CSK2A_SCHPO
ID CSK2A_SCHPO Reviewed; 332 AA.
AC P40231;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 169.
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:0000312|PomBase:SPAC23C11.11}; Synonyms=orb5;
GN ORFNames=SPAC23C11.11 {ECO:0000312|PomBase:SPAC23C11.11};
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 [MRNA].
RX PubMed=8187760; DOI=10.1002/j.1460-2075.1994.tb06481.x;
RA Snell V., Nurse P.;
RT "Genetic analysis of cell morphogenesis in fission yeast -- a role for
RT casein kinase II in the establishment of polarized growth.";
RL EMBO J. 13:2066-2074(1994).
RN [3]
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: 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. {ECO:0000250|UniProtKB:P68400}.
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 two alpha chains, one beta chain and one
CC beta' chain. {ECO:0000250|UniProtKB:P15790}.
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; X74275; CAA52331.1; -; mRNA.
DR EMBL; L29508; AAA19875.1; -; mRNA.
DR EMBL; CU329670; CAB11164.1; -; Genomic_DNA.
DR PIR; S44355; S44355.
DR RefSeq; NP_593642.1; NM_001019073.2.
DR AlphaFoldDB; P40231; -.
DR SMR; P40231; -.
DR BioGRID; 278457; 26.
DR IntAct; P40231; 2.
DR STRING; 4896.SPAC23C11.11.1; -.
DR BindingDB; P40231; -.
DR ChEMBL; CHEMBL1075255; -.
DR iPTMnet; P40231; -.
DR MaxQB; P40231; -.
DR PaxDb; P40231; -.
DR PRIDE; P40231; -.
DR EnsemblFungi; SPAC23C11.11.1; SPAC23C11.11.1:pep; SPAC23C11.11.
DR GeneID; 2541972; -.
DR KEGG; spo:SPAC23C11.11; -.
DR PomBase; SPAC23C11.11; cka1.
DR VEuPathDB; FungiDB:SPAC23C11.11; -.
DR eggNOG; KOG0668; Eukaryota.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; P40231; -.
DR OMA; RAYWDYD; -.
DR PhylomeDB; P40231; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-2514853; Condensation of Prometaphase Chromosomes.
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:P40231; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA: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:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IDA:PomBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IDA:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:PomBase.
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:2000247; P:positive regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..332
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085903"
FT DOMAIN 43..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 67
FT /note="S -> R (in Ref. 1; CAA52331)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="S -> L (in Ref. 1; CAA52331)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..169
FT /note="MID -> IIV (in Ref. 1; CAA52331)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..235
FT /note="DT -> EP (in Ref. 1; CAA52331)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="Missing (in Ref. 1; CAA52331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 39527 MW; BE20AA4405456B72 CRC64;
MNQTEAAPVV SVSRVYAHVN EEMPREYWDY ENMQEVFGYQ DNYEIIRKVG RGKYSEVFEG
LNVLNNSKCI IKVLKPVKYK KIKREIKILQ NLAGGPNIIS LLDIVRDPES KTPSLIFEFV
DNIDFRTLYP TLSDYDIRYY SYELLKALDF CHSRGIMHRD VKPHNVMIDH KKRKLRLIDW
GLAEFYHAGM EYNVRVASRY FKGPELLVDF REYDYSLDIW SFGVMFAALI FKKDTFFRGR
DNYDQLVKIA KVLGTDELFA YVQKYQIVLD RQYDNILGQY PKRDWYSFVN RDNRSLANDE
AIDLLNRLLR YDHQERLTCQ EAMAHPYFQV LK
