Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8CI94 (PYGB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen phosphorylase, brain form
EC=2.4.1.1
Gene names
Name:Pygb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.

Cofactor

Pyridoxal phosphate By similarity.

Enzyme regulation

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

Subunit structure

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

Post-translational modification

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

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence caution

The sequence AAH32209.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 843842Glycogen phosphorylase, brain form
PRO_0000188536

Sites

Binding site761AMP By similarity
Site1091Involved in the association of subunits By similarity
Site1431Involved in the association of subunits By similarity
Site1561May be involved in allosteric control By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue151Phosphoserine; by PHK; in form phosphorylase A By similarity
Modified residue1971Phosphotyrosine Ref.2
Modified residue4731Phosphotyrosine Ref.2
Modified residue6811N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CI94 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AF9F499FBB5B8B0C

FASTA84396,730
        10         20         30         40         50         60 
MAKPLTDSER QKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQTACD EATYQLGLDL 

       130        140        150        160        170        180 
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA 

       190        200        210        220        230        240 
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVLWLDTQ VVLAMPYDTP VPGYKNNTVN 

       250        260        270        280        290        300 
TMRLWSAKAP NDFKLKDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDIIR RFKSSRFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV 

       370        380        390        400        410        420 
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP 

       430        440        450        460        470        480 
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLLLCNPGL AEIIVERIGE GFLTDLSQLK KLLSLVDDEA FIRDVAKVKQ 

       550        560        570        580        590        600 
ENKLKFSAQL EKEYKVKINP ASMFDVHVKR IHEYKRQLLN CLHIITLYNR IKKDPAKAFV 

       610        620        630        640        650        660 
PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVEDVE 

       730        740        750        760        770        780 
ALDQKGYNAR EFYERLPELR QAVDQISSGF FSPKDPDCFK DVVNMLMYHD RFKVFADYEA 

       790        800        810        820        830        840 
YIQCQAQVDR LYRNSKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNL 


PKD

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
[2]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197 AND TYR-473, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC032209 mRNA. Translation: AAH32209.1. Different initiation.
BC035283 mRNA. Translation: AAH35283.1.
IPIIPI00229796.
RefSeqNP_722476.1. NM_153781.1.
UniGeneMm.222584.

3D structure databases

ProteinModelPortalQ8CI94.
SMRQ8CI94. Positions 14-839.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8CI94. 3 interactions.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSiteQ8CI94.

Proteomic databases

PaxDbQ8CI94.
PRIDEQ8CI94.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045441; ENSMUSP00000035743; ENSMUSG00000033059.
GeneID110078.
KEGGmmu:110078.

Organism-specific databases

CTD5834.
MGIMGI:97828. Pygb.

Phylogenomic databases

eggNOGCOG0058.
GeneTreeENSGT00390000016886.
HOGENOMHOG000278444.
HOVERGENHBG006848.
InParanoidQ8CI94.
KOK00688.
OMACASMDLS.
OrthoDBEOG4S1T6F.

Gene expression databases

ArrayExpressQ8CI94.
BgeeQ8CI94.
CleanExMM_PYGB.
GenevestigatorQ8CI94.
GermOnlineENSMUSG00000033059. Mus musculus.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. PTHR11468. 1 hit.
PfamPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsTIGR02093. P_ylase. 1 hit.
PROSITEPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio363279.
SOURCESearch...

Entry information

Entry namePYGB_MOUSE
AccessionPrimary (citable) accession number: Q8CI94
Secondary accession number(s): Q8K283
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents