PGAM1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PGAM1_RAT
• UniProt AC: P25113
• Protein Name: Phosphoglycerate mutase 1
• Gene Name: Pgam1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 254
• 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

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Acetylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	22902405
5	Ubiquitination	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	-
14	Phosphorylation	VLIRHGESAWNLENR EEEECCCCCCCCCCC	43.08	28689409
23	Phosphorylation	WNLENRFSGWYDADL CCCCCCCCCCCCCCC	25.77	21738781
26	Phosphorylation	ENRFSGWYDADLSPA CCCCCCCCCCCCCCC	12.55	27097102
31	Phosphorylation	GWYDADLSPAGHEEA CCCCCCCCCCCHHHH	17.16	22108457
39	Acetylation	PAGHEEAKRGGQALR CCCHHHHHHHHHHHH	55.65	22902405
50	Phosphorylation	QALRDAGYEFDICFT HHHHHCCCEEEEECH	18.36	-
55	S-nitrosocysteine	AGYEFDICFTSVQKR CCCEEEEECHHHHHH	3.07	-
55	S-nitrosylation	AGYEFDICFTSVQKR CCCEEEEECHHHHHH	3.07	22178444
84	Phosphorylation	MWLPVVRTWRLNERH CHHHHHEEEECCCCC	11.88	22673903
92	Phosphorylation	WRLNERHYGGLTGLN EECCCCCCCCCCCCC	21.07	29779826
96	Phosphorylation	ERHYGGLTGLNKAET CCCCCCCCCCCHHHH	42.78	23984901
100	Ubiquitination	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Acetylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	182013
106	Ubiquitination	NKAETAAKHGEAQVK CHHHHHHHHCCCCEE	50.07	-
106	Acetylation	NKAETAAKHGEAQVK CHHHHHHHHCCCCEE	50.07	22902405
113	Ubiquitination	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	-
113	Acetylation	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	22902405
118	Phosphorylation	QVKIWRRSYDVPPPP CEEEEECCCCCCCCC	19.67	29779826
119	Phosphorylation	VKIWRRSYDVPPPPM EEEEECCCCCCCCCC	21.10	27097102
138	Acetylation	PFYSNISKDRRYADL CCCCCCCCCCCCCCC	52.00	22902405
146	Phosphorylation	DRRYADLTEDQLPSC CCCCCCCCCCCCCCH	37.75	23984901
152	Phosphorylation	LTEDQLPSCESLKDT CCCCCCCCHHHHHHH	38.82	23984901
153	S-nitrosylation	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	22178444
153	S-nitrosocysteine	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	-
155	Phosphorylation	DQLPSCESLKDTIAR CCCCCHHHHHHHHHH	45.08	23984901
157	Acetylation	LPSCESLKDTIARAL CCCHHHHHHHHHHHC	63.20	22902405
159	Phosphorylation	SCESLKDTIARALPF CHHHHHHHHHHHCCC	18.23	23984901
176	Acetylation	EEIVPQIKEGKRVLI CCHHHHHHCCCEEEE	55.99	22902405
189	Phosphorylation	LIAAHGNSLRGIVKH EEEECCCHHHHHHHH	24.84	23984901
225	Succinylation	YELDKNLKPIKPMQF EEECCCCCCCCCCCC	54.83	26843850
225	Acetylation	YELDKNLKPIKPMQF EEECCCCCCCCCCCC	54.83	22902405
228	Acetylation	DKNLKPIKPMQFLGD CCCCCCCCCCCCCCC	42.86	22902405
238	Phosphorylation	QFLGDEETVRKAMEA CCCCCHHHHHHHHHH	24.46	22673903
241	Ubiquitination	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	-
251	Succinylation	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	-
251	Succinylation	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	-
251	Acetylation	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	-
251	Ubiquitination	EAVAAQGKVKK---- HHHHHCCCCCC----	38.51	-
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, ...)

Oops, there are no upstream regulatory protein records of PGAM1_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	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.

Oops, there are no SNP-PTM records of PGAM1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of PGAM1_RAT !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
PubMed: 16641100