PGAM4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PGAM4_HUMAN
• UniProt AC: Q8N0Y7
• Protein Name: Probable phosphoglycerate mutase 4
• Gene Name: PGAM4
• Organism: Homo sapiens (Human).
• Sequence Length: 254
• Protein Sequence: MAAYKLVLIRHGESTWNLENRFSCWYDADLSPAGHEEAKRGGQALRDAGYEFDICLTSVQKRVIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSYESPKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLQGIAKHVEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVCKAIEAVAAQGKAKK

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
4	Phosphorylation	----MAAYKLVLIRH ----CCCEEEEEEEC	8.70	27259358
5	Acetylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	18526143
5	Ubiquitination	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	23000965
5	Methylation	---MAAYKLVLIRHG ---CCCEEEEEEECC	27.65	18526143
14	Phosphorylation	VLIRHGESTWNLENR EEEECCCCEECCCCC	43.23	30108239
15	Phosphorylation	LIRHGESTWNLENRF EEECCCCEECCCCCE	17.67	30108239
23	Phosphorylation	WNLENRFSCWYDADL ECCCCCEECEEECCC	10.66	-
26	Phosphorylation	ENRFSCWYDADLSPA CCCEECEEECCCCCC	12.94	-
31	Phosphorylation	CWYDADLSPAGHEEA CEEECCCCCCCHHHH	17.16	26074081
39	Ubiquitination	PAGHEEAKRGGQALR CCCHHHHHHHHHHHH	55.65	22817900
50	Phosphorylation	QALRDAGYEFDICLT HHHHHCCCCCCEECH	18.36	-
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	Sumoylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	-
100	Ubiquitination	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	23000965
100	Acetylation	GGLTGLNKAETAAKH CCCCCCCHHHHHHHH	53.28	12635595
103	Phosphorylation	TGLNKAETAAKHGEA CCCCHHHHHHHHCCC	36.45	28857561
106	Ubiquitination	NKAETAAKHGEAQVK CHHHHHHHHCCCEEE	50.07	23000965
106	Acetylation	NKAETAAKHGEAQVK CHHHHHHHHCCCEEE	50.07	34677459
113	Neddylation	KHGEAQVKIWRRSYD HHCCCEEEEEECCCC	25.19	32015554
113	Ubiquitination	KHGEAQVKIWRRSYD HHCCCEEEEEECCCC	25.19	23000965
113	Acetylation	KHGEAQVKIWRRSYD HHCCCEEEEEECCCC	25.19	22637847
118	Phosphorylation	QVKIWRRSYDVPPPP EEEEEECCCCCCCCC	19.67	22167270
119	Phosphorylation	VKIWRRSYDVPPPPM EEEEECCCCCCCCCC	21.10	22167270
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	23000965
138	Acetylation	PFYSNISKDRRYADL CCCCCCCCCCCCCCC	52.00	-
142	Phosphorylation	NISKDRRYADLTEDQ CCCCCCCCCCCCCCC	12.83	28111955
146	Phosphorylation	DRRYADLTEDQLPSY CCCCCCCCCCCCCCC	37.75	28111955
152	Phosphorylation	LTEDQLPSYESPKDT CCCCCCCCCCCCHHH	50.56	28111955
153	Phosphorylation	TEDQLPSYESPKDTI CCCCCCCCCCCHHHH	20.63	28111955
155	Phosphorylation	DQLPSYESPKDTIAR CCCCCCCCCHHHHHH	29.08	28111955
176	Ubiquitination	EEIVPQIKEGKRVLI CCHHHHHHCCCEEEE	55.99	32015554
222	Ubiquitination	PIVYELDKNLKPIKP CEEEEECCCCCCCCC	76.45	33845483
251	Succinylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	21890473
251	Succinylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	-
251	Ubiquitination	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	27667366
251	Acetylation	EAVAAQGKAKK---- HHHHHHCCCCC----	44.98	-
253	Acetylation	VAAQGKAKK------ HHHHCCCCC------	63.60	-
254	Acetylation	AAQGKAKK------- HHHCCCCC-------	71.13	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PGAM4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PGAM4_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PGAM4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GPX4_HUMAN	GPX4	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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-100 AND LYS-113, ANDMASS SPECTROMETRY.
PubMed: 19608861

"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND MASS SPECTROMETRY.
PubMed: 16916647

Phosphorylation

"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-118, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-92, AND MASSSPECTROMETRY.
PubMed: 19534553

"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-92; TYR-119 AND TYR-133,AND MASS SPECTROMETRY.
PubMed: 18083107