dbPTM

PGAM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGAM1_MOUSE
UniProt AC	Q9DBJ1
Protein Name	Phosphoglycerate mutase 1
Gene Name	Pgam1
Organism	Mus musculus (Mouse).
Sequence Length	254
Subcellular Localization
Protein Description	Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity..
Protein Sequence	MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKVKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAAYKLVLIRH ----CCCEEEEEEEC	8.70	26824392
5	Acetylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	23806337
5	Succinylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	23954790
5	Ubiquitination	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	-
14	Phosphorylation	VLIRHGESAWNLENR EEEECCCCCCCCCCC	43.08	27087446
23	Phosphorylation	WNLENRFSGWYDADL CCCCCCCCCCCCCCC	25.77	21082442
26	Phosphorylation	ENRFSGWYDADLSPA CCCCCCCCCCCCCCC	12.55	23984901
31	Phosphorylation	GWYDADLSPAGHEEA CCCCCCCCCCCHHHH	17.16	26824392
39	Acetylation	PAGHEEAKRGGQALR CCCHHHHHHHHHHHH	55.65	23236377
55	S-nitrosylation	AGYEFDICFTSVQKR CCCEEEEECHHHHHH	3.07	21278135
55	S-nitrosocysteine	AGYEFDICFTSVQKR CCCEEEEECHHHHHH	3.07	-
92	Phosphorylation	WRLNERHYGGLTGLN EECCCCCCCCCCCCC	21.07	25521595
96	Phosphorylation	ERHYGGLTGLNKAET CCCCCCCCCCCHHHH	42.78	25619855
100	Ubiquitination	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Acetylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	71121
100	Malonylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	26073543
103	Phosphorylation	TGLNKAETAAKHGEA CCCCHHHHHHHHCCC	36.45	25367039
106	Ubiquitination	NKAETAAKHGEAQVK CHHHHHHHHCCCCEE	50.07	-
106	Acetylation	NKAETAAKHGEAQVK CHHHHHHHHCCCCEE	50.07	23806337
113	Acetylation	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	23236377
113	Malonylation	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	26320211
113	Ubiquitination	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	-
118	Phosphorylation	QVKIWRRSYDVPPPP CEEEEECCCCCCCCC	19.67	27087446
119	Phosphorylation	VKIWRRSYDVPPPPM EEEEECCCCCCCCCC	21.10	25521595
133	Phosphorylation	MEPDHPFYSNISKDR CCCCCCCCCCCCCCC	12.78	25619855
134	Phosphorylation	EPDHPFYSNISKDRR CCCCCCCCCCCCCCC	28.24	25619855
137	Phosphorylation	HPFYSNISKDRRYAD CCCCCCCCCCCCCCC	32.52	25619855
138	Acetylation	PFYSNISKDRRYADL CCCCCCCCCCCCCCC	52.00	23954790
138	Ubiquitination	PFYSNISKDRRYADL CCCCCCCCCCCCCCC	52.00	-
142	Phosphorylation	NISKDRRYADLTEDQ CCCCCCCCCCCCCCC	12.83	25195567
152	Phosphorylation	LTEDQLPSCESLKDT CCCCCCCCHHHHHHH	38.82	23984901
153	S-nitrosocysteine	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	-
153	S-nitrosylation	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	24895380
153	Glutathionylation	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	24333276
155	Phosphorylation	DQLPSCESLKDTIAR CCCCCHHHHHHHHHH	45.08	25195567
157	Acetylation	LPSCESLKDTIARAL CCCHHHHHHHHHHHC	63.20	22733758
157	Malonylation	LPSCESLKDTIARAL CCCHHHHHHHHHHHC	63.20	26320211
157	Ubiquitination	LPSCESLKDTIARAL CCCHHHHHHHHHHHC	63.20	-
176	Acetylation	EEIVPQIKEGKRVLI CCHHHHHHCCCEEEE	55.99	23236377
176	Ubiquitination	EEIVPQIKEGKRVLI CCHHHHHHCCCEEEE	55.99	-
189	Phosphorylation	LIAAHGNSLRGIVKH EEEECCCHHHHHHHH	24.84	29176673
195	Acetylation	NSLRGIVKHLEGLSE CHHHHHHHHHCCCCH	40.32	23954790
225	Acetylation	YELDKNLKPIKPMQF EEECCCCCCCCCCCC	54.83	23201123
228	Acetylation	DKNLKPIKPMQFLGD CCCCCCCCCCCCCCC	42.86	22826441
241	Malonylation	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	26320211
241	Ubiquitination	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	-
251	Succinylation	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	-
251	Succinylation	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	23806337
251	Malonylation	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	26320211
251	Acetylation	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	23806337
251	Ubiquitination	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	-
253	Malonylation	VAAQGKVKK------ HHHCCCCCC------	57.14	26073543
253	Acetylation	VAAQGKVKK------ HHHCCCCCC------	57.14	-
254	Acetylation	AAQGKVKK------- HHCCCCCC-------	69.43	-

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 PGAM1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
253	K	Acetylation	-
Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition.
254	K	Acetylation	-
Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition.

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 PGAM1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PGAM1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PGAM1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-14, AND MASSSPECTROMETRY.	19367708 [Abstract]
"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 SER-118, 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-26, AND MASSSPECTROMETRY.	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-26, AND MASSSPECTROMETRY.	17947660 [Abstract]

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