CSK2A_DICDI
ID CSK2A_DICDI Reviewed; 337 AA.
AC Q02720; Q550N9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II subunit alpha;
DE EC=2.7.11.1;
GN Name=casK; ORFNames=DDB_G0276885;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1448100; DOI=10.1128/mcb.12.12.5711-5723.1992;
RA Kikkawa U., Mann S.K., Firtel R.A., Hunter T.;
RT "Molecular cloning of casein kinase II alpha subunit from Dictyostelium
RT discoideum and its expression in the life cycle.";
RL Mol. Cell. Biol. 12:5711-5723(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. The alpha chain contains the catalytic site.
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 -!- 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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CK2 subfamily. {ECO:0000305}.
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DR EMBL; L05535; AAA33180.1; -; mRNA.
DR EMBL; AAFI02000019; EAL68944.1; -; Genomic_DNA.
DR PIR; A45038; A45038.
DR RefSeq; XP_642893.1; XM_637801.1.
DR AlphaFoldDB; Q02720; -.
DR SMR; Q02720; -.
DR STRING; 44689.DDB0185025; -.
DR PaxDb; Q02720; -.
DR EnsemblProtists; EAL68944; EAL68944; DDB_G0276885.
DR GeneID; 8620759; -.
DR KEGG; ddi:DDB_G0276885; -.
DR dictyBase; DDB_G0276885; casK.
DR eggNOG; KOG0668; Eukaryota.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; Q02720; -.
DR OMA; RAYWDYD; -.
DR PhylomeDB; Q02720; -.
DR BRENDA; 2.7.11.1; 1939.
DR Reactome; R-DDI-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-DDI-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DDI-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:Q02720; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
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:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
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..337
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085899"
FT DOMAIN 47..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 53..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 337 AA; 39898 MW; 49DE7A7F39E1ED12 CRC64;
MNHSSKKNKN RILRNKARIY CDVNLHKPKE YWNYEALNVK WETQDDYEII RKIGRGKYSE
VFEGANIKNN EKCVIKVLKP VKKKKIKREI KILQNLCGGP NIITLYDVVR DPQSKTPSLI
FEYINNTDFK HLSPTLTDFD VRYYIRELLH ALDFCHSNGI MHRDVKPSNV MIDHQKRKLY
LIDWGLAEFY HPNQDYNVRV ASRPYKGPEL LVDMEDYDYS LDMWSLGCMF AGMLFQKDPF
FHGHDNIDQL VKIVKILGTE EFYAYLDKYG IVVDHTILSI IGKHPKKPWS RFITKENQHL
AVPEAIDFLE KLLRYDPAER LTTREAMEHP YFKPLSH
