PGAM2_MOUSE - dbPTM
PGAM2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGAM2_MOUSE
UniProt AC O70250
Protein Name Phosphoglycerate mutase 2
Gene Name Pgam2
Organism Mus musculus (Mouse).
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 MTTHRLVMVRHGESLWNQENRFCGWFDAELSEKGAEEAKRGATAIKDAKIEFDICYTSVLKRAIRTLWTILDVTDQMWVPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDTPPPPMDEKHNYYTSISKDRRYAGLKPEELPTCESLKDTIARALPFWNEEIAPKIKAGQRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELDQNLKPTKPMRFLGDEETVRKAMEAVAAQGKAK
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 Orthologous
Protein Cluster
2Phosphorylation------MTTHRLVMV
------CCCEEEEEE		31.1724719451
3Phosphorylation-----MTTHRLVMVR
-----CCCEEEEEEC		12.05-
14PhosphorylationVMVRHGESLWNQENR
EEECCCHHHCCCCCC		43.1928464351
23S-nitrosylationWNQENRFCGWFDAEL
CCCCCCCCCCCCHHH		4.2121278135
23S-nitrosocysteineWNQENRFCGWFDAEL
CCCCCCCCCCCCHHH		4.21-
43PhosphorylationEEAKRGATAIKDAKI
HHHHHCCCHHHHCCE		31.5722210690
55S-nitrosocysteineAKIEFDICYTSVLKR
CCEEEEEHHHHHHHH		3.05-
55S-nitrosylationAKIEFDICYTSVLKR
CCEEEEEHHHHHHHH		3.0521278135
58PhosphorylationEFDICYTSVLKRAIR
EEEEHHHHHHHHHHH		10.05-
61UbiquitinationICYTSVLKRAIRTLW
EHHHHHHHHHHHHHH		37.31-
92PhosphorylationWRLNERHYGGLTGLN
EECCCCCCCCCCCCC		21.0725521595
96PhosphorylationERHYGGLTGLNKAET
CCCCCCCCCCCHHHH		42.7825619855
100PhosphoglycerylationGGLTGLNKAETAAKH
CCCCCCCHHHHHHHH		53.28-
100SuccinylationGGLTGLNKAETAAKH
CCCCCCCHHHHHHHH		53.28-
100MalonylationGGLTGLNKAETAAKH
CCCCCCCHHHHHHHH		53.2826320211
100AcetylationGGLTGLNKAETAAKH
CCCCCCCHHHHHHHH		53.2823864654
100UbiquitinationGGLTGLNKAETAAKH
CCCCCCCHHHHHHHH		53.28-
103PhosphorylationTGLNKAETAAKHGEE
CCCCHHHHHHHHCHH		36.4525367039
106UbiquitinationNKAETAAKHGEEQVK
CHHHHHHHHCHHHHH		50.0722790023
113UbiquitinationKHGEEQVKIWRRSFD
HHCHHHHHHHHHCCC		35.9222790023
118PhosphorylationQVKIWRRSFDTPPPP
HHHHHHHCCCCCCCC		20.9224899341
121PhosphorylationIWRRSFDTPPPPMDE
HHHHCCCCCCCCCCC		35.3727742792
129UbiquitinationPPPPMDEKHNYYTSI
CCCCCCCCCCCCCCC		32.6522790023
132PhosphorylationPMDEKHNYYTSISKD
CCCCCCCCCCCCCCC		14.0827742792
133PhosphorylationMDEKHNYYTSISKDR
CCCCCCCCCCCCCCC		10.1827742792
134PhosphorylationDEKHNYYTSISKDRR
CCCCCCCCCCCCCCC		14.8227742792
135PhosphorylationEKHNYYTSISKDRRY
CCCCCCCCCCCCCCC		14.5628542873
137PhosphorylationHNYYTSISKDRRYAG
CCCCCCCCCCCCCCC		28.4228542873
138UbiquitinationNYYTSISKDRRYAGL
CCCCCCCCCCCCCCC		54.2922790023
146UbiquitinationDRRYAGLKPEELPTC
CCCCCCCCHHHCCCC		49.8422790023
152PhosphorylationLKPEELPTCESLKDT
CCHHHCCCCHHHHHH		41.3428464351
153S-nitrosylationKPEELPTCESLKDTI
CHHHCCCCHHHHHHH		2.9321278135
153S-nitrosocysteineKPEELPTCESLKDTI
CHHHCCCCHHHHHHH		2.93-
157UbiquitinationLPTCESLKDTIARAL
CCCCHHHHHHHHHHC		63.2022790023
174UbiquitinationWNEEIAPKIKAGQRV
CCCCHHHHCCCCCEE		48.0622790023
189PhosphorylationLIAAHGNSLRGIVKH
EEEECCCHHHHHHHH		24.8429176673
241SuccinylationGDEETVRKAMEAVAA
CCHHHHHHHHHHHHH		47.99-
241MalonylationGDEETVRKAMEAVAA
CCHHHHHHHHHHHHH		47.9926320211
241AcetylationGDEETVRKAMEAVAA
CCHHHHHHHHHHHHH		47.9923806337
241UbiquitinationGDEETVRKAMEAVAA
CCHHHHHHHHHHHHH		47.99-
251UbiquitinationEAVAAQGKAK-----
HHHHHCCCCC-----		40.7122790023
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
118SPhosphorylationKinasePAK1Q13153
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGAM2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PGAM2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGAM2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 TYR-92, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory