UniProt ID | CSK21_HUMAN | |
---|---|---|
UniProt AC | P68400 | |
Protein Name | Casein kinase II subunit alpha | |
Gene Name | CSNK2A1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 391 | |
Subcellular Localization | Nucleus . | |
Protein 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. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. [PubMed: 11239457] | |
Protein Sequence | MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSGPVPSRA ------CCCCCCCCC | 52.37 | 17192257 | |
7 | Phosphorylation | -MSGPVPSRARVYTD -CCCCCCCCCEEEEE | 38.51 | 19369195 | |
12 | Phosphorylation | VPSRARVYTDVNTHR CCCCCEEEEECCCCC | 7.53 | 28152594 | |
13 | Phosphorylation | PSRARVYTDVNTHRP CCCCEEEEECCCCCC | 30.52 | 28152594 | |
17 | Phosphorylation | RVYTDVNTHRPREYW EEEEECCCCCCHHHC | 21.07 | 28152594 | |
22 | Ubiquitination | VNTHRPREYWDYESH CCCCCCHHHCCCCCC | 54.37 | 24816145 | |
44 | Ubiquitination | DDYQLVRKLGRGKYS HHHHHHHHHCCCCHH | 48.06 | 22817900 | |
49 | Acetylation | VRKLGRGKYSEVFEA HHHHCCCCHHHHHHE | 44.22 | 25953088 | |
49 | Ubiquitination | VRKLGRGKYSEVFEA HHHHCCCCHHHHHHE | 44.22 | 21906983 | |
50 | Phosphorylation | RKLGRGKYSEVFEAI HHHCCCCHHHHHHEE | 16.94 | 20090780 | |
51 | Phosphorylation | KLGRGKYSEVFEAIN HHCCCCHHHHHHEEE | 30.67 | 28152594 | |
60 | Phosphorylation | VFEAINITNNEKVVV HHHEEECCCCCEEEE | 27.74 | 20071362 | |
64 | Ubiquitination | INITNNEKVVVKILK EECCCCCEEEEEEEH | 42.31 | 33845483 | |
68 | Ubiquitination | NNEKVVVKILKPVKK CCCEEEEEEEHHHCH | 30.61 | 29967540 | |
71 | Ubiquitination | KVVVKILKPVKKKKI EEEEEEEHHHCHHHH | 51.76 | - | |
83 | Ubiquitination | KKIKREIKILENLRG HHHHHHHHHHHHCCC | 36.16 | 24816145 | |
89 | Methylation | IKILENLRGGPNIIT HHHHHHCCCCCCEEE | 60.65 | - | |
93 | Ubiquitination | ENLRGGPNIITLADI HHCCCCCCEEEHHHH | 41.38 | 22817900 | |
102 | 2-Hydroxyisobutyrylation | ITLADIVKDPVSRTP EEHHHHHCCCCCCCC | 57.56 | - | |
102 | Acetylation | ITLADIVKDPVSRTP EEHHHHHCCCCCCCC | 57.56 | 23954790 | |
102 | Ubiquitination | ITLADIVKDPVSRTP EEHHHHHCCCCCCCC | 57.56 | 23000965 | |
111 | Ubiquitination | PVSRTPALVFEHVNN CCCCCCEEEEEECCC | 4.83 | 22817900 | |
122 | Ubiquitination | HVNNTDFKQLYQTLT ECCCCCHHHHHHHHC | 42.05 | 21906983 | |
122 | Acetylation | HVNNTDFKQLYQTLT ECCCCCHHHHHHHHC | 42.05 | 22362441 | |
124 | Ubiquitination | NNTDFKQLYQTLTDY CCCCHHHHHHHHCHH | 3.36 | 33845483 | |
125 | Phosphorylation | NTDFKQLYQTLTDYD CCCHHHHHHHHCHHH | 9.28 | 28152594 | |
127 | Phosphorylation | DFKQLYQTLTDYDIR CHHHHHHHHCHHHHH | 20.33 | 28152594 | |
129 | Phosphorylation | KQLYQTLTDYDIRFY HHHHHHHCHHHHHHH | 35.58 | 28152594 | |
131 | Phosphorylation | LYQTLTDYDIRFYMY HHHHHCHHHHHHHHH | 14.18 | 24043423 | |
158 | Ubiquitination | GIMHRDVKPHNVMID CCCCCCCCCCCEEEE | 44.86 | 24816145 | |
163 | Sulfoxidation | DVKPHNVMIDHEHRK CCCCCCEEEECCCCH | 3.46 | 30846556 | |
182 | Phosphorylation | DWGLAEFYHPGQEYN HHHHHCCCCCCCCEE | 9.90 | 11439109 | |
188 | Phosphorylation | FYHPGQEYNVRVASR CCCCCCCEEEEEECH | 15.86 | 29496907 | |
193 | Ubiquitination | QEYNVRVASRYFKGP CCEEEEEECHHCCCC | 4.26 | 22817900 | |
193 | Ubiquitination | QEYNVRVASRYFKGP CCEEEEEECHHCCCC | 4.26 | 21890473 | |
194 | Phosphorylation | EYNVRVASRYFKGPE CEEEEEECHHCCCCE | 25.34 | 28355574 | |
196 | Phosphorylation | NVRVASRYFKGPELL EEEEECHHCCCCEEE | 13.72 | 23186163 | |
209 | Phosphorylation | LLVDYQMYDYSLDMW EEEEEECCCCCHHHH | 9.01 | - | |
217 | Phosphorylation | DYSLDMWSLGCMLAS CCCHHHHHHHHHHHH | 14.30 | 20068231 | |
229 | Malonylation | LASMIFRKEPFFHGH HHHHHHHCCCCCCCC | 60.02 | 26320211 | |
229 | Ubiquitination | LASMIFRKEPFFHGH HHHHHHHCCCCCCCC | 60.02 | 22817900 | |
239 | Phosphorylation | FFHGHDNYDQLVRIA CCCCCCCHHHHHHHH | 15.89 | 28152594 | |
247 | 2-Hydroxyisobutyrylation | DQLVRIAKVLGTEDL HHHHHHHHHHCCHHH | 35.30 | - | |
247 | Acetylation | DQLVRIAKVLGTEDL HHHHHHHHHHCCHHH | 35.30 | 23236377 | |
247 | Ubiquitination | DQLVRIAKVLGTEDL HHHHHHHHHHCCHHH | 35.30 | 21906983 | |
255 | Phosphorylation | VLGTEDLYDYIDKYN HHCCHHHHHHHHHCC | 21.01 | 12628006 | |
257 | Phosphorylation | GTEDLYDYIDKYNIE CCHHHHHHHHHCCCE | 9.47 | 28102081 | |
260 | Ubiquitination | DLYDYIDKYNIELDP HHHHHHHHCCCEECH | 30.55 | 21906983 | |
277 | Phosphorylation | NDILGRHSRKRWERF HHHCCHHHHHHHHHH | 37.83 | 19369195 | |
287 | Phosphorylation | RWERFVHSENQHLVS HHHHHCCCCCCCCCC | 32.70 | 30266825 | |
303 | Ubiquitination | EALDFLDKLLRYDHQ HHHHHHHHHHCCCHH | 52.12 | - | |
319 | Sulfoxidation | RLTAREAMEHPYFYT CCCHHHHHHCCCEEE | 4.10 | 30846556 | |
323 | Phosphorylation | REAMEHPYFYTVVKD HHHHHCCCEEEEEEC | 15.89 | 29496907 | |
326 | Phosphorylation | MEHPYFYTVVKDQAR HHCCCEEEEEECCCC | 14.66 | 26074081 | |
329 | Ubiquitination | PYFYTVVKDQARMGS CCEEEEEECCCCCCC | 39.52 | 22817900 | |
329 | Acetylation | PYFYTVVKDQARMGS CCEEEEEECCCCCCC | 39.52 | 23236377 | |
329 | 2-Hydroxyisobutyrylation | PYFYTVVKDQARMGS CCEEEEEECCCCCCC | 39.52 | - | |
336 | Phosphorylation | KDQARMGSSSMPGGS ECCCCCCCCCCCCCC | 15.19 | 20068231 | |
337 | Phosphorylation | DQARMGSSSMPGGST CCCCCCCCCCCCCCC | 25.56 | 20068231 | |
338 | Phosphorylation | QARMGSSSMPGGSTP CCCCCCCCCCCCCCC | 30.60 | 26074081 | |
343 | Phosphorylation | SSSMPGGSTPVSSAN CCCCCCCCCCCCCCC | 35.14 | 20068231 | |
344 | Phosphorylation | SSMPGGSTPVSSANM CCCCCCCCCCCCCCC | 30.86 | 7592773 | |
344 | O-linked_Glycosylation | SSMPGGSTPVSSANM CCCCCCCCCCCCCCC | 30.86 | 32830957 | |
347 | Phosphorylation | PGGSTPVSSANMMSG CCCCCCCCCCCCCCC | 25.57 | 26074081 | |
347 | O-linked_Glycosylation | PGGSTPVSSANMMSG CCCCCCCCCCCCCCC | 25.57 | 32830957 | |
348 | Phosphorylation | GGSTPVSSANMMSGI CCCCCCCCCCCCCCC | 24.72 | 26074081 | |
348 | O-linked_Glycosylation | GGSTPVSSANMMSGI CCCCCCCCCCCCCCC | 24.72 | 32830957 | |
353 | Phosphorylation | VSSANMMSGISSVPT CCCCCCCCCCCCCCC | 23.39 | 20068231 | |
356 | Phosphorylation | ANMMSGISSVPTPSP CCCCCCCCCCCCCCC | 28.89 | 20068231 | |
357 | Phosphorylation | NMMSGISSVPTPSPL CCCCCCCCCCCCCCC | 30.14 | 28348404 | |
360 | Phosphorylation | SGISSVPTPSPLGPL CCCCCCCCCCCCCCC | 33.95 | 7592773 | |
362 | Phosphorylation | ISSVPTPSPLGPLAG CCCCCCCCCCCCCCC | 34.92 | 7592773 | |
370 | Phosphorylation | PLGPLAGSPVIAAAN CCCCCCCCCEEEEEC | 15.47 | 7592773 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
13 | T | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
182 | Y | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
255 | Y | Phosphorylation | Kinase | FGR | P09769 | PhosphoELM |
255 | Y | Phosphorylation | Kinase | FGR | Q6P6U0 | PSP |
255 | Y | Phosphorylation | Kinase | LYN | P07948 | PhosphoELM |
255 | Y | Phosphorylation | Kinase | LYN | Q07014 | PSP |
344 | T | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
344 | T | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
344 | T | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
360 | T | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
360 | T | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
360 | T | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
360 | T | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
362 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
362 | S | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
362 | S | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
362 | S | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
370 | S | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
370 | S | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
370 | S | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CSK21_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. | |
"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. | |
"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. |