KC1G2_HUMAN - dbPTM
KC1G2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC1G2_HUMAN
UniProt AC P78368
Protein Name Casein kinase I isoform gamma-2
Gene Name CSNK1G2
Organism Homo sapiens (Human).
Sequence Length 415
Subcellular Localization Cytoplasm .
Protein Description Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation..
Protein Sequence MDFDKKGGKGETEEGRRMSKAGGGRSSHGIRSSGTSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLSATEGVPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLITRMEYVHTKSLIYRDVKPENFLVGRPGTKRQHAIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRSGFVFDYEYDWAGKPLPTPIGTVHTDLPSQPQLRDKTQPHSKNQALNSTNGELNADDPTAGHSNAPITAPAEVEVADETKCCCFFKRRKRKSLQRHK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
25MethylationMSKAGGGRSSHGIRS
HCCCCCCCCCCCCCC		37.96-
26PhosphorylationSKAGGGRSSHGIRSS
CCCCCCCCCCCCCCC		29.9326437602
27PhosphorylationKAGGGRSSHGIRSSG
CCCCCCCCCCCCCCC		25.1129052541
32PhosphorylationRSSHGIRSSGTSSGV
CCCCCCCCCCCCCCE		31.0618691976
33PhosphorylationSSHGIRSSGTSSGVL
CCCCCCCCCCCCCEE		35.9228857561
35PhosphorylationHGIRSSGTSSGVLMV
CCCCCCCCCCCEEEE		22.9728348404
36PhosphorylationGIRSSGTSSGVLMVG
CCCCCCCCCCEEEEC		28.7228857561
37PhosphorylationIRSSGTSSGVLMVGP
CCCCCCCCCEEEECC		32.5323312004
51MalonylationPNFRVGKKIGCGNFG
CCCCCCCEECCCCCC		38.1026320211
51UbiquitinationPNFRVGKKIGCGNFG
CCCCCCCEECCCCCC		38.1033845483
64AcetylationFGELRLGKNLYTNEY
CCEEECCCCCCCCCE		48.6626051181
64UbiquitinationFGELRLGKNLYTNEY
CCEEECCCCCCCCCE		48.66-
67PhosphorylationLRLGKNLYTNEYVAI
EECCCCCCCCCEEEE		19.5328152594
68PhosphorylationRLGKNLYTNEYVAIK
ECCCCCCCCCEEEEE		25.4128152594
71PhosphorylationKNLYTNEYVAIKLEP
CCCCCCCEEEEEEEE		9.3928152594
90PhosphorylationAPQLHLEYRFYKQLS
CCCHHEEEHHHHHHH		16.6320071362
93PhosphorylationLHLEYRFYKQLSATE
HHEEEHHHHHHHCCC		6.7120071362
136PhosphorylationLFDLCDRTFTLKTVL
HHHHHCCCCHHHHHH		14.0220068231
138PhosphorylationDLCDRTFTLKTVLMI
HHHCCCCHHHHHHHH		27.0820068231
141PhosphorylationDRTFTLKTVLMIAIQ
CCCCHHHHHHHHHHH		23.2220068231
151PhosphorylationMIAIQLITRMEYVHT
HHHHHHHHHCCCCCC		32.3320068231
158PhosphorylationTRMEYVHTKSLIYRD
HHCCCCCCCCEECCC		16.57-
167UbiquitinationSLIYRDVKPENFLVG
CEECCCCCHHHEECC		51.4029967540
195PhosphorylationDFGLAKEYIDPETKK
EECCCHHHCCHHHHC		15.21-
201UbiquitinationEYIDPETKKHIPYRE
HHCCHHHHCCCCCCC		40.4632015554
208UbiquitinationKKHIPYREHKSLTGT
HCCCCCCCCCCCCCC		50.2321890473
213UbiquitinationYREHKSLTGTARYMS
CCCCCCCCCCCEEEE		39.3123000965
218PhosphorylationSLTGTARYMSINTHL
CCCCCCEEEEHHHHC		7.8629496907
218UbiquitinationSLTGTARYMSINTHL
CCCCCCEEEEHHHHC		7.8627667366
256UbiquitinationSLPWQGLKADTLKER
CCCCCCCCHHHHHHH		51.5521890473
256UbiquitinationSLPWQGLKADTLKER
CCCCCCCCHHHHHHH		51.5523000965
259PhosphorylationWQGLKADTLKERYQK
CCCCCHHHHHHHHHH		44.5917192257
261UbiquitinationGLKADTLKERYQKIG
CCCHHHHHHHHHHHC		42.0923000965
264PhosphorylationADTLKERYQKIGDTK
HHHHHHHHHHHCCCC		18.4322817900
266UbiquitinationTLKERYQKIGDTKRA
HHHHHHHHHCCCCCC		39.4627667366
286UbiquitinationLCENFPEEMATYLRY
HHHCCCHHHHHHHHH		34.0623000965
291UbiquitinationPEEMATYLRYVRRLD
CHHHHHHHHHHHHCH		2.5023000965
296UbiquitinationTYLRYVRRLDFFEKP
HHHHHHHHCHHHCCC		28.6827667366
310UbiquitinationPDYDYLRKLFTDLFD
CCHHHHHHHHHHHHC		45.41-
336PhosphorylationWAGKPLPTPIGTVHT
CCCCCCCCCCCEECC		34.91-
359PhosphorylationRDKTQPHSKNQALNS
CCCCCCCCCCHHHHC		39.73-
366PhosphorylationSKNQALNSTNGELNA
CCCHHHHCCCCCCCC		24.8923401153
367PhosphorylationKNQALNSTNGELNAD
CCHHHHCCCCCCCCC		46.2825159151
377PhosphorylationELNADDPTAGHSNAP
CCCCCCCCCCCCCCC		52.8725159151
381PhosphorylationDDPTAGHSNAPITAP
CCCCCCCCCCCCCCC		33.5023403867
386PhosphorylationGHSNAPITAPAEVEV
CCCCCCCCCCCEEEE		26.0623403867
404UbiquitinationTKCCCFFKRRKRKSL
CCCCEEEHHHCCHHH		30.9229967540
410PhosphorylationFKRRKRKSLQRHK--
EHHHCCHHHHHCC--		33.49-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of KC1G2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC1G2_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 KC1G2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
C43BP_HUMANCOL4A3BPphysical
16189514
SMAD3_HUMANSMAD3physical
18794808
MTA1_HUMANMTA1physical
15077195
WDCP_HUMANC2orf44physical
21900206
RPGP1_HUMANRAP1GAPphysical
21900206
RUN3B_HUMANRUNDC3Bphysical
21900206
DBND2_HUMANDBNDD2physical
16618118
A4_HUMANAPPphysical
21832049
C43BP_HUMANCOL4A3BPphysical
25416956
APBP2_HUMANAPPBP2physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KC1G3_HUMANCSNK1G3physical
28514442
PSF2_HUMANGINS2physical
28514442
C43BP_HUMANCOL4A3BPphysical
28514442
SLD5_HUMANGINS4physical
28514442
DCA16_HUMANDCAF16physical
28514442
PSF3_HUMANGINS3physical
28514442
PSF1_HUMANGINS1physical
28514442
NISCH_HUMANNISCHphysical
28514442
Drug and Disease Associations
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.
Regulatory Network of KC1G2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-366, AND MASSSPECTROMETRY.
"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-366 AND THR-367, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory