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Protein

Glycogen phosphorylase, liver form

Gene

Pygl

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

Enzyme regulationi

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.

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: Ensembl
  • ATP binding Source: Ensembl
  • bile acid binding Source: Ensembl
  • carbohydrate binding Source: RGD
  • drug binding Source: RGD
  • glycogen phosphorylase activity Source: RGD
  • protein homodimerization activity Source: RGD
  • purine nucleobase binding Source: Ensembl
  • pyridoxal phosphate binding Source: GO_Central
  • vitamin binding Source: Ensembl

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: RGD
  • glucose homeostasis Source: Ensembl
  • glycogen catabolic process Source: RGD
  • glycogen metabolic process Source: RGD
  • necroptotic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Nucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-RNO-70221. Glycogen breakdown (glycogenolysis).

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen phosphorylase, liver form (EC:2.4.1.1)
Gene namesi
Name:Pygl
Synonyms:Lgp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620687. Pygl.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • plasma membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 850849Glycogen phosphorylase, liver formPRO_0000188526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase ABy similarity
Modified residuei204 – 2041PhosphotyrosineBy similarity
Modified residuei227 – 2271PhosphotyrosineBy similarity
Modified residuei364 – 3641N6-succinyllysineBy similarity
Modified residuei430 – 4301PhosphoserineBy similarity
Modified residuei524 – 5241PhosphoserineBy similarity
Modified residuei561 – 5611PhosphoserineCombined sources
Modified residuei639 – 6391PhosphoserineCombined sources
Modified residuei681 – 6811N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP09811.
PRIDEiP09811.

PTM databases

iPTMnetiP09811.

Expressioni

Gene expression databases

GenevisibleiP09811. RN.

Interactioni

Subunit structurei

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. Interacts with PPP1R3B.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP09811. 1 interaction.
MINTiMINT-4565487.
STRINGi10116.ENSRNOP00000009183.

Chemistry

BindingDBiP09811.

Structurei

3D structure databases

ProteinModelPortaliP09811.
SMRiP09811. Positions 6-838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
GeneTreeiENSGT00390000016886.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP09811.
KOiK00688.
OMAiFNFEAFN.
OrthoDBiEOG7JQBMK.
PhylomeDBiP09811.
TreeFamiTF300309.

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.

P09811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR
60 70 80 90 100
DYYFALAHTV RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM
110 120 130 140 150
INLGLQNACD EAIYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT
160 170 180 190 200
LGLAAYGYGI RYEYGIFNQK IREGWQVEEA DDWLRHGNPW EKARPEFMLP
210 220 230 240 250
VHFYGRVEHT QAGTKWVDTQ VVLALPYDTP VPGYMNNTVN TMRLWSARAP
260 270 280 290 300
NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
310 320 330 340 350
VAATLQDVIR RFKASKFGSK DGVGTVFDAF PDQVAIQLND THPALAIPEL
360 370 380 390 400
MRIFVDIEKL PWSKAWEITK KTFAYTNHTV LPEALERWPV DLVEKLLPRH
410 420 430 440 450
LQIIYEINQK HLDRIVALFP KDIDRMRRMS LIEEEGGKRI NMAHLCIVGC
460 470 480 490 500
HAVNGVAKIH SDIVKTQVFK DFSELEPDKF QNKTNGITPR RWLLLCNPGL
510 520 530 540 550
ADLIAEKIGE DYVKDLSQLT KLHSFVGDDI FLREIAKVKQ ENKLKFSQFL
560 570 580 590 600
EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV
610 620 630 640 650
PRTVIIGGKA APGYHMAKMI IKLVTSVAEV VNNDPMVGSK LKVIFLENYR
660 670 680 690 700
VSLAEKVIPA TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM
710 720 730 740 750
AEEAGEENLF IFGMRVDDVA ALDKKGYEAK EYYEALPELK LVIDQIDNGF
760 770 780 790 800
FSPNQPDLFK DIINMLFYHD RFKVFADYEA YVKCQEKVSQ LYMNQKAWNT
810 820 830 840 850
MVLRNIAASG KFSSDRTIRE YAKDIWNMEP SDLKISLSKE SSNGVNANGK
Length:850
Mass (Da):97,483
Last modified:January 23, 2007 - v5
Checksum:i0BE9A641DFFF3E0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti667 – 6671I → V in CAA27704 (PubMed:2424788).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63515 mRNA. Translation: CAA45083.1.
BC070901 mRNA. Translation: AAH70901.1.
M85280 Genomic DNA. Translation: AAA41254.1.
J03080 mRNA. Translation: AAA41986.1.
X04069 mRNA. Translation: CAA27704.1.
M59460 mRNA. Translation: AAA41987.1.
PIRiS22338.
RefSeqiNP_071604.1. NM_022268.1.
UniGeneiRn.21399.

Genome annotation databases

EnsembliENSRNOT00000009183; ENSRNOP00000009183; ENSRNOG00000006388.
GeneIDi64035.
KEGGirno:64035.
UCSCiRGD:620687. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63515 mRNA. Translation: CAA45083.1.
BC070901 mRNA. Translation: AAH70901.1.
M85280 Genomic DNA. Translation: AAA41254.1.
J03080 mRNA. Translation: AAA41986.1.
X04069 mRNA. Translation: CAA27704.1.
M59460 mRNA. Translation: AAA41987.1.
PIRiS22338.
RefSeqiNP_071604.1. NM_022268.1.
UniGeneiRn.21399.

3D structure databases

ProteinModelPortaliP09811.
SMRiP09811. Positions 6-838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09811. 1 interaction.
MINTiMINT-4565487.
STRINGi10116.ENSRNOP00000009183.

Chemistry

BindingDBiP09811.
ChEMBLiCHEMBL3239.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

PTM databases

iPTMnetiP09811.

Proteomic databases

PaxDbiP09811.
PRIDEiP09811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009183; ENSRNOP00000009183; ENSRNOG00000006388.
GeneIDi64035.
KEGGirno:64035.
UCSCiRGD:620687. rat.

Organism-specific databases

CTDi5836.
RGDi620687. Pygl.

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
GeneTreeiENSGT00390000016886.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP09811.
KOiK00688.
OMAiFNFEAFN.
OrthoDBiEOG7JQBMK.
PhylomeDBiP09811.
TreeFamiTF300309.

Enzyme and pathway databases

ReactomeiR-RNO-70221. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

PROiP09811.

Gene expression databases

GenevisibleiP09811. RN.

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. "The nucleotide sequence of rat liver glycogen phosphorylase cDNA."
    Schiebel K., Pekel E., Mayer D.
    Biochim. Biophys. Acta 1130:349-351(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. "Characterization of the 5' flanking region of the gene encoding rat liver glycogen phosphorylase."
    Herrick K.R., Gorin F.A., Park E.A., Tait R.C.
    Gene 126:203-211(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "Localization of the muscle, liver, and brain glycogen phosphorylase genes on linkage maps of mouse chromosomes 19, 12, and 2, respectively."
    Glaser T., Matthews K.E., Hudson J.W., Seth P., Houseman D.E., Crerar M.M.
    Genomics 5:510-521(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 333-430.
  5. "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 [GENOMIC DNA] OF 441-850.
    Tissue: Liver.
  6. "The gene encoding rat liver glycogen phosphorylase contains multiple polyadenylation signal sequences."
    Froman B.E., Tait R.C., Gorin F.A., Horwitz B.A., Stern J.S.
    Gene 109:269-274(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 835-850.
    Strain: Zucker.
  7. "Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography."
    Moorhead G., MacKintosh C., Morrice N., Cohen P.
    FEBS Lett. 362:101-105(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R3B.
  8. "Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1."
    Doherty M.J., Moorhead G., Morrice N., Cohen P., Cohen P.T.W.
    FEBS Lett. 375:294-298(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R3B.
  9. "Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1."
    Armstrong C.G., Doherty M.J., Cohen P.T.W.
    Biochem. J. 336:699-704(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R3B.
  10. "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-561 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYGL_RAT
AccessioniPrimary (citable) accession number: P09811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 152 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.