dbPTM

G3P_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G3P_RAT
UniProt AC	P04797
Protein Name	Glyceraldehyde-3-phosphate dehydrogenase
Gene Name	Gapdh
Organism	Rattus norvegicus (Rat).
Sequence Length	333
Subcellular Localization	Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Nucleus. Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with CHP1 to small punctate structures along the microtu
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	MVKVGVNGFGRIGRLVTRAAFSCDKVDIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQAAEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSNRVVDLMAYMASKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	"N6,N6-dimethyllysine"	-----MVKVGVNGFG -----CCEEECCCCH	31.79	-
3	Methylation	-----MVKVGVNGFG -----CCEEECCCCH	31.79	-
7	Deamidated asparagine	-MVKVGVNGFGRIGR -CCEEECCCCHHHHH	33.86	-
7	Deamidation	-MVKVGVNGFGRIGR -CCEEECCCCHHHHH	33.86	-
17	Phosphorylation	GRIGRLVTRAAFSCD HHHHHHHHHHHHCCC	21.12	23984901
22	Phosphorylation	LVTRAAFSCDKVDIV HHHHHHHCCCCEEEE	19.38	29779826
23	S-nitrosocysteine	VTRAAFSCDKVDIVA HHHHHHCCCCEEEEE	4.79	-
23	S-nitrosylation	VTRAAFSCDKVDIVA HHHHHHCCCCEEEEE	4.79	17629318
25	Acetylation	RAAFSCDKVDIVAIN HHHHCCCCEEEEEEC	46.24	26302492
40	Phosphorylation	DPFIDLNYMVYMFQY CCEECCCEEEEEEEE	8.68	-
53	Acetylation	QYDSTHGKFNGTVKA EEECCCCEECCEEEE	28.22	3749035
57	Phosphorylation	THGKFNGTVKAENGK CCCEECCEEEEECCE	21.67	23984901
59	Acetylation	GKFNGTVKAENGKLV CEECCEEEEECCEEE	50.23	22902405
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	22902405
64	Methylation	TVKAENGKLVINGKP EEEEECCEEEECCEE	51.68	-
68	Deamidated asparagine	ENGKLVINGKPITIF ECCEEEECCEEEEEE	44.98	-
68	Deamidation	ENGKLVINGKPITIF ECCEEEECCEEEEEE	44.98	-
70	Acetylation	GKLVINGKPITIFQE CEEEECCEEEEEEEE	28.85	22902405
70	Ubiquitination	GKLVINGKPITIFQE CEEEECCEEEEEEEE	28.85	-
73	Phosphorylation	VINGKPITIFQERDP EECCEEEEEEEECCC	25.02	22673903
101	Phosphorylation	VESTGVFTTMEKAGA EEECCCEECHHHCCC	23.87	23984901
102	Phosphorylation	ESTGVFTTMEKAGAH EECCCEECHHHCCCC	16.33	23984901
105	Acetylation	GVFTTMEKAGAHLKG CCEECHHHCCCCCCC	41.10	25786129
111	Acetylation	EKAGAHLKGGAKRVI HHCCCCCCCCCEEEE	45.49	26302492
111	Succinylation	EKAGAHLKGGAKRVI HHCCCCCCCCCEEEE	45.49	26843850
111	Ubiquitination	EKAGAHLKGGAKRVI HHCCCCCCCCCEEEE	45.49	-
120	Phosphorylation	GAKRVIISAPSADAP CCEEEEEECCCCCCC	24.01	23984901
123	Phosphorylation	RVIISAPSADAPMFV EEEEECCCCCCCEEE	38.20	23984901
137	Acetylation	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	22902405
138	Phosphorylation	MGVNHEKYDNSLKIV EECCHHHCCCCEEEE	19.85	23984901
141	Phosphorylation	NHEKYDNSLKIVSNA CHHHCCCCEEEEECC	28.30	23984901
143	Acetylation	EKYDNSLKIVSNASC HHCCCCEEEEECCCH	40.66	26302492
146	Phosphorylation	DNSLKIVSNASCTTN CCCEEEEECCCHHCC	30.10	25575281
147	Deamidated asparagine	NSLKIVSNASCTTNC CCEEEEECCCHHCCC	25.61	-
147	Deamidation	NSLKIVSNASCTTNC CCEEEEECCCHHCCC	25.61	-
149	Phosphorylation	LKIVSNASCTTNCLA EEEEECCCHHCCCHH	19.08	21738781
150	ADP-ribosylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	-
150	ADP-ribosylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	8626764
150	S-nitrosylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	15951807
150	Succinylation	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	17934141
150	Sulfhydration	KIVSNASCTTNCLAP EEEECCCHHCCCHHH	5.17	-
151	Phosphorylation	IVSNASCTTNCLAPL EEECCCHHCCCHHHH	20.67	21738781
152	Phosphorylation	VSNASCTTNCLAPLA EECCCHHCCCHHHHH	28.41	22817900
153	Deamidated asparagine	SNASCTTNCLAPLAK ECCCHHCCCHHHHHH	10.72	-
153	Deamidation	SNASCTTNCLAPLAK ECCCHHCCCHHHHHH	10.72	-
154	S-nitrosocysteine	NASCTTNCLAPLAKV CCCHHCCCHHHHHHH	3.01	-
154	S-nitrosylation	NASCTTNCLAPLAKV CCCHHCCCHHHHHHH	3.01	16418269
174	Phosphorylation	GIVEGLMTTVHAITA CHHHHHHHHHHHHEE	30.61	27097102
175	Phosphorylation	IVEGLMTTVHAITAT HHHHHHHHHHHHEEE	9.06	27097102
180	Phosphorylation	MTTVHAITATQKTVD HHHHHHHEEEECCCC	25.16	27097102
182	Phosphorylation	TVHAITATQKTVDGP HHHHHEEEECCCCCC	23.19	28689409
184	Acetylation	HAITATQKTVDGPSG HHHEEEECCCCCCCC	46.27	22902405
184	Ubiquitination	HAITATQKTVDGPSG HHHEEEECCCCCCCC	46.27	-
185	Phosphorylation	AITATQKTVDGPSGK HHEEEECCCCCCCCC	17.63	23984901
190	Phosphorylation	QKTVDGPSGKLWRDG ECCCCCCCCCCCCCC	54.83	23984901
192	"N6,N6-dimethyllysine"	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
192	Acetylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	25786129
192	Malonylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
192	Methylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
192	Ubiquitination	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
208	Phosphorylation	AQNIIPASTGAAKAV HHHCCCCCCCHHHHH	23.24	29779826
209	Phosphorylation	QNIIPASTGAAKAVG HHCCCCCCCHHHHHH	32.71	27097102
213	"N6,N6-dimethyllysine"	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
213	Acetylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	25786129
213	Malonylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
213	Methylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
213	Ubiquitination	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
217	Acetylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	25786129
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	22902405
225	Methylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	-
227	O-linked_Glycosylation	PELNGKLTGMAFRVP HHHCCEEEEEEEECC	28.53	54899139
227	Phosphorylation	PELNGKLTGMAFRVP HHHCCEEEEEEEECC	28.53	23984901
235	Phosphorylation	GMAFRVPTPNVSVVD EEEEECCCCCEEEEE	25.33	22817900
239	Phosphorylation	RVPTPNVSVVDLTCR ECCCCCEEEEEEEEE	24.06	23984901
244	Phosphorylation	NVSVVDLTCRLEKPA CEEEEEEEEEECCCC	7.36	30181290
245	S-nitrosocysteine	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	-
245	S-nitrosylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	17629318
245	Succinylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	17934141
249	Acetylation	DLTCRLEKPAKYDDI EEEEEECCCCCHHHH	55.67	26302492
249	Ubiquitination	DLTCRLEKPAKYDDI EEEEEECCCCCHHHH	55.67	-
252	Acetylation	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	26302492
252	Ubiquitination	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	-
253	Phosphorylation	RLEKPAKYDDIKKVV EECCCCCHHHHHHHH	22.43	-
257	Acetylation	PAKYDDIKKVVKQAA CCCHHHHHHHHHHHH	46.65	26302492
257	Ubiquitination	PAKYDDIKKVVKQAA CCCHHHHHHHHHHHH	46.65	-
258	"N6,N6-dimethyllysine"	AKYDDIKKVVKQAAE CCHHHHHHHHHHHHH	53.23	-
258	Acetylation	AKYDDIKKVVKQAAE CCHHHHHHHHHHHHH	53.23	26302492
258	Methylation	AKYDDIKKVVKQAAE CCHHHHHHHHHHHHH	53.23	-
258	Ubiquitination	AKYDDIKKVVKQAAE CCHHHHHHHHHHHHH	53.23	-
261	"N6,N6-dimethyllysine"	DDIKKVVKQAAEGPL HHHHHHHHHHHHCCC	36.89	-
261	Acetylation	DDIKKVVKQAAEGPL HHHHHHHHHHHHCCC	36.89	22902405
261	Methylation	DDIKKVVKQAAEGPL HHHHHHHHHHHHCCC	36.89	-
261	Ubiquitination	DDIKKVVKQAAEGPL HHHHHHHHHHHHCCC	36.89	-
310	Phosphorylation	DNFVKLISWYDNEYG CCHHHEEECCCCCCC	29.98	23984901
314	Deamidated asparagine	KLISWYDNEYGYSNR HEEECCCCCCCCCCH	28.79	-
314	Deamidation	KLISWYDNEYGYSNR HEEECCCCCCCCCCH	28.79	-
316	Phosphorylation	ISWYDNEYGYSNRVV EECCCCCCCCCCHHH	27.84	22673903
318	Phosphorylation	WYDNEYGYSNRVVDL CCCCCCCCCCHHHHH	11.23	22673903
328	Phosphorylation	RVVDLMAYMASKE-- HHHHHHHHHHCCC--	4.54	22673903
331	Phosphorylation	DLMAYMASKE----- HHHHHHHCCC-----	22.31	22673903
332	"N6,N6-dimethyllysine"	LMAYMASKE------ HHHHHHCCC------	58.88	-
332	Acetylation	LMAYMASKE------ HHHHHHCCC------	58.88	22902405
332	Methylation	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_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
150	C	S-nitrosylation	8626764
S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus.
245	C	Phosphorylation	17934141
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	17934141
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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIAH1_RAT	Siah1	physical	15951807
AKT1_RAT	Akt1	physical	20488185
RIPL1_RAT	Rilpl1	physical	19607794

Drug and Disease Associations

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

Regulatory Network of G3P_RAT

Related Literatures of Post-Translational Modification

S-nitrosylation
Reference	PubMed
"GAPDH mediates nitrosylation of nuclear proteins."; Kornberg M.D., Sen N., Hara M.R., Juluri K.R., Nguyen J.V.,Snowman A.M., Law L., Hester L.D., Snyder S.H.; Nat. Cell Biol. 12:1094-1100(2010). Cited for: FUNCTION AS NITROSYLASE, SUBCELLULAR LOCATION, INTERACTION WITH SIRT1,S-NITROSYLATION AT CYS-150, AND MUTAGENESIS OF SER-149; CYS-150;THR-151 AND THR-152.	20972425 [Abstract]
"S-nitrosylated GAPDH initiates apoptotic cell death by nucleartranslocation following Siah1 binding."; Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y.,Takahashi M., Cheah J.H., Tankou S.K., Hester L.D., Ferris C.D.,Hayward S.D., Snyder S.H., Sawa A.; Nat. Cell Biol. 7:665-674(2005). Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIAH1,S-NITROSYLATION AT CYS-150, AND MUTAGENESIS OF CYS-150; LYS-225;PRO-234 AND THR-235.	15951807 [Abstract]
"Posttranslational modification of glyceraldehyde-3-phosphatedehydrogenase by S-nitrosylation and subsequent NADH attachment."; Mohr S., Stamler J.S., Brune B.; J. Biol. Chem. 271:4209-4214(1996). Cited for: S-NITROSYLATION AT CYS-150, ADP-RIBOSYLATION AT CYS-150, ABSENCE OFNITROSYLATION AT CYS-154, AND ACTIVE SITE.	8626764 [Abstract]
"SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures."; Hao G., Derakhshan B., Shi L., Campagne F., Gross S.S.; Proc. Natl. Acad. Sci. U.S.A. 103:1012-1017(2006). Cited for: PROTEIN SEQUENCE OF 144-160, S-NITROSYLATION [LARGE SCALE ANALYSIS] ATCYS-150, AND MASS SPECTROMETRY.	16418269 [Abstract]

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