PYGB_RAT - dbPTM
PYGB_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYGB_RAT
UniProt AC P53534
Protein Name Glycogen phosphorylase, brain form
Gene Name Pygb
Organism Rattus norvegicus (Rat).
Sequence Length 838
Subcellular Localization
Protein Description Glycogen phosphorylase that regulates glycogen mobilization (By similarity). 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 MAKPLTDSERQKQISVRGIAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQTACDEATYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPNGVLWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLKDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKVDWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLAEIIVERIGEGFLTDLSQLKKLLSLVDDEAFIRDVAKVKQENKLKFSAQLEKEYKVKINPCSMFDVHVKRIHEYKRQLLNCLHIITLYNRIKKDPTKTFVPRTVMIGGKAAPGYHMAKMIIKLVTSIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVEDVEALDQKGYNAQEFYERLPELRQAVDQISSGFFSPKDPDCFKDVVNMLMYHDRFKVFADYEAYIQCQAQVDHLYRNPKDWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPP
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------MAKPLTDSE
------CCCCCCHHH
23.36-
3Ubiquitination-----MAKPLTDSER
-----CCCCCCHHHH
38.98-
3Acetylation-----MAKPLTDSER
-----CCCCCCHHHH
38.9822902405
15PhosphorylationSERQKQISVRGIAGL
HHHHHHHHHHCCCCC
11.8528826663
186PhosphorylationEADDWLRYGNPWEKA
ECCCHHHCCCHHHHC
21.0522673903
197PhosphorylationWEKARPEYMLPVHFY
HHHCCCCCEEEEEEE
13.46-
204PhosphorylationYMLPVHFYGRVEHTP
CEEEEEEEECCEECC
6.80-
227PhosphorylationQVVLAMPYDTPVPGY
EEEEECCCCCCCCCC
21.2622673903
254AcetylationAKAPNDFKLKDFNVG
CCCCCCCCCCCCCHH
58.4522902405
256AcetylationAPNDFKLKDFNVGDY
CCCCCCCCCCCHHHH
61.9522902405
364AcetylationVEKVDWDKAWEITKK
HHHCCHHHHHHHHHH
51.6622902405
370AcetylationDKAWEITKKTCAYTN
HHHHHHHHHHHCCCC
52.3122902405
391PhosphorylationALERWPVSMFEKLLP
HHHHCCHHHHHHHHH
17.4222673903
430PhosphorylationVDRLRRMSVIEEGDC
HHHHHHCCEECCCCC
20.3823984901
473PhosphorylationQSVFKDFYELEPEKF
HHHCCCHHHCCHHHH
29.73-
483UbiquitinationEPEKFQNKTNGITPR
CHHHHCCCCCCCCHH
32.36-
520AcetylationLTDLSQLKKLLSLVD
CCCHHHHHHHHHHCC
33.4722902405
521UbiquitinationTDLSQLKKLLSLVDD
CCHHHHHHHHHHCCH
64.35-
524PhosphorylationSQLKKLLSLVDDEAF
HHHHHHHHHCCHHHH
36.4622108457
552AcetylationKFSAQLEKEYKVKIN
CEEECCCHHHCCCCC
74.9622902405
681OtherASGTGNMKFMLNGAL
CCCCCCCEEEECCEE
31.46-
681N6-(pyridoxal phosphate)lysineASGTGNMKFMLNGAL
CCCCCCCEEEECCEE
31.46-
752PhosphorylationQISSGFFSPKDPDCF
HHHCCCCCCCCCCHH
28.8725575281

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-FAMILY-GPS

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

22673903

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 PYGB_RAT !!

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

Oops, there are no PPI records of PYGB_RAT !!

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

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Related Literatures of Post-Translational Modification

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