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Q8BH04

- PCKGM_MOUSE

UniProt

Q8BH04 - PCKGM_MOUSE

Protein

Phosphoenolpyruvate carboxykinase [GTP], mitochondrial

Gene

Pck2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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.By similarity

    Catalytic activityi

    GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

    Cofactori

    Manganese.By similarity
    Binds 1 manganese ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei104 – 1041SubstrateBy similarity
    Binding sitei255 – 2551Substrate; via amide nitrogenBy similarity
    Metal bindingi262 – 2621ManganeseBy similarity
    Binding sitei262 – 2621SubstrateBy similarity
    Metal bindingi282 – 2821Manganese; via tele nitrogenBy similarity
    Binding sitei304 – 3041SubstrateBy similarity
    Active sitei306 – 3061By similarity
    Metal bindingi329 – 3291ManganeseBy similarity
    Binding sitei423 – 4231GTPBy similarity
    Binding sitei454 – 4541GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi305 – 3106GTPBy similarity
    Nucleotide bindingi548 – 5514GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. phosphoenolpyruvate carboxykinase (GTP) activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular response to glucose stimulus Source: Ensembl
    2. gluconeogenesis Source: UniProtKB-UniPathway
    3. NADH oxidation Source: Ensembl
    4. oxaloacetate metabolic process Source: Ensembl
    5. positive regulation of insulin secretion Source: Ensembl
    6. pyruvate metabolic process Source: Ensembl
    7. response to glucocorticoid Source: Ensembl

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Gluconeogenesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxykinase [GTP], mitochondrial (EC:4.1.1.32)
    Short name:
    PEPCK-M
    Gene namesi
    Name:Pck2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1860456. Pck2.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3232MitochondrionBy similarityAdd
    BLAST
    Chaini33 – 640608Phosphoenolpyruvate carboxykinase [GTP], mitochondrialPRO_0000023569Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei457 – 4571N6-succinyllysine1 Publication

    Proteomic databases

    MaxQBiQ8BH04.
    PaxDbiQ8BH04.
    PRIDEiQ8BH04.

    PTM databases

    PhosphoSiteiQ8BH04.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BH04.
    BgeeiQ8BH04.
    GenevestigatoriQ8BH04.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    IntActiQ8BH04. 1 interaction.
    MINTiMINT-4108403.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BH04.
    SMRiQ8BH04. Positions 32-640.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni421 – 4233Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1274.
    GeneTreeiENSGT00390000001912.
    HOGENOMiHOG000191700.
    HOVERGENiHBG053651.
    InParanoidiQ8BH04.
    KOiK01596.
    OrthoDBiEOG7KSX81.
    PhylomeDBiQ8BH04.
    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.

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

    Q8BH04-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAMYLPGLR LSRHGLRPWC WSPCRSIQTL HVLSGDMSQL PAGVRDFVAR    50
    SAHLCQPEGI HICDGTEAEN TAILALLEEQ GLIRKLPKYK NCWLARTDPK 100
    DVARVESKTV IVTPSQRDTV PLLAGGARGQ LGNWMSPDEF QRAVDERFPG 150
    CMQGRIMYVL PFSMGPVGSP LSRIGVQLTD SAYVVASMRI MTRLGTPVLQ 200
    ALGDGDFIKC LHSVGQPLTG HGDPVGQWPC NPEKTLIGHV PDQREIVSFG 250
    SGYGGNSLLG KKCFALRIAS RLARDEGWLA EHMLILGITN PAGKKRYVAA 300
    AFPSACGKTN LAMMRPALPG WKVECVGDDI AWMRFDSEGQ LRAINPENGF 350
    FGVAPGTSAA TNPNAMATIQ SNTLFTNVAE TSDGGVYWEG IDQPLPPGVT 400
    ITSWLGKPWK PGDKEPCAHP NSRFCVPARQ CPIMDPAWEA PEGVPIDAII 450
    FGGRRPKGVP LVYEAFNWRH GVFVGSAMRS ESTAAAEHKG KTIMHDPFAM 500
    RPFFGYNFGR YLEHWLSMEG QKGARLPRIF HVNWFRRDEA GRFLWPGFGE 550
    NARVLDWICR RLEGEDSAQE TPIGLVPKEG ALDLSGLSAV DTSQLFSIPK 600
    DFWEQEVRDI RGYLTEQVNQ DLPKEVLAEL EALEGRVQKM 640
    Length:640
    Mass (Da):70,528
    Last modified:March 1, 2003 - v1
    Checksum:i5CE06D4DF5BBF44E
    GO

    Sequence cautioni

    The sequence BAC26991.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311H → R in AAH10318. (PubMed:15489334)Curated
    Sequence conflicti542 – 5421R → C in AAH10318. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030501 mRNA. Translation: BAC26991.1. Different initiation.
    AK031612 mRNA. Translation: BAC27477.1.
    AK034927 mRNA. Translation: BAC28883.1.
    BC010318 mRNA. Translation: AAH10318.1.
    RefSeqiNP_083270.1. NM_028994.2.
    UniGeneiMm.29856.
    Mm.491140.

    Genome annotation databases

    EnsembliENSMUST00000048781; ENSMUSP00000038555; ENSMUSG00000040618.
    GeneIDi74551.
    KEGGimmu:74551.
    UCSCiuc007tyy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030501 mRNA. Translation: BAC26991.1 . Different initiation.
    AK031612 mRNA. Translation: BAC27477.1 .
    AK034927 mRNA. Translation: BAC28883.1 .
    BC010318 mRNA. Translation: AAH10318.1 .
    RefSeqi NP_083270.1. NM_028994.2.
    UniGenei Mm.29856.
    Mm.491140.

    3D structure databases

    ProteinModelPortali Q8BH04.
    SMRi Q8BH04. Positions 32-640.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BH04. 1 interaction.
    MINTi MINT-4108403.

    PTM databases

    PhosphoSitei Q8BH04.

    Proteomic databases

    MaxQBi Q8BH04.
    PaxDbi Q8BH04.
    PRIDEi Q8BH04.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000048781 ; ENSMUSP00000038555 ; ENSMUSG00000040618 .
    GeneIDi 74551.
    KEGGi mmu:74551.
    UCSCi uc007tyy.1. mouse.

    Organism-specific databases

    CTDi 5106.
    MGIi MGI:1860456. Pck2.

    Phylogenomic databases

    eggNOGi COG1274.
    GeneTreei ENSGT00390000001912.
    HOGENOMi HOG000191700.
    HOVERGENi HBG053651.
    InParanoidi Q8BH04.
    KOi K01596.
    OrthoDBi EOG7KSX81.
    PhylomeDBi Q8BH04.
    TreeFami TF314402.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .

    Miscellaneous databases

    ChiTaRSi PCK2. mouse.
    NextBioi 341064.
    PROi Q8BH04.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BH04.
    Bgeei Q8BH04.
    Genevestigatori Q8BH04.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Pituitary and Testis.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPCKGM_MOUSE
    AccessioniPrimary (citable) accession number: Q8BH04
    Secondary accession number(s): Q8BMM9, Q91Z10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3