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Reviewed, UniProtKB/Swiss-Prot Q9WUB3 (PYGM_MOUSE)

Last modified November 3, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycogen phosphorylase, muscle form
    EC=2.4.1.1
Alternative name(s):
    Myophosphorylase
Gene names
Name: Pygm
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length842 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.

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 842841Glycogen phosphorylase, muscle form
PRO_0000188531

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-acetylserine By similarity
Modified residue151Phosphoserine; by PHK; in form phosphorylase A By similarity
Modified residue3161N6-acetyllysine By similarity
Modified residue4731Phosphotyrosine Ref.3
Modified residue6811N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WUB3-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B55CC8EFF517DCD9

FASTA84297,286
        10         20         30         40         50         60 
MSRPLSDQDK RKQISVRGLA GVENVSELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM 

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

       190        200        210        220        230        240 
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 

       250        260        270        280        290        300 
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDIIR RFKSSKFGSR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERL 

       370        380        390        400        410        420 
DWDKAWDVTV KTCAYTNHTV LPEALERWPV HLMETLLPRH LQIIYEINQR FLNRVAAAFP 

       430        440        450        460        470        480 
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLVLCNPGL AEVIAERIGE DYISDLDQLR KLLSYVDDEA FIRDVAKVKQ 

       550        560        570        580        590        600 
ENKLKFSAYL EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHIITLYNR IKREPNRFMV 

       610        620        630        640        650        660 
PRTIMIGGKA APGYHMAKMI IKLITAIGDV VNHDPAVGDR LRVIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVE 

       730        740        750        760        770        780 
RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE 

       790        800        810        820        830        840 
YIKCQDKVSE LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE 


KI 

« Hide

References

« Hide 'large scale' references
[1]"Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of mice lacking the heart/muscle isoform of the adenine nucleotide translocator."
Murdock D.G., Boone B.E., Esposito L.A., Wallace D.C.
J. Biol. Chem. 274:14429-14433(1999) [PubMed: 10318868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Skeletal muscle.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
[3]"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: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF124787 mRNA. Translation: AAD30476.1.
BC012961 mRNA. Translation: AAH12961.1.
IPIIPI00225275.
RefSeqNP_035354.1.
UniGeneMm.27806

3D structure databases

HSSPHSSP built from PDB template 1K08 based on UniProtKB P00489.
SMRQ9WUB3. Positions 13-836.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9WUB3.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSiteQ9WUB3.

Proteomic databases

PRIDEQ9WUB3.

Genome annotation databases

EnsemblENSMUST00000035269; ENSMUSP00000047564; ENSMUSG00000032648; Mus musculus. [Genome view]
GeneID19309.
KEGGmmu:19309.
UCSCuc008gio.1. mouse.

Organism-specific databases

CTD19309.
MGIMGI:97830. Pygm.

Phylogenomic databases

HOGENOMQ9WUB3.
HOVERGENQ9WUB3.
OMANQKISGG.

Enzyme and pathway databases

BRENDA2.4.1.1. 244.

Gene expression databases

ArrayExpressQ9WUB3.
BgeeQ9WUB3.
CleanExMM_PYGM.
GenevestigatorQ9WUB3.
GermOnlineENSMUSG00000032648. Mus musculus.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. Glyco_trans_35. 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 Resources

NextBio296275.
SOURCESearch...

Entry information

Entry namePYGM_MOUSE
AccessionPrimary (citable) accession number: Q9WUB3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents