CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009861
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Casein kinase II subunit alpha 
Protein Synonyms/Alias
 CK II alpha 
Gene Name
 CSNK2A1 
Gene Synonyms/Alias
 CK2A1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
49VRKLGRGKYSEVFEAubiquitination[1]
102ITLADIVKDPVSRTPacetylation[2]
102ITLADIVKDPVSRTPubiquitination[1]
122HVNNTDFKQLYQTLTubiquitination[1, 3]
260DLYDYIDKYNIELDPubiquitination[1]
329PYFYTVVKDQARMGSubiquitination[1, 4]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 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. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin- mediated degradation. 
Sequence Annotation
 DOMAIN 39 324 Protein kinase.
 NP_BIND 45 53 ATP (By similarity).
 REGION 36 41 Interaction with beta subunit (By
 ACT_SITE 156 156 Proton acceptor.
 BINDING 68 68 ATP (By similarity).
 MOD_RES 344 344 Phosphothreonine; by CDK1.
 MOD_RES 360 360 Phosphothreonine; by CDK1.
 MOD_RES 362 362 Phosphoserine; by CDK1.
 MOD_RES 370 370 Phosphoserine; by CDK1.  
Keyword
 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cell cycle; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 391 AA 
Protein Sequence
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT 60
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD 120
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE 180
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD 240
QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF 300
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT 360
PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q 391 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016581; C:NuRD complex; IDA:BHF-UCL.
 GO:0005886; C:plasma membrane; TAS:ProtInc.
 GO:0016580; C:Sin3 complex; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051879; F:Hsp90 protein binding; TAS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0071174; P:mitotic spindle checkpoint; IMP:UniProtKB.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
 GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
 GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
 GO:0030177; P:positive regulation of Wnt receptor signaling pathway; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS