PYGL_MOUSE - dbPTM
PYGL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYGL_MOUSE
UniProt AC Q9ET01
Protein Name Glycogen phosphorylase, liver form
Gene Name Pygl
Organism Mus musculus (Mouse).
Sequence Length 850
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 (By similarity)..
Protein Sequence MAKPLTDQEKRRQISIRGIVGVENVAELKKGFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIREGWQVEEADDWLRHGNPWEKARPEFMLPVHFYGRVEHTQTGTKWVDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLQDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDVIRRFKASKFGSKDGMGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWAKAWEITKKTFAYTNHTVLPEALERWPVELVEKLLPRHLEIIYEINQKHLDRIVALFPKDISRMRRMSLIEEEGGKRINMAHLCIVGCHAVNGVAKIHSDIVKTQVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLADLIAEKIGEDYVKDLSQLTKLHSFVSDDIFLREIAKVKQENKLKFSQFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVITMYNRIKKDPKKFFVPRTVIIGGKAAPGYHMAKMIIKLITSVAEVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPNQPDLFKDIINMLFYHDRFKVFADYEAYVKCQEKVSQLYMNQKAWNTMVLKNIAASGKFSSDRTIKEYAKDIWNMEPSDLKISLSNESSNGVSANGK
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------MAKPLTDQE
------CCCCCCHHH
23.36-
3Acetylation-----MAKPLTDQEK
-----CCCCCCHHHH
38.986566199
3Malonylation-----MAKPLTDQEK
-----CCCCCCHHHH
38.9826320211
3Ubiquitination-----MAKPLTDQEK
-----CCCCCCHHHH
38.98-
10SuccinylationKPLTDQEKRRQISIR
CCCCHHHHHHCCCHH
47.4423954790
15PhosphorylationQEKRRQISIRGIVGV
HHHHHCCCHHHEECC
9.6317257813
29AcetylationVENVAELKKGFNRHL
CCCHHHHHCCCCCCE
42.2123864654
29MalonylationVENVAELKKGFNRHL
CCCHHHHHCCCCCCE
42.2126320211
29UbiquitinationVENVAELKKGFNRHL
CCCHHHHHCCCCCCE
42.2127667366
30AcetylationENVAELKKGFNRHLH
CCHHHHHCCCCCCEE
79.8123954790
30MalonylationENVAELKKGFNRHLH
CCHHHHHCCCCCCEE
79.8125418362
42UbiquitinationHLHFTLVKDRNVATP
CEEEEEECCCCCCCC
54.83-
75PhosphorylationWIRTQQHYYDKCPKR
HHHHCCHHHHCCCCC
14.71-
76PhosphorylationIRTQQHYYDKCPKRV
HHHCCHHHHCCCCCE
13.5525195567
78AcetylationTQQHYYDKCPKRVYY
HCCHHHHCCCCCEEE
35.9922733758
78MalonylationTQQHYYDKCPKRVYY
HCCHHHHCCCCCEEE
35.9926320211
78UbiquitinationTQQHYYDKCPKRVYY
HCCHHHHCCCCCEEE
35.99-
156PhosphorylationATLGLAAYGYGIRYE
HHHHHHHHHCCCEEE
12.79-
170AcetylationEYGIFNQKIREGWQV
EEECCCHHHCCCCCE
44.8566695399
170MalonylationEYGIFNQKIREGWQV
EEECCCHHHCCCCCE
44.8526320211
170UbiquitinationEYGIFNQKIREGWQV
EEECCCHHHCCCCCE
44.8527667366
204PhosphorylationFMLPVHFYGRVEHTQ
CEEEEEEEEEEEECC
6.8026032504
227PhosphorylationQVVLALPYDTPVPGY
EEEEEECCCCCCCCC
33.04-
277PhosphorylationRNLAENISRVLYPND
HHHHHHHHCCCCCCC
28.1120531401
290AcetylationNDNFFEGKELRLKQE
CCCCCCCCCEECCCE
46.5138026455
290MalonylationNDNFFEGKELRLKQE
CCCCCCCCCEECCCE
46.5126320211
290UbiquitinationNDNFFEGKELRLKQE
CCCCCCCCCEECCCE
46.5127667366
295UbiquitinationEGKELRLKQEYFVVA
CCCCEECCCEEEEEE
34.3522790023
320UbiquitinationKASKFGSKDGMGTVF
HHHHHCCCCCCCCCC
59.6922790023
359AcetylationRIFVDIEKLPWAKAW
HHHCCHHHCCCHHHH
61.2538026431
359MalonylationRIFVDIEKLPWAKAW
HHHCCHHHCCCHHHH
61.2526320211
359UbiquitinationRIFVDIEKLPWAKAW
HHHCCHHHCCCHHHH
61.25-
364AcetylationIEKLPWAKAWEITKK
HHHCCCHHHHHHHCC
50.6066698109
364SuccinylationIEKLPWAKAWEITKK
HHHCCCHHHHHHHCC
50.60-
364SuccinylationIEKLPWAKAWEITKK
HHHCCCHHHHHHHCC
50.6023806337
364UbiquitinationIEKLPWAKAWEITKK
HHHCCCHHHHHHHCC
50.60-
370MalonylationAKAWEITKKTFAYTN
HHHHHHHCCCEEECC
56.3226320211
370UbiquitinationAKAWEITKKTFAYTN
HHHHHHHCCCEEECC
56.3222790023
371MalonylationKAWEITKKTFAYTNH
HHHHHHCCCEEECCC
39.9826320211
371UbiquitinationKAWEITKKTFAYTNH
HHHHHHCCCEEECCC
39.9827667366
395AcetylationWPVELVEKLLPRHLE
CCHHHHHHHHHHHHH
48.0966695283
395UbiquitinationWPVELVEKLLPRHLE
CCHHHHHHHHHHHHH
48.0922790023
410AcetylationIIYEINQKHLDRIVA
HHHHHCHHHHHHHHH
41.4666700179
410MalonylationIIYEINQKHLDRIVA
HHHHHCHHHHHHHHH
41.4626320211
410UbiquitinationIIYEINQKHLDRIVA
HHHHHCHHHHHHHHH
41.46-
421AcetylationRIVALFPKDISRMRR
HHHHHCHHHHHHHHH
61.4366696493
421MalonylationRIVALFPKDISRMRR
HHHHHCHHHHHHHHH
61.4326320211
421UbiquitinationRIVALFPKDISRMRR
HHHHHCHHHHHHHHH
61.4327667366
430PhosphorylationISRMRRMSLIEEEGG
HHHHHHHHHHHCCCC
25.1222324799
438AcetylationLIEEEGGKRINMAHL
HHHCCCCCEEEHHHE
62.057744587
438UbiquitinationLIEEEGGKRINMAHL
HHHCCCCCEEEHHHE
62.0522790023
446S-nitrosylationRINMAHLCIVGCHAV
EEEHHHEEHHHHHHH
1.3722178444
450S-nitrosylationAHLCIVGCHAVNGVA
HHEEHHHHHHHCCCH
0.9822178444
465AcetylationKIHSDIVKTQVFKDF
HHCCHHHHHHCCCCH
33.3166697495
465MalonylationKIHSDIVKTQVFKDF
HHCCHHHHHHCCCCH
33.3126320211
465UbiquitinationKIHSDIVKTQVFKDF
HHCCHHHHHHCCCCH
33.3127667366
470AcetylationIVKTQVFKDFSELEP
HHHHHCCCCHHHCCC
60.0328643137
470MalonylationIVKTQVFKDFSELEP
HHHHHCCCCHHHCCC
60.0326320211
470UbiquitinationIVKTQVFKDFSELEP
HHHHHCCCCHHHCCC
60.0327667366
473PhosphorylationTQVFKDFSELEPDKF
HHCCCCHHHCCCHHH
51.9423984901
479AcetylationFSELEPDKFQNKTNG
HHHCCCHHHCCCCCC
60.6166692015
479UbiquitinationFSELEPDKFQNKTNG
HHHCCCHHHCCCCCC
60.6122790023
483UbiquitinationEPDKFQNKTNGITPR
CCHHHCCCCCCCCHH
32.3622790023
496S-palmitoylationPRRWLLLCNPGLADL
HHHHHHHCCCCHHHH
6.1128526873
514AcetylationKIGEDYVKDLSQLTK
HHCHHHHHCHHHHHH
46.8866694639
514UbiquitinationKIGEDYVKDLSQLTK
HHCHHHHHCHHHHHH
46.8822790023
521AcetylationKDLSQLTKLHSFVSD
HCHHHHHHHHHHHCC
53.4466697089
521UbiquitinationKDLSQLTKLHSFVSD
HCHHHHHHHHHHHCC
53.4422790023
524PhosphorylationSQLTKLHSFVSDDIF
HHHHHHHHHHCCHHH
37.4726487105
527PhosphorylationTKLHSFVSDDIFLRE
HHHHHHHCCHHHHHH
27.7929899451
545UbiquitinationVKQENKLKFSQFLEK
HHHHCCCCHHHHHHH
44.5822790023
552AcetylationKFSQFLEKEYKVKIN
CHHHHHHHHHCCCCC
69.3766692875
552MalonylationKFSQFLEKEYKVKIN
CHHHHHHHHHCCCCC
69.3726320211
552UbiquitinationKFSQFLEKEYKVKIN
CHHHHHHHHHCCCCC
69.3727667366
557MalonylationLEKEYKVKINPSSMF
HHHHHCCCCCHHHHC
32.3926320211
557UbiquitinationLEKEYKVKINPSSMF
HHHHHCCCCCHHHHC
32.39-
561PhosphorylationYKVKINPSSMFDVHV
HCCCCCHHHHCEEEH
29.9122324799
562PhosphorylationKVKINPSSMFDVHVK
CCCCCHHHHCEEEHH
25.4023140645
574PhosphorylationHVKRIHEYKRQLLNC
EHHHHHHHHHHHHHH
9.4129899451
575AcetylationVKRIHEYKRQLLNCL
HHHHHHHHHHHHHHH
30.597822991
581S-palmitoylationYKRQLLNCLHVITMY
HHHHHHHHHHHHHHH
2.5426165157
586PhosphorylationLNCLHVITMYNRIKK
HHHHHHHHHHHHHCC
16.7122817900
588PhosphorylationCLHVITMYNRIKKDP
HHHHHHHHHHHCCCC
7.8222817900
597MalonylationRIKKDPKKFFVPRTV
HHCCCCHHCEECCEE
49.8025418362
597UbiquitinationRIKKDPKKFFVPRTV
HHCCCCHHCEECCEE
49.8027667366
602DimethylationPKKFFVPRTVIIGGK
CHHCEECCEEEECCC
36.00-
602MethylationPKKFFVPRTVIIGGK
CHHCEECCEEEECCC
36.0018965223
609UbiquitinationRTVIIGGKAAPGYHM
CEEEECCCCCCCHHH
35.8422790023
614PhosphorylationGGKAAPGYHMAKMII
CCCCCCCHHHHHHHH
6.3328464351
618UbiquitinationAPGYHMAKMIIKLIT
CCCHHHHHHHHHHHH
24.0522790023
639PhosphorylationNNDPMVGSKLKVIFL
CCCCCCCCEEEEEEE
24.3325521595
640AcetylationNDPMVGSKLKVIFLE
CCCCCCCEEEEEEEE
46.5351084513
640MalonylationNDPMVGSKLKVIFLE
CCCCCCCEEEEEEEE
46.5326320211
640UbiquitinationNDPMVGSKLKVIFLE
CCCCCCCEEEEEEEE
46.53-
642UbiquitinationPMVGSKLKVIFLENY
CCCCCEEEEEEEECC
36.7022790023
656UbiquitinationYRVSLAEKVIPATDL
CCHHHHHHEEECCCH
39.6022790023
681N6-(pyridoxal phosphate)lysineASGTGNMKFMLNGAL
CCCCCCCEEEECCEE
31.46-
681OtherASGTGNMKFMLNGAL
CCCCCCCEEEECCEE
31.46-
724AcetylationDDVAALDKKGYEAKE
HHHHHHCCCCCCHHH
49.2815618597
724MalonylationDDVAALDKKGYEAKE
HHHHHHCCCCCCHHH
49.2826320211
724UbiquitinationDDVAALDKKGYEAKE
HHHHHHCCCCCCHHH
49.2827667366
730AcetylationDKKGYEAKEYYEALP
CCCCCCHHHHHHHCH
34.0238026419
730MalonylationDKKGYEAKEYYEALP
CCCCCCHHHHHHHCH
34.0226320211
730UbiquitinationDKKGYEAKEYYEALP
CCCCCCHHHHHHHCH
34.02-
773UbiquitinationLFYHDRFKVFADYEA
HHHCHHHHEECCHHH
37.0222790023
783MalonylationADYEAYVKCQEKVSQ
CCHHHHHHHHHHHHH
19.9526320211
787MalonylationAYVKCQEKVSQLYMN
HHHHHHHHHHHHHHC
22.7026320211
796AcetylationSQLYMNQKAWNTMVL
HHHHHCHHHHHHHHH
50.8246007433
796UbiquitinationSQLYMNQKAWNTMVL
HHHHHCHHHHHHHHH
50.8222790023
804AcetylationAWNTMVLKNIAASGK
HHHHHHHHHHHHCCC
34.5938026407
804MalonylationAWNTMVLKNIAASGK
HHHHHHHHHHHHCCC
34.5926320211
804UbiquitinationAWNTMVLKNIAASGK
HHHHHHHHHHHHCCC
34.5927667366
809PhosphorylationVLKNIAASGKFSSDR
HHHHHHHCCCCCCCH
33.2324759943
811AcetylationKNIAASGKFSSDRTI
HHHHHCCCCCCCHHH
39.3166701303
811UbiquitinationKNIAASGKFSSDRTI
HHHHHCCCCCCCHHH
39.3122790023
813PhosphorylationIAASGKFSSDRTIKE
HHHCCCCCCCHHHHH
34.5125195567
817PhosphorylationGKFSSDRTIKEYAKD
CCCCCCHHHHHHHHH
41.2025195567
819MalonylationFSSDRTIKEYAKDIW
CCCCHHHHHHHHHHH
44.0226320211
823AcetylationRTIKEYAKDIWNMEP
HHHHHHHHHHHCCCH
49.1766698603
823MalonylationRTIKEYAKDIWNMEP
HHHHHHHHHHHCCCH
49.1726320211
823UbiquitinationRTIKEYAKDIWNMEP
HHHHHHHHHHHCCCH
49.17-
850AcetylationNGVSANGK-------
CCCCCCCC-------
57.907744597

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 PYGL_MOUSE !!

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

Oops, there are no PPI records of PYGL_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND MASSSPECTROMETRY.

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