dbPTM

PGAM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGAM1_HUMAN
UniProt AC	P18669
Protein Name	Phosphoglycerate mutase 1
Gene Name	PGAM1
Organism	Homo sapiens (Human).
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	MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKAKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAYKLVLI ------CCCEEEEEE	21.35	-
4	Phosphorylation	----MAAYKLVLIRH ----CCCEEEEEEEC	8.70	27259358
5	Methylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	19608861
5	Acetylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	23749302
5	Ubiquitination	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	21890473
5	2-Hydroxyisobutyrylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	-
5	Succinylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	23954790
11	Phosphorylation	YKLVLIRHGESAWNL EEEEEEECCCCCCCC	37.06	-
14	Phosphorylation	VLIRHGESAWNLENR EEEECCCCCCCCCCC	43.08	25159151
21	Methylation	SAWNLENRFSGWYDA CCCCCCCCCCCCCCC	20.10	115487181
23	Phosphorylation	WNLENRFSGWYDADL CCCCCCCCCCCCCCC	25.77	23927012
26	Phosphorylation	ENRFSGWYDADLSPA CCCCCCCCCCCCCCC	12.55	27273156
31	Phosphorylation	GWYDADLSPAGHEEA CCCCCCCCCCCHHHH	17.16	23401153
39	Ubiquitination	PAGHEEAKRGGQALR CCCHHHHHHHHHHHH	55.65	-
39	Acetylation	PAGHEEAKRGGQALR CCCHHHHHHHHHHHH	55.65	23954790
39	2-Hydroxyisobutyrylation	PAGHEEAKRGGQALR CCCHHHHHHHHHHHH	55.65	-
39	Malonylation	PAGHEEAKRGGQALR CCCHHHHHHHHHHHH	55.65	26320211
50	Nitration	QALRDAGYEFDICFT HHHHHCCCEEEEECH	18.36	-
50	Phosphorylation	QALRDAGYEFDICFT HHHHHCCCEEEEECH	18.36	20090780
61	Ubiquitination	ICFTSVQKRAIRTLW EECHHHHHHHHHHHH	41.46	-
77	Sulfoxidation	VLDAIDQMWLPVVRT HHHHHHHCHHHHHEE	3.35	30846556
90	Methylation	RTWRLNERHYGGLTG EEEECCCCCCCCCCC	27.53	-
92	Phosphorylation	WRLNERHYGGLTGLN EECCCCCCCCCCCCC	21.07	23401153
92	Nitration	WRLNERHYGGLTGLN EECCCCCCCCCCCCC	21.07	-
96	Phosphorylation	ERHYGGLTGLNKAET CCCCCCCCCCCHHHH	42.78	23312004
100	Sumoylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	19608861
100	Ubiquitination	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	19608861
100	Sumoylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Malonylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	26320211
100	2-Hydroxyisobutyrylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Acetylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	19608861
103	Phosphorylation	TGLNKAETAAKHGEA CCCCHHHHHHHHCCC	36.45	28857561
106	Ubiquitination	NKAETAAKHGEAQVK CHHHHHHHHCCCCEE	50.07	21890473
106	2-Hydroxyisobutyrylation	NKAETAAKHGEAQVK CHHHHHHHHCCCCEE	50.07	-
106	Acetylation	NKAETAAKHGEAQVK CHHHHHHHHCCCCEE	50.07	16916647
113	Malonylation	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	26320211
113	Ubiquitination	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	21906983
113	Acetylation	KHGEAQVKIWRRSYD HHCCCCEEEEECCCC	25.19	23954790
118	Phosphorylation	QVKIWRRSYDVPPPP CEEEEECCCCCCCCC	19.67	22167270
119	Phosphorylation	VKIWRRSYDVPPPPM EEEEECCCCCCCCCC	21.10	22167270
126	Sulfoxidation	YDVPPPPMEPDHPFY CCCCCCCCCCCCCCC	16.79	30846556
133	Phosphorylation	MEPDHPFYSNISKDR CCCCCCCCCCCCCCC	12.78	23927012
134	Phosphorylation	EPDHPFYSNISKDRR CCCCCCCCCCCCCCC	28.24	23927012
137	Phosphorylation	HPFYSNISKDRRYAD CCCCCCCCCCCCCCC	32.52	23927012
138	Ubiquitination	PFYSNISKDRRYADL CCCCCCCCCCCCCCC	52.00	21890473
138	Acetylation	PFYSNISKDRRYADL CCCCCCCCCCCCCCC	52.00	23954790
138	2-Hydroxyisobutyrylation	PFYSNISKDRRYADL CCCCCCCCCCCCCCC	52.00	-
142	Phosphorylation	NISKDRRYADLTEDQ CCCCCCCCCCCCCCC	12.83	28152594
142	Nitration	NISKDRRYADLTEDQ CCCCCCCCCCCCCCC	12.83	-
146	Phosphorylation	DRRYADLTEDQLPSC CCCCCCCCCCCCCCH	37.75	20873877
152	Phosphorylation	LTEDQLPSCESLKDT CCCCCCCCHHHHHHH	38.82	25159151
153	S-nitrosocysteine	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	-
153	Glutathionylation	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	22555962
153	S-nitrosylation	TEDQLPSCESLKDTI CCCCCCCHHHHHHHH	3.78	19483679
155	Phosphorylation	DQLPSCESLKDTIAR CCCCCHHHHHHHHHH	45.08	20873877
157	Acetylation	LPSCESLKDTIARAL CCCHHHHHHHHHHHC	63.20	23749302
157	2-Hydroxyisobutyrylation	LPSCESLKDTIARAL CCCHHHHHHHHHHHC	63.20	-
157	Ubiquitination	LPSCESLKDTIARAL CCCHHHHHHHHHHHC	63.20	2190698
159	Phosphorylation	SCESLKDTIARALPF CHHHHHHHHHHHCCC	18.23	28857561
176	Acetylation	EEIVPQIKEGKRVLI CCHHHHHHCCCEEEE	55.99	23236377
176	Ubiquitination	EEIVPQIKEGKRVLI CCHHHHHHCCCEEEE	55.99	19608861
176	Succinylation	EEIVPQIKEGKRVLI CCHHHHHHCCCEEEE	55.99	23954790
179	Ubiquitination	VPQIKEGKRVLIAAH HHHHHCCCEEEEEEC	40.19	-
189	Phosphorylation	LIAAHGNSLRGIVKH EEEECCCHHHHHHHH	24.84	28348404
195	Ubiquitination	NSLRGIVKHLEGLSE CHHHHHHHHHCCCCH	40.32	-
206	Sulfoxidation	GLSEEAIMELNLPTG CCCHHHHHHCCCCCC	6.54	30846556
225	2-Hydroxyisobutyrylation	YELDKNLKPIKPMQF EEECCCCCCCCCCCC	54.83	-
225	Ubiquitination	YELDKNLKPIKPMQF EEECCCCCCCCCCCC	54.83	-
225	Acetylation	YELDKNLKPIKPMQF EEECCCCCCCCCCCC	54.83	26051181
228	Ubiquitination	DKNLKPIKPMQFLGD CCCCCCCCCCCCCCC	42.86	-
228	Acetylation	DKNLKPIKPMQFLGD CCCCCCCCCCCCCCC	42.86	26051181
238	Phosphorylation	QFLGDEETVRKAMEA CCCCCHHHHHHHHHH	24.46	21406692
241	2-Hydroxyisobutyrylation	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	-
241	Methylation	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	30992507
241	Ubiquitination	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	-
243	Sulfoxidation	EETVRKAMEAVAAQG HHHHHHHHHHHHHHC	3.68	30846556
251	2-Hydroxyisobutyrylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	-
251	Ubiquitination	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	22157007
251	Succinylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	21890473
251	Succinylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	-
251	Malonylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	26320211
251	Acetylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	22157007
253	Methylation	VAAQGKAKK------ HHHHCCCCC------	63.60	116252169
253	Acetylation	VAAQGKAKK------ HHHHCCCCC------	63.60	22157007
253	Ubiquitination	VAAQGKAKK------ HHHHCCCCC------	63.60	-
254	Acetylation	AAQGKAKK------- HHHCCCCC-------	71.13	22157007
254	Ubiquitination	AAQGKAKK------- HHHCCCCC-------	71.13	-

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
23	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
118	S	Phosphorylation	Kinase	PAK1	Q13153	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
253	K	Acetylation	22157007
Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition.
254	K	Acetylation	22157007
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC6_HUMAN	XRCC6	physical	16169070
TYSY_HUMAN	TYMS	physical	22939629
MDM2_HUMAN	MDM2	physical	24567357
ALDR_HUMAN	AKR1B1	physical	26344197
KCRU_HUMAN	CKMT1B	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
LGUL_HUMAN	GLO1	physical	26344197
NTF2_HUMAN	NUTF2	physical	26344197
SERA_HUMAN	PHGDH	physical	26344197
PCP_HUMAN	PRCP	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
RB11A_HUMAN	RAB11A	physical	26344197
RB11B_HUMAN	RAB11B	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
THIO_HUMAN	TXN	physical	26344197

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 PGAM1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1protein-mediated deacetylation."; Hallows W.C., Yu W., Denu J.M.; J. Biol. Chem. 287:3850-3858(2012). Cited for: ACETYLATION AT LYS-251; LYS-253 AND LYS-254, AND DEACETYLATION BYSIRT1.	22157007 [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 SER-14; TYR-26; TYR-92 ANDSER-118, AND MASS SPECTROMETRY.	19690332 [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-14 AND SER-31, AND MASSSPECTROMETRY.	18669648 [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-26, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, AND MASSSPECTROMETRY.	18083107 [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-26, AND MASSSPECTROMETRY.	15592455 [Abstract]

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