KC1G1_HUMAN - dbPTM
KC1G1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KC1G1_HUMAN
UniProt AC Q9HCP0
Protein Name Casein kinase I isoform gamma-1
Gene Name CSNK1G1
Organism Homo sapiens (Human).
Sequence Length 422
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. Regulates fast synaptic transmission mediated by glutamate (By similarity). Phosphorylates CLSPN..
Protein Sequence MDHPSREKDERQRTTKPMAQRSAHCSRPSGSSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLGSAGEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLLSRMEYVHSKNLIYRDVKPENFLIGRQGNKKEHVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRNTPIEALCENFPEEMATYLRYVRRLDFFEKPDYEYLRTLFTDLFEKKGYTFDYAYDWVGRPIPTPVGSVHVDSGASAITRESHTHRDRPSQQQPLRNQVVSSTNGELNVDDPTGAHSNAPITAHAEVEVVEEAKCCCFFKRKRKKTAQRHK
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
14PhosphorylationEKDERQRTTKPMAQR
HHHHHHHCCCCHHHH
30.73-
15PhosphorylationKDERQRTTKPMAQRS
HHHHHHCCCCHHHHH
35.03-
22PhosphorylationTKPMAQRSAHCSRPS
CCCHHHHHHHCCCCC
15.4127422710
26PhosphorylationAQRSAHCSRPSGSSS
HHHHHHCCCCCCCCC
37.0429449344
29PhosphorylationSAHCSRPSGSSSSSG
HHHCCCCCCCCCCCC
50.6327422710
31PhosphorylationHCSRPSGSSSSSGVL
HCCCCCCCCCCCCEE
31.2421712546
32PhosphorylationCSRPSGSSSSSGVLM
CCCCCCCCCCCCEEE
37.4529449344
33PhosphorylationSRPSGSSSSSGVLMV
CCCCCCCCCCCEEEE
30.1628555341
34PhosphorylationRPSGSSSSSGVLMVG
CCCCCCCCCCEEEEC
32.8129449344
35PhosphorylationPSGSSSSSGVLMVGP
CCCCCCCCCEEEECC
34.5629449344
49UbiquitinationPNFRVGKKIGCGNFG
CCCCCCCEECCCCCC
38.10-
62UbiquitinationFGELRLGKNLYTNEY
CCEEECCCCCCCCCE
48.66-
65PhosphorylationLRLGKNLYTNEYVAI
EECCCCCCCCCEEEE
19.5328152594
66PhosphorylationRLGKNLYTNEYVAIK
ECCCCCCCCCEEEEE
25.4128152594
69PhosphorylationKNLYTNEYVAIKLEP
CCCCCCCEEEEEEEE
9.3928152594
88PhosphorylationAPQLHLEYRFYKQLG
CCCHHHHHHHHHHHC
16.6320071362
91PhosphorylationLHLEYRFYKQLGSAG
HHHHHHHHHHHCCCC
6.7120071362
96PhosphorylationRFYKQLGSAGEGLPQ
HHHHHHCCCCCCCCE
41.51-
135PhosphorylationLFDLCDRTFTLKTVL
HHHHHCCCCHHHHHH
14.0220068231
137PhosphorylationDLCDRTFTLKTVLMI
HHHCCCCHHHHHHHH
27.08-
140PhosphorylationDRTFTLKTVLMIAIQ
CCCCHHHHHHHHHHH
23.22-
162PhosphorylationVHSKNLIYRDVKPEN
HHHCCEECCCCCHHH
12.15-
166UbiquitinationNLIYRDVKPENFLIG
CEECCCCCHHHEEEE
51.40-
194PhosphorylationDFGLAKEYIDPETKK
ECCCCHHHCCHHHHC
15.21-
217PhosphorylationSLTGTARYMSINTHL
CCCCCCEEEEHHHHC
7.8629496907
255UbiquitinationSLPWQGLKADTLKER
CCCCCCCCHHHHHHH
51.5521890473
255 (in isoform 1)Ubiquitination-51.5521890473
255 (in isoform 2)Ubiquitination-51.5521890473
255UbiquitinationSLPWQGLKADTLKER
CCCCCCCCHHHHHHH
51.55-
258PhosphorylationWQGLKADTLKERYQK
CCCCCHHHHHHHHHH
44.5917192257
263PhosphorylationADTLKERYQKIGDTK
HHHHHHHHHHHCCCC
18.4318083107
265UbiquitinationTLKERYQKIGDTKRN
HHHHHHHHHCCCCCC
39.46-
273PhosphorylationIGDTKRNTPIEALCE
HCCCCCCCHHHHHHH
29.6724114839
288PhosphorylationNFPEEMATYLRYVRR
CCCHHHHHHHHHHHH
23.0622210691
289PhosphorylationFPEEMATYLRYVRRL
CCHHHHHHHHHHHHC
4.6124114839
309PhosphorylationPDYEYLRTLFTDLFE
CCHHHHHHHHHHHHH
24.51-
317UbiquitinationLFTDLFEKKGYTFDY
HHHHHHHHCCCEEEE
44.132190698
317 (in isoform 1)Ubiquitination-44.1321890473
317 (in isoform 2)Ubiquitination-44.1321890473
344PhosphorylationVGSVHVDSGASAITR
CEEEEECCCCCEECC
34.8617192257
347PhosphorylationVHVDSGASAITRESH
EEECCCCCEECCCCC
24.5918691976
361PhosphorylationHTHRDRPSQQQPLRN
CCCCCCCHHCCCCHH
41.3321082442
373PhosphorylationLRNQVVSSTNGELNV
CHHHHHHCCCCCCCC
17.8123663014
374PhosphorylationRNQVVSSTNGELNVD
HHHHHHCCCCCCCCC
39.4723663014
411UbiquitinationAKCCCFFKRKRKKTA
HEEEEEEHHHCHHHH
36.44-

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 KC1G1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KC1G1_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 KC1G1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDCP_HUMANC2orf44physical
21900206
IKZF1_HUMANIKZF1physical
21900206
F219A_HUMANFAM219Aphysical
21900206
MKRN1_HUMANMKRN1physical
21900206
RUN3B_HUMANRUNDC3Bphysical
21900206
A4_HUMANAPPphysical
21832049
TRAF6_HUMANTRAF6physical
24442433
TF65_HUMANRELAphysical
24442433
CEP76_HUMANCEP76physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KC1G2_HUMANCSNK1G2physical
26186194
KC1G2_HUMANCSNK1G2physical
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 KC1G1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-344 AND SER-361, ANDMASS SPECTROMETRY.

TOP