 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; U08849; AAA21656.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60758.1; -; Genomic_DNA.
DR EMBL; Z74947; CAA99229.1; -; Genomic_DNA.
DR EMBL; AY692981; AAT93000.1; -; Genomic_DNA.
DR EMBL; X82893; CAA58064.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10822.1; -; Genomic_DNA.
DR PIR; A54907; A54907.
DR RefSeq; NP_014682.1; NM_001183458.1.
DR AlphaFoldDB; P38930; -.
DR SMR; P38930; -.
DR BioGRID; 34441; 512.
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-262N; -.
DR IntAct; P38930; 46.
DR MINT; P38930; -.
DR STRING; 4932.YOR039W; -.
DR iPTMnet; P38930; -.
DR MaxQB; P38930; -.
DR PaxDb; P38930; -.
DR PRIDE; P38930; -.
DR EnsemblFungi; YOR039W_mRNA; YOR039W; YOR039W.
DR GeneID; 854204; -.
DR KEGG; sce:YOR039W; -.
DR SGD; S000005565; CKB2.
DR VEuPathDB; FungiDB:YOR039W; -.
DR eggNOG; KOG3092; Eukaryota.
DR GeneTree; ENSGT00390000003781; -.
DR HOGENOM; CLU_034027_3_2_1; -.
DR OMA; DADFGRC; -.
DR BioCyc; YEAST:G3O-33585-MON; -.
DR Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:P38930; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38930; protein.
DR GO; GO:0032545; C:CURI complex; IDA:SGD.
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; IMP: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; 1.
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 Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..258
FT /note="Casein kinase II subunit beta'"
FT /id="PRO_0000068258"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 258 AA; 29842 MW; D6060CB3D70B19A4 CRC64;
MGSRSENVGT VTREGSRVEQ DDVLMDDDSD SSEYVDMWID LFLGRKGHEY FCDVDPEYIT
DRFNLMNLQK TVSKFSYVVQ YIVDDLDDSI LENMTHARLE QLESDSRKLY GLIHARYIIT
IKGLQKMYAK YKEADFGRCP RVYCNLQQLL PVGLHDIPGI DCVKLYCPSC EDLYIPKSSR
HSSIDGAYFG TSFPGMFLQA FPDMVPKHPT KRYVPKIFGF ELHKQAQLTR WQELQRLKLV
EKLESKDVDL TKSGGFKT
