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Protein

Glycogen phosphorylase, muscle form

Gene

Pygm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761AMPBy similarity
Sitei109 – 1091Involved in the association of subunitsBy similarity
Sitei143 – 1431Involved in the association of subunitsBy similarity
Sitei156 – 1561May be involved in allosteric controlBy similarity

GO - Molecular functioni

  • AMP binding Source: RGD
  • carbohydrate binding Source: RGD
  • drug binding Source: RGD
  • glycogen phosphorylase activity Source: RGD
  • protein homodimerization activity Source: RGD
  • pyridoxal phosphate binding Source: RGD

GO - Biological processi

  • cellular calcium ion homeostasis Source: RGD
  • glycogen catabolic process Source: RGD
  • glycogen metabolic process Source: RGD
  • response to cAMP Source: RGD
  • response to hypoxia Source: RGD
  • response to organic substance Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Nucleotide-binding, Pyridoxal phosphate

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen phosphorylase, muscle form (EC:2.4.1.1)
Alternative name(s):
Myophosphorylase
Gene namesi
Name:Pygm
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3461. Pygm.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • sarcoplasmic reticulum Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 842841Glycogen phosphorylase, muscle formPRO_0000188533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase ABy similarity
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei204 – 2041PhosphotyrosineCombined sources
Modified residuei227 – 2271PhosphotyrosineCombined sources
Modified residuei364 – 3641N6-succinyllysineBy similarity
Modified residuei430 – 4301PhosphoserineBy similarity
Modified residuei473 – 4731PhosphotyrosineCombined sources
Modified residuei514 – 5141PhosphoserineCombined sources
Modified residuei524 – 5241PhosphoserineBy similarity
Modified residuei681 – 6811N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei747 – 7471PhosphoserineCombined sources
Modified residuei748 – 7481PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP09812.
PRIDEiP09812.

PTM databases

iPTMnetiP09812.
PhosphoSiteiP09812.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP09812. 1 interaction.
STRINGi10116.ENSRNOP00000028636.

Structurei

3D structure databases

ProteinModelPortaliP09812.
SMRiP09812. Positions 14-842.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP09812.
PhylomeDBiP09812.

Family and domain databases

InterProiIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERiPTHR11468. PTHR11468. 1 hit.
PfamiPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsiTIGR02093. P_ylase. 1 hit.
PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPLSDQDK RKQISVRGLA GVENVSDLKK NFNRHLHFTL VKDRNVATPR
60 70 80 90 100
DYYFALAHTV RDHLVDRWIR TQQHYYAKDP KRIYYLSLEL YMGRTLQNTM
110 120 130 140 150
VNLALENACD EATYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT
160 170 180 190 200
LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA DDWLRYGNPW EKARPEFTLP
210 220 230 240 250
VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN TMRLWSAKAP
260 270 280 290 300
PYFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDKFFEGK ELRLKQEYFV
310 320 330 340 350
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL
360 370 380 390 400
IRILVDLERL DWDKAWDVTV KTCAYTNHTV LPEALERWPV HLMETLLPRH
410 420 430 440 450
LQIIYEINQR FLNRVAAAFP GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS
460 470 480 490 500
HAVNGVARIH SEILKKTIFK DFYELEPHKF QNKTNGITPR RWLVLCNPGL
510 520 530 540 550
AEVIAERIGE EYISDLDQLR KLLSYLDDQA FIRDVAKVKQ ENKLKFSAYL
560 570 580 590 600
ETEYKVHINP NSLFDVQVKR IHEYKRQLLN CLHIITLYNR IKREPNRFMV
610 620 630 640 650
PRTIMIGGKA APGYHMAKMI IKLITAIGDV VNHDPAVGDR FRVIFLENYR
660 670 680 690 700
VSLAEKVIPA ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM
710 720 730 740 750
AEEAGEDNFF IFGMRVEDVE RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF
760 770 780 790 800
FSPKQPDLFK DIVNMVMHHD RFKVFADYEE YIKCQDKVSE LYKNPREWTR
810 820 830 840
MVIRNIATSG KFSSDRTIAQ YAREIWGLEP SRQRLPAPDE KI
Length:842
Mass (Da):97,273
Last modified:January 23, 2007 - v5
Checksum:iEA30BBB63FE69700
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti640 – 6412RF → L (PubMed:2424788).Curated
Sequence conflicti724 – 7241Q → N (PubMed:2424788).Curated
Sequence conflicti766 – 7661V → L in CAA26835 (PubMed:3840433).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10669 mRNA. Translation: AAA41253.1.
X03032 mRNA. Translation: CAA26835.1.
PIRiS34624.
UniGeneiRn.11238.

Genome annotation databases

UCSCiRGD:3461. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10669 mRNA. Translation: AAA41253.1.
X03032 mRNA. Translation: CAA26835.1.
PIRiS34624.
UniGeneiRn.11238.

3D structure databases

ProteinModelPortaliP09812.
SMRiP09812. Positions 14-842.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09812. 1 interaction.
STRINGi10116.ENSRNOP00000028636.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

PTM databases

iPTMnetiP09812.
PhosphoSiteiP09812.

Proteomic databases

PaxDbiP09812.
PRIDEiP09812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3461. rat.

Organism-specific databases

RGDi3461. Pygm.

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP09812.
PhylomeDBiP09812.

Miscellaneous databases

PROiP09812.

Family and domain databases

InterProiIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERiPTHR11468. PTHR11468. 1 hit.
PfamiPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsiTIGR02093. P_ylase. 1 hit.
PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparative analysis of species-independent, isozyme-specific amino-acid substitutions in mammalian muscle, brain and liver glycogen phosphorylases."
    Hudson J.W., Hefferon K.L., Crerar M.M.
    Biochim. Biophys. Acta 1164:197-208(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation of partial cDNAs for rat liver and muscle glycogen phosphorylase isozymes."
    Osawa S., Chiu R.H., McDonough A., Miller T.B. Jr., Johnson G.L.
    FEBS Lett. 202:282-288(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 566-762.
  3. "Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs."
    Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J., Crerar M.M.
    Eur. J. Biochem. 152:267-274(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 763-842.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; TYR-204; TYR-227; TYR-473; SER-514; SER-747 AND SER-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYGM_RAT
AccessioniPrimary (citable) accession number: P09812
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 129 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.