PYGL_HUMAN
ID PYGL_HUMAN Reviewed; 847 AA.
AC P06737; A6NDQ4; B4DUB7; F5H816; O60567; O60752; O60913; Q501V9; Q641R5;
AC Q96G82;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=Glycogen phosphorylase, liver form {ECO:0000305|PubMed:2877458};
DE EC=2.4.1.1 {ECO:0000269|PubMed:22225877};
GN Name=PYGL {ECO:0000312|HGNC:HGNC:9725};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-425.
RC TISSUE=Liver;
RX PubMed=2877458; DOI=10.1073/pnas.83.21.8132;
RA Newgard C.B., Nakano K., Hwang P.K., Fletterick R.J.;
RT "Sequence analysis of the cDNA encoding human liver glycogen phosphorylase
RT reveals tissue-specific codon usage.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8132-8136(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Carty M.D., Clancy Y.C., Soeller W.C.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9536091; DOI=10.1093/hmg/7.5.865;
RA Chang S., Rosenberg M.J., Morton H., Francomano C.A., Biesecker L.G.;
RT "Identification of a mutation in liver glycogen phosphorylase in glycogen
RT storage disease type VI.";
RL Hum. Mol. Genet. 7:865-870(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GSD6 SER-339 AND LYS-377,
RP AND VARIANT ILE-222.
RC TISSUE=Blood;
RX PubMed=9529348; DOI=10.1086/301790;
RA Burwinkel B., Bakker H.D., Herschkovitz E., Moses S.W., Shin Y.S.,
RA Kilimann M.W.;
RT "Mutations in the liver glycogen phosphorylase gene 'PYGL' underlying
RT glycogenosis type VI.";
RL Am. J. Hum. Genet. 62:785-791(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-845.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 482-847 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=3509980;
RA Gorin F.A., Mullinax R.L., Ignacio P.C., Neve R.L., Kurnit D.M.;
RT "McArdle's & Hers' diseases: glycogen phosphorylase transcriptional
RT expression in human tissues.";
RL J. Neurogenet. 4:293-308(1987).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
RP PPP1R3B, SUBCELLULAR LOCATION, ACETYLATION AT LYS-470 AND LYS-796,
RP PHOSPHORYLATION AT SER-15, AND MUTAGENESIS OF LYS-470 AND LYS-796.
RX PubMed=22225877; DOI=10.1016/j.cmet.2011.12.005;
RA Zhang T., Wang S., Lin Y., Xu W., Ye D., Xiong Y., Zhao S., Guan K.L.;
RT "Acetylation negatively regulates glycogen phosphorylase by recruiting
RT protein phosphatase 1.";
RL Cell Metab. 15:75-87(2012).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15] {ECO:0007744|PDB:1EM6, ECO:0007744|PDB:1EXV}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), COFACTOR, AND SUBUNIT.
RX PubMed=10980448; DOI=10.1016/s1074-5521(00)00004-1;
RA Rath V.L., Ammirati M., Danley D.E., Ekstrom J.L., Gibbs E.M., Hynes T.R.,
RA Mathiowetz A.M., McPherson R.K., Olson T.V., Treadway J.L., Hoover D.J.;
RT "Human liver glycogen phosphorylase inhibitors bind at a new allosteric
RT site.";
RL Chem. Biol. 7:677-682(2000).
RN [16] {ECO:0007744|PDB:1FA9, ECO:0007744|PDB:1FC0}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH AMP, SUBUNIT,
RP PHOSPHORYLATION AT SER-15, AND COFACTOR.
RX PubMed=10949035; DOI=10.1016/s1097-2765(05)00006-7;
RA Rath V.L., Ammirati M., LeMotte P.K., Fennell K.F., Mansour M.N.,
RA Danley D.E., Hynes T.R., Schulte G.K., Wasilko D.J., Pandit J.;
RT "Activation of human liver glycogen phosphorylase by alteration of the
RT secondary structure and packing of the catalytic core.";
RL Mol. Cell 6:139-148(2000).
RN [17] {ECO:0007744|PDB:1L5Q, ECO:0007744|PDB:1L5R, ECO:0007744|PDB:1L5S, ECO:0007744|PDB:1L7X}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND COFACTOR.
RX PubMed=12204691; DOI=10.1016/s1074-5521(02)00186-2;
RA Ekstrom J.L., Pauly T.A., Carty M.D., Soeller W.C., Culp J., Danley D.E.,
RA Hoover D.J., Treadway J.L., Gibbs E.M., Fletterick R.J., Day Y.S.,
RA Myszka D.G., Rath V.L.;
RT "Structure-activity analysis of the purine binding site of human liver
RT glycogen phosphorylase.";
RL Chem. Biol. 9:915-924(2002).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000269|PubMed:22225877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000269|PubMed:22225877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000305|PubMed:22225877};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:10980448,
CC ECO:0000269|PubMed:12204691, ECO:0007744|PDB:1EM6,
CC ECO:0007744|PDB:1EXV, ECO:0007744|PDB:1FA9, ECO:0007744|PDB:1FC0,
CC ECO:0007744|PDB:1L5Q, ECO:0007744|PDB:1L5R, ECO:0007744|PDB:1L5S,
CC ECO:0007744|PDB:1L7X};
CC -!- ACTIVITY REGULATION: Allosterically regulated through the non-covalent
CC binding of metabolites, being activated by AMP and inhibited by ATP,
CC ADP, and glucose-6-phosphate. The activity is also controlled by post-
CC translational modifications including phosphorylation and acetylation.
CC {ECO:0000269|PubMed:22225877}.
CC -!- SUBUNIT: Homodimer; enzymatically active (PubMed:10980448,
CC PubMed:10949035). Interacts with PPP1R3B; recruits the phosphatase PP1
CC which dephosphorylates and inactivates PYGL/glycogen phosphorylase
CC (PubMed:22225877). {ECO:0000269|PubMed:10949035,
CC ECO:0000269|PubMed:10980448, ECO:0000269|PubMed:22225877}.
CC -!- INTERACTION:
CC P06737; P11216: PYGB; NbExp=9; IntAct=EBI-2511865, EBI-1047231;
CC P06737; P11217: PYGM; NbExp=3; IntAct=EBI-2511865, EBI-357469;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:22225877}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P06737-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06737-2; Sequence=VSP_045339;
CC -!- PTM: Acetylation, which is up-regulated by glucose and insulin and
CC down-regulated by glucagon, inhibits the glycogen phosphorylase
CC activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1
CC and Ser-15 dephosphorylation. {ECO:0000269|PubMed:22225877}.
CC -!- PTM: Phosphorylation at Ser-15 converts inactive phosphorylase b into
CC active phosphorylase a (PubMed:10949035). Dephosphorylation of Ser-15
CC by phosphatase PP1 inactivates the enzyme (PubMed:22225877).
CC {ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:22225877}.
CC -!- DISEASE: Glycogen storage disease 6 (GSD6) [MIM:232700]: A metabolic
CC disorder characterized by mild to moderate hypoglycemia, mild ketosis,
CC growth retardation, and prominent hepatomegaly. Heart and skeletal
CC muscle are not affected. {ECO:0000269|PubMed:9529348}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14636; AAA52577.1; -; mRNA.
DR EMBL; AF066858; AAC17450.1; -; mRNA.
DR EMBL; AF046798; AAC18079.1; -; Genomic_DNA.
DR EMBL; AF046787; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046788; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046789; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046790; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046791; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046792; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046793; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046794; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046795; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046796; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046797; AAC18079.1; JOINED; Genomic_DNA.
DR EMBL; AF046785; AAC23504.1; -; mRNA.
DR EMBL; Y15233; CAA75517.1; -; mRNA.
DR EMBL; AK300580; BAG62279.1; -; mRNA.
DR EMBL; AL358334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65685.1; -; Genomic_DNA.
DR EMBL; BC009895; AAH09895.3; -; mRNA.
DR EMBL; BC082229; AAH82229.2; -; mRNA.
DR EMBL; BC095850; AAH95850.2; -; mRNA.
DR EMBL; BC110791; AAI10792.2; -; mRNA.
DR EMBL; M36807; AAA35906.1; -; mRNA.
DR CCDS; CCDS32080.1; -. [P06737-1]
DR CCDS; CCDS53894.1; -. [P06737-2]
DR PIR; A25518; A25518.
DR RefSeq; NP_001157412.1; NM_001163940.1. [P06737-2]
DR RefSeq; NP_002854.3; NM_002863.4. [P06737-1]
DR PDB; 1EM6; X-ray; 2.20 A; A/B=1-847.
DR PDB; 1EXV; X-ray; 2.40 A; A/B=1-847.
DR PDB; 1FA9; X-ray; 2.40 A; A=2-847.
DR PDB; 1FC0; X-ray; 2.40 A; A/B=2-847.
DR PDB; 1L5Q; X-ray; 2.25 A; A/B=1-847.
DR PDB; 1L5R; X-ray; 2.10 A; A/B=1-847.
DR PDB; 1L5S; X-ray; 2.10 A; A/B=1-847.
DR PDB; 1L7X; X-ray; 2.30 A; A/B=1-847.
DR PDB; 1XOI; X-ray; 2.10 A; A/B=2-847.
DR PDB; 2ATI; X-ray; 1.90 A; A/B=2-847.
DR PDB; 2QLL; X-ray; 2.56 A; A=1-847.
DR PDB; 2ZB2; X-ray; 2.45 A; A/B=1-847.
DR PDB; 3CEH; X-ray; 2.80 A; A/B=24-832.
DR PDB; 3CEJ; X-ray; 3.30 A; A/B=24-832.
DR PDB; 3CEM; X-ray; 2.47 A; A/B=24-832.
DR PDB; 3DD1; X-ray; 2.57 A; A/B=2-847.
DR PDB; 3DDS; X-ray; 1.80 A; A/B=2-847.
DR PDB; 3DDW; X-ray; 1.90 A; A/B=2-847.
DR PDBsum; 1EM6; -.
DR PDBsum; 1EXV; -.
DR PDBsum; 1FA9; -.
DR PDBsum; 1FC0; -.
DR PDBsum; 1L5Q; -.
DR PDBsum; 1L5R; -.
DR PDBsum; 1L5S; -.
DR PDBsum; 1L7X; -.
DR PDBsum; 1XOI; -.
DR PDBsum; 2ATI; -.
DR PDBsum; 2QLL; -.
DR PDBsum; 2ZB2; -.
DR PDBsum; 3CEH; -.
DR PDBsum; 3CEJ; -.
DR PDBsum; 3CEM; -.
DR PDBsum; 3DD1; -.
DR PDBsum; 3DDS; -.
DR PDBsum; 3DDW; -.
DR AlphaFoldDB; P06737; -.
DR SMR; P06737; -.
DR BioGRID; 111794; 75.
DR IntAct; P06737; 29.
DR MINT; P06737; -.
DR STRING; 9606.ENSP00000216392; -.
DR BindingDB; P06737; -.
DR ChEMBL; CHEMBL2568; -.
DR DrugCentral; P06737; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR GlyGen; P06737; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P06737; -.
DR MetOSite; P06737; -.
DR PhosphoSitePlus; P06737; -.
DR SwissPalm; P06737; -.
DR BioMuta; PYGL; -.
DR DMDM; 6648082; -.
DR EPD; P06737; -.
DR jPOST; P06737; -.
DR MassIVE; P06737; -.
DR MaxQB; P06737; -.
DR PaxDb; P06737; -.
DR PeptideAtlas; P06737; -.
DR PRIDE; P06737; -.
DR ProteomicsDB; 27652; -.
DR ProteomicsDB; 51923; -. [P06737-1]
DR Antibodypedia; 25; 317 antibodies from 31 providers.
DR DNASU; 5836; -.
DR Ensembl; ENST00000216392.8; ENSP00000216392.7; ENSG00000100504.17. [P06737-1]
DR Ensembl; ENST00000544180.6; ENSP00000443787.1; ENSG00000100504.17. [P06737-2]
DR GeneID; 5836; -.
DR KEGG; hsa:5836; -.
DR MANE-Select; ENST00000216392.8; ENSP00000216392.7; NM_002863.5; NP_002854.3.
DR UCSC; uc001wyu.4; human. [P06737-1]
DR CTD; 5836; -.
DR DisGeNET; 5836; -.
DR GeneCards; PYGL; -.
DR GeneReviews; PYGL; -.
DR HGNC; HGNC:9725; PYGL.
DR HPA; ENSG00000100504; Tissue enhanced (liver).
DR MalaCards; PYGL; -.
DR MIM; 232700; phenotype.
DR MIM; 613741; gene.
DR neXtProt; NX_P06737; -.
DR OpenTargets; ENSG00000100504; -.
DR Orphanet; 369; Glycogen storage disease due to liver glycogen phosphorylase deficiency.
DR PharmGKB; PA34068; -.
DR VEuPathDB; HostDB:ENSG00000100504; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; P06737; -.
DR OMA; KHKRTFT; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; P06737; -.
DR TreeFam; TF300309; -.
DR BioCyc; MetaCyc:HS02099-MON; -.
DR BRENDA; 2.4.1.1; 2681.
DR PathwayCommons; P06737; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P06737; -.
DR SIGNOR; P06737; -.
DR BioGRID-ORCS; 5836; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; PYGL; human.
DR EvolutionaryTrace; P06737; -.
DR GenomeRNAi; 5836; -.
DR Pharos; P06737; Tchem.
DR PRO; PR:P06737; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P06737; protein.
DR Bgee; ENSG00000100504; Expressed in blood and 167 other tissues.
DR ExpressionAtlas; P06737; baseline and differential.
DR Genevisible; P06737; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0016208; F:AMP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0032052; F:bile acid binding; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0002060; F:purine nucleobase binding; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019842; F:vitamin binding; IDA:UniProtKB.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:UniProtKB.
DR GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW Carbohydrate metabolism; Cytoplasm; Disease variant; Glycogen metabolism;
KW Glycogen storage disease; Glycosyltransferase; Nucleotide-binding;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..847
FT /note="Glycogen phosphorylase, liver form"
FT /id="PRO_0000188524"
FT BINDING 43..45
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:10949035,
FT ECO:0007744|PDB:1FA9"
FT BINDING 76
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:10949035,
FT ECO:0007744|PDB:1FA9"
FT BINDING 310
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:10949035,
FT ECO:0007744|PDB:1FA9"
FT SITE 109
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT SITE 143
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT SITE 156
FT /note="May be involved in allosteric control"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 15
FT /note="Phosphoserine; by PHK; in form phosphorylase a"
FT /evidence="ECO:0000269|PubMed:10949035,
FT ECO:0000269|PubMed:22225877, ECO:0007744|PDB:1FA9"
FT MOD_RES 364
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET01"
FT MOD_RES 470
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22225877"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET01"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09811"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:10949035,
FT ECO:0000269|PubMed:10980448, ECO:0000269|PubMed:12204691,
FT ECO:0007744|PDB:1EM6, ECO:0007744|PDB:1EXV,
FT ECO:0007744|PDB:1FA9, ECO:0007744|PDB:1FC0,
FT ECO:0007744|PDB:1L5Q, ECO:0007744|PDB:1L5R,
FT ECO:0007744|PDB:1L5S, ECO:0007744|PDB:1L7X"
FT MOD_RES 796
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22225877"
FT VAR_SEQ 82..115
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045339"
FT VARIANT 222
FT /note="V -> I (in dbSNP:rs946616)"
FT /evidence="ECO:0000269|PubMed:9529348"
FT /id="VAR_007907"
FT VARIANT 231
FT /note="V -> E (in dbSNP:rs1042195)"
FT /id="VAR_013095"
FT VARIANT 339
FT /note="N -> S (in GSD6; dbSNP:rs113993976)"
FT /evidence="ECO:0000269|PubMed:9529348"
FT /id="VAR_007908"
FT VARIANT 377
FT /note="N -> K (in GSD6; dbSNP:rs113993977)"
FT /evidence="ECO:0000269|PubMed:9529348"
FT /id="VAR_007909"
FT VARIANT 425
FT /note="R -> P (in dbSNP:rs2228499)"
FT /evidence="ECO:0000269|PubMed:2877458"
FT /id="VAR_034425"
FT VARIANT 698
FT /note="V -> G (in dbSNP:rs35831273)"
FT /id="VAR_034426"
FT VARIANT 715
FT /note="R -> S (in dbSNP:rs1042210)"
FT /id="VAR_013096"
FT VARIANT 806
FT /note="I -> L (in dbSNP:rs34313873)"
FT /id="VAR_034427"
FT VARIANT 845
FT /note="N -> S (in dbSNP:rs78558135)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_069054"
FT MUTAGEN 470
FT /note="K->Q: Decreased glycogen phosphorylase activity."
FT /evidence="ECO:0000269|PubMed:22225877"
FT MUTAGEN 470
FT /note="K->R: Decreased acetylation; when associated with R-
FT 796."
FT /evidence="ECO:0000269|PubMed:22225877"
FT MUTAGEN 796
FT /note="K->Q: Decreased glycogen phosphorylase activity."
FT /evidence="ECO:0000269|PubMed:22225877"
FT MUTAGEN 796
FT /note="K->R: Decreased acetylation; when associated with R-
FT 470."
FT /evidence="ECO:0000269|PubMed:22225877"
FT CONFLICT 2..3
FT /note="AK -> GE (in Ref. 1; AAA52577 and 3; AAC18079)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="V -> E (in Ref. 1; AAA52577)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> Q (in Ref. 1; AAA52577)"
FT /evidence="ECO:0000305"
FT CONFLICT 344..345
FT /note="AL -> RI (in Ref. 1; AAA52577)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="T -> N (in Ref. 1; AAA52577 and 3; AAC18079)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="R -> S (in Ref. 2; AAC17450)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="Missing (in Ref. 8; AAH09895)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="R -> G (in Ref. 5; BAG62279)"
FT /evidence="ECO:0000305"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1FA9"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1FA9"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1FA9"
FT HELIX 19..38
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 220..232
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1L5S"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:1FA9"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 291..314
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1FA9"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:3DDW"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1L5R"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:3CEJ"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 498..508
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 516..525
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 529..553
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:1L5R"
FT STRAND 562..569
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 577..593
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:3CEJ"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 615..633
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 641..646
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 651..657
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:2ATI"
FT HELIX 678..684
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 697..704
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:3DDS"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 716..725
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 729..735
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 737..748
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:3DDS"
FT TURN 756..759
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 760..768
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 774..792
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 795..806
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 810..812
FT /evidence="ECO:0007829|PDB:3DDS"
FT HELIX 814..824
FT /evidence="ECO:0007829|PDB:3DDS"
SQ 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
