| UniProt ID | DCE2_RAT | |
|---|---|---|
| UniProt AC | Q05683 | |
| Protein Name | Glutamate decarboxylase 2 | |
| Gene Name | Gad2 | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 585 | |
| Subcellular Localization |
Cytoplasm, cytosol. Cytoplasmic vesicle. Cell junction, synapse, presynaptic cell membrane Lipid-anchor. Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side. Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Go |
|
| Protein Description | Catalyzes the production of GABA.. | |
| Protein Sequence | MASPGSGFWSFGSEDGSGDPENPGTARAWCQVAQKFTGGIGNKLCALLYGDSEKPAESGGSVTSRAATRKVACTCDQKPCSCPKGDVNYALLHATDLLPACEGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILTHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMLIARYKMFPEVKEKGMAAVPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEVKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHIDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWFVPPSLRVLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MASPGSGFWS -----CCCCCCCCCC | 28.61 | 22673903 | |
| 6 | Phosphorylation | --MASPGSGFWSFGS --CCCCCCCCCCCCC | 33.91 | 8999827 | |
| 10 | Phosphorylation | SPGSGFWSFGSEDGS CCCCCCCCCCCCCCC | 19.91 | 22817900 | |
| 13 | Phosphorylation | SGFWSFGSEDGSGDP CCCCCCCCCCCCCCC | 30.42 | 22817900 | |
| 17 | Phosphorylation | SFGSEDGSGDPENPG CCCCCCCCCCCCCCH | 52.96 | 22673903 | |
| 30 | S-palmitoylation | PGTARAWCQVAQKFT CHHHHHHHHHHHHHH | 1.97 | 8132714 | |
| 45 | S-nitrosylation | GGIGNKLCALLYGDS CCHHHHHHHHHHCCC | 2.40 | 22178444 | |
| 45 | S-palmitoylation | GGIGNKLCALLYGDS CCHHHHHHHHHHCCC | 2.40 | 8132714 | |
| 54 | Acetylation | LLYGDSEKPAESGGS HHHCCCCCCCCCCCC | 54.18 | 22902405 | |
| 78 | Ubiquitination | VACTCDQKPCSCPKG EEEECCCCCCCCCCC | 34.44 | - | |
| 95 | Phosphorylation | NYALLHATDLLPACE CHHEEEHHHCHHHCC | 19.21 | - | |
| 286 | Acetylation | EHSHFSLKKGAAALG CCCCCCCCCCHHHCC | 48.22 | 22902405 | |
| 396 | N6-(pyridoxal phosphate)lysine | SVTWNPHKMMGVPLQ CCCCCHHHCCCCCCC | 31.66 | - | |
| 396 | Other | SVTWNPHKMMGVPLQ CCCCCHHHCCCCCCC | 31.66 | - | |
| 417 | Phosphorylation | REEGLMQSCNQMHAS CHHHHHHHHHHHHHH | 10.89 | - |
| 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 DCE2_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DCE2_RAT !! | ||||||
* 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 DCE2_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DCE2_RAT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Palmitoylation | |
| Reference | PubMed |
| "Amino acid residues 24-31 but not palmitoylation of cysteines 30 and45 are required for membrane anchoring of glutamic acid decarboxylase,GAD65."; Shi Y., Veit B., Baekkeskov S.; J. Cell Biol. 124:927-934(1994). Cited for: PALMITOYLATION AT CYS-30 AND CYS-45, AND MUTAGENESIS OF CYS-30;CYS-45; CYS-73; CYS-75; CYS-80; CYS-82 AND CYS-101. | |
| "Membrane anchoring of the autoantigen GAD65 to microvesicles inpancreatic beta-cells by palmitoylation in the NH2-terminal domain."; Christgau S., Aanstoot H.-J., Schierbeck H., Begley K., Tullin S.,Hejnaes K., Baekkeskov S.; J. Cell Biol. 118:309-320(1992). Cited for: SUBCELLULAR LOCATION, AND PALMITOYLATION. | |
| Phosphorylation | |
| Reference | PubMed |
| "Phosphorylation of serine residues 3, 6, 10, and 13 distinguishesmembrane anchored from soluble glutamic acid decarboxylase 65 and isrestricted to glutamic acid decarboxylase 65alpha."; Namchuk M., Lindsay L., Turck C.W., Kanaani J., Baekkeskov S.; J. Biol. Chem. 272:1548-1557(1997). Cited for: PHOSPHORYLATION AT SER-3; SER-6; SER-10 AND SER-13, ANDBIOPHYSICOCHEMICAL PROPERTIES. | |