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Casein kinase II subunit alpha 3 (CK II alpha 3) (EC 2.7.11.1) (Casein kinase II alpha 1 polypeptide pseudogene)

 CSK23_HUMAN             Reviewed;         391 AA.
Q8NEV1;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
01-MAY-2013, sequence version 2.
25-APR-2018, entry version 118.
RecName: Full=Casein kinase II subunit alpha 3;
Short=CK II alpha 3;
EC=2.7.11.1;
AltName: Full=Casein kinase II alpha 1 polypeptide pseudogene;
Name=CSNK2A3; Synonyms=CSNK2A1P;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1610905; DOI=10.1016/0167-4781(92)90083-C;
Wirkner U., Voss H., Lichter P., Weitz S., Ansorge W., Pyerin W.;
"Human casein kinase II subunit alpha: sequence of a processed
(pseudo)gene and its localization on chromosome 11.";
Biochim. Biophys. Acta 1131:220-222(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8420794; DOI=10.1016/0014-5793(93)81197-8;
Devilat I., Carvallo P.;
"Structure and sequence of an intronless gene for human casein kinase
II-alpha subunit.";
FEBS Lett. 316:114-118(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Platelet;
PubMed=12102635; DOI=10.1021/bi025791r;
Singh L.S., Kalafatis M.;
"Sequencing of full-length cDNA encoding the alpha and beta subunits
of human casein kinase II from human platelets and megakaryocytic
cells. Expression of the casein kinase IIalpha intronless gene in a
megakaryocytic cell line.";
Biochemistry 41:8935-8940(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PML, VARIANT THR-133,
AND TISSUE SPECIFICITY.
PubMed=20625391; DOI=10.1371/journal.pone.0011418;
Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T.,
Jablons D.M., You L.;
"Functional polymorphism of the CK2alpha intronless gene plays
oncogenic roles in lung cancer.";
PLoS ONE 5:E11418-E11418(2010).
-!- FUNCTION: Probable catalytic subunit of a constitutively active
serine/threonine-protein kinase complex that phosphorylates a
large number of substrates containing acidic residues C-terminal
to the phosphorylated serine or threonine. Amplification-dependent
oncogene; promotes cell proliferation and tumorigenesis by down-
regulating expression of the tumor suppressor protein, PML. May
play a role in the pathogenesis of the lung cancer development and
progression. {ECO:0000269|PubMed:20625391}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20625391}.
-!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha
chain and/or alpha' chain) and two regulatory subunits (beta
chains) (By similarity). Interacts with PML. {ECO:0000250,
ECO:0000269|PubMed:20625391}.
-!- TISSUE SPECIFICITY: Detected in blood platelets and megakaryocyte
cell lines. Poorly expressed in lung. Highly expressed in lung
tumor tissues. {ECO:0000269|PubMed:12102635,
ECO:0000269|PubMed:20625391}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CK2 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; X64692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY112721; AAM52224.1; -; mRNA.
EMBL; CH471064; EAW68546.1; -; Genomic_DNA.
RefSeq; NP_001243615.1; NM_001256686.1.
UniGene; Hs.644056; -.
UniGene; Hs.654675; -.
UniGene; Hs.741126; -.
ProteinModelPortal; Q8NEV1; -.
SMR; Q8NEV1; -.
BioGrid; 129460; 1.
ChEMBL; CHEMBL3832943; -.
iPTMnet; Q8NEV1; -.
PhosphoSitePlus; Q8NEV1; -.
BioMuta; CSNK2A3; -.
EPD; Q8NEV1; -.
MaxQB; Q8NEV1; -.
PeptideAtlas; Q8NEV1; -.
PRIDE; Q8NEV1; -.
Ensembl; ENST00000528848; ENSP00000473553; ENSG00000254598.
GeneID; 283106; -.
KEGG; hsa:283106; -.
UCSC; uc001mjp.4; human.
CTD; 283106; -.
DisGeNET; 283106; -.
EuPathDB; HostDB:ENSG00000254598.2; -.
GeneCards; CSNK2A3; -.
H-InvDB; HIX0035927; -.
HGNC; HGNC:2458; CSNK2A3.
HPA; HPA059206; -.
neXtProt; NX_Q8NEV1; -.
OpenTargets; ENSG00000254598; -.
eggNOG; KOG0668; Eukaryota.
eggNOG; ENOG410XNPP; LUCA.
GeneTree; ENSGT00390000004215; -.
HOVERGEN; HBG107282; -.
InParanoid; Q8NEV1; -.
KO; K03097; -.
OMA; NIVRDQQ; -.
OrthoDB; EOG091G0AZY; -.
SignaLink; Q8NEV1; -.
GenomeRNAi; 283106; -.
PRO; PR:Q8NEV1; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000254598; -.
Genevisible; Q8NEV1; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
Polymorphism; Proto-oncogene; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 391 Casein kinase II subunit alpha 3.
/FTId=PRO_0000422194.
DOMAIN 39 324 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 45 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 156 156 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 68 68 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VARIANT 133 133 I -> T (in a lung carcinoma sample;
somatic mutation; shows greater kinase
activity, provides a cell growth
advantage and increases its interaction
with the PML tumor suppressor protein and
PML degradation; dbSNP:rs2071460).
{ECO:0000269|PubMed:20625391}.
/FTId=VAR_069225.
CONFLICT 128 128 L -> F (in Ref. 1; X64692, 3; AAM52224
and 5; EAW68546). {ECO:0000305}.
CONFLICT 217 217 R -> S (in Ref. 1; X64692, 3; AAM52224
and 5; EAW68546). {ECO:0000305}.
CONFLICT 236 236 R -> H (in Ref. 1; X64692).
{ECO:0000305}.
CONFLICT 248 248 F -> V (in Ref. 1; X64692, 3; AAM52224
and 5; EAW68546). {ECO:0000305}.
CONFLICT 287 287 S -> R (in Ref. 1; X64692, 3; AAM52224
and 5; EAW68546). {ECO:0000305}.
CONFLICT 296 296 Missing (in Ref. 1; X64692).
{ECO:0000305}.
CONFLICT 387 387 T -> A (in Ref. 1; X64692, 3; AAM52224
and 5; EAW68546). {ECO:0000305}.
SEQUENCE 391 AA; 45220 MW; D0FA2E3EACB5A064 CRC64;
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWRLGC MLASMIFRKE PFFHGRDNYD
QLVRIAKFLG TEDLYGYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN VMSGISSVPT
PSPLGPLAGS PVIAAANPLG MPVPAATGAQ Q


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