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P35558

- PCKGC_HUMAN

UniProt

P35558 - PCKGC_HUMAN

Protein

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Gene

PCK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.

    Catalytic activityi

    GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

    Cofactori

    Binds 1 manganese ion per subunit.1 Publication

    Enzyme regulationi

    Enzyme activity is enhanced by acetylation.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei87 – 871Substrate
    Binding sitei237 – 2371Substrate; via amide nitrogen
    Metal bindingi244 – 2441Manganese1 Publication
    Binding sitei244 – 2441SubstrateBy similarity
    Metal bindingi264 – 2641Manganese; via tele nitrogen1 Publication
    Binding sitei286 – 2861SubstrateBy similarity
    Active sitei288 – 2881
    Metal bindingi311 – 3111Manganese1 Publication
    Binding sitei405 – 4051GTP
    Binding sitei436 – 4361GTP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi287 – 2926GTP
    Nucleotide bindingi530 – 5334GTP

    GO - Molecular functioni

    1. carboxylic acid binding Source: BHF-UCL
    2. GDP binding Source: Ensembl
    3. GTP binding Source: BHF-UCL
    4. magnesium ion binding Source: BHF-UCL
    5. manganese ion binding Source: BHF-UCL
    6. phosphoenolpyruvate carboxykinase (GTP) activity Source: BHF-UCL

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. drug metabolic process Source: Reactome
    3. gluconeogenesis Source: BHF-UCL
    4. glucose homeostasis Source: BHF-UCL
    5. glucose metabolic process Source: BHF-UCL
    6. glycerol biosynthetic process from pyruvate Source: BHF-UCL
    7. internal protein amino acid acetylation Source: UniProtKB
    8. oxaloacetate metabolic process Source: Ensembl
    9. response to activity Source: Ensembl
    10. response to insulin Source: BHF-UCL
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Gluconeogenesis

    Keywords - Ligandi

    GTP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04751-MONOMER.
    ReactomeiREACT_121388. Abacavir metabolism.
    REACT_1520. Gluconeogenesis.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SABIO-RKP35558.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (EC:4.1.1.32)
    Short name:
    PEPCK-C
    Gene namesi
    Name:PCK1
    Synonyms:PEPCK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:8724. PCK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD) [MIM:261680]: Metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autopsy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701K → R: Abolishes acetylation and increases protein stability; when associated with R-71 and R-594. 1 Publication
    Mutagenesisi71 – 711K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-594. 1 Publication
    Mutagenesisi594 – 5941K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-71. 1 Publication

    Organism-specific databases

    MIMi261680. phenotype.
    Orphaneti79316. Phosphoenolpyruvate carboxykinase 1 deficiency.
    PharmGKBiPA33069.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 622622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]PRO_0000103627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6-acetyllysine; by p300/EP3002 Publications
    Modified residuei71 – 711N6-acetyllysine; by p300/EP3002 Publications
    Modified residuei594 – 5941N6-acetyllysine; by p300/EP3002 Publications

    Post-translational modificationi

    Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5, acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2.2 Publications
    Ubiquitination by UBR5 leads to proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiP35558.
    PaxDbiP35558.
    PRIDEiP35558.

    PTM databases

    PhosphoSiteiP35558.

    Expressioni

    Tissue specificityi

    Major sites of expression are liver, kidney and adipocytes.

    Inductioni

    Regulated by cAMP and insulin.1 Publication

    Gene expression databases

    ArrayExpressiP35558.
    BgeeiP35558.
    CleanExiHS_PCK1.
    GenevestigatoriP35558.

    Organism-specific databases

    HPAiCAB017027.
    HPA006277.
    HPA006507.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi111136. 75 interactions.
    IntActiP35558. 1 interaction.
    MINTiMINT-3013923.
    STRINGi9606.ENSP00000319814.

    Structurei

    Secondary structure

    1
    622
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 144
    Beta strandi15 – 184
    Helixi20 – 223
    Helixi25 – 3814
    Beta strandi41 – 455
    Helixi50 – 6213
    Beta strandi65 – 684
    Beta strandi72 – 743
    Beta strandi76 – 783
    Beta strandi84 – 863
    Helixi89 – 913
    Beta strandi92 – 954
    Helixi99 – 1024
    Beta strandi107 – 1093
    Helixi119 – 12911
    Turni131 – 1366
    Beta strandi137 – 15014
    Beta strandi155 – 1628
    Helixi164 – 17310
    Beta strandi174 – 1774
    Helixi178 – 1847
    Beta strandi190 – 1956
    Helixi214 – 2163
    Beta strandi218 – 2225
    Helixi223 – 2253
    Beta strandi227 – 2326
    Helixi236 – 2394
    Helixi242 – 2487
    Helixi249 – 25810
    Beta strandi261 – 2644
    Beta strandi266 – 2716
    Beta strandi277 – 2837
    Helixi290 – 2945
    Beta strandi304 – 3118
    Beta strandi313 – 3175
    Beta strandi321 – 3266
    Beta strandi330 – 3356
    Turni341 – 3433
    Helixi345 – 3506
    Beta strandi356 – 3594
    Beta strandi361 – 3633
    Beta strandi388 – 3914
    Beta strandi395 – 3973
    Beta strandi405 – 4095
    Helixi410 – 4123
    Turni418 – 4214
    Beta strandi426 – 4349
    Beta strandi438 – 4403
    Beta strandi443 – 4464
    Helixi450 – 4589
    Beta strandi461 – 4633
    Beta strandi475 – 4773
    Helixi479 – 4813
    Turni483 – 4853
    Helixi490 – 49910
    Helixi500 – 5023
    Beta strandi510 – 5145
    Beta strandi525 – 5273
    Helixi530 – 5334
    Helixi534 – 54411
    Beta strandi550 – 5534
    Beta strandi556 – 5594
    Turni561 – 5633
    Helixi574 – 5774
    Helixi582 – 60019
    Helixi601 – 6033
    Helixi606 – 62015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KHBX-ray1.85A1-622[»]
    1KHEX-ray2.40A1-622[»]
    1KHFX-ray2.02A1-622[»]
    1KHGX-ray2.34A1-622[»]
    1M51X-ray2.25A1-622[»]
    1NHXX-ray2.10A1-622[»]
    2GMVX-ray2.30A/B1-622[»]
    ProteinModelPortaliP35558.
    SMRiP35558. Positions 10-622.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35558.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni403 – 4053Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1274.
    HOGENOMiHOG000191700.
    HOVERGENiHBG053651.
    InParanoidiP35558.
    KOiK01596.
    OMAiPDHIHIC.
    OrthoDBiEOG7KSX81.
    PhylomeDBiP35558.
    TreeFamiTF314402.

    Family and domain databases

    Gene3Di3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPiMF_00452. PEPCK_GTP.
    InterProiIPR018091. PEP_carboxykin_GTP_CS.
    IPR013035. PEP_carboxykinase_C.
    IPR008209. PEP_carboxykinase_GTP.
    IPR008210. PEP_carboxykinase_N.
    [Graphical view]
    PANTHERiPTHR11561. PTHR11561. 1 hit.
    PfamiPF00821. PEPCK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
    SUPFAMiSSF68923. SSF68923. 1 hit.
    PROSITEiPS00505. PEPCK_GTP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P35558-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPQLQNGLN LSAKVVQGSL DSLPQAVREF LENNAELCQP DHIHICDGSE    50
    EENGRLLGQM EEEGILRRLK KYDNCWLALT DPRDVARIES KTVIVTQEQR 100
    DTVPIPKTGL SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG 150
    SPLSKIGIEL TDSPYVVASM RIMTRMGTPV LEAVGDGEFV KCLHSVGCPL 200
    PLQKPLVNNW PCNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRM 250
    ASRLAKEEGW LAEHMLILGI TNPEGEKKYL AAAFPSACGK TNLAMMNPSL 300
    PGWKVECVGD DIAWMKFDAQ GHLRAINPEN GFFGVAPGTS VKTNPNAIKT 350
    IQKNTIFTNV AETSDGGVYW EGIDEPLASG VTITSWKNKE WSSEDGEPCA 400
    HPNSRFCTPA SQCPIIDAAW ESPEGVPIEG IIFGGRRPAG VPLVYEALSW 450
    QHGVFVGAAM RSEATAAAEH KGKIIMHDPF AMRPFFGYNF GKYLAHWLSM 500
    AQHPAAKLPK IFHVNWFRKD KEGKFLWPGF GENSRVLEWM FNRIDGKAST 550
    KLTPIGYIPK EDALNLKGLG HINMMELFSI SKEFWEKEVE DIEKYLEDQV 600
    NADLPCEIER EILALKQRIS QM 622
    Length:622
    Mass (Da):69,195
    Last modified:March 7, 2006 - v3
    Checksum:i78D309E0845CC181
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti250 – 2501M → N in AAA02558. (PubMed:8325643)Curated
    Sequence conflicti256 – 2561K → E in AAA60084. (PubMed:8490617)Curated
    Sequence conflicti291 – 2911T → S in AAA02558. (PubMed:8325643)Curated
    Sequence conflicti551 – 5522KL → NV in AAA60084. (PubMed:8490617)Curated
    Sequence conflicti597 – 5971E → V in AAA60084. (PubMed:8490617)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551R → Q.1 Publication
    Corresponds to variant rs28383585 [ dbSNP | Ensembl ].
    VAR_021072
    Natural varianti60 – 601M → T.1 Publication
    Corresponds to variant rs28383586 [ dbSNP | Ensembl ].
    VAR_021073
    Natural varianti138 – 1381T → I.1 Publication
    Corresponds to variant rs28359542 [ dbSNP | Ensembl ].
    VAR_021074
    Natural varianti184 – 1841V → L.5 Publications
    Corresponds to variant rs707555 [ dbSNP | Ensembl ].
    VAR_021075
    Natural varianti267 – 2671I → V.2 Publications
    Corresponds to variant rs8192708 [ dbSNP | Ensembl ].
    VAR_015575
    Natural varianti276 – 2761E → K.1 Publication
    Corresponds to variant rs11552145 [ dbSNP | Ensembl ].
    VAR_021076
    Natural varianti368 – 3681V → I.1 Publication
    Corresponds to variant rs1804160 [ dbSNP | Ensembl ].
    VAR_021077
    Natural varianti427 – 4271P → S.1 Publication
    Corresponds to variant rs28359550 [ dbSNP | Ensembl ].
    VAR_021078
    Natural varianti586 – 5861E → D.1 Publication
    Corresponds to variant rs1042529 [ dbSNP | Ensembl ].
    VAR_042444

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05144 mRNA. Translation: AAA60084.1.
    L12760 Genomic DNA. Translation: AAA02558.1.
    AY794987 Genomic DNA. Translation: AAV50001.1.
    AK290802 mRNA. Translation: BAF83491.1.
    AL035541 Genomic DNA. Translation: CAB55863.1.
    CH471077 Genomic DNA. Translation: EAW75514.1.
    BC023978 mRNA. Translation: AAH23978.1.
    U31519 Genomic DNA. Translation: AAA91026.1.
    CCDSiCCDS13460.1.
    PIRiA45746.
    RefSeqiNP_002582.3. NM_002591.3.
    UniGeneiHs.1872.

    Genome annotation databases

    EnsembliENST00000319441; ENSP00000319814; ENSG00000124253.
    GeneIDi5105.
    KEGGihsa:5105.
    UCSCiuc002xyn.4. human.

    Polymorphism databases

    DMDMi93138710.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05144 mRNA. Translation: AAA60084.1 .
    L12760 Genomic DNA. Translation: AAA02558.1 .
    AY794987 Genomic DNA. Translation: AAV50001.1 .
    AK290802 mRNA. Translation: BAF83491.1 .
    AL035541 Genomic DNA. Translation: CAB55863.1 .
    CH471077 Genomic DNA. Translation: EAW75514.1 .
    BC023978 mRNA. Translation: AAH23978.1 .
    U31519 Genomic DNA. Translation: AAA91026.1 .
    CCDSi CCDS13460.1.
    PIRi A45746.
    RefSeqi NP_002582.3. NM_002591.3.
    UniGenei Hs.1872.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KHB X-ray 1.85 A 1-622 [» ]
    1KHE X-ray 2.40 A 1-622 [» ]
    1KHF X-ray 2.02 A 1-622 [» ]
    1KHG X-ray 2.34 A 1-622 [» ]
    1M51 X-ray 2.25 A 1-622 [» ]
    1NHX X-ray 2.10 A 1-622 [» ]
    2GMV X-ray 2.30 A/B 1-622 [» ]
    ProteinModelPortali P35558.
    SMRi P35558. Positions 10-622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111136. 75 interactions.
    IntActi P35558. 1 interaction.
    MINTi MINT-3013923.
    STRINGi 9606.ENSP00000319814.

    Chemistry

    BindingDBi P35558.
    ChEMBLi CHEMBL2911.

    PTM databases

    PhosphoSitei P35558.

    Polymorphism databases

    DMDMi 93138710.

    Proteomic databases

    MaxQBi P35558.
    PaxDbi P35558.
    PRIDEi P35558.

    Protocols and materials databases

    DNASUi 5105.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319441 ; ENSP00000319814 ; ENSG00000124253 .
    GeneIDi 5105.
    KEGGi hsa:5105.
    UCSCi uc002xyn.4. human.

    Organism-specific databases

    CTDi 5105.
    GeneCardsi GC20P056136.
    H-InvDB HIX0015941.
    HGNCi HGNC:8724. PCK1.
    HPAi CAB017027.
    HPA006277.
    HPA006507.
    MIMi 261680. phenotype.
    614168. gene.
    neXtProti NX_P35558.
    Orphaneti 79316. Phosphoenolpyruvate carboxykinase 1 deficiency.
    PharmGKBi PA33069.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1274.
    HOGENOMi HOG000191700.
    HOVERGENi HBG053651.
    InParanoidi P35558.
    KOi K01596.
    OMAi PDHIHIC.
    OrthoDBi EOG7KSX81.
    PhylomeDBi P35558.
    TreeFami TF314402.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BioCyci MetaCyc:HS04751-MONOMER.
    Reactomei REACT_121388. Abacavir metabolism.
    REACT_1520. Gluconeogenesis.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SABIO-RK P35558.

    Miscellaneous databases

    ChiTaRSi PCK1. human.
    EvolutionaryTracei P35558.
    GeneWikii PCK1.
    GenomeRNAii 5105.
    NextBioi 19702.
    PROi P35558.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35558.
    Bgeei P35558.
    CleanExi HS_PCK1.
    Genevestigatori P35558.

    Family and domain databases

    Gene3Di 3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPi MF_00452. PEPCK_GTP.
    InterProi IPR018091. PEP_carboxykin_GTP_CS.
    IPR013035. PEP_carboxykinase_C.
    IPR008209. PEP_carboxykinase_GTP.
    IPR008210. PEP_carboxykinase_N.
    [Graphical view ]
    PANTHERi PTHR11561. PTHR11561. 1 hit.
    Pfami PF00821. PEPCK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001348. PEP_carboxykinase_GTP. 1 hit.
    SUPFAMi SSF68923. SSF68923. 1 hit.
    PROSITEi PS00505. PEPCK_GTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA sequence and localization of polymorphic human cytosolic phosphoenolpyruvate carboxykinase gene (PCK1) to chromosome 20, band q13.31: PCK1 is not tightly linked to maturity-onset diabetes of the young."
      Stoffel M., Xiang K.S., Espinosa R. III, Cox N.J., le Beau M.M., Bell G.I.
      Hum. Mol. Genet. 2:1-4(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-184 AND ASP-586.
    2. "Phosphoenolpyruvate carboxykinase (GTP): characterization of the human PCK1 gene and localization distal to MODY on chromosome 20."
      Ting C.-N., Burgess D.L., Chamberlain J.S., Keith T.P., Falls K., Meisler M.H.
      Genomics 16:698-706(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-184.
      Tissue: Liver.
    3. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-55; THR-60; ILE-138; VAL-267; LYS-276; ILE-368 AND SER-427.
    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], VARIANT LEU-184.
      Tissue: Kidney.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-184.
    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], VARIANTS LEU-184 AND VAL-267.
      Tissue: Kidney.
    8. "Structural and functional analysis of the human phosphoenolpyruvate carboxykinase gene promoter."
      O'Brien R.M., Printz R.L., Halmi N., Tiesinga J.J., Granner D.K.
      Biochim. Biophys. Acta 1264:284-288(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
    9. "Regulation of phosphoenolpyruvate carboxykinase (GTP) gene transcription."
      Liu J., Hanson R.W.
      Mol. Cell. Biochem. 104:89-100(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. Cited for: ACETYLATION AT LYS-70; LYS-71 AND LYS-594, ENZYME REGULATION, MUTAGENESIS OF LYS-70; LYS-71 AND LYS-594, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase."
      Jiang W., Wang S., Xiao M., Lin Y., Zhou L., Lei Q., Xiong Y., Guan K.L., Zhao S.
      Mol. Cell 43:33-44(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-70; LYS-71 AND LYS-594, DEACETYLATION BY SIRT2, UBIQUITINATION BY UBR5.
    12. "Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site."
      Dunten P., Belunis C., Crowther R., Hollfelder K., Kammlott U., Levin W., Michel H., Ramsey G.B., Swain A., Weber D., Wertheimer S.J.
      J. Mol. Biol. 316:257-264(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GTP ANALOG; PEP AND MANGANESE, GTP-BINDING SITE, COFACTOR.

    Entry informationi

    Entry nameiPCKGC_HUMAN
    AccessioniPrimary (citable) accession number: P35558
    Secondary accession number(s): A8K437, Q8TCA3, Q9UJD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 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

    Miscellaneous

    In eukaryotes there are two isozymes: a cytoplasmic one and a mitochondrial one.

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3