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P11217

- PYGM_HUMAN

UniProt

P11217 - PYGM_HUMAN

Protein

Glycogen phosphorylase, muscle form

Gene

PYGM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 6 (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. glycogen phosphorylase activity Source: ProtInc
    2. nucleotide binding Source: UniProtKB-KW
    3. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glucose metabolic process Source: Reactome
    3. glycogen catabolic process Source: Reactome
    4. glycogen metabolic process Source: ProtInc
    5. 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:HS00949-MONOMER.
    ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).

    Protein family/group databases

    CAZyiGT35. Glycosyltransferase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycogen phosphorylase, muscle form (EC:2.4.1.1)
    Alternative name(s):
    Myophosphorylase
    Gene namesi
    Name:PYGM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9726. PYGM.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria.13 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti116 – 1161L → P in GSD5. 2 Publications
    VAR_014002
    Natural varianti194 – 1941R → W in GSD5. 1 Publication
    VAR_014003
    Natural varianti205 – 2051G → S in GSD5. 5 Publications
    Corresponds to variant rs119103251 [ dbSNP | Ensembl ].
    VAR_003431
    Natural varianti292 – 2921L → P in GSD5; rare mutation. 1 Publication
    VAR_014004
    Natural varianti349 – 3491E → K in GSD5. 1 Publication
    VAR_014005
    Natural varianti397 – 3971L → P in GSD5. 2 Publications
    VAR_003432
    Natural varianti488 – 4881T → N in GSD5. 2 Publications
    VAR_014006
    Natural varianti543 – 5431K → T in GSD5. 2 Publications
    VAR_003433
    Natural varianti602 – 6021R → W in GSD5. 1 Publication
    VAR_014007
    Natural varianti655 – 6551E → K in GSD5. 2 Publications
    VAR_003434
    Natural varianti660 – 6601A → D in GSD5. 2 Publications
    VAR_014008
    Natural varianti666 – 6661Q → E in GSD5. 1 Publication
    VAR_014009
    Natural varianti685 – 6851N → Y in GSD5. 2 Publications
    VAR_014010
    Natural varianti686 – 6861G → R in GSD5. 1 Publication
    VAR_014011
    Natural varianti687 – 6871A → P in GSD5. 1 Publication
    VAR_014012
    Natural varianti704 – 7041A → V in GSD5. 1 Publication
    VAR_014013
    Natural varianti709 – 7091Missing in GSD5; common in Japanese patients. 1 Publication
    VAR_014014
    Natural varianti798 – 7981W → R in GSD5. 3 Publications
    VAR_014015

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease

    Organism-specific databases

    MIMi232600. phenotype.
    Orphaneti368. Glycogen storage disease due to muscle glycogen phosphorylase deficiency.
    PharmGKBiPA34069.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 842841Glycogen phosphorylase, muscle formPRO_0000188529Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase A1 Publication
    Modified residuei473 – 4731PhosphotyrosineBy 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

    MaxQBiP11217.
    PaxDbiP11217.
    PRIDEiP11217.

    PTM databases

    PhosphoSiteiP11217.

    Expressioni

    Gene expression databases

    BgeeiP11217.
    CleanExiHS_PYGM.
    GenevestigatoriP11217.

    Organism-specific databases

    HPAiHPA056003.

    Interactioni

    Subunit structurei

    Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.

    Protein-protein interaction databases

    BioGridi111795. 8 interactions.
    IntActiP11217. 21 interactions.
    MINTiMINT-1134630.
    STRINGi9606.ENSP00000164139.

    Structurei

    Secondary structure

    1
    842
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 104
    Helixi11 – 133
    Helixi25 – 3814
    Turni44 – 463
    Helixi49 – 7830
    Beta strandi82 – 865
    Helixi96 – 1027
    Helixi106 – 1149
    Turni115 – 1173
    Helixi120 – 1267
    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 – 2363
    Beta strandi239 – 24810
    Helixi263 – 2708
    Helixi271 – 2777
    Helixi291 – 31323
    Helixi330 – 3334
    Beta strandi334 – 3418
    Turni342 – 3454
    Helixi346 – 35611
    Helixi362 – 37211
    Beta strandi373 – 3764
    Helixi382 – 3843
    Beta strandi387 – 3893
    Helixi390 – 3967
    Helixi398 – 41821
    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 – 5144
    Helixi516 – 52510
    Helixi529 – 55325
    Beta strandi562 – 5698
    Turni573 – 5764
    Helixi577 – 59317
    Beta strandi602 – 6076
    Helixi615 – 63117
    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
    Helixi730 – 7334
    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
    1Z8DX-ray2.30A1-842[»]
    ProteinModelPortaliP11217.
    SMRiP11217. Positions 3-837.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11217.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycogen phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0058.
    HOGENOMiHOG000278444.
    HOVERGENiHBG006848.
    InParanoidiP11217.
    KOiK00688.
    OMAiCHTVNGV.
    OrthoDBiEOG7JQBMK.
    PhylomeDBiP11217.
    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: P11217-1) [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

    MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR    50
    DYYFALAHTV RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM 100
    VNLALENACD EATYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT 150
    LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA DDWLRYGNPW EKARPEFTLP 200
    VHFYGHVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN TMRLWSAKAP 250
    NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
    VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL 350
    MRILVDLERM DWDKAWDVTV RTCAYTNHTV LPEALERWPV HLLETLLPRH 400
    LQIIYEINQR FLNRVAAAFP GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS 450
    HAVNGVARIH SEILKKTIFK DFYELEPHKF QNKTNGITPR RWLVLCNPGL 500
    AEVIAERIGE DFISDLDQLR KLLSFVDDEA FIRDVAKVKQ ENKLKFAAYL 550
    EREYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKREPNKFFV 600
    PRTVMIGGKA APGYHMAKMI IRLVTAIGDV VNHDPAVGDR LRVIFLENYR 650
    VSLAEKVIPA ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM 700
    AEEAGEENFF IFGMRVEDVD KLDQRGYNAQ EYYDRIPELR QVIEQLSSGF 750
    FSPKQPDLFK DIVNMLMHHD RFKVFADYED YIKCQEKVSA LYKNPREWTR 800
    MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE AI 842
    Length:842
    Mass (Da):97,092
    Last modified:January 23, 2007 - v6
    Checksum:iEBDB7D80D740B68F
    GO
    Isoform 2 (identifier: P11217-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         82-169: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:754
    Mass (Da):87,317
    Checksum:iF5C64CA460DA3FC9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti791 – 7911L → W in AAA60231. (PubMed:3447177)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti116 – 1161L → P in GSD5. 2 Publications
    VAR_014002
    Natural varianti194 – 1941R → W in GSD5. 1 Publication
    VAR_014003
    Natural varianti205 – 2051G → S in GSD5. 5 Publications
    Corresponds to variant rs119103251 [ dbSNP | Ensembl ].
    VAR_003431
    Natural varianti292 – 2921L → P in GSD5; rare mutation. 1 Publication
    VAR_014004
    Natural varianti349 – 3491E → K in GSD5. 1 Publication
    VAR_014005
    Natural varianti397 – 3971L → P in GSD5. 2 Publications
    VAR_003432
    Natural varianti414 – 4141R → G.
    Corresponds to variant rs11231866 [ dbSNP | Ensembl ].
    VAR_061198
    Natural varianti488 – 4881T → N in GSD5. 2 Publications
    VAR_014006
    Natural varianti543 – 5431K → T in GSD5. 2 Publications
    VAR_003433
    Natural varianti602 – 6021R → W in GSD5. 1 Publication
    VAR_014007
    Natural varianti655 – 6551E → K in GSD5. 2 Publications
    VAR_003434
    Natural varianti660 – 6601A → D in GSD5. 2 Publications
    VAR_014008
    Natural varianti666 – 6661Q → E in GSD5. 1 Publication
    VAR_014009
    Natural varianti685 – 6851N → Y in GSD5. 2 Publications
    VAR_014010
    Natural varianti686 – 6861G → R in GSD5. 1 Publication
    VAR_014011
    Natural varianti687 – 6871A → P in GSD5. 1 Publication
    VAR_014012
    Natural varianti704 – 7041A → V in GSD5. 1 Publication
    VAR_014013
    Natural varianti709 – 7091Missing in GSD5; common in Japanese patients. 1 Publication
    VAR_014014
    Natural varianti798 – 7981W → R in GSD5. 3 Publications
    VAR_014015

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei82 – 16988Missing in isoform 2. 1 PublicationVSP_043047Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32598
    , M32579, M32580, M32581, M32582, M32583, M32584, M32585, M32586, M32587, M32588, M32589, M32590, M32591, M32592, M32593, M32594, M32595, M32596, M32597 Genomic DNA. Translation: AAA60231.1.
    U94777
    , U94774, U94775, U94776 Genomic DNA. Translation: AAC52081.1.
    AF066859 mRNA. Translation: AAC17451.1.
    AK056607 mRNA. Translation: BAG51762.1.
    AP001462 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74284.1.
    BC126392 mRNA. Translation: AAI26393.1.
    BC130514 mRNA. Translation: AAI30515.1.
    X03031 mRNA. Translation: CAA26834.1.
    M16013 mRNA. Translation: AAA36216.1.
    CCDSiCCDS53659.1. [P11217-2]
    CCDS8079.1. [P11217-1]
    PIRiA27335.
    RefSeqiNP_001158188.1. NM_001164716.1. [P11217-2]
    NP_005600.1. NM_005609.2. [P11217-1]
    UniGeneiHs.154084.

    Genome annotation databases

    EnsembliENST00000164139; ENSP00000164139; ENSG00000068976. [P11217-1]
    ENST00000377432; ENSP00000366650; ENSG00000068976. [P11217-2]
    GeneIDi5837.
    KEGGihsa:5837.
    UCSCiuc001oax.4. human. [P11217-1]
    uc001oay.4. human. [P11217-2]

    Polymorphism databases

    DMDMi3041717.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32598
    , M32579 , M32580 , M32581 , M32582 , M32583 , M32584 , M32585 , M32586 , M32587 , M32588 , M32589 , M32590 , M32591 , M32592 , M32593 , M32594 , M32595 , M32596 , M32597 Genomic DNA. Translation: AAA60231.1 .
    U94777
    , U94774 , U94775 , U94776 Genomic DNA. Translation: AAC52081.1 .
    AF066859 mRNA. Translation: AAC17451.1 .
    AK056607 mRNA. Translation: BAG51762.1 .
    AP001462 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74284.1 .
    BC126392 mRNA. Translation: AAI26393.1 .
    BC130514 mRNA. Translation: AAI30515.1 .
    X03031 mRNA. Translation: CAA26834.1 .
    M16013 mRNA. Translation: AAA36216.1 .
    CCDSi CCDS53659.1. [P11217-2 ]
    CCDS8079.1. [P11217-1 ]
    PIRi A27335.
    RefSeqi NP_001158188.1. NM_001164716.1. [P11217-2 ]
    NP_005600.1. NM_005609.2. [P11217-1 ]
    UniGenei Hs.154084.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z8D X-ray 2.30 A 1-842 [» ]
    ProteinModelPortali P11217.
    SMRi P11217. Positions 3-837.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111795. 8 interactions.
    IntActi P11217. 21 interactions.
    MINTi MINT-1134630.
    STRINGi 9606.ENSP00000164139.

    Chemistry

    BindingDBi P11217.
    ChEMBLi CHEMBL3526.
    DrugBanki DB00114. Pyridoxal Phosphate.

    Protein family/group databases

    CAZyi GT35. Glycosyltransferase Family 35.

    PTM databases

    PhosphoSitei P11217.

    Polymorphism databases

    DMDMi 3041717.

    Proteomic databases

    MaxQBi P11217.
    PaxDbi P11217.
    PRIDEi P11217.

    Protocols and materials databases

    DNASUi 5837.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000164139 ; ENSP00000164139 ; ENSG00000068976 . [P11217-1 ]
    ENST00000377432 ; ENSP00000366650 ; ENSG00000068976 . [P11217-2 ]
    GeneIDi 5837.
    KEGGi hsa:5837.
    UCSCi uc001oax.4. human. [P11217-1 ]
    uc001oay.4. human. [P11217-2 ]

    Organism-specific databases

    CTDi 5837.
    GeneCardsi GC11M064513.
    GeneReviewsi PYGM.
    HGNCi HGNC:9726. PYGM.
    HPAi HPA056003.
    MIMi 232600. phenotype.
    608455. gene.
    neXtProti NX_P11217.
    Orphaneti 368. Glycogen storage disease due to muscle glycogen phosphorylase deficiency.
    PharmGKBi PA34069.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0058.
    HOGENOMi HOG000278444.
    HOVERGENi HBG006848.
    InParanoidi P11217.
    KOi K00688.
    OMAi CHTVNGV.
    OrthoDBi EOG7JQBMK.
    PhylomeDBi P11217.
    TreeFami TF300309.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00949-MONOMER.
    Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).

    Miscellaneous databases

    EvolutionaryTracei P11217.
    GenomeRNAii 5837.
    NextBioi 22746.
    PROi P11217.
    SOURCEi Search...

    Gene expression databases

    Bgeei P11217.
    CleanExi HS_PYGM.
    Genevestigatori P11217.

    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. "Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase."
      Burke J., Hwang P.K., Anderson L., Lebo R., Gorin F., Fletterick R.J.
      Proteins 2:177-187(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular diagnosis of McArdle disease: revised genomic structure of the myophosphorylase gene and identification of a novel mutation."
      Kubisch C., Wicklein E.M., Jentsch T.J.
      Hum. Mutat. 12:27-32(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. 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: Muscle.
    4. "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).
      Tissue: Tongue.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
    8. "Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs."
      Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J., Crerar M.M.
      Eur. J. Biochem. 152:267-274(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 676-842 (ISOFORM 1).
    9. "Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis."
      Gautron S., Daegelen D., Mennecier F., Dubocq D., Kahn A., Dreyfus J.-C.
      J. Clin. Invest. 79:275-281(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 455-676 (ISOFORM 1).
    10. "Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties."
      Carty T.J., Tu J., Graves D.J.
      J. Biol. Chem. 250:4980-4985(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15.
    11. "Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease)."
      Tsujino S., Shanske S., Dimauro S.
      N. Engl. J. Med. 329:241-245(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSD5 SER-205 AND THR-543.
    12. "Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease)."
      Tsujino S., Shanske S., Martinuzzi A., Heiman-Patterson T., Dimauro S.
      Hum. Mutat. 6:276-277(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSD5 PRO-397 AND LYS-655.
    13. "The molecular genetic basis of myophosphorylase deficiency (McArdle's disease)."
      Tsujino S., Shanske S., Nonaka I., DiMauro S.
      Muscle Nerve 3:S23-S27(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSD5 SER-205; PRO-292; PRO-397; THR-543; LYS-655 AND PHE-709 DEL.
    14. Cited for: VARIANTS GSD5 GLU-666 AND ARG-686.
    15. "A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact."
      Gamez J., Fernandez R., Bruno C., Andreu A.L., Cervera C., Navarro C., Schwartz S., Dimauro S.
      Muscle Nerve 22:1136-1138(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD5 PRO-116.
    16. "A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease."
      Andreu A.L., Bruno C., Tamburino L., Gamez J., Shanske S., Cervera C., Navarro C., DiMauro S.
      Neuromuscul. Disord. 9:171-173(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSD5 SER-205 AND TYR-685.
    17. "McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient."
      Rubio J.C., Martin M.A., Garcia A., Campos Y., Cabello A., Culebras J.M., Arenas J.
      Neuromuscul. Disord. 9:174-175(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD5 SER-205.
    18. "A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease."
      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.
      Arch. Neurol. 57:217-219(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD5 ARG-798.
    19. "A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease."
      Rubio J.C., Martin M.A., Campos Y., Auciello R., Cabello A., Arenas J.
      Muscle Nerve 23:129-131(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD5 ARG-798.
    20. "A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease."
      Rubio J.C., Martin M.A., Campos Y., Cabello A., Arenas J.
      Neuromuscul. Disord. 10:138-140(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD5 ASN-488.
    21. "A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease."
      Martin M.A., Rubio J.C., Campos Y., Ricoy J.R., Cabello A., Arenas J.
      Neuromuscul. Disord. 10:447-449(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD5 ASP-660.
    22. Cited for: VARIANTS GSD5 PRO-116; TRP-194; SER-205; LYS-349; ASN-488; TRP-602; ASP-660; TYR-685; VAL-704 AND ARG-798.
    23. "Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease."
      Bruno C., Lanzillo R., Biedi C., Iadicicco L., Minetti C., Santoro L.
      Neuromuscul. Disord. 12:498-500(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD5 PRO-687.

    Entry informationi

    Entry nameiPYGM_HUMAN
    AccessioniPrimary (citable) accession number: P11217
    Secondary accession number(s): A0AVK1, A6NDY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 177 of the entry and version 6 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 11
      Human chromosome 11: 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