PGAM1_RAT - dbPTM
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
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 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 Orthologous
Protein Cluster
5Acetylation---MAAYKLVLIRHG
---CCCEEEEEEECC
27.6522902405
5Ubiquitination---MAAYKLVLIRHG
---CCCEEEEEEECC
27.65-
14PhosphorylationVLIRHGESAWNLENR
EEEECCCCCCCCCCC
43.0828689409
23PhosphorylationWNLENRFSGWYDADL
CCCCCCCCCCCCCCC
25.7721738781
26PhosphorylationENRFSGWYDADLSPA
CCCCCCCCCCCCCCC
12.5527097102
31PhosphorylationGWYDADLSPAGHEEA
CCCCCCCCCCCHHHH
17.1622108457
39AcetylationPAGHEEAKRGGQALR
CCCHHHHHHHHHHHH
55.6522902405
50PhosphorylationQALRDAGYEFDICFT
HHHHHCCCEEEEECH
18.36-
55S-nitrosocysteineAGYEFDICFTSVQKR
CCCEEEEECHHHHHH
3.07-
55S-nitrosylationAGYEFDICFTSVQKR
CCCEEEEECHHHHHH
3.0722178444
84PhosphorylationMWLPVVRTWRLNERH
CHHHHHEEEECCCCC
11.8822673903
92PhosphorylationWRLNERHYGGLTGLN
EECCCCCCCCCCCCC
21.0729779826
96PhosphorylationERHYGGLTGLNKAET
CCCCCCCCCCCHHHH
42.7823984901
100UbiquitinationGGLTGLNKAETAAKH
CCCCCCCHHHHHHHH
53.28-
100AcetylationGGLTGLNKAETAAKH
CCCCCCCHHHHHHHH
53.28182013
106UbiquitinationNKAETAAKHGEAQVK
CHHHHHHHHCCCCEE
50.07-
106AcetylationNKAETAAKHGEAQVK
CHHHHHHHHCCCCEE
50.0722902405
113UbiquitinationKHGEAQVKIWRRSYD
HHCCCCEEEEECCCC
25.19-
113AcetylationKHGEAQVKIWRRSYD
HHCCCCEEEEECCCC
25.1922902405
118PhosphorylationQVKIWRRSYDVPPPP
CEEEEECCCCCCCCC
19.6729779826
119PhosphorylationVKIWRRSYDVPPPPM
EEEEECCCCCCCCCC
21.1027097102
138AcetylationPFYSNISKDRRYADL
CCCCCCCCCCCCCCC
52.0022902405
146PhosphorylationDRRYADLTEDQLPSC
CCCCCCCCCCCCCCH
37.7523984901
152PhosphorylationLTEDQLPSCESLKDT
CCCCCCCCHHHHHHH
38.8223984901
153S-nitrosylationTEDQLPSCESLKDTI
CCCCCCCHHHHHHHH
3.7822178444
153S-nitrosocysteineTEDQLPSCESLKDTI
CCCCCCCHHHHHHHH
3.78-
155PhosphorylationDQLPSCESLKDTIAR
CCCCCHHHHHHHHHH
45.0823984901
157AcetylationLPSCESLKDTIARAL
CCCHHHHHHHHHHHC
63.2022902405
159PhosphorylationSCESLKDTIARALPF
CHHHHHHHHHHHCCC
18.2323984901
176AcetylationEEIVPQIKEGKRVLI
CCHHHHHHCCCEEEE
55.9922902405
189PhosphorylationLIAAHGNSLRGIVKH
EEEECCCHHHHHHHH
24.8423984901
225SuccinylationYELDKNLKPIKPMQF
EEECCCCCCCCCCCC
54.8326843850
225AcetylationYELDKNLKPIKPMQF
EEECCCCCCCCCCCC
54.8322902405
228AcetylationDKNLKPIKPMQFLGD
CCCCCCCCCCCCCCC
42.8622902405
238PhosphorylationQFLGDEETVRKAMEA
CCCCCHHHHHHHHHH
24.4622673903
241UbiquitinationGDEETVRKAMEAVAA
CCHHHHHHHHHHHHH
47.99-
251SuccinylationEAVAAQGKVKK----
HHHHHCCCCCC----
38.51-
251SuccinylationEAVAAQGKVKK----
HHHHHCCCCCC----
38.51-
251AcetylationEAVAAQGKVKK----
HHHHHCCCCCC----
38.51-
251UbiquitinationEAVAAQGKVKK----
HHHHHCCCCCC----
38.51-
253AcetylationVAAQGKVKK------
HHHCCCCCC------
57.14-
254AcetylationAAQGKVKK-------
HHCCCCCC-------
69.43-

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

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
253KAcetylation

-
254KAcetylation

-

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PGAM1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGAM1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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