Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Casein kinase II subunit alpha  

UniProtKB / Swiss-Prot ID :  CSK21_HUMAN

Gene Name (Synonyms) : 
CSNK2A1, CK2A1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  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. 

Protein Sequence MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKIL...
Predicted Secondary Structure CCCCCCCHHCCCCCCCCCCCCCCCEEEEEEEECCCCCCEEEEEEEEECCCEEEEEEEECCCCCEEEEEEC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2Phosphoserine---MSGPVP
---CCCCCC
52.37HPRD
Link
2Phosphoserine---MSGPVP
---CCCCCC
52.37Phosphositeplus
Link
2Phosphoserine.---MSGPVP
---CCCCCC
52.37UniProtKB
Link
7PhosphoserineGPVPSRARV
CCCCCHHCC
38.51Phosphositeplus
Link
7Phosphoserine.GPVPSRARV
CCCCCHHCC
38.51UniProtKB
Link
49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LGRGKYSEV
EEECCCEEE
44.22Phosphositeplus
Link
50PhosphotyrosineGRGKYSEVF
EECCCEEEE
16.94Phosphositeplus
Link
50Phosphotyrosine.GRGKYSEVF
EECCCEEEE
16.94UniProtKB
Link
102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ADIVKDPVS
EEEEECCCC
57.56Phosphositeplus
Link
102N6-acetyllysineADIVKDPVS
EEEEECCCC
57.56HPRD
Link
102N6-acetyllysineADIVKDPVS
EEEEECCCC
57.56Phosphositeplus
Link
102N6-acetyllysine.ADIVKDPVS
EEEEECCCC
57.56UniProtKB
Link
122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NTDFKQLYQ
CCHHHHHHH
42.05Phosphositeplus
Link
125Phosphotyrosine.FKQLYQTLT
HHHHHHCCC
9.28UniProtKB
Link
127PhosphothreonineQLYQTLTDY
HHHHCCCHH
20.33Phosphositeplus
Link
127Phosphothreonine.QLYQTLTDY
HHHHCCCHH
20.33UniProtKB
Link
182PhosphotyrosineLAEFYHPGQ
EEEEECCCC
9.90HPRD
Link
182PhosphotyrosineLAEFYHPGQ
EEEEECCCC
9.90Phosphositeplus
Link
194PhosphoserineVRVASRYFK
EEEEECCCC
25.34HPRD
Link
194Phosphoserine.VRVASRYFK
EEEEECCCC
25.34UniProtKB
Link
217PhosphoserineLDMWSLGCM
CHHHHHHHH
14.30HPRD
Link
229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MIFRKEPFF
HHHCCCCCC
60.02Phosphositeplus
Link
247Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VRIAKVLGT
HHHHHHHCC
35.30Phosphositeplus
Link
255PhosphotyrosineTEDLYDYID
CCCHHHHHH
21.01Phosphositeplus
Link
255Phosphotyrosine (Lyn;Fgr)TEDLYDYID
CCCHHHHHH
21.01PhosphoELM
Link
255Phosphotyrosine.TEDLYDYID
CCCHHHHHH
21.01UniProtKB
Link
260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DYIDKYNIE
HHHHHCCCC
30.55Phosphositeplus
Link
277PhosphoserineLGRHSRKRW
CCCCCCCCC
37.83Phosphositeplus
Link
277Phosphoserine.LGRHSRKRW
CCCCCCCCC
37.83UniProtKB
Link
287PhosphoserineRFVHSENQH
CCCCCCCCC
32.70Phosphositeplus
Link
287Phosphoserine.RFVHSENQH
CCCCCCCCC
32.70UniProtKB
Link
329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YTVVKDQAR
CCCCCCCCC
39.52Phosphositeplus
Link
343PhosphoserineMPGGSTPVS
CCCCCCCCC
35.14HPRD
Link-
344PhosphothreoninePGGSTPVSS
CCCCCCCCC
30.86Phosphositeplus
Link-
344Phosphothreonine (CDK1)PGGSTPVSS
CCCCCCCCC
30.86HPRD
Link-
344Phosphothreonine (CDK_group;CDK_group;CDK1;CDK1)PGGSTPVSS
CCCCCCCCC
30.86PhosphoELM
Link-
344Phosphothreonine; by CDK1.PGGSTPVSS
CCCCCCCCC
30.86UniProtKB
Link-
353PhosphoserineANMMSGISS
HHHHHHHHH
23.39HPRD
Link-
356PhosphoserineMSGISSVPT
HHHHHHCCC
28.89HPRD
Link-
360PhosphothreonineSSVPTPSPL
HHCCCCCCC
33.95Phosphositeplus
Link-
360Phosphothreonine (CDK1)SSVPTPSPL
HHCCCCCCC
33.95HPRD
Link-
360Phosphothreonine (CDK_group;CDK_group;CDK1;CDK1)SSVPTPSPL
HHCCCCCCC
33.95PhosphoELM
Link-
360Phosphothreonine; by CDK1.SSVPTPSPL
HHCCCCCCC
33.95UniProtKB
Link-
362PhosphoserineVPTPSPLGP
CCCCCCCCC
34.92Phosphositeplus
Link-
362Phosphoserine (CDK1)VPTPSPLGP
CCCCCCCCC
34.92HPRD
Link-
362Phosphoserine (CDK_group;CDK_group;CDK1;CDK1)VPTPSPLGP
CCCCCCCCC
34.92PhosphoELM
Link-
362Phosphoserine; by CDK1.VPTPSPLGP
CCCCCCCCC
34.92UniProtKB
Link-
370PhosphoserinePLAGSPVIA
CCCCCCEEE
15.47Phosphositeplus
Link-
370Phosphoserine (CDK1)PLAGSPVIA
CCCCCCEEE
15.47HPRD
Link-
370Phosphoserine (CDK_group;CDK_group;CDK1;CDK1)PLAGSPVIA
CCCCCCEEE
15.47PhosphoELM
Link-
370Phosphoserine; by CDK1.PLAGSPVIA
CCCCCCEEE
15.47UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
XRCC1_HUMANphosphorylation reactionMINT-51183MINT15367657
1433B_HUMANphysical interactionMINT-50947MINT15324660
1433S_HUMANphysical interactionMINT-3975397MINT15778465
CSK2B_HUMANphysical interactionMINT-62611MINT14667819
CSK2B_HUMANphysical interactionMINT-62709MINT14667819
CSK2B_HUMANphysical interactionMINT-62785MINT14667819
XRCC4_HUMANphosphorylation reactionMINT-51176MINT15385968
HIF1A_HUMANphosphorylation reactionMINT-4791613MINT17382325
KANK2_HUMANphosphorylation reactionMINT-4961111MINT17476305
CSK2B_HUMANphysical interactionDIP:40144EDIP11574463
CSK2B_HUMANphysical interaction
phosphorylation
phosphorylation
direct interaction
physical interaction
EBI-1371656
EBI-603094
EBI-60
intact10094392
12769847
12769847
11574463
14667819
WASP_HUMANphosphorylation
phosphorylation
EBI-603094
EBI-603083
intact12769847
12769847
ZHX1_HUMANphysical interactionEBI-729834
intact16169070
PML_HUMANphosphorylation
phosphorylation
EBI-983533
EBI-983553
intact16873060
16873060
ARRB2_HUMANin vitro
in vivo
HPRD:00277HPRD11877451
APEX1_HUMANin vitroHPRD:00277HPRD10023679
CD20_HUMANin vitroHPRD:00277HPRD7678037
BRCA1_HUMANin vitroHPRD:00277HPRD10403822
CASQ2_HUMANin vitro
in vivo
HPRD:00277HPRD1985907
CAV1_HUMANin vitroHPRD:00277HPRD8058322
HDAC1_HUMANin vitroHPRD:00277HPRD11602581
HCLS1_HUMANin vitroHPRD:00277HPRD10806407
IF5_HUMANin vitro
in vivo
HPRD:00277HPRD11861906
GMFB_HUMANin vitroHPRD:00277HPRD9030586
7598724
PTEN_HUMANin vitro
in vivo
HPRD:00277HPRD12297295
VDR_HUMANin vitroHPRD:00277HPRD8622969
IPP2_HUMANin vitroHPRD:00277HPRD8288648
BID_HUMANin vitro
in vivo
HPRD:00277HPRD11583622
4EBP1_HUMANin vitro
in vivo
HPRD:00277HPRD9806882
11146653
12588975
TF7L2_HUMANin vitroHPRD:00277HPRD11711551
PP1R8_HUMANin vitroHPRD:00277HPRD9407077
IL16_HUMANin vitro
in vivo
HPRD:00277HPRD12450396
KIF1C_HUMANin vitro
in vivo
HPRD:00277HPRD10559254
EI2BE_HUMANin vitro
in vivo
HPRD:00277HPRD11500362
PPR1B_HUMANin vitroHPRD:00277HPRD2557337
FAF1_HUMANin vitroHPRD:00277HPRD11378439
11713579
CTDP1_HUMANin vitro
in vivo
HPRD:00277HPRD12591939
CDC37_HUMANin vivoHPRD:00277HPRD12930845
15082798
RGS19_HUMANin vivoHPRD:00277HPRD10760275
10993892
HDAC2_HUMANin vitro
in vivo
HPRD:00277HPRD12176973
12082111
NOL3_HUMANin vitro
in vivo
HPRD:00277HPRD12191471
TF2AY_HUMANin vitroHPRD:00277HPRD12107178
SPIB_HUMANin vitro
in vivo
HPRD:00277HPRD8632909
10618498
VAMP4_HUMANin vitroHPRD:00277HPRD14608369
15345747
PACS1_HUMANin vitro
in vivo
HPRD:00277HPRD14633983
ERH_HUMANin vitroHPRD:00277HPRD9074495
HS105_HUMANin vitroHPRD:00277HPRD12558502
10772927
ACCN3_HUMANin vitroHPRD:00277HPRD9886053
UB2R2_HUMANin vitro
in vivo
HPRD:00277HPRD12037680
GBRR1_HUMANin vitroHPRD:00277HPRD12175859
KLF1_HUMANin vitro
in vivo
HPRD:00277HPRD9722526
PRGR_HUMANin vitroHPRD:00277HPRD7983041
PSA3_HUMANin vitro
in vivo
HPRD:00277HPRD8619999
CTNB1_HUMANin vitro
in vivo
HPRD:00277HPRD12432063
12700239
MPIP2_HUMANin vitro
in vivo
HPRD:00277HPRD12527891
CLCB_HUMANin vitroHPRD:00277HPRD3128543
ATF1_HUMANin vitro
in vivo
HPRD:00277HPRD9685505
CREM_HUMANin vitro
in vivo
HPRD:00277HPRD8404858
DDIT3_HUMANin vitroHPRD:00277HPRD12876286
DNL1_HUMANin vivoHPRD:00277HPRD10523317
15302935
TOP2A_HUMANin vivoHPRD:00277HPRD9804834
8939955
11940573
EGR1_HUMANin vitro
in vivo
HPRD:00277HPRD8662759
GYS1_HUMANin vitroHPRD:00277HPRD2117608
HS90A_HUMANin vitro
in vivo
HPRD:00277HPRD7794926
2492519
HSF1_HUMANin vitroHPRD:00277HPRD12659875
HXB7_HUMANin vitroHPRD:00277HPRD11290787
IBP3_HUMANin vitro
in vivo
HPRD:00277HPRD10650937
IRS1_HUMANin vitroHPRD:00277HPRD8349691
IF16_HUMANin vitroHPRD:00277HPRD11115400
STMN1_HUMANin vitro
in vivo
HPRD:00277HPRD8376365
8002936
CD45_HUMANin vivoHPRD:00277HPRD10066810
CD5_HUMANin vitro
in vivo
HPRD:00277HPRD9834084
LEG3_HUMANin vitro
in vivo
HPRD:00277HPRD10961987
8253806
MAX_HUMANin vitro
in vivo
HPRD:00277HPRD11535131
8247525
MYF5_HUMANin vitroHPRD:00277HPRD9461343
SYUA_HUMANin vitro
in vivo
HPRD:00277HPRD10617630
10852916
IKBA_HUMANin vitro
in vivo
HPRD:00277HPRD8622692
10398585
TF65_HUMANin vitro
in vivo
HPRD:00277HPRD10938077
HNRPC_HUMANin vitro
in vivo
HPRD:00277HPRD12564933
MYCN_HUMANin vitro
in vivo
HPRD:00277HPRD1425701
JUN_HUMANin vitro
in vivo
HPRD:00277HPRD9685505
1516134
OSTP_HUMANin vitroHPRD:00277HPRD8663267
G6PI_HUMANin vitro
in vivo
HPRD:00277HPRD11004567
PTN1_HUMANin vitro
in vivo
HPRD:00277HPRD8491187
9600099
RAD_HUMANin vitroHPRD:00277HPRD7876254
9677319
STX1A_HUMANin vitro
in vivo
HPRD:00277HPRD10844023
9930733
SP1_HUMANin vitroHPRD:00277HPRD9153193
MYB_HUMANin vitro
in vivo
HPRD:00277HPRD11313925
MYC_HUMANin vivoHPRD:00277HPRD2663470
P53_HUMANin vitro
in vivo
HPRD:00277HPRD10747897
10348343
10884347
11709713
11883897
10951572
12628923
CADH1_HUMANin vitro
in vivo
HPRD:00277HPRD10671552
VMAT2_HUMANin vitroHPRD:00277HPRD9045708
VTNC_HUMANin vitro
in vivo
HPRD:00277HPRD9733784
ACACA_HUMANin vitroHPRD:00277HPRD2900140
FA5_HUMANin vivoHPRD:00277HPRD9525959
PIN4_HUMANin vitro
in vivo
HPRD:00277HPRD12860119
WASP_HUMANin vitro
in vivo
HPRD:00277HPRD12769847
L1CAM_HUMANin vitroHPRD:00277HPRD8592152
SAT1_HUMANin vitroHPRD:00277HPRD8954982
AQP4_HUMANin vitroHPRD:00277HPRD11742978
TCP4_HUMANin vitro
in vivo
HPRD:00277HPRD7809103
TF2AA_HUMANin vitro
in vivo
HPRD:00277HPRD11278496
NKX25_HUMANin vivoHPRD:00277HPRD9858576
SRF_HUMANin vitroHPRD:00277HPRD1740119
2046671
EF1B_HUMANin vivoHPRD:00277HPRD14729942
15302935
8547318
15345747
MEF2C_HUMANin vitro
in vivo
HPRD:00277HPRD8663403
HMGA1_HUMANin vitroHPRD:00277HPRD11034995
2806554
PSN2_HUMANin vitro
in vivo
HPRD:00277HPRD8972483
9990034
9558331
MAZ_HUMANin vitro
in vivo
HPRD:00277HPRD10448092
ABCA1_HUMANin vitroHPRD:00277HPRD15218032
ZHX1_HUMANyeast 2-hybridHPRD:00277HPRD16169070
CSK21_HUMANin vivoHPRD:00277HPRD2192260
PRIO_HUMANin vitroHPRD:00277HPRD11062072
SSRP1_HUMANin vitroHPRD:00277HPRD15659405
CUTL2_HUMANin vitroHPRD:00277HPRD9446557
HMOX2_HUMANin vitroHPRD:00277HPRD14527438
XRCC1_HUMANin vitroHPRD:00277HPRD15066279
IF2B_HUMANin vitroHPRD:00277HPRD8024572
HDAC3_HUMANin vitroHPRD:00277HPRD15805470
RBX2_HUMANin vitroHPRD:00277HPRD12748192
JAM1_HUMANin vitroHPRD:00277HPRD7646439
XRCC4_HUMANin vitro
in vivo
HPRD:00277HPRD15385968
NOLC1_HUMANin vitroHPRD:00277HPRD7657714
CASP2_HUMANin vitro
in vivo
HPRD:00277HPRD16193064
RAGP1_HUMANin vitroHPRD:00277HPRD16428860
TSPY1_HUMANin vitroHPRD:00277HPRD16426576
SHOX_HUMANin vitroHPRD:00277HPRD16325853
ARNT_HUMANin vitroHPRD:00277HPRD16129408
THIC_HUMANin vitroHPRD:00277HPRD16331323
PEDF_HUMANin vitroHPRD:00277HPRD16322471
HES6_HUMANin vitroHPRD:00277HPRD12972610
AIP_HUMANin vitroHPRD:00277HPRD12361709
C1R_HUMANin vivoHPRD:00277HPRD8635594
NEUM_HUMANin vitroHPRD:00277HPRD1828073
FKBP4_HUMANin vitroHPRD:00277HPRD9405642
HIF1A_HUMANin vitroHPRD:00277HPRD17382325
SPTB2_HUMANin vitro
in vivo
HPRD:00277HPRD17088250
XRCC1_HUMANENSP00000339247STRING
SSRP1_HUMANENSP00000339247STRING
DVL3_HUMANENSP00000339247STRING
CTNB1_HUMANENSP00000339247STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation of casein kinase II by p34cdc2. Identification ofphosphorylation sites using phosphorylation site mutants in vitro.";
Bosc D.G., Slominski E., Sichler C., Litchfield D.W.;
J. Biol. Chem. 270:25872-25878(1995).
Cited for: PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-194; SER-362 ANDSER-370, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-7; TYR-50;TYR-125; THR-127; TYR-255; SER-277 AND SER-287, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures