GGCT_HUMAN - dbPTM
GGCT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GGCT_HUMAN
UniProt AC O75223
Protein Name Gamma-glutamylcyclotransferase
Gene Name GGCT
Organism Homo sapiens (Human).
Sequence Length 188
Subcellular Localization
Protein Description Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis..
Protein Sequence MANSGCKDVTGPDEESFLYFAYGSNLLTERIHLRNPSAAFFCVARLQDFKLDFGNSQGKTSQTWHGGIATIFQSPGDEVWGVVWKMNKSNLNSLDEQEGVKSGMYVVIEVKVATQEGKEITCRSYLMTNYESAPPSPQYKKIICMGAKENGLPLEYQEKLKAIEPNDYTGKVSEEIEDIIKKGETQTL
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
16PhosphorylationVTGPDEESFLYFAYG
CCCCCHHHHHHEEEC
20.6427251275
24PhosphorylationFLYFAYGSNLLTERI
HHHEEECCCCCEEEE
16.1922673903
37PhosphorylationRIHLRNPSAAFFCVA
EEECCCCCHHHHHEE
35.4620873877
42GlutathionylationNPSAAFFCVARLQDF
CCCHHHHHEEECCEE
1.5722555962
50AcetylationVARLQDFKLDFGNSQ
EEECCEEEEECCCCC
56.2727452117
56PhosphorylationFKLDFGNSQGKTSQT
EEEECCCCCCCCCCE
40.4627794612
89PhosphorylationVVWKMNKSNLNSLDE
EEEEECHHHCCCCCC
41.3628348404
93PhosphorylationMNKSNLNSLDEQEGV
ECHHHCCCCCCCCCC
40.1225849741
118AcetylationKVATQEGKEITCRSY
EEEECCCCEEEEEEE
45.2326051181
118UbiquitinationKVATQEGKEITCRSY
EEEECCCCEEEEEEE
45.23-
128PhosphorylationTCRSYLMTNYESAPP
EEEEEEECCCCCCCC
31.8627080861
130PhosphorylationRSYLMTNYESAPPSP
EEEEECCCCCCCCCC
11.3327080861
132PhosphorylationYLMTNYESAPPSPQY
EEECCCCCCCCCCCC
35.4027080861
136PhosphorylationNYESAPPSPQYKKII
CCCCCCCCCCCCEEE
24.4725159151
139PhosphorylationSAPPSPQYKKIICMG
CCCCCCCCCEEEEEC
20.0323917254
140UbiquitinationAPPSPQYKKIICMGA
CCCCCCCCEEEEECC
32.0421890473
140AcetylationAPPSPQYKKIICMGA
CCCCCCCCEEEEECC
32.0426051181
140 (in isoform 1)Ubiquitination-32.0421890473
141UbiquitinationPPSPQYKKIICMGAK
CCCCCCCEEEEECCH
32.16-
148AcetylationKIICMGAKENGLPLE
EEEEECCHHHCCCHH
46.0826051181
159UbiquitinationLPLEYQEKLKAIEPN
CCHHHHHHHHCCCCC
39.50-
161UbiquitinationLEYQEKLKAIEPNDY
HHHHHHHHCCCCCCC
59.39-
168PhosphorylationKAIEPNDYTGKVSEE
HCCCCCCCCCCCHHH
24.8322673903
169PhosphorylationAIEPNDYTGKVSEEI
CCCCCCCCCCCHHHH
33.1322673903
173PhosphorylationNDYTGKVSEEIEDII
CCCCCCCHHHHHHHH
32.7626657352
1812-HydroxyisobutyrylationEEIEDIIKKGETQTL
HHHHHHHHHCCCCCC
55.87-
187PhosphorylationIKKGETQTL------
HHHCCCCCC------
41.6824719451

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 GGCT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GGCT_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 GGCT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ITPA_HUMANITPAphysical
26344197
SCLY_HUMANSCLYphysical
26344197
WDR1_HUMANWDR1physical
26344197

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 GGCT_HUMAN

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Related Literatures of Post-Translational Modification

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