PMGY_SCHPO - dbPTM
PMGY_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMGY_SCHPO
UniProt AC P36623
Protein Name Phosphoglycerate mutase
Gene Name gpm1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 211
Subcellular Localization
Protein Description
Protein Sequence MTTEAAPNLLVLTRHGESEWNKLNLFTGWKDPALSETGIKEAKLGGERLKSRGYKFDIAFTSALQRAQKTCQIILEEVGEPNLETIKSEKLNERYYGDLQGLNKDDARKKWGAEQVQIWRRSYDIAPPNGESLKDTAERVLPYYKSTIVPHILKGEKVLIAAHGNSLRALIMDLEGLTGDQIVKRELATGVPIVYHLDKDGKYVSKELIDN
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------MTTEAAPNL
------CCCCCCCCE
33.0924763107
13PhosphorylationAPNLLVLTRHGESEW
CCCEEEEECCCCCCH
17.0921712547
18PhosphorylationVLTRHGESEWNKLNL
EEECCCCCCHHHCCC
53.1321712547
35PhosphorylationGWKDPALSETGIKEA
CCCCCCHHHHCCCCH
34.9128889911
37PhosphorylationKDPALSETGIKEAKL
CCCCHHHHCCCCHHH
40.6128889911
61PhosphorylationYKFDIAFTSALQRAQ
CCCCCHHHHHHHHHH
12.2225720772
62PhosphorylationKFDIAFTSALQRAQK
CCCCHHHHHHHHHHH
22.1128889911
88PhosphorylationPNLETIKSEKLNERY
CCHHHHHHHHHHHHH
35.7928889911
95PhosphorylationSEKLNERYYGDLQGL
HHHHHHHHHHCCCCC
12.9628889911
96PhosphorylationEKLNERYYGDLQGLN
HHHHHHHHHCCCCCC
15.4728889911
122PhosphorylationQVQIWRRSYDIAPPN
HHHHHHHHCCCCCCC
20.7028889911
123PhosphorylationVQIWRRSYDIAPPNG
HHHHHHHCCCCCCCC
15.0125720772
136PhosphorylationNGESLKDTAERVLPY
CCCCHHHHHHHHHHH
28.9127738172
146PhosphorylationRVLPYYKSTIVPHIL
HHHHHHHHHCHHHHH
13.7721712547
147PhosphorylationVLPYYKSTIVPHILK
HHHHHHHHCHHHHHC
23.1124763107
166PhosphorylationLIAAHGNSLRALIMD
EEEECCHHHHHHHHC
24.6728889911
189PhosphorylationIVKRELATGVPIVYH
HHHHHHCCCCCEEEE
51.8725720772
203PhosphorylationHLDKDGKYVSKELID
EECCCCCEEEHHHHC
18.5825720772
205PhosphorylationDKDGKYVSKELIDN-
CCCCCEEEHHHHCC-
19.8128889911

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 PMGY_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 PMGY_SCHPO !!

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

Oops, there are no PPI records of PMGY_SCHPO !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; SER-62; TYR-96 ANDSER-166, AND MASS SPECTROMETRY.

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