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Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase)

 PYGM_HUMAN              Reviewed;         842 AA.
P11217; A0AVK1; A6NDY6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 6.
25-OCT-2017, entry version 207.
RecName: Full=Glycogen phosphorylase, muscle form;
EC=2.4.1.1;
AltName: Full=Myophosphorylase;
Name=PYGM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3447177; DOI=10.1002/prot.340020303;
Burke J., Hwang P.K., Anderson L., Lebo R., Gorin F., Fletterick R.J.;
"Intron/exon structure of the human gene for the muscle isozyme of
glycogen phosphorylase.";
Proteins 2:177-187(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9633816;
DOI=10.1002/(SICI)1098-1004(1998)12:1<27::AID-HUMU4>3.0.CO;2-#;
Kubisch C., Wicklein E.M., Jentsch T.J.;
"Molecular diagnosis of McArdle disease: revised genomic structure of
the myophosphorylase gene and identification of a novel mutation.";
Hum. Mutat. 12:27-32(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Muscle;
Carty M.D., Clancy Y.C., Soeller W.C.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 676-842 (ISOFORM 1).
PubMed=3840433; DOI=10.1111/j.1432-1033.1985.tb09193.x;
Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J.,
Crerar M.M.;
"Comparative sequence analysis of rat, rabbit, and human muscle
glycogen phosphorylase cDNAs.";
Eur. J. Biochem. 152:267-274(1985).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 455-676 (ISOFORM 1).
PubMed=3466902; DOI=10.1172/JCI112794;
Gautron S., Daegelen D., Mennecier F., Dubocq D., Kahn A.,
Dreyfus J.-C.;
"Molecular mechanisms of McArdle's disease (muscle glycogen
phosphorylase deficiency). RNA and DNA analysis.";
J. Clin. Invest. 79:275-281(1987).
[10]
PHOSPHORYLATION AT SER-15.
PubMed=1150650;
Carty T.J., Tu J., Graves D.J.;
"Regulation of glycogen phosphorylase. Role of the peptide region
surrounding the phosphoserine residue in determining enzyme
properties.";
J. Biol. Chem. 250:4980-4985(1975).
[11]
VARIANTS GSD5 SER-205 AND THR-543.
PubMed=8316268; DOI=10.1056/NEJM199307223290404;
Tsujino S., Shanske S., Dimauro S.;
"Molecular genetic heterogeneity of myophosphorylase deficiency
(McArdle's disease).";
N. Engl. J. Med. 329:241-245(1993).
[12]
VARIANTS GSD5 PRO-397 AND LYS-655.
PubMed=8535454; DOI=10.1002/humu.1380060318;
Tsujino S., Shanske S., Martinuzzi A., Heiman-Patterson T.,
Dimauro S.;
"Two novel missense mutations (E654K, L396P) in Caucasian patients
with myophosphorylase deficiency (McArdle's disease).";
Hum. Mutat. 6:276-277(1995).
[13]
VARIANTS GSD5 SER-205; PRO-292; PRO-397; THR-543; LYS-655 AND PHE-709
DEL.
PubMed=7603523; DOI=10.1002/mus.880181407;
Tsujino S., Shanske S., Nonaka I., DiMauro S.;
"The molecular genetic basis of myophosphorylase deficiency (McArdle's
disease).";
Muscle Nerve 3:S23-S27(1995).
[14]
VARIANTS GSD5 GLU-666 AND ARG-686.
PubMed=9506549; DOI=10.1002/ana.410430310;
Vorgerd M., Kubisch C., Burwinkel B., Reichmann H., Mortier W.,
Tettenborn B., Pongratz D., Lindemuth R., Tegenthoff M., Malin J.P.,
Kilimann M.W.;
"Mutation analysis in myophosphorylase deficiency (McArdle's
disease).";
Ann. Neurol. 43:326-331(1998).
[15]
VARIANT GSD5 PRO-116.
PubMed=10417800;
DOI=10.1002/(SICI)1097-4598(199908)22:8<1136::AID-MUS21>3.0.CO;2-2;
Gamez J., Fernandez R., Bruno C., Andreu A.L., Cervera C., Navarro C.,
Schwartz S., Dimauro S.;
"A new mutation in the regulatory domain of the myophosphorylase gene
affecting protein dimer contact.";
Muscle Nerve 22:1136-1138(1999).
[16]
VARIANTS GSD5 SER-205 AND TYR-685.
PubMed=10382911; DOI=10.1016/S0960-8966(98)00125-4;
Andreu A.L., Bruno C., Tamburino L., Gamez J., Shanske S., Cervera C.,
Navarro C., DiMauro S.;
"A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish
patient with McArdle's disease.";
Neuromuscul. Disord. 9:171-173(1999).
[17]
VARIANT GSD5 SER-205.
PubMed=10382912; DOI=10.1016/S0960-8966(98)00127-8;
Rubio J.C., Martin M.A., Garcia A., Campos Y., Cabello A.,
Culebras J.M., Arenas J.;
"McArdle's disease associated with homozygosity for the missense
mutation Gly204Ser of the myophosphorylase gene in a Spanish
patient.";
Neuromuscul. Disord. 9:174-175(1999).
[18]
VARIANT GSD5 ARG-798.
PubMed=10681080; DOI=10.1001/archneur.57.2.217;
Fernandez R., Navarro C., Andreu A.L., Bruno C., Shanske S., Gamez J.,
Teijeira S., Hernandez I., Teijeiro A., Fernandez J.M., Musumeci O.,
DiMauro S.;
"A novel missense mutation (W797R) in the myophosphorylase gene in
Spanish patients with McArdle disease.";
Arch. Neurol. 57:217-219(2000).
[19]
VARIANT GSD5 ARG-798.
PubMed=10590419;
DOI=10.1002/(SICI)1097-4598(200001)23:1<129::AID-MUS20>3.0.CO;2-F;
Rubio J.C., Martin M.A., Campos Y., Auciello R., Cabello A.,
Arenas J.;
"A missense mutation W797R in the myophosphorylase gene in a Spanish
patient with McArdle's disease.";
Muscle Nerve 23:129-131(2000).
[20]
VARIANT GSD5 ASN-488.
PubMed=10714589; DOI=10.1016/S0960-8966(99)00082-6;
Rubio J.C., Martin M.A., Campos Y., Cabello A., Arenas J.;
"A missense mutation T487N in the myophosphorylase gene in a Spanish
patient with McArdle's disease.";
Neuromuscul. Disord. 10:138-140(2000).
[21]
VARIANT GSD5 ASP-660.
PubMed=10899452; DOI=10.1016/S0960-8966(99)00124-8;
Martin M.A., Rubio J.C., Campos Y., Ricoy J.R., Cabello A., Arenas J.;
"A homozygous missense mutation (A659D) in the myophosphorylase gene
in a Spanish patient with McArdle's disease.";
Neuromuscul. Disord. 10:447-449(2000).
[22]
VARIANTS GSD5 PRO-116; TRP-194; SER-205; LYS-349; ASN-488; TRP-602;
ASP-660; TYR-685; VAL-704 AND ARG-798.
PubMed=11706962; DOI=10.1002/ana.1225.abs;
Martin M.A., Rubio J.C., Buchbinder J., Fernandez-Hojas R.,
del Hoyo P., Teijeira S., Gamez J., Navarro C., Fernandez J.M.,
Cabello A., Campos Y., Cervera C., Culebras J.M., Andreu A.L.,
Fletterick R.J., Arenas J.;
"Molecular heterogeneity of myophosphorylase deficiency (McArdle's
disease): a genotype-phenotype correlation study.";
Ann. Neurol. 50:574-581(2001).
[23]
VARIANT GSD5 PRO-687.
PubMed=12031624; DOI=10.1016/S0960-8966(01)00320-0;
Bruno C., Lanzillo R., Biedi C., Iadicicco L., Minetti C., Santoro L.;
"Two new mutations in the myophosphorylase gene in Italian patients
with McArdle's disease.";
Neuromuscul. Disord. 12:498-500(2002).
-!- 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:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- 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.
-!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
enzymatically active phosphorylase A.
-!- INTERACTION:
O43741:PRKAB2; NbExp=5; IntAct=EBI-357469, EBI-1053424;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-357469, EBI-741158;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11217-1; Sequence=Displayed;
Name=2;
IsoId=P11217-2; Sequence=VSP_043047;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
(unphosphorylated) to phosphorylase A.
{ECO:0000269|PubMed:1150650}.
-!- DISEASE: Glycogen storage disease 5 (GSD5) [MIM:232600]: A
metabolic disorder resulting in myopathy characterized by exercise
intolerance, cramps, muscle weakness and recurrent myoglobinuria.
{ECO:0000269|PubMed:10382911, ECO:0000269|PubMed:10382912,
ECO:0000269|PubMed:10417800, ECO:0000269|PubMed:10590419,
ECO:0000269|PubMed:10681080, ECO:0000269|PubMed:10714589,
ECO:0000269|PubMed:10899452, ECO:0000269|PubMed:11706962,
ECO:0000269|PubMed:12031624, ECO:0000269|PubMed:7603523,
ECO:0000269|PubMed:8316268, ECO:0000269|PubMed:8535454,
ECO:0000269|PubMed:9506549}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; M32598; AAA60231.1; -; Genomic_DNA.
EMBL; M32579; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32580; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32581; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32582; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32583; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32584; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32585; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32586; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32587; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32588; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32589; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32590; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32591; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32592; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32593; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32594; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32595; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32596; AAA60231.1; JOINED; Genomic_DNA.
EMBL; M32597; AAA60231.1; JOINED; Genomic_DNA.
EMBL; U94777; AAC52081.1; -; Genomic_DNA.
EMBL; U94774; AAC52081.1; JOINED; Genomic_DNA.
EMBL; U94775; AAC52081.1; JOINED; Genomic_DNA.
EMBL; U94776; AAC52081.1; JOINED; Genomic_DNA.
EMBL; AF066859; AAC17451.1; -; mRNA.
EMBL; AK056607; BAG51762.1; -; mRNA.
EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74284.1; -; Genomic_DNA.
EMBL; BC126392; AAI26393.1; -; mRNA.
EMBL; BC130514; AAI30515.1; -; mRNA.
EMBL; X03031; CAA26834.1; -; mRNA.
EMBL; M16013; AAA36216.1; -; mRNA.
CCDS; CCDS53659.1; -. [P11217-2]
CCDS; CCDS8079.1; -. [P11217-1]
PIR; A27335; A27335.
RefSeq; NP_001158188.1; NM_001164716.1. [P11217-2]
RefSeq; NP_005600.1; NM_005609.3. [P11217-1]
UniGene; Hs.154084; -.
PDB; 1Z8D; X-ray; 2.30 A; A=1-842.
PDBsum; 1Z8D; -.
ProteinModelPortal; P11217; -.
SMR; P11217; -.
BioGrid; 111795; 15.
IntAct; P11217; 25.
MINT; MINT-1134630; -.
STRING; 9606.ENSP00000164139; -.
BindingDB; P11217; -.
ChEMBL; CHEMBL3526; -.
DrugBank; DB04544; 1-Deoxy-1-Acetylamino-Beta-D-Gluco-2-Heptulopyranosonamide.
DrugBank; DB04013; 1-Deoxy-1-Methoxycarbamido-Beta-D-Gluco-2-Heptulopyranosonamide.
DrugBank; DB03657; 1-Deoxy-1-Methoxycarbamido-Beta-D-Glucopyranose.
DrugBank; DB02320; 1-N-Acetyl-Beta-D-Glucosamine.
DrugBank; DB02604; 2-Deoxy-Glucose-6-Phosphate.
DrugBank; DB04044; 4-{2-[(3-Nitrobenzoyl)Amino]Phenoxy}Phthalic Acid.
DrugBank; DB03383; 5-Chloro-1h-Indole-2-Carboxylic Acid [1-(4-Fluorobenzyl)-2-(4-Hydroxypiperidin-1yl)-2-Oxoethyl]Amide.
DrugBank; DB02720; Alpha-D-Glucopyranosyl-2-Carboxylic Acid Amide.
DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DrugBank; DB02843; Alpha-D-Glucose-1-Phosphate.
DrugBank; DB01823; Beta-D-Glucopyranose Spirohydantoin.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB03286; C-(1-Azido-Alpha-D-Glucopyranosyl) Formamide.
DrugBank; DB02719; C-(1-Hydrogyl-Beta-D-Glucopyranosyl) Formamide.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB02348; Fluoro-Phosphite Ion.
DrugBank; DB04195; Heptulose-2-Phosphate.
DrugBank; DB02519; Indirubin-5-Sulphonate.
DrugBank; DB04566; Inosinic Acid.
DrugBank; DB04083; N'-Pyridoxyl-Lysine-5'-Monophosphate.
DrugBank; DB03218; N-Acetyl-N'-Beta-D-Glucopyranosyl Urea.
DrugBank; DB04295; N-Benzoyl-N'-Beta-D-Glucopyranosyl Urea.
DrugBank; DB02471; Nojirimycine Tetrazole.
DrugBank; DB04522; Phosphonoserine.
DrugBank; DB00114; Pyridoxal Phosphate.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; P11217; -.
PhosphoSitePlus; P11217; -.
BioMuta; PYGM; -.
DMDM; 3041717; -.
EPD; P11217; -.
MaxQB; P11217; -.
PaxDb; P11217; -.
PeptideAtlas; P11217; -.
PRIDE; P11217; -.
DNASU; 5837; -.
Ensembl; ENST00000164139; ENSP00000164139; ENSG00000068976. [P11217-1]
Ensembl; ENST00000377432; ENSP00000366650; ENSG00000068976. [P11217-2]
GeneID; 5837; -.
KEGG; hsa:5837; -.
UCSC; uc001oax.5; human. [P11217-1]
CTD; 5837; -.
DisGeNET; 5837; -.
EuPathDB; HostDB:ENSG00000068976.13; -.
GeneCards; PYGM; -.
GeneReviews; PYGM; -.
HGNC; HGNC:9726; PYGM.
HPA; HPA056003; -.
MalaCards; PYGM; -.
MIM; 232600; phenotype.
MIM; 608455; gene.
neXtProt; NX_P11217; -.
OpenTargets; ENSG00000068976; -.
Orphanet; 368; Glycogen storage disease due to muscle glycogen phosphorylase deficiency.
PharmGKB; PA34069; -.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
GeneTree; ENSGT00390000016886; -.
HOGENOM; HOG000278444; -.
HOVERGEN; HBG006848; -.
InParanoid; P11217; -.
KO; K00688; -.
OMA; WLEMSIN; -.
OrthoDB; EOG091G03RB; -.
PhylomeDB; P11217; -.
TreeFam; TF300309; -.
BioCyc; MetaCyc:HS00949-MONOMER; -.
Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
EvolutionaryTrace; P11217; -.
GenomeRNAi; 5837; -.
PRO; PR:P11217; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000068976; -.
CleanEx; HS_PYGM; -.
Genevisible; P11217; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
CDD; cd04300; GT1_Glycogen_Phosphorylase; 1.
InterPro; IPR011833; Glycg_phsphrylas.
InterPro; IPR000811; Glyco_trans_35.
InterPro; IPR035090; Pyridoxal_P_attach_site.
PANTHER; PTHR11468; PTHR11468; 1.
Pfam; PF00343; Phosphorylase; 1.
PIRSF; PIRSF000460; Pprylas_GlgP; 1.
TIGRFAMs; TIGR02093; P_ylase; 1.
PROSITE; PS00102; PHOSPHORYLASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
Carbohydrate metabolism; Complete proteome; Disease mutation;
Glycogen metabolism; Glycogen storage disease; Glycosyltransferase;
Nucleotide-binding; Phosphoprotein; Polymorphism; Pyridoxal phosphate;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00489}.
CHAIN 2 842 Glycogen phosphorylase, muscle form.
/FTId=PRO_0000188529.
BINDING 76 76 AMP. {ECO:0000250}.
SITE 109 109 Involved in the association of subunits.
{ECO:0000250}.
SITE 143 143 Involved in the association of subunits.
{ECO:0000250}.
SITE 156 156 May be involved in allosteric control.
{ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P00489}.
MOD_RES 15 15 Phosphoserine; by PHK; in form
phosphorylase A.
{ECO:0000269|PubMed:1150650}.
MOD_RES 204 204 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 227 227 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 364 364 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9ET01}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WUB3}.
MOD_RES 473 473 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9WUB3}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ET01}.
MOD_RES 681 681 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000250|UniProtKB:P09812}.
VAR_SEQ 82 169 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043047.
VARIANT 116 116 L -> P (in GSD5; dbSNP:rs776680924).
{ECO:0000269|PubMed:10417800,
ECO:0000269|PubMed:11706962}.
/FTId=VAR_014002.
VARIANT 194 194 R -> W (in GSD5; dbSNP:rs376581557).
{ECO:0000269|PubMed:11706962}.
/FTId=VAR_014003.
VARIANT 205 205 G -> S (in GSD5; dbSNP:rs119103251).
{ECO:0000269|PubMed:10382911,
ECO:0000269|PubMed:10382912,
ECO:0000269|PubMed:11706962,
ECO:0000269|PubMed:7603523,
ECO:0000269|PubMed:8316268}.
/FTId=VAR_003431.
VARIANT 292 292 L -> P (in GSD5; rare mutation;
dbSNP:rs780375860).
{ECO:0000269|PubMed:7603523}.
/FTId=VAR_014004.
VARIANT 349 349 E -> K (in GSD5).
{ECO:0000269|PubMed:11706962}.
/FTId=VAR_014005.
VARIANT 397 397 L -> P (in GSD5).
{ECO:0000269|PubMed:7603523,
ECO:0000269|PubMed:8535454}.
/FTId=VAR_003432.
VARIANT 414 414 R -> G (in dbSNP:rs11231866).
/FTId=VAR_061198.
VARIANT 488 488 T -> N (in GSD5).
{ECO:0000269|PubMed:10714589,
ECO:0000269|PubMed:11706962}.
/FTId=VAR_014006.
VARIANT 543 543 K -> T (in GSD5; dbSNP:rs119103252).
{ECO:0000269|PubMed:7603523,
ECO:0000269|PubMed:8316268}.
/FTId=VAR_003433.
VARIANT 602 602 R -> W (in GSD5; dbSNP:rs750195683).
{ECO:0000269|PubMed:11706962}.
/FTId=VAR_014007.
VARIANT 655 655 E -> K (in GSD5; dbSNP:rs119103253).
{ECO:0000269|PubMed:7603523,
ECO:0000269|PubMed:8535454}.
/FTId=VAR_003434.
VARIANT 660 660 A -> D (in GSD5).
{ECO:0000269|PubMed:10899452,
ECO:0000269|PubMed:11706962}.
/FTId=VAR_014008.
VARIANT 666 666 Q -> E (in GSD5; dbSNP:rs119103256).
{ECO:0000269|PubMed:9506549}.
/FTId=VAR_014009.
VARIANT 685 685 N -> Y (in GSD5).
{ECO:0000269|PubMed:10382911,
ECO:0000269|PubMed:11706962}.
/FTId=VAR_014010.
VARIANT 686 686 G -> R (in GSD5; dbSNP:rs144081869).
{ECO:0000269|PubMed:9506549}.
/FTId=VAR_014011.
VARIANT 687 687 A -> P (in GSD5).
{ECO:0000269|PubMed:12031624}.
/FTId=VAR_014012.
VARIANT 704 704 A -> V (in GSD5).
{ECO:0000269|PubMed:11706962}.
/FTId=VAR_014013.
VARIANT 709 709 Missing (in GSD5; common in Japanese
patients). {ECO:0000269|PubMed:7603523}.
/FTId=VAR_014014.
VARIANT 798 798 W -> R (in GSD5; dbSNP:rs119103258).
{ECO:0000269|PubMed:10590419,
ECO:0000269|PubMed:10681080,
ECO:0000269|PubMed:11706962}.
/FTId=VAR_014015.
CONFLICT 791 791 L -> W (in Ref. 1; AAA60231).
{ECO:0000305}.
HELIX 7 10 {ECO:0000244|PDB:1Z8D}.
HELIX 11 13 {ECO:0000244|PDB:1Z8D}.
HELIX 25 38 {ECO:0000244|PDB:1Z8D}.
TURN 44 46 {ECO:0000244|PDB:1Z8D}.
HELIX 49 78 {ECO:0000244|PDB:1Z8D}.
STRAND 82 86 {ECO:0000244|PDB:1Z8D}.
HELIX 96 102 {ECO:0000244|PDB:1Z8D}.
HELIX 106 114 {ECO:0000244|PDB:1Z8D}.
TURN 115 117 {ECO:0000244|PDB:1Z8D}.
HELIX 120 126 {ECO:0000244|PDB:1Z8D}.
HELIX 136 150 {ECO:0000244|PDB:1Z8D}.
STRAND 155 160 {ECO:0000244|PDB:1Z8D}.
STRAND 168 172 {ECO:0000244|PDB:1Z8D}.
STRAND 175 179 {ECO:0000244|PDB:1Z8D}.
TURN 183 186 {ECO:0000244|PDB:1Z8D}.
HELIX 195 197 {ECO:0000244|PDB:1Z8D}.
STRAND 199 204 {ECO:0000244|PDB:1Z8D}.
STRAND 206 210 {ECO:0000244|PDB:1Z8D}.
STRAND 213 218 {ECO:0000244|PDB:1Z8D}.
STRAND 220 232 {ECO:0000244|PDB:1Z8D}.
STRAND 234 236 {ECO:0000244|PDB:1Z8D}.
STRAND 239 248 {ECO:0000244|PDB:1Z8D}.
HELIX 263 270 {ECO:0000244|PDB:1Z8D}.
HELIX 271 277 {ECO:0000244|PDB:1Z8D}.
HELIX 291 313 {ECO:0000244|PDB:1Z8D}.
HELIX 330 333 {ECO:0000244|PDB:1Z8D}.
STRAND 334 341 {ECO:0000244|PDB:1Z8D}.
TURN 342 345 {ECO:0000244|PDB:1Z8D}.
HELIX 346 356 {ECO:0000244|PDB:1Z8D}.
HELIX 362 372 {ECO:0000244|PDB:1Z8D}.
STRAND 373 376 {ECO:0000244|PDB:1Z8D}.
HELIX 382 384 {ECO:0000244|PDB:1Z8D}.
STRAND 387 389 {ECO:0000244|PDB:1Z8D}.
HELIX 390 396 {ECO:0000244|PDB:1Z8D}.
HELIX 398 418 {ECO:0000244|PDB:1Z8D}.
HELIX 423 429 {ECO:0000244|PDB:1Z8D}.
STRAND 431 433 {ECO:0000244|PDB:1Z8D}.
STRAND 435 437 {ECO:0000244|PDB:1Z8D}.
STRAND 439 441 {ECO:0000244|PDB:1Z8D}.
HELIX 442 448 {ECO:0000244|PDB:1Z8D}.
STRAND 451 457 {ECO:0000244|PDB:1Z8D}.
HELIX 458 466 {ECO:0000244|PDB:1Z8D}.
TURN 467 469 {ECO:0000244|PDB:1Z8D}.
HELIX 470 475 {ECO:0000244|PDB:1Z8D}.
HELIX 477 479 {ECO:0000244|PDB:1Z8D}.
STRAND 480 482 {ECO:0000244|PDB:1Z8D}.
HELIX 490 495 {ECO:0000244|PDB:1Z8D}.
HELIX 498 508 {ECO:0000244|PDB:1Z8D}.
HELIX 511 514 {ECO:0000244|PDB:1Z8D}.
HELIX 516 525 {ECO:0000244|PDB:1Z8D}.
HELIX 529 553 {ECO:0000244|PDB:1Z8D}.
STRAND 562 569 {ECO:0000244|PDB:1Z8D}.
TURN 573 576 {ECO:0000244|PDB:1Z8D}.
HELIX 577 593 {ECO:0000244|PDB:1Z8D}.
STRAND 602 607 {ECO:0000244|PDB:1Z8D}.
HELIX 615 631 {ECO:0000244|PDB:1Z8D}.
TURN 635 637 {ECO:0000244|PDB:1Z8D}.
HELIX 638 640 {ECO:0000244|PDB:1Z8D}.
STRAND 641 646 {ECO:0000244|PDB:1Z8D}.
HELIX 651 657 {ECO:0000244|PDB:1Z8D}.
HELIX 658 660 {ECO:0000244|PDB:1Z8D}.
STRAND 662 666 {ECO:0000244|PDB:1Z8D}.
TURN 670 672 {ECO:0000244|PDB:1Z8D}.
HELIX 678 684 {ECO:0000244|PDB:1Z8D}.
STRAND 688 691 {ECO:0000244|PDB:1Z8D}.
HELIX 697 704 {ECO:0000244|PDB:1Z8D}.
HELIX 706 708 {ECO:0000244|PDB:1Z8D}.
STRAND 709 711 {ECO:0000244|PDB:1Z8D}.
HELIX 716 725 {ECO:0000244|PDB:1Z8D}.
HELIX 730 733 {ECO:0000244|PDB:1Z8D}.
HELIX 737 748 {ECO:0000244|PDB:1Z8D}.
TURN 749 751 {ECO:0000244|PDB:1Z8D}.
TURN 756 759 {ECO:0000244|PDB:1Z8D}.
HELIX 760 768 {ECO:0000244|PDB:1Z8D}.
HELIX 774 792 {ECO:0000244|PDB:1Z8D}.
HELIX 795 806 {ECO:0000244|PDB:1Z8D}.
HELIX 810 812 {ECO:0000244|PDB:1Z8D}.
HELIX 814 824 {ECO:0000244|PDB:1Z8D}.
SEQUENCE 842 AA; 97092 MW; EBDB7D80D740B68F CRC64;
MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGHVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERM
DWDKAWDVTV RTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVLCNPGL AEVIAERIGE DFISDLDQLR KLLSFVDDEA FIRDVAKVKQ
ENKLKFAAYL EREYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKREPNKFFV
PRTVMIGGKA APGYHMAKMI IRLVTAIGDV VNHDPAVGDR LRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD
KLDQRGYNAQ EYYDRIPELR QVIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYED
YIKCQEKVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE
AI


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