CRGC_HUMAN - dbPTM
CRGC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRGC_HUMAN
UniProt AC P07315
Protein Name Gamma-crystallin C
Gene Name CRYGC
Organism Homo sapiens (Human).
Sequence Length 174
Subcellular Localization
Protein Description Crystallins are the dominant structural components of the vertebrate eye lens..
Protein Sequence MGKITFYEDRAFQGRSYETTTDCPNLQPYFSRCNSIRVESGCWMLYERPNYQGQQYLLRRGEYPDYQQWMGLSDSIRSCCLIPQTVSHRLRLYEREDHKGLMMELSEDCPSIQDRFHLSEIRSLHVLEGCWVLYELPNYRGRQYLLRPQEYRRCQDWGAMDAKAGSLRRVVDLY
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
5Phosphorylation---MGKITFYEDRAF
---CCCEEEEECCCC
24.5325404012
7Phosphorylation-MGKITFYEDRAFQG
-CCCEEEEECCCCCC
14.3125404012
16PhosphorylationDRAFQGRSYETTTDC
CCCCCCCCEEECCCC
33.8624043423
17PhosphorylationRAFQGRSYETTTDCP
CCCCCCCEEECCCCC
18.8824043423
19PhosphorylationFQGRSYETTTDCPNL
CCCCCEEECCCCCCC
27.1124043423
20PhosphorylationQGRSYETTTDCPNLQ
CCCCEEECCCCCCCH
14.5424043423
21PhosphorylationGRSYETTTDCPNLQP
CCCEEECCCCCCCHH
42.9224043423
23MethylationSYETTTDCPNLQPYF
CEEECCCCCCCHHHH
1.9512876325
29PhosphorylationDCPNLQPYFSRCNSI
CCCCCHHHHHHCCCE
10.9624043423
31PhosphorylationPNLQPYFSRCNSIRV
CCCHHHHHHCCCEEE
30.0424043423
63PhosphorylationYLLRRGEYPDYQQWM
HHHHCCCCCCHHHHH
12.2922817900
66PhosphorylationRRGEYPDYQQWMGLS
HCCCCCCHHHHHCCC
9.7122817900
80MethylationSDSIRSCCLIPQTVS
CHHHHHHCCCCHHHH
3.99-
119PhosphorylationIQDRFHLSEIRSLHV
HHHHHCHHHHHHHHH
23.5424719451

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 CRGC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRGC_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 CRGC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRYAA_HUMANCRYAAphysical
11700327
CRYAB_HUMANCRYABphysical
11700327
CRBB2_HUMANCRYBB2physical
11700327
CRGC_HUMANCRYGCphysical
11700327
CRGC_HUMANCRYGCphysical
12601044
CRYAA_HUMANCRYAAphysical
12601044
CRYAB_HUMANCRYABphysical
12601044
CRBB2_HUMANCRYBB2physical
12601044
CRGD_HUMANCRYGDphysical
12601044
HSPB1_HUMANHSPB1physical
12601044
HSPB2_HUMANHSPB2physical
12601044
CRGB_HUMANCRYGBphysical
26186194
CRGB_HUMANCRYGBphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604307Cataract 2, multiple types (CTRCT2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRGC_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Methylation and carbamylation of human gamma-crystallins.";
Lapko V.N., Smith D.L., Smith J.B.;
Protein Sci. 12:1762-1774(2003).
Cited for: METHYLATION AT CYS-23, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Shotgun identification of protein modifications from proteincomplexes and lens tissue.";
MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M.,Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I.,Yates J.R. III;
Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63 AND TYR-66,SUSCEPTIBILITY TO OXIDATION, AND MASS SPECTROMETRY.

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