PYGM_MOUSE - dbPTM
PYGM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYGM_MOUSE
UniProt AC Q9WUB3
Protein Name Glycogen phosphorylase, muscle form
Gene Name Pygm
Organism Mus musculus (Mouse).
Sequence Length 842
Subcellular Localization
Protein Description Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties..
Protein Sequence MSRPLSDQDKRKQISVRGLAGVENVSELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGSRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERLDWDKAWDVTVKTCAYTNHTVLPEALERWPVHLMETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFSAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHIITLYNRIKREPNRFMVPRTIMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVERLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYIKCQDKVSELYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEKI
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
2Acetylation------MSRPLSDQD
------CCCCCCHHH
42.48-
2Phosphorylation------MSRPLSDQD
------CCCCCCHHH
42.4827742792
6Phosphorylation--MSRPLSDQDKRKQ
--CCCCCCHHHHHHC
35.5919854140
10UbiquitinationRPLSDQDKRKQISVR
CCCCHHHHHHCCCHH
56.7322790023
15PhosphorylationQDKRKQISVRGLAGV
HHHHHCCCHHHHHCC
11.8522817900
26PhosphorylationLAGVENVSELKKNFN
HHCCCCHHHHHHHHC
49.1222210690
29UbiquitinationVENVSELKKNFNRHL
CCCHHHHHHHHCCCE
41.4422790023
29AcetylationVENVSELKKNFNRHL
CCCHHHHHHHHCCCE
41.4419863713
42UbiquitinationHLHFTLVKDRNVATP
CEEEEEECCCCCCCC
54.8322790023
76PhosphorylationIRTQQHYYEKDPKRI
HHHCCHHHHCCCCCE
17.8728464351
78UbiquitinationTQQHYYEKDPKRIYY
HCCHHHHCCCCCEEE
64.3127667366
143S-nitrosylationGLGRLAACFLDSMAT
HHHHHHHHHHHHHHH
2.6421278135
143S-nitrosocysteineGLGRLAACFLDSMAT
HHHHHHHHHHHHHHH
2.64-
156PhosphorylationATLGLAAYGYGIRYE
HHHHHHHHCCCCEEE
12.79-
172S-nitrosocysteineGIFNQKICGGWQMEE
EECCCEECCCCCCHH
5.48-
172S-nitrosylationGIFNQKICGGWQMEE
EECCCEECCCCCCHH
5.4821278135
186PhosphorylationEADDWLRYGNPWEKA
HHHCHHHCCCHHHHC
21.0528542873
198PhosphorylationEKARPEFTLPVHFYG
HHCCCCCEECEEEEE
28.6128464351
204PhosphorylationFTLPVHFYGRVEHTS
CEECEEEEEEEEECC
6.8028542873
210PhosphorylationFYGRVEHTSQGAKWV
EEEEEEECCCCCCEE
14.8328464351
211PhosphorylationYGRVEHTSQGAKWVD
EEEEEECCCCCCEEE
28.6428542873
227PhosphorylationQVVLAMPYDTPVPGY
EEEEECCCCCCCCCC
21.26-
241PhosphorylationYRNNVVNTMRLWSAK
CCCCCHHHHHHHCCC
7.6428464351
248UbiquitinationTMRLWSAKAPNDFNL
HHHHHCCCCCCCCCC
59.8822790023
277PhosphorylationRNLAENISRVLYPND
HHHHHHHHCCCCCCC
28.1120531401
290UbiquitinationNDNFFEGKELRLKQE
CCCCCCCCCCCCCCE
46.5122790023
290AcetylationNDNFFEGKELRLKQE
CCCCCCCCCCCCCCE
46.5124588079
316UbiquitinationIRRFKSSKFGSRDPV
HHHHHHCCCCCCCCC
61.9222790023
325PhosphorylationGSRDPVRTNFDAFPD
CCCCCCCCCCCCCCC
40.2328464351
344PhosphorylationQLNDTHPSLAIPELM
ECCCCCHHHHHHHHH
23.8728542873
364SuccinylationLERLDWDKAWDVTVK
HHHCCHHHHCCEEEE
47.31-
364UbiquitinationLERLDWDKAWDVTVK
HHHCCHHHHCCEEEE
47.3122790023
373S-nitrosylationWDVTVKTCAYTNHTV
CCEEEEECCCCCCCC
1.9521278135
373S-nitrosocysteineWDVTVKTCAYTNHTV
CCEEEEECCCCCCCC
1.95-
405PhosphorylationPRHLQIIYEINQRFL
HHHHHHHHHHHHHHH
16.6428464351
430PhosphorylationVDRLRRMSLVEEGAV
HHHHHHHHHHHHCCC
27.7027742792
446S-nitrosylationRINMAHLCIAGSHAV
EEEHHHHHHHCHHHH
1.1221278135
446S-nitrosocysteineRINMAHLCIAGSHAV
EEEHHHHHHHCHHHH
1.12-
461PhosphorylationNGVARIHSEILKKTI
CCHHHHCHHHHHHHH
24.7828542873
467PhosphorylationHSEILKKTIFKDFYE
CHHHHHHHHCCCHHH
30.02-
473PhosphorylationKTIFKDFYELEPHKF
HHHCCCHHHCCCHHC
29.7327742792
483UbiquitinationEPHKFQNKTNGITPR
CCHHCCCCCCCCCCC
32.3622790023
496S-nitrosylationPRRWLVLCNPGLAEV
CCCEEEEECCCHHHH
4.5021278135
496S-nitrosocysteinePRRWLVLCNPGLAEV
CCCEEEEECCCHHHH
4.50-
507MethylationLAEVIAERIGEDYIS
HHHHHHHHHCCCHHC
32.9458859215
514PhosphorylationRIGEDYISDLDQLRK
HHCCCHHCCHHHHHH
26.3728464351
521UbiquitinationSDLDQLRKLLSYVDD
CCHHHHHHHHHHCCH
63.4722790023
524PhosphorylationDQLRKLLSYVDDEAF
HHHHHHHHHCCHHHH
33.2822210690
562PhosphorylationKVHINPNSLFDVQVK
EEECCCCCCHHHHHH
31.5028542873
574PhosphorylationQVKRIHEYKRQLLNC
HHHHHHHHHHHHHHH
9.4129899451
575AcetylationVKRIHEYKRQLLNCL
HHHHHHHHHHHHHHH
30.5915618663
581S-palmitoylationYKRQLLNCLHIITLY
HHHHHHHHHHHHHHH
2.7026165157
614PhosphorylationGGKAAPGYHMAKMII
CCCCCCCHHHHHHHH
6.3322871156
618UbiquitinationAPGYHMAKMIIKLIT
CCCHHHHHHHHHHHH
24.0522790023
656UbiquitinationYRVSLAEKVIPAADL
CCHHHHHHHCCHHHH
39.6022790023
681N6-(pyridoxal phosphate)lysineASGTGNMKFMLNGAL
CCCCCCCEEEECCEE
31.46-
681OtherASGTGNMKFMLNGAL
CCCCCCCEEEECCEE
31.46-
732PhosphorylationRGYNAQEYYDRIPEL
CCCCHHHHHHHHHHH
9.8928542873
733PhosphorylationGYNAQEYYDRIPELR
CCCHHHHHHHHHHHH
9.6728464351
747PhosphorylationRQIIEQLSSGFFSPK
HHHHHHHHCCCCCCC
28.2728464351
748PhosphorylationQIIEQLSSGFFSPKQ
HHHHHHHCCCCCCCC
48.49-
754UbiquitinationSSGFFSPKQPDLFKD
HCCCCCCCCCCHHHH
73.5822790023
783UbiquitinationADYEEYIKCQDKVSE
CCHHHHHHCHHHHHH
25.5822790023
784S-nitrosocysteineDYEEYIKCQDKVSEL
CHHHHHHCHHHHHHH
4.61-
784S-nitrosylationDYEEYIKCQDKVSEL
CHHHHHHCHHHHHHH
4.6121278135
809PhosphorylationVIRNIATSGKFSSDR
HHHHHHHCCCCCCCH
30.8528542873
811UbiquitinationRNIATSGKFSSDRTI
HHHHHCCCCCCCHHH
41.6722790023
813PhosphorylationIATSGKFSSDRTIAQ
HHHCCCCCCCHHHHH
34.5119854140
821PhosphorylationSDRTIAQYAREIWGV
CCHHHHHHHHHHHCC
9.9019854140
831PhosphorylationEIWGVEPSRQRLPAP
HHHCCCCCCCCCCCC
27.7828542873
841UbiquitinationRLPAPDEKI------
CCCCCCCCC------
62.1822790023

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
15SPhosphorylationKinasePHK-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
15SPhosphorylation

-

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 PYGM_MOUSE !!

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

Oops, there are no PPI records of PYGM_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473, AND MASSSPECTROMETRY.

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