CSK22_HUMAN

(non-specific serine/threonine protein kinase from Homo sapiens; EC 2.7.11.1)

ATP + a protein = ADP + a phosphoprotein

Accession Code:P19784
Organism:Homo sapiens
Number of AA:350
Molecular Weight:41213
Source:Swiss-Prot
Sequences with same EC No.:


Sequence: ->fasta
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0  MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK YSEVFEAINI
60  TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID TVKDPVSKTP ALVFEYINNT
120  DFKQLYQILT DFDIRFYMYE LLKALDYCHS KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA
180  EFYHPAQEYN VRVASRYFKG PELLVDYQMY DYSLDMWSLG CMLASMIFRR EPFFHGQDNY
240  DQLVRIAKVL GTEELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD
300  LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCADNA VLSSGLTAAR

Data linked to the same EC Number and organism:
Activating Compound: 35
Application: 8
Cloned(Commentary): 35
Crystallization (Commentary): 2
Engineering: 45
Inhibitors: 73
KM Value [mM]: 7
Ligands: 313
Localization: 46
Metals/Ions: 6
Molecular Weight [Da]: 1
Natural Substrates/ Products (Substrates): 103
PDB ID: 970
Posttranslational Modification: 20
Product: 139
Purification (Commentary): 10
Reaction: 1
Reference by Title: 15175
Source Tissue: 108
Specific Activity [micromol/min/mg]: 2
Substrate: 139
Substrates and Products (Substrate): 193
Subunits: 11
Synonyms: 181
Temperature Optimum [°C]: 20
Turnover Number [1/s]: 4
pH Optimum: 17
Cofactor: 2
Ki Value [mM]: 18
Natural Substrate: 65
Natural Product: 65
pI Value: 2
IC50 Value: 41
Organism_taxonomy_ncbi_term: 2
Activating Compound (protein specific): 37
Application (protein specific): 8
Cloned(Commentary) (protein specific): 59
Cofactor (protein specific): 5
Crystallization (Commentary) (protein specific): 2
Engineering (protein specific): 45
IC50 Value (protein specific): 41
Inhibitors (protein specific): 74
Ki Value [mM] (protein specific): 18
KM Value [mM] (protein specific): 7
Localization (protein specific): 52
Metals/Ions (protein specific): 7
Molecular Weight [Da] (protein specific): 1
Natural Substrates/ Products (Substrates) (protein specific): 106
Posttranslational Modification (protein specific): 22
Purification (Commentary) (protein specific): 11
Reference by Title (protein specific): 15193
Source Tissue (protein specific): 146
Specific Activity [micromol/min/mg] (protein specific): 2
Substrates and Products (Substrate) (protein specific): 198
Subunits (protein specific): 12
Temperature Optimum [°C] (protein specific): 22
Turnover Number [1/s] (protein specific): 4
pH Optimum (protein specific): 17
pI Value (protein specific): 2
General Information: 7
General Information (protein specific): 7

Sequence related references:
Sequence ReferenceAuthorsTitleJournalVolumePagesYearLink to PubMed
5581Lozeman F.J.,Litchfield D.W.,Piening C.,Takio K.,Walsh K.A.,Krebs E.G.Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II.Biochemistry298436 - 84471990 PubMed
5582The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).Genome Res.142121 - 21272004 PubMed
5583Keller D.M.,Zeng X.,Wang Y.,Zhang Q.H.,Kapoor M.,Shu H.,Goodman R.,Lozano G.,Zhao Y.,Lu H.A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1.Mol. Cell7283 - 2922001 PubMed
5584Sayed M.,Pelech S.,Wong C.,Marotta A.,Salh B.Protein kinase CK2 is involved in G2 arrest and apoptosis following spindle damage in epithelial cells.Oncogene206994 - 70052001 PubMed
5585Keller D.M.,Lu H.p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex.J. Biol. Chem.27750206 - 502132002 PubMed
5586Shin S.,Lee Y.,Kim W.,Ko H.,Choi H.,Kim K.Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8.EMBO J.243532 - 35422005 PubMed
5587Daub H.,Olsen J.V.,Bairlein M.,Gnad F.,Oppermann F.S.,Korner R.,Greff Z.,Keri G.,Stemmann O.,Mann M.Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Mol. Cell31438 - 4482008 PubMed
5588Oppermann F.S.,Gnad F.,Olsen J.V.,Hornberger R.,Greff Z.,Keri G.,Mann M.,Daub H.Large-scale proteomics analysis of the human kinome.Mol. Cell. Proteomics81751 - 17642009 PubMed
5589Choudhary C.,Kumar C.,Gnad F.,Nielsen M.L.,Rehman M.,Walther T.,Olsen J.V.,Mann M.Lysine acetylation targets protein complexes and co-regulates major cellular functions.Science325834 - 8402009 PubMed
5590Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.Initial characterization of the human central proteome.BMC Syst. Biol.517 - 172011 PubMed
5591Meggio F.,Pinna L.A.One-thousand-and-one substrates of protein kinase CK2?FASEB J.17349 - 3682003 PubMed
5592Niefind K.,Raaf J.,Issinger O.G.Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights.Cell. Mol. Life Sci.661800 - 18162009 PubMed
5593St-Denis N.A.,Litchfield D.W.Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival.Cell. Mol. Life Sci.661817 - 18292009 PubMed
5594Filhol O.,Cochet C.Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair.Cell. Mol. Life Sci.661830 - 18392009 PubMed
5595Miyata Y.Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery.Cell. Mol. Life Sci.661840 - 18492009 PubMed
5596Dominguez I.,Sonenshein G.E.,Seldin D.C.Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer.Cell. Mol. Life Sci.661850 - 18572009 PubMed
5597Nakaniwa T.,Kinoshita T.,Sekiguchi Y.,Tada T.,Nakanishi I.,Kitaura K.,Suzuki Y.,Ohno H.,Hirasawa A.,Tsujimoto G.Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor.Acta Crystallogr. F6575 - 792009 PubMed
5598Bischoff N.,Olsen B.,Raaf J.,Bretner M.,Issinger O.G.,Niefind K.Structure of the human protein kinase CK2 catalytic subunit CK2alpha' and interaction thermodynamics with the regulatory subunit CK2beta.J. Mol. Biol.4071 - 122011 PubMed
5599Greenman C.,Stephens P.,Smith R.,Dalgliesh G.L.,Hunter C.,Bignell G.,Davies H.,Teague J.,Butler A.,Stevens C.,Edkins S.,O'Meara S.,Vastrik I.,Schmidt E.E.,Avis T.,Barthorpe S.,Bhamra G.,Buck G.,Choudhury B.,Clements J.,Cole J.,Dicks E.,Forbes S.,Gray K.,Halliday K.,Harrison R.,Hills K.,Hinton J.,Jenkinson A.,Jones D.,Menzies A.,Mironenko T.,Perry J.,Raine K.,Richardson D.,Shepherd R.,Small A.,Tofts C.,Varian J.,Webb T.,West S.,Widaa S.,Yates A.,Cahill D.P.,Louis D.N.,Goldstraw P.,Nicholson A.G.,Brasseur F.,Looijenga L.,Weber B.L.,Chiew Y.-E.,DeFazio A.,Greaves M.F.,Green A.R.,Campbell P.,Birney E.,Easton D.F.,Chenevix-Trench G.,Tan M.-H.,Khoo S.K.,Teh B.T.,Yuen S.T.,Leung S.Y.,Wooster R.,Futreal P.A.,Stratton M.R.Patterns of somatic mutation in human cancer genomes.Nature446153 - 1582007 PubMed