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P53534 · PYGB_RAT

  • Protein
    Glycogen phosphorylase, brain form
  • Gene
    Pygb
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

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

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Activity regulation

Activity of phosphorylase is controlled both by allosteric means (through the non-covalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site43AMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Site76Participates in a stacking interaction with the adenine ring of AMP
Site109Involved in the association of subunits
Site143Involved in the association of subunits
Site156May be involved in allosteric control
Binding site197AMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site310AMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site569pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentcytoplasm
Molecular Functioncarbohydrate binding
Molecular Functionglycogen phosphorylase activity
Molecular Functionidentical protein binding
Molecular Functionlinear malto-oligosaccharide phosphorylase activity
Molecular Functionorganic cyclic compound binding
Molecular Functionpyridoxal phosphate binding
Molecular FunctionSHG alpha-glucan phosphorylase activity
Biological Processglycogen catabolic process
Biological Processglycogen metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycogen phosphorylase, brain form
  • EC number

Gene names

    • Name
      Pygb

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P53534

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001885382-838Glycogen phosphorylase, brain form
Modified residue15Phosphoserine
Modified residue197Phosphotyrosine
Modified residue473Phosphotyrosine
Modified residue524Phosphoserine
Modified residue681N6-(pyridoxal phosphate)lysine

Post-translational modification

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region677-678Pyridoxal 5'-phosphate

Sequence similarities

Belongs to the glycogen phosphorylase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    838
  • Mass (Da)
    96,174
  • Last updated
    2007-01-23 v3
  • MD5 Checksum
    B8020B8E513E6E4D24DBF8B35283AF31
MAKPLTDSERQKQISVRGIAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQTACDEATYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPNGVLWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLKDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKVDWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLAEIIVERIGEGFLTDLSQLKKLLSLVDDEAFIRDVAKVKQENKLKFSAQLEKEYKVKINPCSMFDVHVKRIHEYKRQLLNCLHIITLYNRIKKDPTKTFVPRTVMIGGKAAPGYHMAKMIIKLVTSIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVEDVEALDQKGYNAQEFYERLPELRQAVDQISSGFFSPKDPDCFKDVVNMLMYHDRFKVFADYEAYIQCQAQVDHLYRNPKDWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPP

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6GKE5A0A8I6GKE5_RATPygb838
A0A8I6G9W3A0A8I6G9W3_RATPygb775
G3V6Y6G3V6Y6_RATPygb846

Features

Showing features for sequence conflict, non-terminal residue.

Type
IDPosition(s)Description
Sequence conflict589in Ref. 3; AAA40815
Non-terminal residue838

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L10668
EMBL· GenBank· DDBJ
AAA41252.1
EMBL· GenBank· DDBJ
mRNA
M27726
EMBL· GenBank· DDBJ
AAA40815.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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