UniProt ID | G3P_RABIT | |
---|---|---|
UniProt AC | P46406 | |
Protein Name | Glyceraldehyde-3-phosphate dehydrogenase | |
Gene Name | GAPDH | |
Organism | Oryctolagus cuniculus (Rabbit). | |
Sequence Length | 333 | |
Subcellular Localization | Cytoplasm, cytosol. Nucleus. Cytoplasm, cytoskeleton. Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal.. | |
Protein Description | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Also participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (By similarity).. | |
Protein Sequence | MVKVGVNGFGRIGRLVTRAAFNSGKVDVVAINDPFIDLHYMVYMFQYDSTHGKFHGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKAAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSATHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMVHMASKE | |
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 | "N6,N6-dimethyllysine" | -----MVKVGVNGFG -----CCEEECCCCC | 31.79 | - | |
3 | Methylation | -----MVKVGVNGFG -----CCEEECCCCC | 31.79 | - | |
7 | Deamidation | -MVKVGVNGFGRIGR -CCEEECCCCCHHHH | 33.86 | - | |
7 | Deamidated asparagine | -MVKVGVNGFGRIGR -CCEEECCCCCHHHH | 33.86 | - | |
40 | Phosphorylation | DPFIDLHYMVYMFQY CCCEEEEEEEEEEEE | 8.79 | - | |
47 | Nitration | YMVYMFQYDSTHGKF EEEEEEEEECCCCEE | 10.70 | - | |
59 | Acetylation | GKFHGTVKAENGKLV CEEEEEEEEECCEEE | 50.23 | - | |
62 | Deamidation | HGTVKAENGKLVING EEEEEEECCEEEECC | 58.73 | - | |
62 | Deamidated asparagine | HGTVKAENGKLVING EEEEEEECCEEEECC | 58.73 | - | |
64 | "N6,N6-dimethyllysine" | TVKAENGKLVINGKA EEEEECCEEEECCEE | 51.68 | - | |
64 | Methylation | TVKAENGKLVINGKA EEEEECCEEEECCEE | 51.68 | - | |
68 | Deamidation | ENGKLVINGKAITIF ECCEEEECCEEEEEE | 38.13 | - | |
68 | Deamidated asparagine | ENGKLVINGKAITIF ECCEEEECCEEEEEE | 38.13 | - | |
73 | Phosphorylation | VINGKAITIFQERDP EECCEEEEEEEECCC | 22.16 | - | |
92 | Nitration | WGDAGAEYVVESTGV CCCCCCEEEEEECCC | 14.84 | - | |
120 | Phosphorylation | GAKRVIISAPSADAP CCEEEEEECCCCCCC | 24.01 | - | |
146 | Phosphorylation | DNSLKIVSNASCTTN CCCEEEEECCCHHHC | 30.10 | - | |
147 | Deamidated asparagine | NSLKIVSNASCTTNC CCEEEEECCCHHHCC | 25.61 | - | |
147 | Deamidation | NSLKIVSNASCTTNC CCEEEEECCCHHHCC | 25.61 | - | |
149 | Phosphorylation | LKIVSNASCTTNCLA EEEEECCCHHHCCHH | 19.08 | - | |
150 | Glutathionylation | KIVSNASCTTNCLAP EEEECCCHHHCCHHH | 5.17 | 10092623 | |
150 | S-nitrosylation | KIVSNASCTTNCLAP EEEECCCHHHCCHHH | 5.17 | - | |
150 | Succinylation | KIVSNASCTTNCLAP EEEECCCHHHCCHHH | 5.17 | 17934141 | |
150 | Sulfhydration | KIVSNASCTTNCLAP EEEECCCHHHCCHHH | 5.17 | - | |
150 | ADP-ribosylation | KIVSNASCTTNCLAP EEEECCCHHHCCHHH | 5.17 | - | |
150 | ADP-ribosylation | KIVSNASCTTNCLAP EEEECCCHHHCCHHH | 5.17 | - | |
151 | Phosphorylation | IVSNASCTTNCLAPL EEECCCHHHCCHHHH | 20.67 | - | |
153 | Deamidated asparagine | SNASCTTNCLAPLAK ECCCHHHCCHHHHHH | 10.72 | - | |
153 | Deamidation | SNASCTTNCLAPLAK ECCCHHHCCHHHHHH | 10.72 | - | |
154 | Glutathionylation | NASCTTNCLAPLAKV CCCHHHCCHHHHHHH | 3.01 | 10092623 | |
175 | Phosphorylation | IVEGLMTTVHAITAT HHHHHHHHHHHHHEE | 9.06 | - | |
180 | Phosphorylation | MTTVHAITATQKTVD HHHHHHHHEEECCCC | 25.16 | - | |
182 | Phosphorylation | TVHAITATQKTVDGP HHHHHHEEECCCCCC | 23.19 | - | |
184 | Acetylation | HAITATQKTVDGPSG HHHHEEECCCCCCCC | 46.27 | 4316369 | |
192 | Malonylation | TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC | 49.57 | - | |
192 | Methylation | TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC | 49.57 | - | |
192 | Acetylation | TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC | 49.57 | - | |
192 | "N6,N6-dimethyllysine" | TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC | 49.57 | - | |
209 | Phosphorylation | QNIIPASTGAAKAVG HHCCCCCCCHHHHHH | 32.71 | - | |
213 | Malonylation | PASTGAAKAVGKVIP CCCCCHHHHHHHHHH | 42.97 | - | |
213 | Methylation | PASTGAAKAVGKVIP CCCCCHHHHHHHHHH | 42.97 | - | |
213 | "N6,N6-dimethyllysine" | PASTGAAKAVGKVIP CCCCCHHHHHHHHHH | 42.97 | - | |
217 | Acetylation | GAAKAVGKVIPELNG CHHHHHHHHHHHHCC | 30.32 | - | |
223 | Deamidated asparagine | GKVIPELNGKLTGMA HHHHHHHCCEEEEEE | 43.84 | - | |
223 | Deamidation | GKVIPELNGKLTGMA HHHHHHHCCEEEEEE | 43.84 | - | |
225 | "N6,N6-dimethyllysine" | VIPELNGKLTGMAFR HHHHHCCEEEEEEEE | 41.63 | - | |
225 | Methylation | VIPELNGKLTGMAFR HHHHHCCEEEEEEEE | 41.63 | - | |
225 | Acetylation | VIPELNGKLTGMAFR HHHHHCCEEEEEEEE | 41.63 | - | |
227 | Phosphorylation | PELNGKLTGMAFRVP HHHCCEEEEEEEECC | 28.53 | - | |
235 | Phosphorylation | GMAFRVPTPNVSVVD EEEEECCCCCEEEEE | 25.33 | - | |
239 | Phosphorylation | RVPTPNVSVVDLTCR ECCCCCEEEEEEEEE | 24.06 | - | |
245 | S-nitrosocysteine | VSVVDLTCRLEKAAK EEEEEEEEEHHHHHC | 6.42 | - | |
245 | Succinylation | VSVVDLTCRLEKAAK EEEEEEEEEHHHHHC | 6.42 | 17934141 | |
245 | S-palmitoylation | VSVVDLTCRLEKAAK EEEEEEEEEHHHHHC | 6.42 | 16128592 | |
245 | S-nitrosylation | VSVVDLTCRLEKAAK EEEEEEEEEHHHHHC | 6.42 | - | |
252 | Acetylation | CRLEKAAKYDDIKKV EEHHHHHCHHHHHHH | 54.81 | - | |
258 | "N6,N6-dimethyllysine" | AKYDDIKKVVKQASE HCHHHHHHHHHHHCC | 53.23 | - | |
258 | Methylation | AKYDDIKKVVKQASE HCHHHHHHHHHHHCC | 53.23 | - | |
261 | Methylation | DDIKKVVKQASEGPL HHHHHHHHHHCCCCC | 43.04 | - | |
261 | "N6,N6-dimethyllysine" | DDIKKVVKQASEGPL HHHHHHHHHHCCCCC | 43.04 | - | |
310 | Phosphorylation | DHFVKLISWYDNEFG HHHHHHHHHCCCCCC | 29.98 | - | |
312 | Nitration | FVKLISWYDNEFGYS HHHHHHHCCCCCCCH | 11.33 | - | |
314 | Deamidation | KLISWYDNEFGYSNR HHHHHCCCCCCCHHH | 30.69 | - | |
314 | Deamidated asparagine | KLISWYDNEFGYSNR HHHHHCCCCCCCHHH | 30.69 | - | |
318 | Nitration | WYDNEFGYSNRVVDL HCCCCCCCHHHHHHH | 14.21 | - | |
331 | Phosphorylation | DLMVHMASKE----- HHHHHHHCCC----- | 29.73 | - | |
332 | "N6,N6-dimethyllysine" | LMVHMASKE------ HHHHHHCCC------ | 58.88 | - | |
332 | Methylation | LMVHMASKE------ HHHHHHCCC------ | 58.88 | - |
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 G3P_RABIT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of G3P_RABIT !! |
* 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 G3P_RABIT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of G3P_RABIT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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