dbPTM

PGAM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGAM2_HUMAN
UniProt AC	P15259
Protein Name	Phosphoglycerate mutase 2
Gene Name	PGAM2
Organism	Homo sapiens (Human).
Sequence Length	253
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	MATHRLVMVRHGESTWNQENRFCGWFDAELSEKGTEEAKRGAKAIKDAKMEFDICYTSVLKRAIRTLWAILDGTDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDIPPPPMDEKHPYYNSISKERRYAGLKPGELPTCESLKDTIARALPFWNEEIVPQIKAGKRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELNKELKPTKPMQFLGDEETVRKAMEAVAAQGKAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MATHRLVMVR -----CCCEEEEEEE	13.26	26074081
14	Phosphorylation	VMVRHGESTWNQENR EEEECCCCCCCCCCC	43.23	26074081
15	Phosphorylation	MVRHGESTWNQENRF EEECCCCCCCCCCCC	24.92	26074081
33	Acetylation	FDAELSEKGTEEAKR CCHHHHHHCHHHHHH	68.69	30584417
39	Acetylation	EKGTEEAKRGAKAIK HHCHHHHHHHHHHHH	55.43	30584411
90	Methylation	RTWRLNERHYGGLTG EEEECCCCCCCCCCC	27.53	-
92	Phosphorylation	WRLNERHYGGLTGLN EECCCCCCCCCCCCC	21.07	23401153
96	Phosphorylation	ERHYGGLTGLNKAET CCCCCCCCCCCHHHH	42.78	23312004
100	Sumoylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Phosphoglycerylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Ubiquitination	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	23000965
100	Sumoylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Acetylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	23954790
103	Phosphorylation	TGLNKAETAAKHGEE CCCCHHHHHHHHCHH	36.45	28857561
106	Ubiquitination	NKAETAAKHGEEQVK CHHHHHHHHCHHHHH	50.07	23000965
113	Ubiquitination	KHGEEQVKIWRRSFD HHCHHHHHHHHHCCC	35.92	-
118	Phosphorylation	QVKIWRRSFDIPPPP HHHHHHHCCCCCCCC	20.78	26437602
132	Phosphorylation	PMDEKHPYYNSISKE CCCCCCCCCCCCCHH	18.26	26437602
133	Phosphorylation	MDEKHPYYNSISKER CCCCCCCCCCCCHHH	13.59	26437602
135	Phosphorylation	EKHPYYNSISKERRY CCCCCCCCCCHHHHC	16.47	26437602
137	Phosphorylation	HPYYNSISKERRYAG CCCCCCCCHHHHCCC	28.43	19764811
142	Phosphorylation	SISKERRYAGLKPGE CCCHHHHCCCCCCCC	15.96	26437602
152	Phosphorylation	LKPGELPTCESLKDT CCCCCCCCHHHHHHH	41.34	19764811
176	Ubiquitination	EEIVPQIKAGKRVLI CCHHHHHHCCCEEEE	45.93	22817900
179	Ubiquitination	VPQIKAGKRVLIAAH HHHHHCCCEEEEEEC	44.16	22817900
189	Phosphorylation	LIAAHGNSLRGIVKH EEEECCCCHHHHHHH	24.84	28348404
195	Ubiquitination	NSLRGIVKHLEGMSD CCHHHHHHHHCCCCC	40.32	22817900
238	Phosphorylation	QFLGDEETVRKAMEA CCCCCHHHHHHHHHH	24.46	21406692
241	Methylation	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	30992519
241	Ubiquitination	GDEETVRKAMEAVAA CCHHHHHHHHHHHHH	47.99	23000965
251	Neddylation	EAVAAQGKAK----- HHHHHCCCCC-----	40.71	32015554
251	Ubiquitination	EAVAAQGKAK----- HHHHHCCCCC-----	40.71	16196087
251	Malonylation	EAVAAQGKAK----- HHHHHCCCCC-----	40.71	26320211
251	Acetylation	EAVAAQGKAK----- HHHHHCCCCC-----	40.71	25953088
253	Ubiquitination	VAAQGKAK------- HHHCCCCC-------	65.44	24816145

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
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:24567357

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PGAM2_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 PGAM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	24567357
PGAM1_HUMAN	PGAM1	physical	26186194
PGAM4_HUMAN	PGAM4	physical	26186194
PMGE_HUMAN	BPGM	physical	26186194
NTF2_HUMAN	NUTF2	physical	26344197
THIO_HUMAN	TXN	physical	26344197
PGAM4_HUMAN	PGAM4	physical	28514442
PMGE_HUMAN	BPGM	physical	28514442
PGAM1_HUMAN	PGAM1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
261670	Glycogen storage disease 10 (GSD10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PGAM2_HUMAN

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-195, AND MASSSPECTROMETRY.	17370265 [Abstract]