dbPTM

G3P_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G3P_MOUSE
UniProt AC	P16858
Protein Name	Glyceraldehyde-3-phosphate dehydrogenase
Gene Name	Gapdh
Organism	Mus musculus (Mouse).
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..
Protein Sequence	MVKVGVNGFGRIGRLVTRAAICSGKVEIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPTNIKWGEAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSNRVVDLMAYMASKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	"N6,N6-dimethyllysine"	-----MVKVGVNGFG -----CCEECCCCCH	31.79	-
3	Malonylation	-----MVKVGVNGFG -----CCEECCCCCH	31.79	26320211
3	Methylation	-----MVKVGVNGFG -----CCEECCCCCH	31.79	-
3	Succinylation	-----MVKVGVNGFG -----CCEECCCCCH	31.79	23954790
3	Ubiquitination	-----MVKVGVNGFG -----CCEECCCCCH	31.79	-
7	Deamidated asparagine	-MVKVGVNGFGRIGR -CCEECCCCCHHHHH	33.86	-
7	Deamidation	-MVKVGVNGFGRIGR -CCEECCCCCHHHHH	33.86	-
17	Phosphorylation	GRIGRLVTRAAICSG HHHHHHHHHHHHHCC	21.12	26060331
22	Glutathionylation	LVTRAAICSGKVEIV HHHHHHHHCCCEEEE	3.63	24333276
23	Phosphorylation	VTRAAICSGKVEIVA HHHHHHHCCCEEEEE	35.22	28542873
25	Ubiquitination	RAAICSGKVEIVAIN HHHHHCCCEEEEEEE	22.02	-
40	Phosphorylation	DPFIDLNYMVYMFQY CCEECCCEEEEEEEE	8.68	-
57	Phosphorylation	THGKFNGTVKAENGK CCCEECCEEEEECCE	21.67	22802335
59	Acetylation	GKFNGTVKAENGKLV CEECCEEEEECCEEE	50.23	23864654
59	Malonylation	GKFNGTVKAENGKLV CEECCEEEEECCEEE	50.23	26320211
59	Succinylation	GKFNGTVKAENGKLV CEECCEEEEECCEEE	50.23	23806337
59	Ubiquitination	GKFNGTVKAENGKLV CEECCEEEEECCEEE	50.23	-
62	Deamidated asparagine	NGTVKAENGKLVING CCEEEEECCEEEECC	58.73	-
62	Deamidation	NGTVKAENGKLVING CCEEEEECCEEEECC	58.73	-
64	"N6,N6-dimethyllysine"	TVKAENGKLVINGKP EEEEECCEEEECCEE	51.68	-
64	Acetylation	TVKAENGKLVINGKP EEEEECCEEEECCEE	51.68	23201123
64	Malonylation	TVKAENGKLVINGKP EEEEECCEEEECCEE	51.68	26320211
64	Methylation	TVKAENGKLVINGKP EEEEECCEEEECCEE	51.68	-
64	Ubiquitination	TVKAENGKLVINGKP EEEEECCEEEECCEE	51.68	-
68	Deamidated asparagine	ENGKLVINGKPITIF ECCEEEECCEEEEEE	44.98	-
68	Deamidation	ENGKLVINGKPITIF ECCEEEECCEEEEEE	44.98	-
70	Acetylation	GKLVINGKPITIFQE CEEEECCEEEEEEEE	28.85	22826441
70	Malonylation	GKLVINGKPITIFQE CEEEECCEEEEEEEE	28.85	25418362
70	Succinylation	GKLVINGKPITIFQE CEEEECCEEEEEEEE	28.85	23806337
70	Ubiquitination	GKLVINGKPITIFQE CEEEECCEEEEEEEE	28.85	-
73	Phosphorylation	VINGKPITIFQERDP EECCEEEEEEEECCC	25.02	20139300
81	Phosphorylation	IFQERDPTNIKWGEA EEEECCCCCCCCCCC	54.59	26824392
84	Acetylation	ERDPTNIKWGEAGAE ECCCCCCCCCCCCCE	51.74	23954790
84	Ubiquitination	ERDPTNIKWGEAGAE ECCCCCCCCCCCCCE	51.74	-
102	Phosphorylation	ESTGVFTTMEKAGAH EECCCEECHHHCCCC	16.33	-
105	Acetylation	GVFTTMEKAGAHLKG CCEECHHHCCCCCCC	41.10	22826441
105	Malonylation	GVFTTMEKAGAHLKG CCEECHHHCCCCCCC	41.10	26320211
105	Succinylation	GVFTTMEKAGAHLKG CCEECHHHCCCCCCC	41.10	23806337
105	Ubiquitination	GVFTTMEKAGAHLKG CCEECHHHCCCCCCC	41.10	-
111	Acetylation	EKAGAHLKGGAKRVI HHCCCCCCCCCEEEE	45.49	23864654
111	Ubiquitination	EKAGAHLKGGAKRVI HHCCCCCCCCCEEEE	45.49	-
120	Phosphorylation	GAKRVIISAPSADAP CCEEEEEECCCCCCC	24.01	26643407
123	Phosphorylation	RVIISAPSADAPMFV EEEEECCCCCCCEEE	38.20	26643407
137	Acetylation	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	23806337
137	Malonylation	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	26320211
137	Succinylation	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	23806337
137	Ubiquitination	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	-
138	Phosphorylation	MGVNHEKYDNSLKIV EECCHHHCCCCEEEE	19.85	26643407
141	Phosphorylation	NHEKYDNSLKIVSNA CHHHCCCCEEEEECC	28.30	26643407
143	Acetylation	EKYDNSLKIVSNASC HHCCCCEEEEECCCH	40.66	22733758
143	Malonylation	EKYDNSLKIVSNASC HHCCCCEEEEECCCH	40.66	26320211
143	Ubiquitination	EKYDNSLKIVSNASC HHCCCCEEEEECCCH	40.66	-
146	Phosphorylation	DNSLKIVSNASCTTN CCCEEEEECCCHHCC	30.10	22942356
147	Deamidated asparagine	NSLKIVSNASCTTNC CCEEEEECCCHHCCC	25.61	-
147	Deamidation	NSLKIVSNASCTTNC CCEEEEECCCHHCCC	25.61	-
149	Phosphorylation	LKIVSNASCTTNCLA EEEEECCCHHCCCHH	19.08	25521595
150	ADP-ribosylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	-
150	ADP-ribosylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	-
150	Glutathionylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	24333276
150	S-nitrosylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	24895380
150	S-palmitoylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	28526873
150	Succinylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	-
150	Sulfhydration	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	19903941
151	Phosphorylation	IVSNASCTTNCLAPL EEECCCHHCCCHHHH	20.67	25521595
152	Phosphorylation	VSNASCTTNCLAPLA EECCCHHCCCHHHHH	28.41	23984901
153	Deamidated asparagine	SNASCTTNCLAPLAK ECCCHHCCCHHHHHH	10.72	-
153	Deamidation	SNASCTTNCLAPLAK ECCCHHCCCHHHHHH	10.72	-
154	S-nitrosocysteine	NASCTTNCLAPLAKV CCCHHCCCHHHHHHH	3.01	-
154	Glutathionylation	NASCTTNCLAPLAKV CCCHHCCCHHHHHHH	3.01	24333276
154	S-nitrosylation	NASCTTNCLAPLAKV CCCHHCCCHHHHHHH	3.01	24895380
154	S-palmitoylation	NASCTTNCLAPLAKV CCCHHCCCHHHHHHH	3.01	28526873
160	Ubiquitination	NCLAPLAKVIHDNFG CCHHHHHHHHHCCCC	49.78	-
174	Phosphorylation	GIVEGLMTTVHAITA CHHHHHHHHHHHHEE	30.61	26239621
175	Phosphorylation	IVEGLMTTVHAITAT HHHHHHHHHHHHEEE	9.06	26239621
180	Phosphorylation	MTTVHAITATQKTVD HHHHHHHEEEECCCC	25.16	25521595
182	Phosphorylation	TVHAITATQKTVDGP HHHHHEEEECCCCCC	23.19	25521595
184	Acetylation	HAITATQKTVDGPSG HHHEEEECCCCCCCC	46.27	23954790
184	Malonylation	HAITATQKTVDGPSG HHHEEEECCCCCCCC	46.27	26073543
184	Ubiquitination	HAITATQKTVDGPSG HHHEEEECCCCCCCC	46.27	-
185	Phosphorylation	AITATQKTVDGPSGK HHEEEECCCCCCCCC	17.63	26239621
190	Phosphorylation	QKTVDGPSGKLWRDG ECCCCCCCCCCCCCC	54.83	26239621
192	"N6,N6-dimethyllysine"	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
192	Acetylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	23864654
192	Malonylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	26320211
192	Methylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
192	Succinylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	23806337
192	Ubiquitination	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
208	O-linked_Glycosylation	AQNIIPASTGAAKAV HHHCCCCCCCHHHHH	23.24	28528544
208	Phosphorylation	AQNIIPASTGAAKAV HHHCCCCCCCHHHHH	23.24	25521595
209	Phosphorylation	QNIIPASTGAAKAVG HHCCCCCCCHHHHHH	32.71	25521595
213	"N6,N6-dimethyllysine"	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
213	Acetylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	23864654
213	Malonylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	26320211
213	Methylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
213	Succinylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	23806337
213	Ubiquitination	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
217	Acetylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	23864654
217	Malonylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	26320211
217	Succinylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	23954790
217	Ubiquitination	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	Acetylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	23806337
225	Malonylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	26320211
225	Methylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	-
225	Succinylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	23806337
225	Ubiquitination	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	-
227	Phosphorylation	PELNGKLTGMAFRVP HHHCCEEEEEEEECC	28.53	28542873
232	Methylation	KLTGMAFRVPTPNVS EEEEEEEECCCCCEE	24.78	-
235	Phosphorylation	GMAFRVPTPNVSVVD EEEEECCCCCEEEEE	25.33	26643407
239	Phosphorylation	RVPTPNVSVVDLTCR ECCCCCEEEEEEEEE	24.06	26643407
244	Phosphorylation	NVSVVDLTCRLEKPA CEEEEEEEEEECCCC	7.36	28542873
245	S-nitrosocysteine	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	-
245	Glutathionylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	24333276
245	S-nitrosylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	24895380
245	S-palmitoylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	28526873
245	Succinylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	-
249	Malonylation	DLTCRLEKPAKYDDI EEEEEECCCCCHHHH	55.67	26320211
249	Ubiquitination	DLTCRLEKPAKYDDI EEEEEECCCCCHHHH	55.67	-
252	Acetylation	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	23201123
252	Malonylation	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	26320211
252	Succinylation	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	23954790
252	Ubiquitination	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	-
253	Nitration	RLEKPAKYDDIKKVV EECCCCCHHHHHHHH	22.43	-
253	Phosphorylation	RLEKPAKYDDIKKVV EECCCCCHHHHHHHH	22.43	-
257	Acetylation	PAKYDDIKKVVKQAS CCCHHHHHHHHHHHH	46.65	23201123
257	Ubiquitination	PAKYDDIKKVVKQAS CCCHHHHHHHHHHHH	46.65	-
258	"N6,N6-dimethyllysine"	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	-
258	Methylation	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	-
258	Ubiquitination	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	-
261	"N6,N6-dimethyllysine"	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	-
261	Acetylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	23806337
261	Malonylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	26320211
261	Methylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	-
261	Succinylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	23806337
261	Ubiquitination	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	-
264	Phosphorylation	KKVVKQASEGPLKGI HHHHHHHHCCCCCEE	40.36	25521595
274	Phosphorylation	PLKGILGYTEDQVVS CCCEECCCCCCCEEE	11.96	26239621
275	Phosphorylation	LKGILGYTEDQVVSC CCEECCCCCCCEEEE	31.15	26239621
281	Phosphorylation	YTEDQVVSCDFNSNS CCCCCEEEEECCCCC	14.76	26239621
282	S-nitrosocysteine	TEDQVVSCDFNSNSH CCCCEEEEECCCCCC	4.71	-
282	Glutathionylation	TEDQVVSCDFNSNSH CCCCEEEEECCCCCC	4.71	24333276
282	S-nitrosylation	TEDQVVSCDFNSNSH CCCCEEEEECCCCCC	4.71	21278135
286	Phosphorylation	VVSCDFNSNSHSSTF EEEEECCCCCCCCCC	39.44	26239621
288	Phosphorylation	SCDFNSNSHSSTFDA EEECCCCCCCCCCCC	25.27	26239621
290	Phosphorylation	DFNSNSHSSTFDAGA ECCCCCCCCCCCCCC	30.78	26239621
291	Phosphorylation	FNSNSHSSTFDAGAG CCCCCCCCCCCCCCC	27.89	26239621
292	Phosphorylation	NSNSHSSTFDAGAGI CCCCCCCCCCCCCCE	28.66	26239621
310	Phosphorylation	DNFVKLISWYDNEYG CCHHHEEECCCCCCC	29.98	22499769
312	Phosphorylation	FVKLISWYDNEYGYS HHHEEECCCCCCCCC	11.33	22499769
314	Deamidated asparagine	KLISWYDNEYGYSNR HEEECCCCCCCCCCH	28.79	-
314	Deamidation	KLISWYDNEYGYSNR HEEECCCCCCCCCCH	28.79	-
316	Phosphorylation	ISWYDNEYGYSNRVV EECCCCCCCCCCHHH	27.84	28542873
318	Phosphorylation	WYDNEYGYSNRVVDL CCCCCCCCCCHHHHH	11.23	22499769
319	Phosphorylation	YDNEYGYSNRVVDLM CCCCCCCCCHHHHHH	17.50	22499769
328	Phosphorylation	RVVDLMAYMASKE-- HHHHHHHHHHCCC--	4.54	28542873
331	Phosphorylation	DLMAYMASKE----- HHHHHHHCCC-----	22.31	28638064
332	"N6,N6-dimethyllysine"	LMAYMASKE------ HHHHHHCCC------	58.88	-
332	Acetylation	LMAYMASKE------ HHHHHHCCC------	58.88	23806337
332	Methylation	LMAYMASKE------ HHHHHHCCC------	58.88	-
332	Succinylation	LMAYMASKE------ HHHHHHCCC------	58.88	23954790
332	Ubiquitination	LMAYMASKE------ HHHHHHCCC------	58.88	-

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 G3P_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
150	C	Phosphorylation	19903941
S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity).
150	C	S-nitrosylation	19903941
S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity).
245	C	Phosphorylation	-
S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity).
245	C	S-nitrosylation	-
S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity).

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 G3P_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of G3P_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of G3P_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-209, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312; TYR-316; TYR-318AND TYR-328, AND MASS SPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316 AND TYR-318, ANDMASS SPECTROMETRY.	17947660 [Abstract]

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