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P11216

- PYGB_HUMAN

UniProt

P11216 - PYGB_HUMAN

Protein

Glycogen phosphorylase, brain form

Gene

PYGB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 5 (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 non-covalent 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: UniProtKB
    2. 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: UniProtKB
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02178-MONOMER.
    ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).

    Protein family/group databases

    CAZyiGT35. Glycosyltransferase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycogen phosphorylase, brain form (EC:2.4.1.1)
    Gene namesi
    Name:PYGB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9723. PYGB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34066.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 843842Glycogen phosphorylase, brain formPRO_0000188535Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase ACurated
    Modified residuei197 – 1971PhosphotyrosineBy similarity
    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.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11216.
    PaxDbiP11216.
    PeptideAtlasiP11216.
    PRIDEiP11216.

    PTM databases

    PhosphoSiteiP11216.

    Expressioni

    Gene expression databases

    ArrayExpressiP11216.
    BgeeiP11216.
    CleanExiHS_PYGB.
    GenevestigatoriP11216.

    Organism-specific databases

    HPAiHPA031067.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi111792. 17 interactions.
    IntActiP11216. 1 interaction.
    STRINGi9606.ENSP00000216962.

    Structurei

    3D structure databases

    ProteinModelPortaliP11216.
    SMRiP11216. Positions 14-839.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycogen phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0058.
    HOVERGENiHBG006848.
    InParanoidiP11216.
    KOiK00688.
    OMAiMDQISSG.
    OrthoDBiEOG7JQBMK.
    PhylomeDBiP11216.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P11216-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR    50
    DYFFALAHTV RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM 100
    VNLGLQNACD EAIYQLGLDL EELEEIEEDA GLGNGGLGRL AACFLDSMAT 150
    LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA DDWLRYGNPW EKARPEYMLP 200
    VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN TMRLWSAKAP 250
    NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
    VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL 350
    MRILVDVEKV DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH 400
    LEIIYAINQR HLDHVAALFP GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS 450
    HAVNGVARIH SEIVKQSVFK DFYELEPEKF QNKTNGITPR RWLLLCNPGL 500
    ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ ENKLKFSAFL 550
    EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV 600
    PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR 650
    VSLAEKVIPA ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM 700
    AEEAGAENLF IFGLRVEDVE ALDRKGYNAR EYYDHLPELK QAVDQISSGF 750
    FSPKEPDCFK DIVNMLMHHD RFKVFADYEA YMQCQAQVDQ LYRNPKEWTK 800
    KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNI PRD 843
    Length:843
    Mass (Da):96,696
    Last modified:January 23, 2007 - v5
    Checksum:i810BFAD3002CACB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 32AK → GE(PubMed:3346228)Curated
    Sequence conflicti2 – 32AK → GE(PubMed:2615594)Curated
    Sequence conflicti248 – 2481K → R in AAA59597. (PubMed:3346228)Curated
    Sequence conflicti302 – 3021A → G in AAA59597. (PubMed:3346228)Curated
    Sequence conflicti835 – 8439IPPPNIPRD → LQHLPHPEWESGGATCWAPP ELCTHLAMY in AAA59597. (PubMed:3346228)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti303 – 3031A → S.
    Corresponds to variant rs2228976 [ dbSNP | Ensembl ].
    VAR_034428
    Natural varianti502 – 5021D → N.
    Corresponds to variant rs2227891 [ dbSNP | Ensembl ].
    VAR_020212

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03544 mRNA. Translation: AAA59597.1.
    U47025 mRNA. Translation: AAB60395.1.
    AL121772 Genomic DNA. Translation: CAC00661.1.
    BC017045 mRNA. Translation: AAH17045.1.
    BC030795 mRNA. Translation: AAH30795.1.
    CCDSiCCDS13171.1.
    PIRiA40138.
    RefSeqiNP_002853.2. NM_002862.3.
    XP_006723664.1. XM_006723601.1.
    UniGeneiHs.368157.

    Genome annotation databases

    EnsembliENST00000216962; ENSP00000216962; ENSG00000100994.
    GeneIDi5834.
    KEGGihsa:5834.
    UCSCiuc002wup.3. human.

    Polymorphism databases

    DMDMi20178317.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03544 mRNA. Translation: AAA59597.1 .
    U47025 mRNA. Translation: AAB60395.1 .
    AL121772 Genomic DNA. Translation: CAC00661.1 .
    BC017045 mRNA. Translation: AAH17045.1 .
    BC030795 mRNA. Translation: AAH30795.1 .
    CCDSi CCDS13171.1.
    PIRi A40138.
    RefSeqi NP_002853.2. NM_002862.3.
    XP_006723664.1. XM_006723601.1.
    UniGenei Hs.368157.

    3D structure databases

    ProteinModelPortali P11216.
    SMRi P11216. Positions 14-839.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111792. 17 interactions.
    IntActi P11216. 1 interaction.
    STRINGi 9606.ENSP00000216962.

    Chemistry

    BindingDBi P11216.
    ChEMBLi CHEMBL3856.
    DrugBanki DB00114. Pyridoxal Phosphate.

    Protein family/group databases

    CAZyi GT35. Glycosyltransferase Family 35.

    PTM databases

    PhosphoSitei P11216.

    Polymorphism databases

    DMDMi 20178317.

    Proteomic databases

    MaxQBi P11216.
    PaxDbi P11216.
    PeptideAtlasi P11216.
    PRIDEi P11216.

    Protocols and materials databases

    DNASUi 5834.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216962 ; ENSP00000216962 ; ENSG00000100994 .
    GeneIDi 5834.
    KEGGi hsa:5834.
    UCSCi uc002wup.3. human.

    Organism-specific databases

    CTDi 5834.
    GeneCardsi GC20P025228.
    HGNCi HGNC:9723. PYGB.
    HPAi HPA031067.
    MIMi 138550. gene.
    neXtProti NX_P11216.
    PharmGKBi PA34066.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0058.
    HOVERGENi HBG006848.
    InParanoidi P11216.
    KOi K00688.
    OMAi MDQISSG.
    OrthoDBi EOG7JQBMK.
    PhylomeDBi P11216.
    TreeFami TF300309.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02178-MONOMER.
    Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).

    Miscellaneous databases

    ChiTaRSi PYGB. human.
    GenomeRNAii 5834.
    NextBioi 22736.
    PROi P11216.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11216.
    Bgeei P11216.
    CleanExi HS_PYGB.
    Genevestigatori P11216.

    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. "Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes."
      Newgard C.B., Littman D.R., van Genderen C., Smith M., Fletterick R.J.
      J. Biol. Chem. 263:3850-3857(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences."
      Gelinas R.P., Froman B.E., McElroy F., Tait R.C., Gorin F.A.
      Brain Res. Mol. Brain Res. 6:177-185(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Lung and Skin.
    5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Tissue: Platelet.
    6. Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 18-30; 51-61; 71-78; 193-206; 271-278; 353-359; 388-395; 400-425; 508-520; 522-533; 546-552; 558-569; 577-590; 623-640; 657-681; 731-754 AND 817-823, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon adenocarcinoma.
    7. "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].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPYGB_HUMAN
    AccessioniPrimary (citable) accession number: P11216
    Secondary accession number(s): Q96AK1, Q9NPX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 169 of the entry and version 5 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

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3