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P00518

- PHKG1_RABIT

UniProt

P00518 - PHKG1_RABIT

Protein

Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

Gene

PHKG1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3.2 Publications

    Catalytic activityi

    2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
    ATP + [tau protein] = ADP + [tau protein] phosphate.
    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491ATPPROSITE-ProRule annotation
    Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphorylase kinase activity Source: UniProtKB-EC
    3. tau-protein kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycogen biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Kinase, Muscle protein, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.19. 1749.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC:2.7.11.19)
    Alternative name(s):
    Phosphorylase kinase subunit gamma-1
    Serine/threonine-protein kinase PHKG1 (EC:2.7.11.1, EC:2.7.11.26)
    Gene namesi
    Name:PHKG1
    Synonyms:PHKG
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. phosphorylase kinase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 387386Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoformPRO_0000086510Add
    BLAST

    Interactioni

    Subunit structurei

    Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin.

    Protein-protein interaction databases

    DIPiDIP-48334N.
    STRINGi9986.ENSOCUP00000011717.

    Structurei

    Secondary structure

    1
    387
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni17 – 193
    Beta strandi20 – 289
    Beta strandi30 – 3910
    Turni40 – 434
    Beta strandi44 – 529
    Turni55 – 584
    Helixi61 – 8121
    Beta strandi90 – 956
    Beta strandi97 – 1059
    Helixi112 – 1198
    Helixi124 – 14320
    Helixi153 – 1553
    Beta strandi156 – 1583
    Beta strandi164 – 1663
    Helixi188 – 1903
    Helixi193 – 2008
    Helixi210 – 22516
    Helixi235 – 24410
    Turni251 – 2533
    Helixi254 – 2563
    Helixi259 – 26810
    Helixi273 – 2753
    Helixi279 – 2824
    Helixi286 – 2883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PHKX-ray2.20A2-299[»]
    1QL6X-ray2.40A2-299[»]
    2PHKX-ray2.60A15-291[»]
    ProteinModelPortaliP00518.
    SMRiP00518. Positions 15-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00518.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 288269Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni303 – 32725Calmodulin-binding (domain-N)Add
    BLAST
    Regioni343 – 36725Calmodulin-binding (domain-C)Add
    BLAST

    Domaini

    The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117716.
    HOGENOMiHOG000233016.
    HOVERGENiHBG106193.

    Family and domain databases

    InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR011009. Kinase-like_dom.
    IPR002291. Phosph_kin_gamma.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24347. PTHR24347. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01049. PHOSPHBKNASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00518-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRDAALPGS HSTHGFYENY EPKEILGRGV SSVVRRCIHK PTCKEYAVKI    50
    IDVTGGGSFS AEEVQELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF 100
    FLVFDLMKKG ELFDYLTEKV TLSEKETRKI MRALLEVICA LHKLNIVHRD 150
    LKPENILLDD DMNIKLTDFG FSCQLDPGEK LREVCGTPSY LAPEIIECSM 200
    NDNHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR MIMSGNYQFG 250
    SPEWDDYSDT VKDLVSRFLV VQPQKRYTAE EALAHPFFQQ YVVEEVRHFS 300
    PRGKFKVICL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY 350
    AFRIYGHWVK KGQQQNRAAL FENTPKAVLF SLAEDDY 387
    Length:387
    Mass (Da):44,803
    Last modified:January 23, 2007 - v2
    Checksum:i0EC8710C2A4C1BE8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00684 mRNA. Translation: CAA68682.1.
    PIRiS00075. KIRBFG.
    RefSeqiNP_001095175.1. NM_001101705.1.
    UniGeneiOcu.2086.

    Genome annotation databases

    EnsembliENSOCUT00000013615; ENSOCUP00000011717; ENSOCUG00000013618.
    GeneIDi100009297.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00684 mRNA. Translation: CAA68682.1 .
    PIRi S00075. KIRBFG.
    RefSeqi NP_001095175.1. NM_001101705.1.
    UniGenei Ocu.2086.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PHK X-ray 2.20 A 2-299 [» ]
    1QL6 X-ray 2.40 A 2-299 [» ]
    2PHK X-ray 2.60 A 15-291 [» ]
    ProteinModelPortali P00518.
    SMRi P00518. Positions 15-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48334N.
    STRINGi 9986.ENSOCUP00000011717.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSOCUT00000013615 ; ENSOCUP00000011717 ; ENSOCUG00000013618 .
    GeneIDi 100009297.

    Organism-specific databases

    CTDi 5260.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117716.
    HOGENOMi HOG000233016.
    HOVERGENi HBG106193.

    Enzyme and pathway databases

    BRENDAi 2.7.11.19. 1749.

    Miscellaneous databases

    EvolutionaryTracei P00518.

    Family and domain databases

    InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR011009. Kinase-like_dom.
    IPR002291. Phosph_kin_gamma.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24347. PTHR24347. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01049. PHOSPHBKNASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase."
      da Cruz e Silva E.F., Cohen P.T.W.
      FEBS Lett. 220:36-42(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: New Zealand white.
    2. "Homology of the gamma subunit of phosphorylase b kinase with cAMP-dependent protein kinase."
      Reimann E.M., Titani K., Ericsson L.H., Wade R.D., Fischer E.H., Walsh K.A.
      Biochemistry 23:4185-4192(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-387.
    3. "The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin."
      Dasgupta M., Honeycutt T., Blumenthal D.K.
      J. Biol. Chem. 264:17156-17163(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALMODULIN-BINDING DOMAINS.
    4. "Phosphorylase kinase phosphorylates the calmodulin-binding regulatory regions of neuronal tissue-specific proteins B-50 (GAP-43) and neurogranin."
      Paudel H.K., Zwiers H., Wang J.H.
      J. Biol. Chem. 268:6207-6213(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF GAP43 AND NRGN/RC3.
    5. "Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory."
      Dasgupta M., Blumenthal D.K.
      J. Biol. Chem. 270:22283-22289(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALMODULIN-BINDING DOMAINS.
    6. "Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product."
      Owen D.J., Noble M.E.M., Garman E.F., Papageorgiou A.C., Johnson L.N.
      Structure 3:467-482(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-292.
    7. "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase."
      Paudel H.K.
      J. Biol. Chem. 272:1777-1785(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
    8. "The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition."
      Lowe E.D., Noble M.E.M., Skamnaki V.T., Oikonomakos N.G., Owen D.J., Johnson L.N.
      EMBO J. 16:6646-6658(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-299.

    Entry informationi

    Entry nameiPHKG1_RABIT
    AccessioniPrimary (citable) accession number: P00518
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3