dbPTM

G3P_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G3P_HUMAN
UniProt AC	P04406
Protein Name	Glyceraldehyde-3-phosphate dehydrogenase
Gene Name	GAPDH
Organism	Homo sapiens (Human).
Sequence Length	335
Subcellular Localization	Cytoplasm, cytosol . Nucleus. Cytoplasm, perinuclear region . Membrane . Cytoplasm, cytoskeleton. Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnucl
Protein Description	Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. 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. 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 (By similarity). 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. 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	MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	"N6,N6-dimethyllysine"	---MGKVKVGVNGFG ---CCCEEEECCCCC	36.44	-
5	2-Hydroxyisobutyrylation	---MGKVKVGVNGFG ---CCCEEEECCCCC	36.44	-
5	Acetylation	---MGKVKVGVNGFG ---CCCEEEECCCCC	36.44	25953088
5	Malonylation	---MGKVKVGVNGFG ---CCCEEEECCCCC	36.44	26320211
5	Methylation	---MGKVKVGVNGFG ---CCCEEEECCCCC	36.44	18183946
5	Ubiquitination	---MGKVKVGVNGFG ---CCCEEEECCCCC	36.44	21890473
9	Deamidated asparagine	GKVKVGVNGFGRIGR CCEEEECCCCCHHHH	33.86	-
9	Deamidation	GKVKVGVNGFGRIGR CCEEEECCCCCHHHH	33.86	18183946
13	Methylation	VGVNGFGRIGRLVTR EECCCCCHHHHHHHH	26.40	-
19	Acetylation	GRIGRLVTRAAFNSG CHHHHHHHHHHHHCC	21.12	19608861
19	Phosphorylation	GRIGRLVTRAAFNSG CHHHHHHHHHHHHCC	21.12	27273156
19	Ubiquitination	GRIGRLVTRAAFNSG CHHHHHHHHHHHHCC	21.12	19608861
25	Phosphorylation	VTRAAFNSGKVDIVA HHHHHHHCCCCEEEE	33.27	20058876
27	Acetylation	RAAFNSGKVDIVAIN HHHHHCCCCEEEEEC	36.23	21466224
27	Phosphoglycerylation	RAAFNSGKVDIVAIN HHHHHCCCCEEEEEC	36.23	-
27	Ubiquitination	RAAFNSGKVDIVAIN HHHHHCCCCEEEEEC	36.23	-
42	Acetylation	DPFIDLNYMVYMFQY CCEECCCEEEEEEEE	8.68	19608861
42	Phosphorylation	DPFIDLNYMVYMFQY CCEECCCEEEEEEEE	8.68	22817900
42	Ubiquitination	DPFIDLNYMVYMFQY CCEECCCEEEEEEEE	8.68	19608861
43	Sulfoxidation	PFIDLNYMVYMFQYD CEECCCEEEEEEEEE	1.37	30846556
45	Phosphorylation	IDLNYMVYMFQYDST ECCCEEEEEEEEECC	3.91	22673903
46	Methionine sulfoxide	DLNYMVYMFQYDSTH CCCEEEEEEEEECCC	0.85	-
46	Oxidation	DLNYMVYMFQYDSTH CCCEEEEEEEEECCC	0.85	25086035
46	Sulfoxidation	DLNYMVYMFQYDSTH CCCEEEEEEEEECCC	0.85	25086035
49	Phosphorylation	YMVYMFQYDSTHGKF EEEEEEEEECCCCEE	10.70	25884760
51	Phosphorylation	VYMFQYDSTHGKFHG EEEEEEECCCCEEEE	19.85	22673903
52	Phosphorylation	YMFQYDSTHGKFHGT EEEEEECCCCEEEEE	31.58	22673903
55	Acetylation	QYDSTHGKFHGTVKA EEECCCCEEEEEEEE	26.95	21466224
55	Ubiquitination	QYDSTHGKFHGTVKA EEECCCCEEEEEEEE	26.95	-
59	Phosphorylation	THGKFHGTVKAENGK CCCEEEEEEEECCCE	15.40	30576142
61	Sumoylation	GKFHGTVKAENGKLV CEEEEEEEECCCEEE	50.23	-
61	2-Hydroxyisobutyrylation	GKFHGTVKAENGKLV CEEEEEEEECCCEEE	50.23	-
61	Acetylation	GKFHGTVKAENGKLV CEEEEEEEECCCEEE	50.23	19608861
61	Malonylation	GKFHGTVKAENGKLV CEEEEEEEECCCEEE	50.23	30639696
61	Sumoylation	GKFHGTVKAENGKLV CEEEEEEEECCCEEE	50.23	19608861
61	Ubiquitination	GKFHGTVKAENGKLV CEEEEEEEECCCEEE	50.23	21890473
64	Deamidated asparagine	HGTVKAENGKLVING EEEEEECCCEEEECC	58.73	-
64	Deamidation	HGTVKAENGKLVING EEEEEECCCEEEECC	58.73	18183946
66	"N6,N6-dimethyllysine"	TVKAENGKLVINGNP EEEECCCEEEECCCE	51.68	-
66	2-Hydroxyisobutyrylation	TVKAENGKLVINGNP EEEECCCEEEECCCE	51.68	-
66	Acetylation	TVKAENGKLVINGNP EEEECCCEEEECCCE	51.68	23749302
66	Methylation	TVKAENGKLVINGNP EEEECCCEEEECCCE	51.68	18183946
66	Ubiquitination	TVKAENGKLVINGNP EEEECCCEEEECCCE	51.68	21890473
70	Deamidated asparagine	ENGKLVINGNPITIF CCCEEEECCCEEEEE	36.39	-
70	Deamidation	ENGKLVINGNPITIF CCCEEEECCCEEEEE	36.39	18183946
75	Phosphorylation	VINGNPITIFQERDP EECCCEEEEEEECCH	19.59	23927012
80	Methylation	PITIFQERDPSKIKW EEEEEEECCHHHCCC	50.81	-
83	O-linked_Glycosylation	IFQERDPSKIKWGDA EEEECCHHHCCCCCC	51.83	28510447
83	Phosphorylation	IFQERDPSKIKWGDA EEEECCHHHCCCCCC	51.83	22167270
84	Acetylation	FQERDPSKIKWGDAG EEECCHHHCCCCCCC	54.41	23954790
84	Ubiquitination	FQERDPSKIKWGDAG EEECCHHHCCCCCCC	54.41	21890473
86	2-Hydroxyisobutyrylation	ERDPSKIKWGDAGAE ECCHHHCCCCCCCCE	49.19	-
86	Acetylation	ERDPSKIKWGDAGAE ECCHHHCCCCCCCCE	49.19	26822725
86	Ubiquitination	ERDPSKIKWGDAGAE ECCHHHCCCCCCCCE	49.19	21890473
94	Phosphorylation	WGDAGAEYVVESTGV CCCCCCEEEEEECCC	14.84	27259358
98	Phosphorylation	GAEYVVESTGVFTTM CCEEEEEECCCEECH	20.89	27251275
99	Phosphorylation	AEYVVESTGVFTTME CEEEEEECCCEECHH	24.69	27251275
103	Phosphorylation	VESTGVFTTMEKAGA EEECCCEECHHHCCC	23.87	28857561
104	Phosphorylation	ESTGVFTTMEKAGAH EECCCEECHHHCCCH	16.33	28857561
105	Sulfoxidation	STGVFTTMEKAGAHL ECCCEECHHHCCCHH	4.52	30846556
107	Acetylation	GVFTTMEKAGAHLQG CCEECHHHCCCHHCC	41.10	23954790
107	Malonylation	GVFTTMEKAGAHLQG CCEECHHHCCCHHCC	41.10	26320211
107	Ubiquitination	GVFTTMEKAGAHLQG CCEECHHHCCCHHCC	41.10	-
117	2-Hydroxyisobutyrylation	AHLQGGAKRVIISAP CHHCCCCEEEEEECC	50.93	-
117	Acetylation	AHLQGGAKRVIISAP CHHCCCCEEEEEECC	50.93	23749302
117	Ubiquitination	AHLQGGAKRVIISAP CHHCCCCEEEEEECC	50.93	21906983
122	Phosphorylation	GAKRVIISAPSADAP CCEEEEEECCCCCCC	24.01	18183946
125	Phosphorylation	RVIISAPSADAPMFV EEEEECCCCCCCEEE	38.20	21712546
130	Sulfoxidation	APSADAPMFVMGVNH CCCCCCCEEEEECCH	4.19	21406390
133	Sulfoxidation	ADAPMFVMGVNHEKY CCCCEEEEECCHHHC	3.20	30846556
139	2-Hydroxyisobutyrylation	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	-
139	Acetylation	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	21466224
139	Malonylation	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	26320211
139	Ubiquitination	VMGVNHEKYDNSLKI EEECCHHHCCCCEEE	50.80	21890473
140	Nitration	MGVNHEKYDNSLKII EECCHHHCCCCEEEE	19.85	-
140	Phosphorylation	MGVNHEKYDNSLKII EECCHHHCCCCEEEE	19.85	25849741
143	Phosphorylation	NHEKYDNSLKIISNA CHHHCCCCEEEEECC	28.30	19702290
144	Acetylation	HEKYDNSLKIISNAS HHHCCCCEEEEECCC	6.07	19608861
144	Ubiquitination	HEKYDNSLKIISNAS HHHCCCCEEEEECCC	6.07	19608861
145	2-Hydroxyisobutyrylation	EKYDNSLKIISNASC HHCCCCEEEEECCCC	37.50	-
145	Acetylation	EKYDNSLKIISNASC HHCCCCEEEEECCCC	37.50	23954790
145	Malonylation	EKYDNSLKIISNASC HHCCCCEEEEECCCC	37.50	26320211
145	Ubiquitination	EKYDNSLKIISNASC HHCCCCEEEEECCCC	37.50	21890473
148	Phosphorylation	DNSLKIISNASCTTN CCCEEEEECCCCCCC	29.80	30266825
149	Deamidated asparagine	NSLKIISNASCTTNC CCEEEEECCCCCCCC	26.01	-
149	Deamidation	NSLKIISNASCTTNC CCEEEEECCCCCCCC	26.01	18183946
151	Phosphorylation	LKIISNASCTTNCLA EEEEECCCCCCCCHH	19.08	29255136
152	ADP-ribosylation	KIISNASCTTNCLAP EEEECCCCCCCCHHH	5.17	-
152	ADP-ribosylation	KIISNASCTTNCLAP EEEECCCCCCCCHHH	5.17	-
152	S-nitrosylation	KIISNASCTTNCLAP EEEECCCCCCCCHHH	5.17	20140087
152	S-palmitoylation	KIISNASCTTNCLAP EEEECCCCCCCCHHH	5.17	29575903
152	Succinylation	KIISNASCTTNCLAP EEEECCCCCCCCHHH	5.17	-
152	Sulfhydration	KIISNASCTTNCLAP EEEECCCCCCCCHHH	5.17	-
153	Phosphorylation	IISNASCTTNCLAPL EEECCCCCCCCHHHH	20.67	22322096
154	Phosphorylation	ISNASCTTNCLAPLA EECCCCCCCCHHHHH	28.41	30266825
155	Deamidated asparagine	SNASCTTNCLAPLAK ECCCCCCCCHHHHHH	10.72	-
155	Deamidation	SNASCTTNCLAPLAK ECCCCCCCCHHHHHH	10.72	18183946
156	S-nitrosocysteine	NASCTTNCLAPLAKV CCCCCCCCHHHHHHH	3.01	-
156	Glutathionylation	NASCTTNCLAPLAKV CCCCCCCCHHHHHHH	3.01	22555962
156	S-nitrosylation	NASCTTNCLAPLAKV CCCCCCCCHHHHHHH	3.01	25040305
156	S-palmitoylation	NASCTTNCLAPLAKV CCCCCCCCHHHHHHH	3.01	29575903
162	Acetylation	NCLAPLAKVIHDNFG CCHHHHHHHHHCCCC	49.78	18552833
162	Methylation	NCLAPLAKVIHDNFG CCHHHHHHHHHCCCC	49.78	-
162	Sumoylation	NCLAPLAKVIHDNFG CCHHHHHHHHHCCCC	49.78	-
162	Ubiquitination	NCLAPLAKVIHDNFG CCHHHHHHHHHCCCC	49.78	-
175	Sulfoxidation	FGIVEGLMTTVHAIT CCHHHHHHHHHHHHH	4.31	30846556
176	Phosphorylation	GIVEGLMTTVHAITA CHHHHHHHHHHHHHE	30.61	24972180
177	Phosphorylation	IVEGLMTTVHAITAT HHHHHHHHHHHHHEE	9.06	30266825
182	Phosphorylation	MTTVHAITATQKTVD HHHHHHHHEEECCCC	25.16	30266825
184	Phosphorylation	TVHAITATQKTVDGP HHHHHHEEECCCCCC	23.19	29255136
186	2-Hydroxyisobutyrylation	HAITATQKTVDGPSG HHHHEEECCCCCCCC	46.27	-
186	Acetylation	HAITATQKTVDGPSG HHHHEEECCCCCCCC	46.27	5908143
186	Sumoylation	HAITATQKTVDGPSG HHHHEEECCCCCCCC	46.27	28112733
186	Ubiquitination	HAITATQKTVDGPSG HHHHEEECCCCCCCC	46.27	19608861
187	Phosphorylation	AITATQKTVDGPSGK HHHEEECCCCCCCCC	17.63	19764811
192	Phosphorylation	QKTVDGPSGKLWRDG ECCCCCCCCCCCCCC	54.83	28985074
194	"N6,N6-dimethyllysine"	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
194	2-Hydroxyisobutyrylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
194	Acetylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	19608861
194	Malonylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	26320211
194	Methylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	18183946
194	Sumoylation	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
194	Ubiquitination	TVDGPSGKLWRDGRG CCCCCCCCCCCCCCC	49.57	-
200	Methylation	GKLWRDGRGALQNII CCCCCCCCCHHHHHC	31.34	-
210	O-linked_Glycosylation	LQNIIPASTGAAKAV HHHHCCCCCCHHHHH	23.24	28510447
210	Phosphorylation	LQNIIPASTGAAKAV HHHHCCCCCCHHHHH	23.24	29255136
211	Phosphorylation	QNIIPASTGAAKAVG HHHCCCCCCHHHHHH	32.71	29255136
215	"N6,N6-dimethyllysine"	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
215	2-Hydroxyisobutyrylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
215	Acetylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	23954790
215	Malonylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	26320211
215	Methylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	18183946
215	Sumoylation	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	-
215	Ubiquitination	PASTGAAKAVGKVIP CCCCCHHHHHHHHHH	42.97	21890473
219	"N6,N6-dimethyllysine"	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	-
219	2-Hydroxyisobutyrylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	-
219	Acetylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	19608861
219	Malonylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	26320211
219	Methylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	-
219	Sumoylation	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	-
219	Ubiquitination	GAAKAVGKVIPELNG CHHHHHHHHHHHHCC	30.32	21890473
225	Deamidated asparagine	GKVIPELNGKLTGMA HHHHHHHCCEEEEEE	43.84	-
225	Deamidation	GKVIPELNGKLTGMA HHHHHHHCCEEEEEE	43.84	18183946
227	"N6,N6-dimethyllysine"	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	-
227	Acetylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	19608861
227	Methylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	18183946
227	Succinylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	23954790
227	Sumoylation	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	-
227	Ubiquitination	VIPELNGKLTGMAFR HHHHHCCEEEEEEEE	41.63	21890473
229	Phosphorylation	PELNGKLTGMAFRVP HHHCCEEEEEEEECC	28.53	18183946
231	Sulfoxidation	LNGKLTGMAFRVPTA HCCEEEEEEEECCCC	2.41	30846556
237	Phosphorylation	GMAFRVPTANVSVVD EEEEECCCCCEEEEE	28.18	28985074
241	Phosphorylation	RVPTANVSVVDLTCR ECCCCCEEEEEEEEE	19.07	29255136
246	Phosphorylation	NVSVVDLTCRLEKPA CEEEEEEEEEECCCC	7.36	29978859
247	S-nitrosocysteine	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	-
247	Glutathionylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	22555962
247	S-nitrosylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	25417112
247	S-palmitoylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	29575903
247	Succinylation	VSVVDLTCRLEKPAK EEEEEEEEEECCCCC	6.42	-
251	Acetylation	DLTCRLEKPAKYDDI EEEEEECCCCCHHHH	55.67	25953088
251	Malonylation	DLTCRLEKPAKYDDI EEEEEECCCCCHHHH	55.67	26320211
251	Ubiquitination	DLTCRLEKPAKYDDI EEEEEECCCCCHHHH	55.67	21906983
254	2-Hydroxyisobutyrylation	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	-
254	Acetylation	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	19608861
254	Sumoylation	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	-
254	Ubiquitination	CRLEKPAKYDDIKKV EEECCCCCHHHHHHH	58.71	21906983
255	Phosphorylation	RLEKPAKYDDIKKVV EECCCCCHHHHHHHH	22.43	28796482
259	Acetylation	PAKYDDIKKVVKQAS CCCHHHHHHHHHHHH	46.65	23236377
259	Sumoylation	PAKYDDIKKVVKQAS CCCHHHHHHHHHHHH	46.65	-
259	Ubiquitination	PAKYDDIKKVVKQAS CCCHHHHHHHHHHHH	46.65	21906983
260	"N6,N6-dimethyllysine"	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	-
260	Acetylation	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	25953088
260	Methylation	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	18183946
260	Sumoylation	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	-
260	Ubiquitination	AKYDDIKKVVKQASE CCHHHHHHHHHHHHC	53.23	-
263	"N6,N6-dimethyllysine"	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	-
263	2-Hydroxyisobutyrylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	-
263	Acetylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	21466224
263	Malonylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	26320211
263	Methylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	18183946
263	Sumoylation	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	-
263	Ubiquitination	DDIKKVVKQASEGPL HHHHHHHHHHHCCCC	43.04	21890473
266	Phosphorylation	KKVVKQASEGPLKGI HHHHHHHHCCCCCEE	40.36	29396449
271	Acetylation	QASEGPLKGILGYTE HHHCCCCCEEECCCE	47.22	26051181
271	Ubiquitination	QASEGPLKGILGYTE HHHCCCCCEEECCCE	47.22	21906983
276	Nitration	PLKGILGYTEHQVVS CCCEEECCCEEEEEC	12.90	-
276	Phosphorylation	PLKGILGYTEHQVVS CCCEEECCCEEEEEC	12.90	-
284	Phosphorylation	TEHQVVSSDFNSDTH CEEEEECCCCCCCCC	34.31	-
288	Phosphorylation	VVSSDFNSDTHSSTF EECCCCCCCCCCCCC	43.83	26437602
290	O-linked_Glycosylation	SSDFNSDTHSSTFDA CCCCCCCCCCCCCCC	24.39	OGP
290	Phosphorylation	SSDFNSDTHSSTFDA CCCCCCCCCCCCCCC	24.39	26437602
294	Phosphorylation	NSDTHSSTFDAGAGI CCCCCCCCCCCCCCE	28.66	26437602
312	Phosphorylation	DHFVKLISWYDNEFG HHHHHHHHHCCCCCC	29.98	18183946
314	Nitration	FVKLISWYDNEFGYS HHHHHHHCCCCCCCH	11.33	-
314	Phosphorylation	FVKLISWYDNEFGYS HHHHHHHCCCCCCCH	11.33	27273156
316	Deamidated asparagine	KLISWYDNEFGYSNR HHHHHCCCCCCCHHH	30.69	-
316	Deamidation	KLISWYDNEFGYSNR HHHHHCCCCCCCHHH	30.69	18183946
320	Nitration	WYDNEFGYSNRVVDL HCCCCCCCHHHHHHH	14.21	-
320	Phosphorylation	WYDNEFGYSNRVVDL HCCCCCCCHHHHHHH	14.21	21712546
321	Phosphorylation	YDNEFGYSNRVVDLM CCCCCCCHHHHHHHH	20.66	28796482
323	Methylation	NEFGYSNRVVDLMAH CCCCCHHHHHHHHHH	24.72	-
328	Sulfoxidation	SNRVVDLMAHMASKE HHHHHHHHHHHHCCC	1.76	21406390
331	Sulfoxidation	VVDLMAHMASKE--- HHHHHHHHHCCC---	3.06	30846556
333	Phosphorylation	DLMAHMASKE----- HHHHHHHCCC-----	29.73	22617229
334	"N6,N6-dimethyllysine"	LMAHMASKE------ HHHHHHCCC------	58.88	-
334	2-Hydroxyisobutyrylation	LMAHMASKE------ HHHHHHCCC------	58.88	-
334	Acetylation	LMAHMASKE------ HHHHHHCCC------	58.88	23954790
334	Malonylation	LMAHMASKE------ HHHHHHCCC------	58.88	26320211
334	Methylation	LMAHMASKE------ HHHHHHCCC------	58.88	18183946
334	Ubiquitination	LMAHMASKE------ 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
42	Y	Phosphorylation	Kinase	SRC	P12931	PSP
122	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
237	T	Phosphorylation	Kinase	AKT2	P31751	PSP
241	S	Phosphorylation	Kinase	PKCD	Q05655	PSP
246	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
46	M	Oxidation	25086035
Oxidation at Met-46 may play a pivotal role in the formation of these insoluble structures.
105	M	Oxidation	25086035
It has been proposed to destabilize nearby residues, increasing the likelihood of secondary oxidative damages, including oxidation of Tyr-45 and Met-105.
152	C	S-nitrosylation	23332158
S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus (By similarity).
247	C	Phosphorylation	22771119
S-nitrosylation of Cys-247 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.
247	C	S-nitrosylation	22771119
S-nitrosylation of Cys-247 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.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
QRIC2_HUMAN	QRICH2	physical	17353931
THIO_HUMAN	TXN	physical	17353931
STIP1_HUMAN	STIP1	physical	12887926
NPAT_HUMAN	NPAT	physical	12887926
PO2F1_HUMAN	POU2F1	physical	12887926
KPCI_HUMAN	PRKCI	physical	11724794
ATX1_HUMAN	ATXN1	physical	8872471
ANDR_HUMAN	AR	physical	8872471
PDIA2_HUMAN	PDIA2	physical	11488911
SET_HUMAN	SET	physical	16474839
CCNB1_HUMAN	CCNB1	physical	16474839
RBM5_HUMAN	RBM5	physical	21900206
SYK_HUMAN	KARS	physical	21900206
HES1_HUMAN	HES1	physical	21900206
ACTC_HUMAN	ACTC1	physical	21900206
AATM_HUMAN	GOT2	physical	21900206
NFYC_HUMAN	NFYC	physical	21900206
OSMR_HUMAN	OSMR	physical	21900206
OSTF1_HUMAN	OSTF1	physical	21900206
1433E_HUMAN	YWHAE	physical	21900206
EP300_HUMAN	EP300	physical	18552833
G3P_HUMAN	GAPDH	physical	16510976
KAT5_HUMAN	KAT5	physical	15383276
NPM_HUMAN	NPM1	physical	23027902
A4_HUMAN	APP	physical	21832049
PGK1_HUMAN	PGK1	physical	22939629
TPIS_HUMAN	TPI1	physical	22939629
KPYM_HUMAN	PKM	physical	22939629
PGAM1_HUMAN	PGAM1	physical	22939629
OLA1_HUMAN	OLA1	physical	22939629
PABP2_HUMAN	PABPN1	physical	22939629
ROA3_HUMAN	HNRNPA3	physical	22939629
RFA2_HUMAN	RPA2	physical	16169070
G3P_HUMAN	GAPDH	physical	21988832
CPNS1_HUMAN	CAPNS1	physical	22863883
HS71L_HUMAN	HSPA1L	physical	22863883
MAT2B_HUMAN	MAT2B	physical	22863883
PPP5_HUMAN	PPP5C	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
G3P_HUMAN	GAPDH	physical	22134915
M3K5_HUMAN	MAP3K5	physical	25391652
SIAH1_HUMAN	SIAH1	physical	25391652
G3PT_HUMAN	GAPDHS	physical	26186194
ASPC1_HUMAN	ASPSCR1	physical	26186194
AK1A1_HUMAN	AKR1A1	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
CTBP1_HUMAN	CTBP1	physical	26344197
DPYD_HUMAN	DPYD	physical	26344197
DTNB_HUMAN	DTNB	physical	26344197
DUT_HUMAN	DUT	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
ENOG_HUMAN	ENO2	physical	26344197
ENOB_HUMAN	ENO3	physical	26344197
GDPP1_HUMAN	GDPGP1	physical	26344197
GLOD4_HUMAN	GLOD4	physical	26344197
GPD1L_HUMAN	GPD1L	physical	26344197
MSRB3_HUMAN	MSRB3	physical	26344197
PGAM1_HUMAN	PGAM1	physical	26344197
PGAM2_HUMAN	PGAM2	physical	26344197
KPYM_HUMAN	PKM	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
P4R3A_HUMAN	SMEK1	physical	26344197
TNG2_HUMAN	TANGO2	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
PGK1_HUMAN	PGK1	physical	9308888
KNL1_HUMAN	CASC5	physical	26496610
MED8_HUMAN	MED8	physical	26496610
AN36A_HUMAN	ANKRD36	physical	26496610
G3PT_HUMAN	GAPDHS	physical	28514442
ASPC1_HUMAN	ASPSCR1	physical	28514442

Drug and Disease Associations

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

Regulatory Network of G3P_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-186; LYS-194;LYS-219; LYS-227 AND LYS-254, AND MASS SPECTROMETRY.	19608861 [Abstract]
Deamidation
Reference	PubMed
"Strategy for comprehensive identification of post-translationalmodifications in cellular proteins, including low abundantmodifications: application to glyceraldehyde-3-phosphatedehydrogenase."; Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.; J. Proteome Res. 7:587-602(2008). Cited for: PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 ANDSER-312, DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155;ASN-225 AND ASN-316, AND METHYLATION AT LYS-5; LYS-66; LYS-194;LYS-215; LYS-227; LYS-260; LYS-263 AND LYS-334.	18183946 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-194 AND LYS-215.	21908771 [Abstract]
Methylation
Reference	PubMed
"Strategy for comprehensive identification of post-translationalmodifications in cellular proteins, including low abundantmodifications: application to glyceraldehyde-3-phosphatedehydrogenase."; Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.; J. Proteome Res. 7:587-602(2008). Cited for: PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 ANDSER-312, DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155;ASN-225 AND ASN-316, AND METHYLATION AT LYS-5; LYS-66; LYS-194;LYS-215; LYS-227; LYS-260; LYS-263 AND LYS-334.	18183946 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-194 AND LYS-215.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184; SER-210; THR-211AND SER-312, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; THR-154 ANDTHR-211, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151 AND THR-184,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Strategy for comprehensive identification of post-translationalmodifications in cellular proteins, including low abundantmodifications: application to glyceraldehyde-3-phosphatedehydrogenase."; Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.; J. Proteome Res. 7:587-602(2008). Cited for: PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 ANDSER-312, DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155;ASN-225 AND ASN-316, AND METHYLATION AT LYS-5; LYS-66; LYS-194;LYS-215; LYS-227; LYS-260; LYS-263 AND LYS-334.	18183946 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.	17081983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-320, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, AND MASSSPECTROMETRY.	15592455 [Abstract]

show

show

show

show

show