DCE1_HUMAN - dbPTM
DCE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCE1_HUMAN
UniProt AC Q99259
Protein Name Glutamate decarboxylase 1
Gene Name GAD1
Organism Homo sapiens (Human).
Sequence Length 594
Subcellular Localization
Protein Description Catalyzes the production of GABA..
Protein Sequence MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEKSRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEVVDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWSSKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAPKIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
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---MASSTPSSSATS
---CCCCCCCCCCCC
25.3722210691
22PhosphorylationAGADPNTTNLRPTTY
CCCCCCCCCCCCCCH
38.6122210691
28PhosphorylationTTNLRPTTYDTWCGV
CCCCCCCCHHHHCHH
23.2922210691
60UbiquitinationRTNSLEEKSRLVSAF
HCCCHHHHHHHHHHH
31.34-
61PhosphorylationTNSLEEKSRLVSAFK
CCCHHHHHHHHHHHH
33.8423898821
65PhosphorylationEEKSRLVSAFKERQS
HHHHHHHHHHHHHHH
32.3623898821
68UbiquitinationSRLVSAFKERQSSKN
HHHHHHHHHHHHCCC
52.26-
74UbiquitinationFKERQSSKNLLSCEN
HHHHHHCCCCCCCCC
57.78-
78PhosphorylationQSSKNLLSCENSDRD
HHCCCCCCCCCCHHH
23.66-
91DephosphorylationRDARFRRTETDFSNL
HHHHHHCCCCHHHHH
38.6915147202
91PhosphorylationRDARFRRTETDFSNL
HHHHHHCCCCHHHHH
38.6915147202
175PhosphorylationILVDCRDTLKYGVRT
HHHHHHHHHHHCCCC
13.0527251275
175 (in isoform 3)Phosphorylation-13.0527251275
182 (in isoform 3)Phosphorylation-37.1227251275
192 (in isoform 3)Phosphorylation-15.6327251275
193PhosphorylationRFFNQLSTGLDIIGL
HHHHHHHCCCCCEEE
50.8127251275
193 (in isoform 3)Phosphorylation-50.8127251275
265PhosphorylationYSIMAARYKYFPEVK
HHHHHHHHHHCCCCC
12.81-
293PhosphorylationTSEQSHYSIKKAGAA
ECCCCCCCCCHHHHC
23.6224719451
405N6-(pyridoxal phosphate)lysineSVTWNPHKMMGVLLQ
CCCCCHHHHHHHHHH
31.66-
405OtherSVTWNPHKMMGVLLQ
CCCCCHHHHHHHHHH
31.66-
489PhosphorylationKCLELAEYLYAKIKN
HHHHHHHHHHHHHCC
10.2118083107
491PhosphorylationLELAEYLYAKIKNRE
HHHHHHHHHHHCCHH
12.6318083107
571PhosphorylationNFFRMVISNPAATQS
CEEEEHHCCCCCCHH
25.9218452278
578PhosphorylationSNPAATQSDIDFLIE
CCCCCCHHHHHHHHH
31.98-

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
91TPhosphorylationKinasePRKACAP17612
GPS
91TPhosphorylationKinasePKA-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCE1_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 DCE1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
3HAO_HUMANHAAOphysical
16189514
DCE2_HUMANGAD2physical
7836456
STK3_HUMANSTK3physical
25416956
3HAO_HUMANHAAOphysical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
CKLF5_HUMANCMTM5physical
25416956
FGFR1_HUMANFGFR1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603513Cerebral palsy, spastic quadriplegic 1 (CPSQ1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCE1_HUMAN

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Related Literatures of Post-Translational Modification

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