CSK2B_SCHPO
ID CSK2B_SCHPO Reviewed; 231 AA.
AC P40232; Q9US19;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Casein kinase II subunit beta;
DE Short=CK II beta;
GN Name=ckb1 {ECO:0000312|PomBase:SPAC1851.03};
GN ORFNames=SPAC1851.03 {ECO:0000312|PomBase:SPAC1851.03};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8264625; DOI=10.1128/mcb.14.1.576-586.1994;
RA Roussou I., Draetta G.;
RT "The Schizosaccharomyces pombe casein kinase II alpha and beta subunits:
RT evolutionary conservation and positive role of the beta subunit.";
RL Mol. Cell. Biol. 14:576-586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 two alpha chains, one beta chain and one
CC beta' chain. {ECO:0000250|UniProtKB:P43639}.
CC -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250|UniProtKB:P67870}.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
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DR EMBL; X74274; CAA52330.1; -; mRNA.
DR EMBL; CU329670; CAB62429.1; -; Genomic_DNA.
DR PIR; T50126; T50126.
DR RefSeq; NP_594606.1; NM_001020034.2.
DR AlphaFoldDB; P40232; -.
DR SMR; P40232; -.
DR BioGRID; 279020; 18.
DR STRING; 4896.SPAC1851.03.1; -.
DR MaxQB; P40232; -.
DR PaxDb; P40232; -.
DR PRIDE; P40232; -.
DR EnsemblFungi; SPAC1851.03.1; SPAC1851.03.1:pep; SPAC1851.03.
DR PomBase; SPAC1851.03; ckb1.
DR VEuPathDB; FungiDB:SPAC1851.03; -.
DR eggNOG; KOG3092; Eukaryota.
DR HOGENOM; CLU_034027_3_2_1; -.
DR InParanoid; P40232; -.
DR OMA; DADFGRC; -.
DR PhylomeDB; P40232; -.
DR Reactome; R-SPO-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SPO-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:P40232; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005956; C:protein kinase CK2 complex; IPI:PomBase.
DR GO; GO:0034456; C:UTP-C complex; ISO:PomBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:PomBase.
DR GO; GO:0090053; P:positive regulation of pericentric heterochromatin assembly; IMP:CACAO.
DR GO; GO:0006468; P:protein phosphorylation; IMP:CACAO.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IC:PomBase.
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 2: Evidence at transcript level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..231
FT /note="Casein kinase II subunit beta"
FT /id="PRO_0000068255"
FT CONFLICT 134
FT /note="T -> A (in Ref. 1; CAA52330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 26677 MW; 6874315013421683 CRC64;
MQLYSSESES DDSQYWVDWF LGLKGNEFFC EVDEDFIQDR FNLTGLSHEV PHYSQSLDLI
LDVLDPDLPE EVQDEVEASA RHLYGLIHAR YILTAQGLYK MLEKYKKCDF GHCPRVLCNG
QPMLPVGLSD IAHTKSVKLY CPRCEDVYTP KSQRHASIDG AYFGTSFPHM LFQVYPELAV
PKSQERYIPR IFGFKVHSYS ATFKKQDVYK EKQKKRLQGA EAESKNKLAI T
