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P15735

- PHKG2_HUMAN

UniProt

P15735 - PHKG2_HUMAN

Protein

Phosphorylase b kinase gamma catalytic chain, liver/testis isoform

Gene

PHKG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM By similarity.By similarity

    Catalytic activityi

    2 ATP + phosphorylase b = 2 ADP + phosphorylase a.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531ATPPROSITE-ProRule annotation
    Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphorylase kinase activity Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB
    4. tau-protein kinase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. generation of precursor metabolites and energy Source: ProtInc
    3. glucose metabolic process Source: Reactome
    4. glycogen biosynthetic process Source: InterPro
    5. glycogen catabolic process Source: Reactome
    6. glycogen metabolic process Source: ProtInc
    7. positive regulation of glycogen catabolic process Source: UniProtKB
    8. protein phosphorylation Source: ProtInc
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08155-MONOMER.
    BRENDAi2.7.11.19. 2681.
    ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
    SignaLinkiP15735.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphorylase b kinase gamma catalytic chain, liver/testis isoform (EC:2.7.11.19)
    Short name:
    PHK-gamma-LT
    Short name:
    PHK-gamma-T
    Alternative name(s):
    PSK-C3
    Phosphorylase kinase subunit gamma-2
    Gene namesi
    Name:PHKG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:8931. PHKG2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. phosphorylase kinase complex Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Glycogen storage disease 9C (GSD9C) [MIM:613027]: A metabolic disorder manifesting in infancy with hepatomegaly, growth retardation, hypotonia, liver dysfunction, and elevated plasma aminotransferases and lipids. These symptoms improve with age in most cases; however, some patients may develop hepatic fibrosis or cirrhosis.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061V → E in GSD9C. 1 Publication
    VAR_009517
    Natural varianti157 – 1571E → K in GSD9C. 1 Publication
    VAR_020854
    Natural varianti189 – 1891G → E in GSD9C. 1 Publication
    VAR_009518
    Natural varianti215 – 2151D → N in GSD9C. 1 Publication
    VAR_020855

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease

    Organism-specific databases

    MIMi613027. phenotype.
    Orphaneti264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
    PharmGKBiPA33272.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Phosphorylase b kinase gamma catalytic chain, liver/testis isoformPRO_0000086512Add
    BLAST

    Proteomic databases

    MaxQBiP15735.
    PaxDbiP15735.
    PRIDEiP15735.

    PTM databases

    PhosphoSiteiP15735.

    Expressioni

    Gene expression databases

    ArrayExpressiP15735.
    BgeeiP15735.
    CleanExiHS_PHKG2.
    GenevestigatoriP15735.

    Organism-specific databases

    HPAiHPA055455.

    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.1 Publication

    Protein-protein interaction databases

    BioGridi111279. 20 interactions.
    IntActiP15735. 19 interactions.
    STRINGi9606.ENSP00000329968.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2311
    Beta strandi24 – 329
    Beta strandi34 – 4310
    Turni44 – 463
    Beta strandi49 – 568
    Helixi64 – 8421
    Beta strandi93 – 10715
    Helixi115 – 1228
    Helixi127 – 14620
    Helixi156 – 1583
    Beta strandi159 – 1613
    Beta strandi167 – 1693
    Helixi191 – 1933
    Helixi196 – 2016
    Helixi214 – 22815
    Helixi238 – 24710
    Helixi254 – 2574
    Beta strandi258 – 2603
    Helixi262 – 27110
    Turni276 – 2783
    Helixi282 – 2876
    Helixi289 – 2913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y7JX-ray2.50A/B/C/D6-293[»]
    ProteinModelPortaliP15735.
    SMRiP15735. Positions 10-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 291268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni306 – 33025Calmodulin-binding (domain-N)By similarityAdd
    BLAST
    Regioni346 – 37025Calmodulin-binding (domain-C)By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233016.
    HOVERGENiHBG106193.
    InParanoidiP15735.
    KOiK00871.
    OrthoDBiEOG7JMGDM.
    PhylomeDBiP15735.
    TreeFamiTF320349.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15735-1) [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

    MTLDVGPEDE LPDWAAAKEF YQKYDPKDVI GRGVSSVVRR CVHRATGHEF    50
    AVKIMEVTAE RLSPEQLEEV REATRRETHI LRQVAGHPHI ITLIDSYESS 100
    SFMFLVFDLM RKGELFDYLT EKVALSEKET RSIMRSLLEA VSFLHANNIV 150
    HRDLKPENIL LDDNMQIRLS DFGFSCHLEP GEKLRELCGT PGYLAPEILK 200
    CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL MLRMIMEGQY 250
    QFSSPEWDDR SSTVKDLISR LLQVDPEARL TAEQALQHPF FERCEGSQPW 300
    NLTPRQRFRV AVWTVLAAGR VALSTHRVRP LTKNALLRDP YALRSVRHLI 350
    DNCAFRLYGH WVKKGEQQNR AALFQHRPPG PFPIMGPEEE GDSAAITEDE 400
    AVLVLG 406
    Length:406
    Mass (Da):46,442
    Last modified:April 1, 1990 - v1
    Checksum:iE991CFF2D3D70F60
    GO
    Isoform 2 (identifier: P15735-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         362-374: VKKGEQQNRAALF → IRKQWIGKLMACV
         375-406: Missing.

    Show »
    Length:374
    Mass (Da):43,158
    Checksum:iD0E2416820A68AA7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461A → P in AAA36518. (PubMed:2948189)Curated
    Sequence conflicti176 – 1761C → S in AAA36518. (PubMed:2948189)Curated
    Sequence conflicti179 – 1791E → D in AAA36518. (PubMed:2948189)Curated
    Sequence conflicti212 – 2143KEV → LVD in AAA36518. (PubMed:2948189)Curated
    Sequence conflicti221 – 2211V → E in AAA36518. (PubMed:2948189)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061V → E in GSD9C. 1 Publication
    VAR_009517
    Natural varianti157 – 1571E → K in GSD9C. 1 Publication
    VAR_020854
    Natural varianti189 – 1891G → E in GSD9C. 1 Publication
    VAR_009518
    Natural varianti215 – 2151D → N in GSD9C. 1 Publication
    VAR_020855
    Natural varianti247 – 2471E → G.
    Corresponds to variant rs34006569 [ dbSNP | Ensembl ].
    VAR_051658
    Natural varianti317 – 3171A → T.1 Publication
    VAR_040996

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei362 – 37413VKKGE…RAALF → IRKQWIGKLMACV in isoform 2. 1 PublicationVSP_041858Add
    BLAST
    Alternative sequencei375 – 40632Missing in isoform 2. 1 PublicationVSP_041859Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31606 mRNA. Translation: AAA36442.1.
    Y11950, Y11951 Genomic DNA. Translation: CAA72694.1.
    AK289492 mRNA. Translation: BAF82181.1.
    AK293551 mRNA. Translation: BAG57028.1.
    AC106886 Genomic DNA. No translation available.
    BC002541 mRNA. Translation: AAH02541.1.
    M14503 mRNA. Translation: AAA36518.1.
    CCDSiCCDS10690.1. [P15735-1]
    CCDS54002.1. [P15735-2]
    PIRiA40069. KIHUCT.
    RefSeqiNP_000285.1. NM_000294.2. [P15735-1]
    NP_001165903.1. NM_001172432.1. [P15735-2]
    UniGeneiHs.65735.

    Genome annotation databases

    EnsembliENST00000424889; ENSP00000388571; ENSG00000156873. [P15735-2]
    ENST00000563588; ENSP00000455607; ENSG00000156873. [P15735-1]
    GeneIDi5261.
    KEGGihsa:5261.
    UCSCiuc002dzk.2. human. [P15735-1]
    uc021tgo.1. human. [P15735-2]

    Polymorphism databases

    DMDMi125536.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31606 mRNA. Translation: AAA36442.1 .
    Y11950 , Y11951 Genomic DNA. Translation: CAA72694.1 .
    AK289492 mRNA. Translation: BAF82181.1 .
    AK293551 mRNA. Translation: BAG57028.1 .
    AC106886 Genomic DNA. No translation available.
    BC002541 mRNA. Translation: AAH02541.1 .
    M14503 mRNA. Translation: AAA36518.1 .
    CCDSi CCDS10690.1. [P15735-1 ]
    CCDS54002.1. [P15735-2 ]
    PIRi A40069. KIHUCT.
    RefSeqi NP_000285.1. NM_000294.2. [P15735-1 ]
    NP_001165903.1. NM_001172432.1. [P15735-2 ]
    UniGenei Hs.65735.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y7J X-ray 2.50 A/B/C/D 6-293 [» ]
    ProteinModelPortali P15735.
    SMRi P15735. Positions 10-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111279. 20 interactions.
    IntActi P15735. 19 interactions.
    STRINGi 9606.ENSP00000329968.

    Chemistry

    BindingDBi P15735.
    ChEMBLi CHEMBL2349.
    GuidetoPHARMACOLOGYi 2147.

    PTM databases

    PhosphoSitei P15735.

    Polymorphism databases

    DMDMi 125536.

    Proteomic databases

    MaxQBi P15735.
    PaxDbi P15735.
    PRIDEi P15735.

    Protocols and materials databases

    DNASUi 5261.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000424889 ; ENSP00000388571 ; ENSG00000156873 . [P15735-2 ]
    ENST00000563588 ; ENSP00000455607 ; ENSG00000156873 . [P15735-1 ]
    GeneIDi 5261.
    KEGGi hsa:5261.
    UCSCi uc002dzk.2. human. [P15735-1 ]
    uc021tgo.1. human. [P15735-2 ]

    Organism-specific databases

    CTDi 5261.
    GeneCardsi GC16P030759.
    GeneReviewsi PHKG2.
    HGNCi HGNC:8931. PHKG2.
    HPAi HPA055455.
    MIMi 172471. gene.
    613027. phenotype.
    neXtProti NX_P15735.
    Orphaneti 264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
    PharmGKBi PA33272.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233016.
    HOVERGENi HBG106193.
    InParanoidi P15735.
    KOi K00871.
    OrthoDBi EOG7JMGDM.
    PhylomeDBi P15735.
    TreeFami TF320349.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08155-MONOMER.
    BRENDAi 2.7.11.19. 2681.
    Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).
    SignaLinki P15735.

    Miscellaneous databases

    ChiTaRSi PHKG2. human.
    GeneWikii PHKG2.
    GenomeRNAii 5261.
    NextBioi 20322.
    PROi P15735.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15735.
    Bgeei P15735.
    CleanExi HS_PHKG2.
    Genevestigatori P15735.

    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. "Messenger ribonucleic acid encoding an apparent isoform of phosphorylase kinase catalytic subunit is abundant in the adult testis."
      Hanks S.K.
      Mol. Endocrinol. 3:110-116(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Liver glycogenosis due to phosphorylase kinase deficiency: PHKG2 gene structure and mutations associated with cirrhosis."
      Burwinkel B., Shiomi S., Al Zaben A., Kilimann M.W.
      Hum. Mol. Genet. 7:149-154(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Tissue: Liver.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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.
    6. "Homology probing: identification of cDNA clones encoding members of the protein-serine kinase family."
      Hanks S.K.
      Proc. Natl. Acad. Sci. U.S.A. 84:388-392(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 129-273.
    7. "Autosomal recessive liver phosphorylase kinase deficiency caused by a novel splice-site mutation in the gene encoding the liver gamma subunit (PHKG2)."
      van Beurden E.A., de Graaf M., Wendel U., Gitzelmann R., Berger R., van den Berg I.E.
      Biochem. Biophys. Res. Commun. 236:544-548(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN GSD9C.
    8. "Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure."
      Brushia R.J., Walsh D.A.
      Front. Biosci. 4:D618-D641(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, STRUCTURE.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Structure of human phosphorylase kinase, gamma 2."
      Structural genomics consortium (SGC)
      Submitted (FEB-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 6-293 IN COMPLEX WITH INHIBITOR.
    11. "Mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit (PHKG2) cause autosomal liver glycogenosis in the gsd rat and in humans."
      Maichele A.J., Burwinkel B., Maire I., Sovik O., Kilimann M.W.
      Nat. Genet. 14:337-340(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSD9C GLU-106 AND GLU-189.
    12. "Severe phenotype of phosphorylase kinase-deficient liver glycogenosis with mutations in the PHKG2 gene."
      Burwinkel B., Rootwelt T., Kvittingen E.A., Chakraborty P.K., Kilimann M.W.
      Pediatr. Res. 54:834-839(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSD9C LYS-157 AND ASN-215.
    13. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-317.

    Entry informationi

    Entry nameiPHKG2_HUMAN
    AccessioniPrimary (citable) accession number: P15735
    Secondary accession number(s): A8K0C7
    , B4DEB7, E9PEU3, P11800
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 166 of the entry and version 1 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, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3