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Glycogen phosphorylase, liver form (EC 2.4.1.1)

 PYGL_HUMAN              Reviewed;         847 AA.
P06737; A6NDQ4; B4DUB7; F5H816; O60567; O60752; O60913; Q501V9;
Q641R5; Q96G82;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 207.
RecName: Full=Glycogen phosphorylase, liver form;
EC=2.4.1.1;
Name=PYGL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-425.
TISSUE=Liver;
PubMed=2877458; DOI=10.1073/pnas.83.21.8132;
Newgard C.B., Nakano K., Hwang P.K., Fletterick R.J.;
"Sequence analysis of the cDNA encoding human liver glycogen
phosphorylase reveals tissue-specific codon usage.";
Proc. Natl. Acad. Sci. U.S.A. 83:8132-8136(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Carty M.D., Clancy Y.C., Soeller W.C.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9536091; DOI=10.1093/hmg/7.5.865;
Chang S., Rosenberg M.J., Morton H., Francomano C.A., Biesecker L.G.;
"Identification of a mutation in liver glycogen phosphorylase in
glycogen storage disease type VI.";
Hum. Mol. Genet. 7:865-870(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GSD6 SER-339 AND
LYS-377, AND VARIANT ILE-222.
TISSUE=Blood;
PubMed=9529348; DOI=10.1086/301790;
Burwinkel B., Bakker H.D., Herschkovitz E., Moses S.W., Shin Y.S.,
Kilimann M.W.;
"Mutations in the liver glycogen phosphorylase gene 'PYGL' underlying
glycogenosis type VI.";
Am. J. Hum. Genet. 62:785-791(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
SER-845.
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, Skin, and Uterus;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 482-847 (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=3509980;
Gorin F.A., Mullinax R.L., Ignacio P.C., Neve R.L., Kurnit D.M.;
"McArdle's & Hers' diseases: glycogen phosphorylase transcriptional
expression in human tissues.";
J. Neurogenet. 4:293-308(1987).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=10980448; DOI=10.1016/S1074-5521(00)00004-1;
Rath V.L., Ammirati M., Danley D.E., Ekstrom J.L., Gibbs E.M.,
Hynes T.R., Mathiowetz A.M., McPherson R.K., Olson T.V.,
Treadway J.L., Hoover D.J.;
"Human liver glycogen phosphorylase inhibitors bind at a new
allosteric site.";
Chem. Biol. 7:677-682(2000).
[15]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND PHOSPHORYLATION AT SER-15.
PubMed=10949035; DOI=10.1016/S1097-2765(05)00006-7;
Rath V.L., Ammirati M., LeMotte P.K., Fennell K.F., Mansour M.N.,
Danley D.E., Hynes T.R., Schulte G.K., Wasilko D.J., Pandit J.;
"Activation of human liver glycogen phosphorylase by alteration of the
secondary structure and packing of the catalytic core.";
Mol. Cell 6:139-148(2000).
[16]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=12204691; DOI=10.1016/S1074-5521(02)00186-2;
Ekstrom J.L., Pauly T.A., Carty M.D., Soeller W.C., Culp J.,
Danley D.E., Hoover D.J., Treadway J.L., Gibbs E.M., Fletterick R.J.,
Day Y.S., Myszka D.G., Rath V.L.;
"Structure-activity analysis of the purine binding site of human liver
glycogen phosphorylase.";
Chem. Biol. 9:915-924(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. Interacts with PPP1R3B (By
similarity). {ECO:0000250}.
-!- INTERACTION:
P11216:PYGB; NbExp=8; IntAct=EBI-2511865, EBI-1047231;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P06737-1; Sequence=Displayed;
Name=2;
IsoId=P06737-2; Sequence=VSP_045339;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
(unphosphorylated) to phosphorylase A.
{ECO:0000269|PubMed:10949035}.
-!- DISEASE: Glycogen storage disease 6 (GSD6) [MIM:232700]: A
metabolic disorder characterized by mild to moderate hypoglycemia,
mild ketosis, growth retardation, and prominent hepatomegaly.
Heart and skeletal muscle are not affected.
{ECO:0000269|PubMed:9529348}. 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; M14636; AAA52577.1; -; mRNA.
EMBL; AF066858; AAC17450.1; -; mRNA.
EMBL; AF046798; AAC18079.1; -; Genomic_DNA.
EMBL; AF046787; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046788; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046789; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046790; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046791; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046792; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046793; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046794; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046795; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046796; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046797; AAC18079.1; JOINED; Genomic_DNA.
EMBL; AF046785; AAC23504.1; -; mRNA.
EMBL; Y15233; CAA75517.1; -; mRNA.
EMBL; AK300580; BAG62279.1; -; mRNA.
EMBL; AL358334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW65685.1; -; Genomic_DNA.
EMBL; BC009895; AAH09895.3; -; mRNA.
EMBL; BC082229; AAH82229.2; -; mRNA.
EMBL; BC095850; AAH95850.2; -; mRNA.
EMBL; BC110791; AAI10792.2; -; mRNA.
EMBL; M36807; AAA35906.1; -; mRNA.
CCDS; CCDS32080.1; -. [P06737-1]
CCDS; CCDS53894.1; -. [P06737-2]
PIR; A25518; A25518.
RefSeq; NP_001157412.1; NM_001163940.1. [P06737-2]
RefSeq; NP_002854.3; NM_002863.4. [P06737-1]
UniGene; Hs.282417; -.
PDB; 1EM6; X-ray; 2.20 A; A/B=1-847.
PDB; 1EXV; X-ray; 2.40 A; A/B=1-847.
PDB; 1FA9; X-ray; 2.40 A; A=2-847.
PDB; 1FC0; X-ray; 2.40 A; A/B=2-847.
PDB; 1L5Q; X-ray; 2.25 A; A/B=1-847.
PDB; 1L5R; X-ray; 2.10 A; A/B=1-847.
PDB; 1L5S; X-ray; 2.10 A; A/B=1-847.
PDB; 1L7X; X-ray; 2.30 A; A/B=1-847.
PDB; 1XOI; X-ray; 2.10 A; A/B=2-847.
PDB; 2ATI; X-ray; 1.90 A; A/B=2-847.
PDB; 2QLL; X-ray; 2.56 A; A=1-847.
PDB; 2ZB2; X-ray; 2.45 A; A/B=1-847.
PDB; 3CEH; X-ray; 2.80 A; A/B=24-832.
PDB; 3CEJ; X-ray; 3.30 A; A/B=24-832.
PDB; 3CEM; X-ray; 2.47 A; A/B=24-832.
PDB; 3DD1; X-ray; 2.57 A; A/B=2-847.
PDB; 3DDS; X-ray; 1.80 A; A/B=2-847.
PDB; 3DDW; X-ray; 1.90 A; A/B=2-847.
PDBsum; 1EM6; -.
PDBsum; 1EXV; -.
PDBsum; 1FA9; -.
PDBsum; 1FC0; -.
PDBsum; 1L5Q; -.
PDBsum; 1L5R; -.
PDBsum; 1L5S; -.
PDBsum; 1L7X; -.
PDBsum; 1XOI; -.
PDBsum; 2ATI; -.
PDBsum; 2QLL; -.
PDBsum; 2ZB2; -.
PDBsum; 3CEH; -.
PDBsum; 3CEJ; -.
PDBsum; 3CEM; -.
PDBsum; 3DD1; -.
PDBsum; 3DDS; -.
PDBsum; 3DDW; -.
ProteinModelPortal; P06737; -.
SMR; P06737; -.
BioGrid; 111794; 48.
IntAct; P06737; 14.
MINT; MINT-1208599; -.
STRING; 9606.ENSP00000216392; -.
BindingDB; P06737; -.
ChEMBL; CHEMBL2568; -.
DrugBank; DB02320; 1-N-Acetyl-Beta-D-Glucosamine.
DrugBank; DB03288; 5-Chloro-1h-Indole-2-Carboxylic Acid{[Cyclopentyl-(2-Hydroxy-Ethyl)-Carbamoyl]-Methyl}-Amide.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB02089; CP-526423.
DrugBank; DB07968; N-(2-CHLORO-4-FLUOROBENZOYL)-N'-(5-HYDROXY-2-METHOXYPHENYL)UREA.
DrugBank; DB04522; Phosphonoserine.
DrugBank; DB05044; PSN357.
DrugBank; DB00114; Pyridoxal Phosphate.
DrugBank; DB08844; Uric Acid.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; P06737; -.
PhosphoSitePlus; P06737; -.
BioMuta; PYGL; -.
DMDM; 6648082; -.
EPD; P06737; -.
MaxQB; P06737; -.
PaxDb; P06737; -.
PeptideAtlas; P06737; -.
PRIDE; P06737; -.
DNASU; 5836; -.
Ensembl; ENST00000216392; ENSP00000216392; ENSG00000100504. [P06737-1]
Ensembl; ENST00000544180; ENSP00000443787; ENSG00000100504. [P06737-2]
GeneID; 5836; -.
KEGG; hsa:5836; -.
UCSC; uc001wyu.4; human. [P06737-1]
CTD; 5836; -.
DisGeNET; 5836; -.
EuPathDB; HostDB:ENSG00000100504.16; -.
GeneCards; PYGL; -.
HGNC; HGNC:9725; PYGL.
HPA; HPA000962; -.
HPA; HPA004119; -.
MalaCards; PYGL; -.
MIM; 232700; phenotype.
MIM; 613741; gene.
neXtProt; NX_P06737; -.
OpenTargets; ENSG00000100504; -.
Orphanet; 369; Glycogen storage disease due to liver glycogen phosphorylase deficiency.
PharmGKB; PA34068; -.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
GeneTree; ENSGT00390000016886; -.
HOVERGEN; HBG006848; -.
InParanoid; P06737; -.
KO; K00688; -.
OMA; ARDIWNM; -.
OrthoDB; EOG091G03RB; -.
PhylomeDB; P06737; -.
TreeFam; TF300309; -.
BioCyc; MetaCyc:HS02099-MONOMER; -.
BRENDA; 2.4.1.1; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
SIGNOR; P06737; -.
ChiTaRS; PYGL; human.
EvolutionaryTrace; P06737; -.
GenomeRNAi; 5836; -.
PRO; PR:P06737; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100504; -.
CleanEx; HS_PYGL; -.
ExpressionAtlas; P06737; baseline and differential.
Genevisible; P06737; 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:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0016208; F:AMP binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0032052; F:bile acid binding; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0005536; F:glucose binding; NAS:UniProtKB.
GO; GO:0008184; F:glycogen phosphorylase activity; IDA:MGI.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
GO; GO:0002060; F:purine nucleobase binding; IDA:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0019842; F:vitamin binding; IDA:UniProtKB.
GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
GO; GO:0005977; P:glycogen metabolic process; IMP:UniProtKB.
GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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:0000244|PubMed:19413330}.
CHAIN 2 847 Glycogen phosphorylase, liver form.
/FTId=PRO_0000188524.
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-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 15 15 Phosphoserine; by PHK; in form
phosphorylase A.
{ECO:0000269|PubMed:10949035}.
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 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ET01}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000250|UniProtKB:P09811}.
MOD_RES 639 639 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 681 681 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VAR_SEQ 82 115 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045339.
VARIANT 222 222 V -> I (in dbSNP:rs946616).
{ECO:0000269|PubMed:9529348}.
/FTId=VAR_007907.
VARIANT 231 231 V -> E (in dbSNP:rs1042195).
/FTId=VAR_013095.
VARIANT 339 339 N -> S (in GSD6; dbSNP:rs113993976).
{ECO:0000269|PubMed:9529348}.
/FTId=VAR_007908.
VARIANT 377 377 N -> K (in GSD6; dbSNP:rs113993977).
{ECO:0000269|PubMed:9529348}.
/FTId=VAR_007909.
VARIANT 425 425 R -> P (in dbSNP:rs2228499).
{ECO:0000269|PubMed:2877458}.
/FTId=VAR_034425.
VARIANT 698 698 V -> G (in dbSNP:rs35831273).
/FTId=VAR_034426.
VARIANT 715 715 R -> S (in dbSNP:rs1042210).
/FTId=VAR_013096.
VARIANT 806 806 I -> L (in dbSNP:rs34313873).
/FTId=VAR_034427.
VARIANT 845 845 N -> S (in dbSNP:rs78558135).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_069054.
CONFLICT 2 3 AK -> GE (in Ref. 1; AAA52577 and 3;
AAC18079). {ECO:0000305}.
CONFLICT 83 83 V -> E (in Ref. 1; AAA52577).
{ECO:0000305}.
CONFLICT 323 323 A -> Q (in Ref. 1; AAA52577).
{ECO:0000305}.
CONFLICT 344 345 AL -> RI (in Ref. 1; AAA52577).
{ECO:0000305}.
CONFLICT 369 369 T -> N (in Ref. 1; AAA52577 and 3;
AAC18079). {ECO:0000305}.
CONFLICT 570 570 R -> S (in Ref. 2; AAC17450).
{ECO:0000305}.
CONFLICT 683 683 Missing (in Ref. 8; AAH09895).
{ECO:0000305}.
CONFLICT 715 715 R -> G (in Ref. 5; BAG62279).
{ECO:0000305}.
TURN 8 10 {ECO:0000244|PDB:1FA9}.
HELIX 11 13 {ECO:0000244|PDB:1FA9}.
STRAND 14 17 {ECO:0000244|PDB:1FA9}.
HELIX 19 38 {ECO:0000244|PDB:3DDS}.
HELIX 44 46 {ECO:0000244|PDB:3DDS}.
HELIX 49 62 {ECO:0000244|PDB:3DDS}.
HELIX 65 78 {ECO:0000244|PDB:3DDS}.
STRAND 82 86 {ECO:0000244|PDB:3DDS}.
STRAND 90 93 {ECO:0000244|PDB:3DDS}.
HELIX 96 102 {ECO:0000244|PDB:3DDS}.
HELIX 106 115 {ECO:0000244|PDB:3DDS}.
HELIX 120 125 {ECO:0000244|PDB:3DDS}.
STRAND 130 135 {ECO:0000244|PDB:3DDS}.
HELIX 136 150 {ECO:0000244|PDB:3DDS}.
STRAND 155 160 {ECO:0000244|PDB:3DDS}.
STRAND 168 172 {ECO:0000244|PDB:3DDS}.
STRAND 175 179 {ECO:0000244|PDB:3DDS}.
TURN 183 186 {ECO:0000244|PDB:3DDS}.
HELIX 195 197 {ECO:0000244|PDB:3DDS}.
STRAND 199 204 {ECO:0000244|PDB:3DDS}.
STRAND 206 210 {ECO:0000244|PDB:3DDS}.
STRAND 213 218 {ECO:0000244|PDB:3DDS}.
STRAND 220 232 {ECO:0000244|PDB:3DDS}.
STRAND 234 237 {ECO:0000244|PDB:1L5S}.
STRAND 239 248 {ECO:0000244|PDB:3DDS}.
HELIX 255 260 {ECO:0000244|PDB:1FA9}.
HELIX 263 268 {ECO:0000244|PDB:3DDS}.
HELIX 270 274 {ECO:0000244|PDB:3DDS}.
HELIX 275 277 {ECO:0000244|PDB:3DDS}.
HELIX 291 314 {ECO:0000244|PDB:3DDS}.
STRAND 315 317 {ECO:0000244|PDB:1FA9}.
STRAND 322 325 {ECO:0000244|PDB:3DDW}.
HELIX 327 329 {ECO:0000244|PDB:1L5R}.
HELIX 330 333 {ECO:0000244|PDB:3DDS}.
STRAND 334 341 {ECO:0000244|PDB:3DDS}.
TURN 342 345 {ECO:0000244|PDB:3DDS}.
HELIX 346 356 {ECO:0000244|PDB:3DDS}.
HELIX 362 372 {ECO:0000244|PDB:3DDS}.
STRAND 373 376 {ECO:0000244|PDB:3DDS}.
HELIX 382 384 {ECO:0000244|PDB:3DDS}.
STRAND 387 389 {ECO:0000244|PDB:3DDS}.
HELIX 390 396 {ECO:0000244|PDB:3DDS}.
HELIX 398 418 {ECO:0000244|PDB:3DDS}.
STRAND 419 421 {ECO:0000244|PDB:3CEJ}.
HELIX 423 429 {ECO:0000244|PDB:3DDS}.
STRAND 431 433 {ECO:0000244|PDB:3DDS}.
STRAND 435 437 {ECO:0000244|PDB:3DDS}.
STRAND 439 441 {ECO:0000244|PDB:3DDS}.
HELIX 442 448 {ECO:0000244|PDB:3DDS}.
STRAND 451 457 {ECO:0000244|PDB:3DDS}.
HELIX 458 466 {ECO:0000244|PDB:3DDS}.
TURN 467 469 {ECO:0000244|PDB:3DDS}.
HELIX 470 475 {ECO:0000244|PDB:3DDS}.
HELIX 477 479 {ECO:0000244|PDB:3DDS}.
STRAND 480 482 {ECO:0000244|PDB:3DDS}.
HELIX 490 495 {ECO:0000244|PDB:3DDS}.
HELIX 498 508 {ECO:0000244|PDB:3DDS}.
HELIX 511 513 {ECO:0000244|PDB:3DDS}.
HELIX 516 525 {ECO:0000244|PDB:3DDS}.
HELIX 529 553 {ECO:0000244|PDB:3DDS}.
STRAND 554 556 {ECO:0000244|PDB:1L5R}.
STRAND 562 569 {ECO:0000244|PDB:3DDS}.
TURN 573 576 {ECO:0000244|PDB:3DDS}.
HELIX 577 593 {ECO:0000244|PDB:3DDS}.
STRAND 595 597 {ECO:0000244|PDB:3CEJ}.
STRAND 602 607 {ECO:0000244|PDB:3DDS}.
HELIX 615 633 {ECO:0000244|PDB:3DDS}.
TURN 635 637 {ECO:0000244|PDB:3DDS}.
HELIX 638 640 {ECO:0000244|PDB:3DDS}.
STRAND 641 646 {ECO:0000244|PDB:3DDS}.
HELIX 651 657 {ECO:0000244|PDB:3DDS}.
HELIX 658 660 {ECO:0000244|PDB:3DDS}.
STRAND 662 666 {ECO:0000244|PDB:3DDS}.
TURN 670 672 {ECO:0000244|PDB:2ATI}.
HELIX 678 684 {ECO:0000244|PDB:3DDS}.
STRAND 688 691 {ECO:0000244|PDB:3DDS}.
HELIX 697 704 {ECO:0000244|PDB:3DDS}.
HELIX 706 708 {ECO:0000244|PDB:3DDS}.
STRAND 709 711 {ECO:0000244|PDB:3DDS}.
HELIX 716 725 {ECO:0000244|PDB:3DDS}.
HELIX 729 735 {ECO:0000244|PDB:3DDS}.
HELIX 737 748 {ECO:0000244|PDB:3DDS}.
TURN 749 751 {ECO:0000244|PDB:3DDS}.
TURN 756 759 {ECO:0000244|PDB:3DDS}.
HELIX 760 768 {ECO:0000244|PDB:3DDS}.
HELIX 774 792 {ECO:0000244|PDB:3DDS}.
HELIX 795 806 {ECO:0000244|PDB:3DDS}.
HELIX 810 812 {ECO:0000244|PDB:3DDS}.
HELIX 814 824 {ECO:0000244|PDB:3DDS}.
SEQUENCE 847 AA; 97149 MW; 74017E8125FB5735 CRC64;
MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR DYYFALAHTV
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDI
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA
DDWLRYGNPW EKSRPEFMLP VHFYGKVEHT NTGTKWIDTQ VVLALPYDTP VPGYMNNTVN
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKASKFGST RGAGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL
PWSKAWELTQ KTFAYTNHTV LPEALERWPV DLVEKLLPRH LEIIYEINQK HLDRIVALFP
KDVDRLRRMS LIEEEGSKRI NMAHLCIVGS HAVNGVAKIH SDIVKTKVFK DFSELEPDKF
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT KLHSFLGDDV FLRELAKVKQ
ENKLKFSQFL ETEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVITMYNR IKKDPKKLFV
PRTVIIGGKA APGYHMAKMI IKLITSVADV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRIDDVA
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPKQPDLFK DIINMLFYHD RFKVFADYEA
YVKCQDKVSQ LYMNPKAWNT MVLKNIAASG KFSSDRTIKE YAQNIWNVEP SDLKISLSNE
SNKVNGN


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