CSK21_XENLA
ID CSK21_XENLA Reviewed; 392 AA.
AC P28020;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P68400};
GN Name=csnk2a1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=1544409; DOI=10.1016/0014-5793(92)80556-v;
RA Jedlicki A., Hinrichs M.V., Allende C., Allende J.E.;
RT "The cDNAs coding for the alpha- and beta-subunits of Xenopus laevis casein
RT kinase II.";
RL FEBS Lett. 297:280-284(1992).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Allende J.E.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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. Regulates numerous cellular
CC processes, such as cell cycle progression, apoptosis and transcription,
CC as well as viral infection. May act as a regulatory node which
CC integrates and coordinates numerous signals leading to an appropriate
CC cellular response. During mitosis, functions as a component of the
CC p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains
CC cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Can
CC also negatively regulate apoptosis. Phosphorylates the caspases CASP9
CC and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects
CC CASP9 from cleavage and activation by CASP8, and inhibits the
CC dimerization of CASP2 and activation of CASP8 (By similarity). Plays an
CC important role in the circadian clock function by phosphorylating
CC ARNTL/BMAL1 (By similarity). {ECO:0000250|UniProtKB:P19139,
CC 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
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 an alpha chain, an alpha' and two beta
CC chains.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P68400}.
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; X62375; CAA44238.2; -; mRNA.
DR PIR; S20404; S20404.
DR AlphaFoldDB; P28020; -.
DR SMR; P28020; -.
DR BRENDA; 2.7.11.1; 6725.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN 1..392
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085894"
FT DOMAIN 39..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 334..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 392 AA; 45187 MW; 94189BAE50770CF9 CRC64;
MSGPVPSRAR VYTDVNTHRP RDYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD
QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
LDKLLRYDHQ TRLTAREAMD HPYFYPIVKD QSRMGGSNMP SGSSTPVSSA SMMSGISTVP
TPSALGSLAG SPVISATNTL GTPVAAAAGA TQ
