dbPTM

PGK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGK1_HUMAN
UniProt AC	P00558
Protein Name	Phosphoglycerate kinase 1
Gene Name	PGK1
Organism	Homo sapiens (Human).
Sequence Length	417
Subcellular Localization	Cytoplasm.
Protein Description	In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). [PubMed: 2324090 May play a role in sperm motility]
Protein Sequence	MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSLSNKLTL ------CCCCCCCCC	40.27	22814378
2	Phosphorylation	------MSLSNKLTL ------CCCCCCCCC	40.27	28464451
4	Phosphorylation	----MSLSNKLTLDK ----CCCCCCCCCCC	25.31	28464451
6	2-Hydroxyisobutyrylation	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	-
6	Acetylation	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	26822725
6	Succinylation	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	-
6	Succinylation	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	-
6	Ubiquitination	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	-
8	Phosphorylation	MSLSNKLTLDKLDVK CCCCCCCCCCCCCCC	34.22	28857561
11	Ubiquitination	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	21890473
11	2-Hydroxyisobutyrylation	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	-
11	Acetylation	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	19608861
11	Ubiquitination	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	21890473
13	Ubiquitination	KLTLDKLDVKGKRVV CCCCCCCCCCCCEEE	45.91	-
15	Acetylation	TLDKLDVKGKRVVMR CCCCCCCCCCEEEEE	59.38	25953088
15	Malonylation	TLDKLDVKGKRVVMR CCCCCCCCCCEEEEE	59.38	26320211
15	Ubiquitination	TLDKLDVKGKRVVMR CCCCCCCCCCEEEEE	59.38	-
17	Ubiquitination	DKLDVKGKRVVMRVD CCCCCCCCEEEEEEE	35.98	-
20	Acetylation	DVKGKRVVMRVDFNV CCCCCEEEEEEEECC	2.05	-
20	Ubiquitination	DVKGKRVVMRVDFNV CCCCCEEEEEEEECC	2.05	-
28	Ubiquitination	MRVDFNVPMKNNQIT EEEEECCCCCCCCCC	29.18	-
29	Sulfoxidation	RVDFNVPMKNNQITN EEEECCCCCCCCCCC	6.72	21406390
30	Ubiquitination	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	21890473
30	2-Hydroxyisobutyrylation	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	-
30	Acetylation	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	23954790
30	Malonylation	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	26320211
30	Methylation	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	22637755
30	Sumoylation	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	19608861
30	Ubiquitination	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	21890473
35	O-linked_Glycosylation	PMKNNQITNNQRIKA CCCCCCCCCCHHHHH	20.53	31911580
35	Phosphorylation	PMKNNQITNNQRIKA CCCCCCCCCCHHHHH	20.53	20071362
39	Methylation	NQITNNQRIKAAVPS CCCCCCHHHHHHCCC	34.20	115487233
41	2-Hydroxyisobutyrylation	ITNNQRIKAAVPSIK CCCCHHHHHHCCCCE	32.27	-
41	Malonylation	ITNNQRIKAAVPSIK CCCCHHHHHHCCCCE	32.27	26320211
41	Ubiquitination	ITNNQRIKAAVPSIK CCCCHHHHHHCCCCE	32.27	-
46	O-linked_Glycosylation	RIKAAVPSIKFCLDN HHHHHCCCCEEEECC	31.63	31911580
46	Phosphorylation	RIKAAVPSIKFCLDN HHHHHCCCCEEEECC	31.63	28985074
47	Acetylation	IKAAVPSIKFCLDNG HHHHCCCCEEEECCC	3.03	-
47	Ubiquitination	IKAAVPSIKFCLDNG HHHHCCCCEEEECCC	3.03	-
48	Ubiquitination	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	21890473
48	Acetylation	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	19608861
48	Succinylation	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	-
48	Succinylation	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	19608861
48	Ubiquitination	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	21890473
50	S-nitrosocysteine	AVPSIKFCLDNGAKS HCCCCEEEECCCCCE	3.86	-
50	S-nitrosylation	AVPSIKFCLDNGAKS HCCCCEEEECCCCCE	3.86	22178444
50	S-palmitoylation	AVPSIKFCLDNGAKS HCCCCEEEECCCCCE	3.86	29575903
56	2-Hydroxyisobutyrylation	FCLDNGAKSVVLMSH EEECCCCCEEEEECC	45.22	-
56	Acetylation	FCLDNGAKSVVLMSH EEECCCCCEEEEECC	45.22	26051181
56	Ubiquitination	FCLDNGAKSVVLMSH EEECCCCCEEEEECC	45.22	-
57	Phosphorylation	CLDNGAKSVVLMSHL EECCCCCEEEEECCC	19.54	26356563
58	Ubiquitination	LDNGAKSVVLMSHLG ECCCCCEEEEECCCC	3.65	-
61	Sulfoxidation	GAKSVVLMSHLGRPD CCCEEEEECCCCCCC	1.28	30846556
62	Phosphorylation	AKSVVLMSHLGRPDG CCEEEEECCCCCCCC	16.05	26356563
63	Acetylation	KSVVLMSHLGRPDGV CEEEEECCCCCCCCC	20.52	-
63	Ubiquitination	KSVVLMSHLGRPDGV CEEEEECCCCCCCCC	20.52	-
69	Acetylation	SHLGRPDGVPMPDKY CCCCCCCCCCCCCCC	28.27	-
69	Ubiquitination	SHLGRPDGVPMPDKY CCCCCCCCCCCCCCC	28.27	-
72	Sulfoxidation	GRPDGVPMPDKYSLE CCCCCCCCCCCCCCH	6.61	30846556
75	Ubiquitination	DGVPMPDKYSLEPVA CCCCCCCCCCCHHHH	30.76	21890473
75	Acetylation	DGVPMPDKYSLEPVA CCCCCCCCCCCHHHH	30.76	19608861
75	Malonylation	DGVPMPDKYSLEPVA CCCCCCCCCCCHHHH	30.76	26320211
75	Ubiquitination	DGVPMPDKYSLEPVA CCCCCCCCCCCHHHH	30.76	21890473
76	Nitration	GVPMPDKYSLEPVAV CCCCCCCCCCHHHHH	26.35	-
76	Phosphorylation	GVPMPDKYSLEPVAV CCCCCCCCCCHHHHH	26.35	25159151
77	Phosphorylation	VPMPDKYSLEPVAVE CCCCCCCCCHHHHHH	31.81	27259358
78	Acetylation	PMPDKYSLEPVAVEL CCCCCCCCHHHHHHH	8.60	-
78	Ubiquitination	PMPDKYSLEPVAVEL CCCCCCCCHHHHHHH	8.60	-
86	Ubiquitination	EPVAVELKSLLGKDV HHHHHHHHHHCCCCE	26.08	21890473
86	2-Hydroxyisobutyrylation	EPVAVELKSLLGKDV HHHHHHHHHHCCCCE	26.08	-
86	Acetylation	EPVAVELKSLLGKDV HHHHHHHHHHCCCCE	26.08	19608861
86	Ubiquitination	EPVAVELKSLLGKDV HHHHHHHHHHCCCCE	26.08	21890473
87	Phosphorylation	PVAVELKSLLGKDVL HHHHHHHHHCCCCEE	41.26	22617229
91	2-Hydroxyisobutyrylation	ELKSLLGKDVLFLKD HHHHHCCCCEEEECC	44.63	-
91	Acetylation	ELKSLLGKDVLFLKD HHHHHCCCCEEEECC	44.63	23954790
91	Ubiquitination	ELKSLLGKDVLFLKD HHHHHCCCCEEEECC	44.63	21890473
97	2-Hydroxyisobutyrylation	GKDVLFLKDCVGPEV CCCEEEECCCCCHHH	41.57	-
97	Acetylation	GKDVLFLKDCVGPEV CCCEEEECCCCCHHH	41.57	19608861
97	Other	GKDVLFLKDCVGPEV CCCEEEECCCCCHHH	41.57	29775581
97	Ubiquitination	GKDVLFLKDCVGPEV CCCEEEECCCCCHHH	41.57	21890473
99	S-nitrosocysteine	DVLFLKDCVGPEVEK CEEEECCCCCHHHHH	3.49	-
99	S-nitrosylation	DVLFLKDCVGPEVEK CEEEECCCCCHHHHH	3.49	22178444
103	Acetylation	LKDCVGPEVEKACAN ECCCCCHHHHHHHCC	58.33	-
103	Ubiquitination	LKDCVGPEVEKACAN ECCCCCHHHHHHHCC	58.33	-
105	Acetylation	DCVGPEVEKACANPA CCCCHHHHHHHCCCC	33.02	-
106	Acetylation	CVGPEVEKACANPAA CCCHHHHHHHCCCCC	54.67	23954790
106	Ubiquitination	CVGPEVEKACANPAA CCCHHHHHHHCCCCC	54.67	-
108	S-nitrosocysteine	GPEVEKACANPAAGS CHHHHHHHCCCCCCC	5.79	-
108	Glutathionylation	GPEVEKACANPAAGS CHHHHHHHCCCCCCC	5.79	22555962
108	S-nitrosylation	GPEVEKACANPAAGS CHHHHHHHCCCCCCC	5.79	18335467
108	S-palmitoylation	GPEVEKACANPAAGS CHHHHHHHCCCCCCC	5.79	29575903
113	Acetylation	KACANPAAGSVILLE HHHCCCCCCCEEEEE	16.43	-
113	Ubiquitination	KACANPAAGSVILLE HHHCCCCCCCEEEEE	16.43	-
115	Phosphorylation	CANPAAGSVILLENL HCCCCCCCEEEEECC	10.97	21712546
118	Acetylation	PAAGSVILLENLRFH CCCCCEEEEECCEEE	4.62	-
118	Ubiquitination	PAAGSVILLENLRFH CCCCCEEEEECCEEE	4.62	-
123	Methylation	VILLENLRFHVEEEG EEEEECCEEEEEECC	31.07	115487217
128	Acetylation	NLRFHVEEEGKGKDA CCEEEEEECCCCCCC	71.59	-
128	Ubiquitination	NLRFHVEEEGKGKDA CCEEEEEECCCCCCC	71.59	-
131	N6-malonyllysine	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	-
131	Acetylation	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	19608861
131	Malonylation	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	26320211
131	Ubiquitination	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	19608861
133	Acetylation	VEEEGKGKDASGNKV EEECCCCCCCCCCCC	54.32	23749302
136	Phosphorylation	EGKGKDASGNKVKAE CCCCCCCCCCCCCCC	53.70	28857561
139	Ubiquitination	GKDASGNKVKAEPAK CCCCCCCCCCCCHHH	48.95	-
141	Acetylation	DASGNKVKAEPAKIE CCCCCCCCCCHHHHH	48.95	23749302
141	Malonylation	DASGNKVKAEPAKIE CCCCCCCCCCHHHHH	48.95	26320211
141	Ubiquitination	DASGNKVKAEPAKIE CCCCCCCCCCHHHHH	48.95	-
146	Ubiquitination	KVKAEPAKIEAFRAS CCCCCHHHHHHHHHH	52.36	21890473
146	2-Hydroxyisobutyrylation	KVKAEPAKIEAFRAS CCCCCHHHHHHHHHH	52.36	-
146	Acetylation	KVKAEPAKIEAFRAS CCCCCHHHHHHHHHH	52.36	19608861
146	Ubiquitination	KVKAEPAKIEAFRAS CCCCCHHHHHHHHHH	52.36	21890473
153	Phosphorylation	KIEAFRASLSKLGDV HHHHHHHHHHHHCCE	28.99	25159151
155	Phosphorylation	EAFRASLSKLGDVYV HHHHHHHHHHCCEEE	24.28	29523821
156	Ubiquitination	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	21890473
156	Ubiquitination	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	21890473
156	2-Hydroxyisobutyrylation	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	-
156	Acetylation	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	23954790
156	Malonylation	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	26320211
156	Ubiquitination	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	21890473
161	Nitration	LSKLGDVYVNDAFGT HHHHCCEEECCCCCC	9.77	-
161	Phosphorylation	LSKLGDVYVNDAFGT HHHHCCEEECCCCCC	9.77	28796482
163	Acetylation	KLGDVYVNDAFGTAH HHCCEEECCCCCCCC	19.73	-
163	Ubiquitination	KLGDVYVNDAFGTAH HHCCEEECCCCCCCC	19.73	-
164	Ubiquitination	LGDVYVNDAFGTAHR HCCEEECCCCCCCCC	32.98	-
168	Phosphorylation	YVNDAFGTAHRAHSS EECCCCCCCCCCCHH	16.91	28857561
171	Ubiquitination	DAFGTAHRAHSSMVG CCCCCCCCCCHHCCC	31.37	21890473
174	O-linked_Glycosylation	GTAHRAHSSMVGVNL CCCCCCCHHCCCCCC	21.10	31911580
174	Phosphorylation	GTAHRAHSSMVGVNL CCCCCCCHHCCCCCC	21.10	20068231
175	O-linked_Glycosylation	TAHRAHSSMVGVNLP CCCCCCHHCCCCCCC	13.97	31911580
175	Phosphorylation	TAHRAHSSMVGVNLP CCCCCCHHCCCCCCC	13.97	20068231
176	Sulfoxidation	AHRAHSSMVGVNLPQ CCCCCHHCCCCCCCC	3.22	21406390
184	Ubiquitination	VGVNLPQKAGGFLMK CCCCCCCCCCCEECH	47.24	21890473
184	2-Hydroxyisobutyrylation	VGVNLPQKAGGFLMK CCCCCCCCCCCEECH	47.24	-
184	Acetylation	VGVNLPQKAGGFLMK CCCCCCCCCCCEECH	47.24	25953088
184	Ubiquitination	VGVNLPQKAGGFLMK CCCCCCCCCCCEECH	47.24	21906983
188	Ubiquitination	LPQKAGGFLMKKELN CCCCCCCEECHHHHH	6.19	21890473
191	2-Hydroxyisobutyrylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	-
191	Acetylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	23749302
191	Malonylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	32601280
191	Methylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	24883637
191	Succinylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	-
191	Succinylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	-
191	Ubiquitination	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	-
192	Ubiquitination	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	21890473
192	Acetylation	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	-
192	Ubiquitination	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	21890473
192	2-Hydroxyisobutyrylation	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	-
192	Malonylation	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	26320211
192	Ubiquitination	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	21890473
196	Nitration	LMKKELNYFAKALES ECHHHHHHHHHHHHC	19.96	-
196	Phosphorylation	LMKKELNYFAKALES ECHHHHHHHHHHHHC	19.96	27273156
199	Ubiquitination	KELNYFAKALESPER HHHHHHHHHHHCCCC	43.54	21890473
199	Acetylation	KELNYFAKALESPER HHHHHHHHHHHCCCC	43.54	19608861
199	Ubiquitination	KELNYFAKALESPER HHHHHHHHHHHCCCC	43.54	21890473
203	Phosphorylation	YFAKALESPERPFLA HHHHHHHCCCCCCCH	32.67	29255136
216	Ubiquitination	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	21890473
216	2-Hydroxyisobutyrylation	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	-
216	Acetylation	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	23954790
216	Other	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	29775581
216	Ubiquitination	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	21890473
220	Ubiquitination	GGAKVADKIQLINNM CCHHHHHHHHHHHHH	23.71	21890473
220	2-Hydroxyisobutyrylation	GGAKVADKIQLINNM CCHHHHHHHHHHHHH	23.71	-
220	Acetylation	GGAKVADKIQLINNM CCHHHHHHHHHHHHH	23.71	23954790
220	Malonylation	GGAKVADKIQLINNM CCHHHHHHHHHHHHH	23.71	26320211
220	Ubiquitination	GGAKVADKIQLINNM CCHHHHHHHHHHHHH	23.71	21890473
227	Sulfoxidation	KIQLINNMLDKVNEM HHHHHHHHHHHHHHH	4.41	21406390
234	Sulfoxidation	MLDKVNEMIIGGGMA HHHHHHHHHCCCHHH	1.97	28465586
236	Ubiquitination	DKVNEMIIGGGMAFT HHHHHHHCCCHHHHH	3.96	21890473
239	Acetylation	NEMIIGGGMAFTFLK HHHHCCCHHHHHHHH	10.07	-
239	Ubiquitination	NEMIIGGGMAFTFLK HHHHCCCHHHHHHHH	10.07	-
240	Sulfoxidation	EMIIGGGMAFTFLKV HHHCCCHHHHHHHHH	2.91	30846556
243	Phosphorylation	IGGGMAFTFLKVLNN CCCHHHHHHHHHHCC	20.65	22817900
244	Ubiquitination	GGGMAFTFLKVLNNM CCHHHHHHHHHHCCC	5.12	-
246	Ubiquitination	GMAFTFLKVLNNMEI HHHHHHHHHHCCCCC	40.25	-
251	Ubiquitination	FLKVLNNMEIGTSLF HHHHHCCCCCCCCCC	3.75	-
251	Sulfoxidation	FLKVLNNMEIGTSLF HHHHHCCCCCCCCCC	3.75	21406390
255	O-linked_Glycosylation	LNNMEIGTSLFDEEG HCCCCCCCCCCCHHH	28.11	31911580
255	Phosphorylation	LNNMEIGTSLFDEEG HCCCCCCCCCCCHHH	28.11	21712546
256	Phosphorylation	NNMEIGTSLFDEEGA CCCCCCCCCCCHHHH	23.09	21712546
263	Acetylation	SLFDEEGAKIVKDLM CCCCHHHHHHHHHHH	11.15	-
263	Ubiquitination	SLFDEEGAKIVKDLM CCCCHHHHHHHHHHH	11.15	-
264	2-Hydroxyisobutyrylation	LFDEEGAKIVKDLMS CCCHHHHHHHHHHHH	59.91	-
264	Acetylation	LFDEEGAKIVKDLMS CCCHHHHHHHHHHHH	59.91	25953088
264	Ubiquitination	LFDEEGAKIVKDLMS CCCHHHHHHHHHHHH	59.91	21906983
267	Ubiquitination	EEGAKIVKDLMSKAE HHHHHHHHHHHHHHH	48.93	21890473
267	2-Hydroxyisobutyrylation	EEGAKIVKDLMSKAE HHHHHHHHHHHHHHH	48.93	-
267	Acetylation	EEGAKIVKDLMSKAE HHHHHHHHHHHHHHH	48.93	19608861
267	Ubiquitination	EEGAKIVKDLMSKAE HHHHHHHHHHHHHHH	48.93	21890473
271	Phosphorylation	KIVKDLMSKAEKNGV HHHHHHHHHHHHCCC	35.69	22673903
272	2-Hydroxyisobutyrylation	IVKDLMSKAEKNGVK HHHHHHHHHHHCCCE	46.75	-
272	Acetylation	IVKDLMSKAEKNGVK HHHHHHHHHHHCCCE	46.75	25953088
272	Ubiquitination	IVKDLMSKAEKNGVK HHHHHHHHHHHCCCE	46.75	-
275	Acetylation	DLMSKAEKNGVKITL HHHHHHHHCCCEEEE	64.95	7964599
279	Ubiquitination	KAEKNGVKITLPVDF HHHHCCCEEEEECCE	31.22	-
281	Phosphorylation	EKNGVKITLPVDFVT HHCCCEEEEECCEEE	21.20	21712546
288	Phosphorylation	TLPVDFVTADKFDEN EEECCEEEHHHCCCC	29.18	21712546
291	Ubiquitination	VDFVTADKFDENAKT CCEEEHHHCCCCCCC	52.85	21890473
291	2-Hydroxyisobutyrylation	VDFVTADKFDENAKT CCEEEHHHCCCCCCC	52.85	-
291	Acetylation	VDFVTADKFDENAKT CCEEEHHHCCCCCCC	52.85	19608861
291	Ubiquitination	VDFVTADKFDENAKT CCEEEHHHCCCCCCC	52.85	21890473
294	Ubiquitination	VTADKFDENAKTGQA EEHHHCCCCCCCCCC	63.32	-
295	Acetylation	TADKFDENAKTGQAT EHHHCCCCCCCCCCE	48.89	-
295	Ubiquitination	TADKFDENAKTGQAT EHHHCCCCCCCCCCE	48.89	-
297	Ubiquitination	DKFDENAKTGQATVA HHCCCCCCCCCCEEE	65.84	-
298	Phosphorylation	KFDENAKTGQATVAS HCCCCCCCCCCEEEC	31.92	21406692
302	Phosphorylation	NAKTGQATVASGIPA CCCCCCCEEECCCCC	14.55	21406692
304	Ubiquitination	KTGQATVASGIPAGW CCCCCEEECCCCCCC	9.55	-
305	Phosphorylation	TGQATVASGIPAGWM CCCCEEECCCCCCCC	32.68	21406692
312	Sulfoxidation	SGIPAGWMGLDCGPE CCCCCCCCCCCCCCH	3.60	30846556
316	Glutathionylation	AGWMGLDCGPESSKK CCCCCCCCCCHHHHH	13.57	22555962
320	Phosphorylation	GLDCGPESSKKYAEA CCCCCCHHHHHHHHH	51.06	21406692
321	Phosphorylation	LDCGPESSKKYAEAV CCCCCHHHHHHHHHH	31.35	21406692
322	2-Hydroxyisobutyrylation	DCGPESSKKYAEAVT CCCCHHHHHHHHHHH	60.11	-
322	Acetylation	DCGPESSKKYAEAVT CCCCHHHHHHHHHHH	60.11	25953088
322	Ubiquitination	DCGPESSKKYAEAVT CCCCHHHHHHHHHHH	60.11	-
323	2-Hydroxyisobutyrylation	CGPESSKKYAEAVTR CCCHHHHHHHHHHHH	52.20	-
323	Acetylation	CGPESSKKYAEAVTR CCCHHHHHHHHHHHH	52.20	23749302
323	Other	CGPESSKKYAEAVTR CCCHHHHHHHHHHHH	52.20	29775581
323	Ubiquitination	CGPESSKKYAEAVTR CCCHHHHHHHHHHHH	52.20	19608861
324	Phosphorylation	GPESSKKYAEAVTRA CCHHHHHHHHHHHHH	17.26	26437602
325	Acetylation	PESSKKYAEAVTRAK CHHHHHHHHHHHHHH	13.72	-
325	Ubiquitination	PESSKKYAEAVTRAK CHHHHHHHHHHHHHH	13.72	-
329	Phosphorylation	KKYAEAVTRAKQIVW HHHHHHHHHHHHHHH	31.77	26437602
332	Ubiquitination	AEAVTRAKQIVWNGP HHHHHHHHHHHHCCC	36.95	21906983
333	Acetylation	EAVTRAKQIVWNGPV HHHHHHHHHHHCCCC	34.19	-
333	Ubiquitination	EAVTRAKQIVWNGPV HHHHHHHHHHHCCCC	34.19	21890473
353	Acetylation	EAFARGTKALMDEVV HHHHHHHHHHHHHHH	42.20	23749302
353	Malonylation	EAFARGTKALMDEVV HHHHHHHHHHHHHHH	42.20	26320211
353	Ubiquitination	EAFARGTKALMDEVV HHHHHHHHHHHHHHH	42.20	-
354	Acetylation	AFARGTKALMDEVVK HHHHHHHHHHHHHHH	14.14	-
354	Ubiquitination	AFARGTKALMDEVVK HHHHHHHHHHHHHHH	14.14	-
356	Sulfoxidation	ARGTKALMDEVVKAT HHHHHHHHHHHHHHH	5.02	21406390
360	Acetylation	KALMDEVVKATSRGC HHHHHHHHHHHCCCC	3.08	-
360	Ubiquitination	KALMDEVVKATSRGC HHHHHHHHHHHCCCC	3.08	-
361	Ubiquitination	ALMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	21890473
361	2-Hydroxyisobutyrylation	ALMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	-
361	Acetylation	ALMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	23954790
361	Malonylation	ALMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	26320211
361	Ubiquitination	ALMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	21890473
363	Phosphorylation	MDEVVKATSRGCITI HHHHHHHHCCCCEEE	17.15	28857561
364	Phosphorylation	DEVVKATSRGCITII HHHHHHHCCCCEEEE	31.38	28857561
365	Methylation	EVVKATSRGCITIIG HHHHHHCCCCEEEEC	39.38	115487225
367	Glutathionylation	VKATSRGCITIIGGG HHHHCCCCEEEECCC	2.11	22555962
367	S-nitrosylation	VKATSRGCITIIGGG HHHHCCCCEEEECCC	2.11	22178444
367	S-palmitoylation	VKATSRGCITIIGGG HHHHCCCCEEEECCC	2.11	29575903
369	Phosphorylation	ATSRGCITIIGGGDT HHCCCCEEEECCCCC	15.60	28857561
378	Ubiquitination	IGGGDTATCCAKWNT ECCCCCEEEECCCCC	15.37	-
378	Phosphorylation	IGGGDTATCCAKWNT ECCCCCEEEECCCCC	15.37	28857561
379	S-nitrosylation	GGGDTATCCAKWNTE CCCCCEEEECCCCCC	1.65	22178444
379	S-palmitoylation	GGGDTATCCAKWNTE CCCCCEEEECCCCCC	1.65	29575903
380	S-nitrosylation	GGDTATCCAKWNTED CCCCEEEECCCCCCC	3.66	22178444
380	S-palmitoylation	GGDTATCCAKWNTED CCCCEEEECCCCCCC	3.66	29575903
382	2-Hydroxyisobutyrylation	DTATCCAKWNTEDKV CCEEEECCCCCCCCE	27.36	-
382	Acetylation	DTATCCAKWNTEDKV CCEEEECCCCCCCCE	27.36	23954790
382	Ubiquitination	DTATCCAKWNTEDKV CCEEEECCCCCCCCE	27.36	-
388	2-Hydroxyisobutyrylation	AKWNTEDKVSHVSTG CCCCCCCCEEEEECC	39.13	-
388	Acetylation	AKWNTEDKVSHVSTG CCCCCCCCEEEEECC	39.13	23954790
388	Ubiquitination	AKWNTEDKVSHVSTG CCCCCCCCEEEEECC	39.13	-
390	Phosphorylation	WNTEDKVSHVSTGGG CCCCCCEEEEECCCC	24.74	20068231
393	Phosphorylation	EDKVSHVSTGGGASL CCCEEEEECCCCHHH	18.86	20068231
394	Phosphorylation	DKVSHVSTGGGASLE CCEEEEECCCCHHHH	38.46	25693802
399	Phosphorylation	VSTGGGASLELLEGK EECCCCHHHHHHCCC	26.17	25849741
406	Acetylation	SLELLEGKVLPGVDA HHHHHCCCCCCCCCH	31.09	23954790
406	Ubiquitination	SLELLEGKVLPGVDA HHHHHCCCCCCCCCH	31.09	19608861
415	O-linked_Glycosylation	LPGVDALSNI----- CCCCCHHCCC-----	33.91	31911580
415	Phosphorylation	LPGVDALSNI----- CCCCCHHCCC-----	33.91	29507054

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
203	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
243	T	Phosphorylation	Kinase	PDK1	O15530	PSP
256	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
324	Y	Phosphorylation	Kinase	PGK1	P00558	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PGK1_HUMAN !!

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 PGK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TPIS_HUMAN	TPI1	physical	22939629
TBA4A_HUMAN	TUBA4A	physical	22939629
SCOT1_HUMAN	OXCT1	physical	22939629
AK1A1_HUMAN	AKR1A1	physical	26344197
ALDR_HUMAN	AKR1B1	physical	26344197
AK1BA_HUMAN	AKR1B10	physical	26344197
ALDOA_HUMAN	ALDOA	physical	26344197
ALDOC_HUMAN	ALDOC	physical	26344197
ARPC3_HUMAN	ARPC3	physical	26344197
XPO2_HUMAN	CSE1L	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
ENOG_HUMAN	ENO2	physical	26344197
ENOB_HUMAN	ENO3	physical	26344197
G3P_HUMAN	GAPDH	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
SF01_HUMAN	SF1	physical	26344197
1433S_HUMAN	SFN	physical	26344197
SFPQ_HUMAN	SFPQ	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
1433E_HUMAN	YWHAE	physical	26344197
1433T_HUMAN	YWHAQ	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300653	Phosphoglycerate kinase 1 deficiency (PGK1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00709	Lamivudine

Regulatory Network of PGK1_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-11; LYS-30; LYS-48; LYS-75;LYS-86; LYS-97; LYS-131; LYS-146; LYS-199; LYS-267; LYS-291; LYS-323AND LYS-406, AND MASS SPECTROMETRY.	19608861 [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-131.	21908771 [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-131.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"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-203, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-243, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.	17287340 [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-203, AND MASSSPECTROMETRY.	17081983 [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-196, AND MASSSPECTROMETRY.	15592455 [Abstract]