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P06737

- PYGL_HUMAN

UniProt

P06737 - PYGL_HUMAN

Protein

Glycogen phosphorylase, liver form

Gene

PYGL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    Pyridoxal phosphate.

    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

    1. AMP binding Source: UniProtKB
    2. ATP binding Source: UniProtKB
    3. bile acid binding Source: UniProtKB
    4. drug binding Source: UniProtKB
    5. glucose binding Source: UniProtKB
    6. glycogen phosphorylase activity Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB
    8. purine nucleobase binding Source: UniProtKB
    9. pyridoxal phosphate binding Source: InterPro
    10. vitamin binding Source: UniProtKB

    GO - Biological processi

    1. 5-phosphoribose 1-diphosphate biosynthetic process Source: Ensembl
    2. carbohydrate metabolic process Source: Reactome
    3. glucose homeostasis Source: UniProtKB
    4. glucose metabolic process Source: Reactome
    5. glycogen catabolic process Source: Reactome
    6. glycogen metabolic process Source: UniProtKB
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Keywords - Ligandi

    Nucleotide-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02099-MONOMER.
    ReactomeiREACT_1008. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9725. PYGL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. plasma membrane Source: HPA

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti339 – 3391N → S in GSD6. 1 Publication
    VAR_007908
    Natural varianti377 – 3771N → K in GSD6. 1 Publication
    VAR_007909

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease

    Organism-specific databases

    MIMi232700. phenotype.
    Orphaneti369. Glycogen storage disease due to liver glycogen phosphorylase deficiency.
    PharmGKBiPA34068.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 847846Glycogen phosphorylase, liver formPRO_0000188524Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase A1 Publication
    Modified residuei364 – 3641N6-succinyllysineBy similarity
    Modified residuei681 – 6811N6-(pyridoxal phosphate)lysineBy similarity

    Post-translational modificationi

    Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP06737.
    PaxDbiP06737.
    PeptideAtlasiP06737.
    PRIDEiP06737.

    PTM databases

    PhosphoSiteiP06737.

    Expressioni

    Gene expression databases

    ArrayExpressiP06737.
    BgeeiP06737.
    CleanExiHS_PYGL.
    GenevestigatoriP06737.

    Organism-specific databases

    HPAiHPA000962.
    HPA004119.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi111794. 23 interactions.
    IntActiP06737. 8 interactions.
    MINTiMINT-1208599.
    STRINGi9606.ENSP00000216392.

    Structurei

    Secondary structure

    1
    847
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 103
    Helixi11 – 133
    Beta strandi14 – 174
    Helixi19 – 3820
    Helixi44 – 463
    Helixi49 – 6214
    Helixi65 – 7814
    Beta strandi82 – 865
    Beta strandi90 – 934
    Helixi96 – 1027
    Helixi106 – 11510
    Helixi120 – 1256
    Beta strandi130 – 1356
    Helixi136 – 15015
    Beta strandi155 – 1606
    Beta strandi168 – 1725
    Beta strandi175 – 1795
    Turni183 – 1864
    Helixi195 – 1973
    Beta strandi199 – 2046
    Beta strandi206 – 2105
    Beta strandi213 – 2186
    Beta strandi220 – 23213
    Beta strandi234 – 2374
    Beta strandi239 – 24810
    Helixi255 – 2606
    Helixi263 – 2686
    Helixi270 – 2745
    Helixi275 – 2773
    Helixi291 – 31424
    Beta strandi315 – 3173
    Beta strandi322 – 3254
    Helixi327 – 3293
    Helixi330 – 3334
    Beta strandi334 – 3418
    Turni342 – 3454
    Helixi346 – 35611
    Helixi362 – 37211
    Beta strandi373 – 3764
    Helixi382 – 3843
    Beta strandi387 – 3893
    Helixi390 – 3967
    Helixi398 – 41821
    Beta strandi419 – 4213
    Helixi423 – 4297
    Beta strandi431 – 4333
    Beta strandi435 – 4373
    Beta strandi439 – 4413
    Helixi442 – 4487
    Beta strandi451 – 4577
    Helixi458 – 4669
    Turni467 – 4693
    Helixi470 – 4756
    Helixi477 – 4793
    Beta strandi480 – 4823
    Helixi490 – 4956
    Helixi498 – 50811
    Helixi511 – 5133
    Helixi516 – 52510
    Helixi529 – 55325
    Beta strandi554 – 5563
    Beta strandi562 – 5698
    Turni573 – 5764
    Helixi577 – 59317
    Beta strandi595 – 5973
    Beta strandi602 – 6076
    Helixi615 – 63319
    Turni635 – 6373
    Helixi638 – 6403
    Beta strandi641 – 6466
    Helixi651 – 6577
    Helixi658 – 6603
    Beta strandi662 – 6665
    Turni670 – 6723
    Helixi678 – 6847
    Beta strandi688 – 6914
    Helixi697 – 7048
    Helixi706 – 7083
    Beta strandi709 – 7113
    Helixi716 – 72510
    Helixi729 – 7357
    Helixi737 – 74812
    Turni749 – 7513
    Turni756 – 7594
    Helixi760 – 7689
    Helixi774 – 79219
    Helixi795 – 80612
    Helixi810 – 8123
    Helixi814 – 82411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EM6X-ray2.20A/B1-847[»]
    1EXVX-ray2.40A/B1-847[»]
    1FA9X-ray2.40A2-847[»]
    1FC0X-ray2.40A/B2-847[»]
    1L5QX-ray2.25A/B1-847[»]
    1L5RX-ray2.10A/B1-847[»]
    1L5SX-ray2.10A/B1-847[»]
    1L7XX-ray2.30A/B1-847[»]
    1XOIX-ray2.10A/B2-847[»]
    2ATIX-ray1.90A/B2-847[»]
    2QLLX-ray2.56A1-847[»]
    2ZB2X-ray2.45A/B1-847[»]
    3CEHX-ray2.80A/B24-832[»]
    3CEJX-ray3.30A/B24-832[»]
    3CEMX-ray2.47A/B24-832[»]
    3DD1X-ray2.57A/B2-847[»]
    3DDSX-ray1.80A/B2-847[»]
    3DDWX-ray1.90A/B2-847[»]
    ProteinModelPortaliP06737.
    SMRiP06737. Positions 6-839.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06737.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycogen phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0058.
    HOVERGENiHBG006848.
    InParanoidiP06737.
    KOiK00688.
    OMAiDLVNMLF.
    PhylomeDBiP06737.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06737-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR    50
    DYYFALAHTV RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM 100
    INLGLQNACD EAIYQLGLDI EELEEIEEDA GLGNGGLGRL AACFLDSMAT 150
    LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA DDWLRYGNPW EKSRPEFMLP 200
    VHFYGKVEHT NTGTKWIDTQ VVLALPYDTP VPGYMNNTVN TMRLWSARAP 250
    NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
    VAATLQDIIR RFKASKFGST RGAGTVFDAF PDQVAIQLND THPALAIPEL 350
    MRIFVDIEKL PWSKAWELTQ KTFAYTNHTV LPEALERWPV DLVEKLLPRH 400
    LEIIYEINQK HLDRIVALFP KDVDRLRRMS LIEEEGSKRI NMAHLCIVGS 450
    HAVNGVAKIH SDIVKTKVFK DFSELEPDKF QNKTNGITPR RWLLLCNPGL 500
    AELIAEKIGE DYVKDLSQLT KLHSFLGDDV FLRELAKVKQ ENKLKFSQFL 550
    ETEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVITMYNR IKKDPKKLFV 600
    PRTVIIGGKA APGYHMAKMI IKLITSVADV VNNDPMVGSK LKVIFLENYR 650
    VSLAEKVIPA TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM 700
    AEEAGEENLF IFGMRIDDVA ALDKKGYEAK EYYEALPELK LVIDQIDNGF 750
    FSPKQPDLFK DIINMLFYHD RFKVFADYEA YVKCQDKVSQ LYMNPKAWNT 800
    MVLKNIAASG KFSSDRTIKE YAQNIWNVEP SDLKISLSNE SNKVNGN 847
    Length:847
    Mass (Da):97,149
    Last modified:January 23, 2007 - v4
    Checksum:i74017E8125FB5735
    GO
    Isoform 2 (identifier: P06737-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         82-115: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:813
    Mass (Da):93,134
    Checksum:i40B7DB0528A64AAA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 32AK → GE in AAA52577. (PubMed:2877458)Curated
    Sequence conflicti2 – 32AK → GE in AAC18079. (PubMed:9536091)Curated
    Sequence conflicti83 – 831V → E in AAA52577. (PubMed:2877458)Curated
    Sequence conflicti323 – 3231A → Q in AAA52577. (PubMed:2877458)Curated
    Sequence conflicti344 – 3452AL → RI in AAA52577. (PubMed:2877458)Curated
    Sequence conflicti369 – 3691T → N in AAA52577. (PubMed:2877458)Curated
    Sequence conflicti369 – 3691T → N in AAC18079. (PubMed:9536091)Curated
    Sequence conflicti570 – 5701R → S in AAC17450. 1 PublicationCurated
    Sequence conflicti683 – 6831Missing in AAH09895. (PubMed:15489334)Curated
    Sequence conflicti715 – 7151R → G in BAG62279. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti222 – 2221V → I.1 Publication
    Corresponds to variant rs946616 [ dbSNP | Ensembl ].
    VAR_007907
    Natural varianti231 – 2311V → E.
    Corresponds to variant rs1042195 [ dbSNP | Ensembl ].
    VAR_013095
    Natural varianti339 – 3391N → S in GSD6. 1 Publication
    VAR_007908
    Natural varianti377 – 3771N → K in GSD6. 1 Publication
    VAR_007909
    Natural varianti425 – 4251R → P.1 Publication
    Corresponds to variant rs2228499 [ dbSNP | Ensembl ].
    VAR_034425
    Natural varianti698 – 6981V → G.
    Corresponds to variant rs35831273 [ dbSNP | Ensembl ].
    VAR_034426
    Natural varianti715 – 7151R → S.
    Corresponds to variant rs1042210 [ dbSNP | Ensembl ].
    VAR_013096
    Natural varianti806 – 8061I → L.
    Corresponds to variant rs34313873 [ dbSNP | Ensembl ].
    VAR_034427
    Natural varianti845 – 8451N → S.1 Publication
    Corresponds to variant rs78558135 [ dbSNP | Ensembl ].
    VAR_069054

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei82 – 11534Missing in isoform 2. 1 PublicationVSP_045339Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14636 mRNA. Translation: AAA52577.1.
    AF066858 mRNA. Translation: AAC17450.1.
    AF046798
    , AF046787, AF046788, AF046789, AF046790, AF046791, AF046792, AF046793, AF046794, AF046795, AF046796, AF046797 Genomic DNA. Translation: AAC18079.1.
    AF046785 mRNA. Translation: AAC23504.1.
    Y15233 mRNA. Translation: CAA75517.1.
    AK300580 mRNA. Translation: BAG62279.1.
    AL358334 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65685.1.
    BC009895 mRNA. Translation: AAH09895.3.
    BC082229 mRNA. Translation: AAH82229.2.
    BC095850 mRNA. Translation: AAH95850.2.
    BC110791 mRNA. Translation: AAI10792.2.
    M36807 mRNA. Translation: AAA35906.1.
    CCDSiCCDS32080.1. [P06737-1]
    CCDS53894.1. [P06737-2]
    PIRiA25518.
    RefSeqiNP_001157412.1. NM_001163940.1. [P06737-2]
    NP_002854.3. NM_002863.4. [P06737-1]
    UniGeneiHs.282417.

    Genome annotation databases

    EnsembliENST00000216392; ENSP00000216392; ENSG00000100504. [P06737-1]
    ENST00000544180; ENSP00000443787; ENSG00000100504. [P06737-2]
    GeneIDi5836.
    KEGGihsa:5836.
    UCSCiuc001wyu.3. human. [P06737-1]

    Polymorphism databases

    DMDMi6648082.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14636 mRNA. Translation: AAA52577.1 .
    AF066858 mRNA. Translation: AAC17450.1 .
    AF046798
    , AF046787 , AF046788 , AF046789 , AF046790 , AF046791 , AF046792 , AF046793 , AF046794 , AF046795 , AF046796 , AF046797 Genomic DNA. Translation: AAC18079.1 .
    AF046785 mRNA. Translation: AAC23504.1 .
    Y15233 mRNA. Translation: CAA75517.1 .
    AK300580 mRNA. Translation: BAG62279.1 .
    AL358334 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65685.1 .
    BC009895 mRNA. Translation: AAH09895.3 .
    BC082229 mRNA. Translation: AAH82229.2 .
    BC095850 mRNA. Translation: AAH95850.2 .
    BC110791 mRNA. Translation: AAI10792.2 .
    M36807 mRNA. Translation: AAA35906.1 .
    CCDSi CCDS32080.1. [P06737-1 ]
    CCDS53894.1. [P06737-2 ]
    PIRi A25518.
    RefSeqi NP_001157412.1. NM_001163940.1. [P06737-2 ]
    NP_002854.3. NM_002863.4. [P06737-1 ]
    UniGenei Hs.282417.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EM6 X-ray 2.20 A/B 1-847 [» ]
    1EXV X-ray 2.40 A/B 1-847 [» ]
    1FA9 X-ray 2.40 A 2-847 [» ]
    1FC0 X-ray 2.40 A/B 2-847 [» ]
    1L5Q X-ray 2.25 A/B 1-847 [» ]
    1L5R X-ray 2.10 A/B 1-847 [» ]
    1L5S X-ray 2.10 A/B 1-847 [» ]
    1L7X X-ray 2.30 A/B 1-847 [» ]
    1XOI X-ray 2.10 A/B 2-847 [» ]
    2ATI X-ray 1.90 A/B 2-847 [» ]
    2QLL X-ray 2.56 A 1-847 [» ]
    2ZB2 X-ray 2.45 A/B 1-847 [» ]
    3CEH X-ray 2.80 A/B 24-832 [» ]
    3CEJ X-ray 3.30 A/B 24-832 [» ]
    3CEM X-ray 2.47 A/B 24-832 [» ]
    3DD1 X-ray 2.57 A/B 2-847 [» ]
    3DDS X-ray 1.80 A/B 2-847 [» ]
    3DDW X-ray 1.90 A/B 2-847 [» ]
    ProteinModelPortali P06737.
    SMRi P06737. Positions 6-839.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111794. 23 interactions.
    IntActi P06737. 8 interactions.
    MINTi MINT-1208599.
    STRINGi 9606.ENSP00000216392.

    Chemistry

    BindingDBi P06737.
    ChEMBLi CHEMBL2568.
    DrugBanki DB00131. Adenosine monophosphate.
    DB00114. Pyridoxal Phosphate.
    DB00140. Riboflavin.

    Protein family/group databases

    CAZyi GT35. Glycosyltransferase Family 35.

    PTM databases

    PhosphoSitei P06737.

    Polymorphism databases

    DMDMi 6648082.

    Proteomic databases

    MaxQBi P06737.
    PaxDbi P06737.
    PeptideAtlasi P06737.
    PRIDEi P06737.

    Protocols and materials databases

    DNASUi 5836.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216392 ; ENSP00000216392 ; ENSG00000100504 . [P06737-1 ]
    ENST00000544180 ; ENSP00000443787 ; ENSG00000100504 . [P06737-2 ]
    GeneIDi 5836.
    KEGGi hsa:5836.
    UCSCi uc001wyu.3. human. [P06737-1 ]

    Organism-specific databases

    CTDi 5836.
    GeneCardsi GC14M051324.
    HGNCi HGNC:9725. PYGL.
    HPAi HPA000962.
    HPA004119.
    MIMi 232700. phenotype.
    613741. gene.
    neXtProti NX_P06737.
    Orphaneti 369. Glycogen storage disease due to liver glycogen phosphorylase deficiency.
    PharmGKBi PA34068.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0058.
    HOVERGENi HBG006848.
    InParanoidi P06737.
    KOi K00688.
    OMAi DLVNMLF.
    PhylomeDBi P06737.
    TreeFami TF300309.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02099-MONOMER.
    Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).

    Miscellaneous databases

    ChiTaRSi PYGL. human.
    EvolutionaryTracei P06737.
    GenomeRNAii 5836.
    NextBioi 22742.
    PROi P06737.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06737.
    Bgeei P06737.
    CleanExi HS_PYGL.
    Genevestigatori P06737.

    Family and domain databases

    InterProi IPR011833. Glycg_phsphrylas.
    IPR000811. Glyco_trans_35.
    [Graphical view ]
    PANTHERi PTHR11468. PTHR11468. 1 hit.
    Pfami PF00343. Phosphorylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000460. Pprylas_GlgP. 1 hit.
    TIGRFAMsi TIGR02093. P_ylase. 1 hit.
    PROSITEi PS00102. PHOSPHORYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage."
      Newgard C.B., Nakano K., Hwang P.K., Fletterick R.J.
      Proc. Natl. Acad. Sci. U.S.A. 83:8132-8136(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-425.
      Tissue: Liver.
    2. Carty M.D., Clancy Y.C., Soeller W.C.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI."
      Chang S., Rosenberg M.J., Morton H., Francomano C.A., Biesecker L.G.
      Hum. Mol. Genet. 7:865-870(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Mutations in the liver glycogen phosphorylase gene 'PYGL' underlying glycogenosis type VI."
      Burwinkel B., Bakker H.D., Herschkovitz E., Moses S.W., Shin Y.S., Kilimann M.W.
      Am. J. Hum. Genet. 62:785-791(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GSD6 SER-339 AND LYS-377, VARIANT ILE-222.
      Tissue: Blood.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-845.
    6. "The DNA sequence and analysis of human chromosome 14."
      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.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Placenta, Skin and Uterus.
    9. "McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues."
      Gorin F.A., Mullinax R.L., Ignacio P.C., Neve R.L., Kurnit D.M.
      J. Neurogenet. 4:293-308(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 482-847 (ISOFORM 1).
      Tissue: Fetal brain.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    14. "Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core."
      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.
      Mol. Cell 6:139-148(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), PHOSPHORYLATION AT SER-15.
    15. "Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase."
      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.
      Chem. Biol. 9:915-924(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

    Entry informationi

    Entry nameiPYGL_HUMAN
    AccessioniPrimary (citable) accession number: P06737
    Secondary accession number(s): A6NDQ4
    , B4DUB7, F5H816, O60567, O60752, O60913, Q501V9, Q641R5, Q96G82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 178 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3