dbPTM

PGK1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGK1_MOUSE
UniProt AC	P09411
Protein Name	Phosphoglycerate kinase 1
Gene Name	Pgk1
Organism	Mus musculus (Mouse).
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). May play a role in sperm motility..
Protein Sequence	MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAAELKSLLGKDVLFLKDCVGPEVENACANPAAGTVILLENLRFHVEEEGKGKDASGNKVKAEPAKIDAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLYDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGTESSKKYAEAVGRAKQIVWNGPVGVFEWEAFARGTKSLMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSLSNKLTL ------CCCCCCCCC	40.27	23806337
2	Phosphorylation	------MSLSNKLTL ------CCCCCCCCC	40.27	25266776
4	Phosphorylation	----MSLSNKLTLDK ----CCCCCCCCCCC	25.31	25266776
6	Acetylation	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	23806337
6	Succinylation	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	-
6	Succinylation	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	23806337
6	Ubiquitination	--MSLSNKLTLDKLD --CCCCCCCCCCCCC	39.20	-
8	Phosphorylation	MSLSNKLTLDKLDVK CCCCCCCCCCCCCCC	34.22	23984901
11	Acetylation	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	23806337
11	Malonylation	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	26320211
11	Succinylation	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	-
11	Ubiquitination	SNKLTLDKLDVKGKR CCCCCCCCCCCCCCE	50.10	27667366
15	Malonylation	TLDKLDVKGKRVVMR CCCCCCCCCCEEEEE	59.38	26320211
15	Ubiquitination	TLDKLDVKGKRVVMR CCCCCCCCCCEEEEE	59.38	-
30	Acetylation	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	22637757
30	Malonylation	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	26073543
30	Ubiquitination	VDFNVPMKNNQITNN EEECCCCCCCCCCCC	46.83	27667366
41	Acetylation	ITNNQRIKAAVPSIK CCCCHHHHHHCCCCE	32.27	22826441
41	Malonylation	ITNNQRIKAAVPSIK CCCCHHHHHHCCCCE	32.27	26320211
41	Ubiquitination	ITNNQRIKAAVPSIK CCCCHHHHHHCCCCE	32.27	27667366
48	Acetylation	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	23806337
48	Malonylation	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	26320211
48	Succinylation	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	-
48	Succinylation	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	23806337
48	Ubiquitination	KAAVPSIKFCLDNGA HHHCCCCEEEECCCC	34.07	-
50	S-nitrosocysteine	AVPSIKFCLDNGAKS HCCCCEEEECCCCCE	3.86	-
50	Glutathionylation	AVPSIKFCLDNGAKS HCCCCEEEECCCCCE	3.86	24333276
50	S-nitrosylation	AVPSIKFCLDNGAKS HCCCCEEEECCCCCE	3.86	24926564
50	S-palmitoylation	AVPSIKFCLDNGAKS HCCCCEEEECCCCCE	3.86	28526873
62	Phosphorylation	AKSVVLMSHLGRPDG CCEEEEECCCCCCCC	16.05	-
75	Acetylation	DGVPMPDKYSLEPVA CCCCCCCCCCCHHHH	30.76	22826441
75	Malonylation	DGVPMPDKYSLEPVA CCCCCCCCCCCHHHH	30.76	26320211
75	Ubiquitination	DGVPMPDKYSLEPVA CCCCCCCCCCCHHHH	30.76	-
76	Phosphorylation	GVPMPDKYSLEPVAA CCCCCCCCCCHHHHH	26.35	25521595
77	Phosphorylation	VPMPDKYSLEPVAAE CCCCCCCCCHHHHHH	31.81	25521595
86	Acetylation	EPVAAELKSLLGKDV HHHHHHHHHHHCCCE	30.48	22826441
86	Ubiquitination	EPVAAELKSLLGKDV HHHHHHHHHHHCCCE	30.48	22790023
87	Phosphorylation	PVAAELKSLLGKDVL HHHHHHHHHHCCCEE	41.26	26745281
91	Acetylation	ELKSLLGKDVLFLKD HHHHHHCCCEEEEEC	44.63	23806337
91	Succinylation	ELKSLLGKDVLFLKD HHHHHHCCCEEEEEC	44.63	23806337
91	Ubiquitination	ELKSLLGKDVLFLKD HHHHHHCCCEEEEEC	44.63	-
97	Acetylation	GKDVLFLKDCVGPEV CCCEEEEECCCCHHH	41.57	-
97	Other	GKDVLFLKDCVGPEV CCCEEEEECCCCHHH	41.57	-
99	S-nitrosocysteine	DVLFLKDCVGPEVEN CEEEEECCCCHHHHH	3.49	-
99	Glutathionylation	DVLFLKDCVGPEVEN CEEEEECCCCHHHHH	3.49	24333276
99	S-nitrosylation	DVLFLKDCVGPEVEN CEEEEECCCCHHHHH	3.49	24895380
99	S-palmitoylation	DVLFLKDCVGPEVEN CEEEEECCCCHHHHH	3.49	28526873
108	Glutathionylation	GPEVENACANPAAGT CHHHHHHCCCCCCCE	5.92	24333276
108	S-nitrosylation	GPEVENACANPAAGT CHHHHHHCCCCCCCE	5.92	24895380
108	S-palmitoylation	GPEVENACANPAAGT CHHHHHHCCCCCCCE	5.92	28526873
115	Phosphorylation	CANPAAGTVILLENL CCCCCCCEEEEEECE	10.31	26239621
131	N6-malonyllysine	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	-
131	Acetylation	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	22733758
131	Malonylation	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	26073543
131	Ubiquitination	FHVEEEGKGKDASGN EEEEECCCCCCCCCC	67.10	27667366
133	Acetylation	VEEEGKGKDASGNKV EEECCCCCCCCCCCC	54.32	23954790
133	Malonylation	VEEEGKGKDASGNKV EEECCCCCCCCCCCC	54.32	26320211
141	Acetylation	DASGNKVKAEPAKID CCCCCCCCCCHHHHH	48.95	23864654
141	Ubiquitination	DASGNKVKAEPAKID CCCCCCCCCCHHHHH	48.95	22790023
146	Acetylation	KVKAEPAKIDAFRAS CCCCCHHHHHHHHHH	52.41	23201123
146	Malonylation	KVKAEPAKIDAFRAS CCCCCHHHHHHHHHH	52.41	26320211
146	Ubiquitination	KVKAEPAKIDAFRAS CCCCCHHHHHHHHHH	52.41	27667366
153	Phosphorylation	KIDAFRASLSKLGDV HHHHHHHHHHHHCCE	28.99	29176673
155	Phosphorylation	DAFRASLSKLGDVYV HHHHHHHHHHCCEEE	24.28	29176673
156	Acetylation	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	22637685
156	Malonylation	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	26320211
156	Ubiquitination	AFRASLSKLGDVYVN HHHHHHHHHCCEEEC	62.88	22790023
161	Phosphorylation	LSKLGDVYVNDAFGT HHHHCCEEECCCCCC	9.77	-
168	Phosphorylation	YVNDAFGTAHRAHSS EECCCCCCCCCCCHH	16.91	-
174	Phosphorylation	GTAHRAHSSMVGVNL CCCCCCCHHCCCCCC	21.10	28464351
184	Ubiquitination	VGVNLPQKAGGFLMK CCCCCCCCCCCEECH	47.24	22790023
191	Acetylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	23806337
191	Malonylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	26320211
191	Succinylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	-
191	Succinylation	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	23806337
191	Ubiquitination	KAGGFLMKKELNYFA CCCCEECHHHHHHHH	45.29	27667366
192	Acetylation	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	23806337
192	Malonylation	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	26320211
192	Succinylation	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	-
192	Ubiquitination	AGGFLMKKELNYFAK CCCEECHHHHHHHHH	54.17	27667366
196	Phosphorylation	LMKKELNYFAKALES ECHHHHHHHHHHHHC	19.96	28542873
199	Acetylation	KELNYFAKALESPER HHHHHHHHHHHCCCC	43.54	23954790
199	Ubiquitination	KELNYFAKALESPER HHHHHHHHHHHCCCC	43.54	-
203	Phosphorylation	YFAKALESPERPFLA HHHHHHHCCCCCCCH	32.67	24925903
216	Acetylation	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	23236377
216	Other	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	-
216	Ubiquitination	LAILGGAKVADKIQL CHHHCCHHHHHHHHH	41.03	22790023
220	Acetylation	GGAKVADKIQLINNM CCHHHHHHHHHHHHH	23.71	23236377
220	Ubiquitination	GGAKVADKIQLINNM CCHHHHHHHHHHHHH	23.71	22790023
264	Acetylation	LYDEEGAKIVKDLMS CCCHHHHHHHHHHHH	59.91	23236377
264	Ubiquitination	LYDEEGAKIVKDLMS CCCHHHHHHHHHHHH	59.91	22790023
267	Acetylation	EEGAKIVKDLMSKAE HHHHHHHHHHHHHHH	48.93	22637741
267	Malonylation	EEGAKIVKDLMSKAE HHHHHHHHHHHHHHH	48.93	26320211
267	Ubiquitination	EEGAKIVKDLMSKAE HHHHHHHHHHHHHHH	48.93	27667366
272	Acetylation	IVKDLMSKAEKNGVK HHHHHHHHHHHCCCE	46.75	22826441
272	Ubiquitination	IVKDLMSKAEKNGVK HHHHHHHHHHHCCCE	46.75	22790023
279	Succinylation	KAEKNGVKITLPVDF HHHHCCCEEEEECCE	31.22	23954790
279	Ubiquitination	KAEKNGVKITLPVDF HHHHCCCEEEEECCE	31.22	27667366
291	Acetylation	VDFVTADKFDENAKT CCEEEHHHCCCCCCC	52.85	23806337
291	Malonylation	VDFVTADKFDENAKT CCEEEHHHCCCCCCC	52.85	26320211
291	Ubiquitination	VDFVTADKFDENAKT CCEEEHHHCCCCCCC	52.85	27667366
316	S-nitrosocysteine	AGWMGLDCGTESSKK CCEECCCCCCHHHHH	9.75	-
316	S-nitrosylation	AGWMGLDCGTESSKK CCEECCCCCCHHHHH	9.75	21278135
316	S-palmitoylation	AGWMGLDCGTESSKK CCEECCCCCCHHHHH	9.75	28526873
318	Phosphorylation	WMGLDCGTESSKKYA EECCCCCCHHHHHHH	38.74	22210690
320	Phosphorylation	GLDCGTESSKKYAEA CCCCCCHHHHHHHHH	47.50	20139300
321	Phosphorylation	LDCGTESSKKYAEAV CCCCCHHHHHHHHHH	27.25	20139300
322	Acetylation	DCGTESSKKYAEAVG CCCCHHHHHHHHHHH	60.11	129277
322	Malonylation	DCGTESSKKYAEAVG CCCCHHHHHHHHHHH	60.11	26320211
323	Acetylation	CGTESSKKYAEAVGR CCCHHHHHHHHHHHC	52.20	23806337
323	Malonylation	CGTESSKKYAEAVGR CCCHHHHHHHHHHHC	52.20	26320211
323	Other	CGTESSKKYAEAVGR CCCHHHHHHHHHHHC	52.20	-
323	Ubiquitination	CGTESSKKYAEAVGR CCCHHHHHHHHHHHC	52.20	27667366
324	Phosphorylation	GTESSKKYAEAVGRA CCHHHHHHHHHHHCC	17.26	26239621
352	Phosphorylation	WEAFARGTKSLMDEV HHHHHHCCHHHHHHH	16.35	25777480
353	Acetylation	EAFARGTKSLMDEVV HHHHHCCHHHHHHHH	44.40	23806337
353	Malonylation	EAFARGTKSLMDEVV HHHHHCCHHHHHHHH	44.40	26320211
353	Ubiquitination	EAFARGTKSLMDEVV HHHHHCCHHHHHHHH	44.40	-
354	Phosphorylation	AFARGTKSLMDEVVK HHHHCCHHHHHHHHH	28.85	22942356
361	Acetylation	SLMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	23806337
361	Malonylation	SLMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	26320211
361	Succinylation	SLMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	-
361	Ubiquitination	SLMDEVVKATSRGCI HHHHHHHHHHCCCCE	51.64	-
363	Phosphorylation	MDEVVKATSRGCITI HHHHHHHHCCCCEEE	17.15	23984901
364	Phosphorylation	DEVVKATSRGCITII HHHHHHHCCCCEEEE	31.38	23984901
367	S-nitrosocysteine	VKATSRGCITIIGGG HHHHCCCCEEEECCC	2.11	-
367	Glutathionylation	VKATSRGCITIIGGG HHHHCCCCEEEECCC	2.11	24333276
367	S-nitrosylation	VKATSRGCITIIGGG HHHHCCCCEEEECCC	2.11	24895380
369	Phosphorylation	ATSRGCITIIGGGDT HHCCCCEEEECCCCC	15.60	23984901
379	Glutathionylation	GGGDTATCCAKWNTE CCCCCEEEECCCCCC	1.65	24333276
379	S-nitrosylation	GGGDTATCCAKWNTE CCCCCEEEECCCCCC	1.65	24895380
380	S-nitrosocysteine	GGDTATCCAKWNTED CCCCEEEECCCCCCC	3.66	-
380	Glutathionylation	GGDTATCCAKWNTED CCCCEEEECCCCCCC	3.66	24333276
380	S-nitrosylation	GGDTATCCAKWNTED CCCCEEEECCCCCCC	3.66	24895380
388	Acetylation	AKWNTEDKVSHVSTG CCCCCCCCEEEEECC	39.13	23806337
388	Malonylation	AKWNTEDKVSHVSTG CCCCCCCCEEEEECC	39.13	26320211
388	Ubiquitination	AKWNTEDKVSHVSTG CCCCCCCCEEEEECC	39.13	-
390	Phosphorylation	WNTEDKVSHVSTGGG CCCCCCEEEEECCCC	24.74	15648052
399	Phosphorylation	VSTGGGASLELLEGK EECCCCCHHHHHCCC	26.17	29514104
406	Acetylation	SLELLEGKVLPGVDA HHHHHCCCCCCCCCH	31.09	23954790
415	Phosphorylation	LPGVDALSNV----- CCCCCHHCCC-----	36.95	26643407

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 PGK1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PGK1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PGK1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PGK1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND MASSSPECTROMETRY.	15648052 [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-76 AND TYR-196, AND MASSSPECTROMETRY.	18034455 [Abstract]