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Q9Z2V4

- PCKGC_MOUSE

UniProt

Q9Z2V4 - PCKGC_MOUSE

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Protein

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Gene
Pck1, Pepck
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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.UniRule annotation

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.UniRule annotation

Cofactori

Binds 1 manganese ion per subunit By similarity.UniRule annotation

Enzyme regulationi

Enzyme activity is enhanced by acetylation By similarity.UniRule annotation

Pathwayi

Sites

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

Regions

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

GO - Molecular functioni

  1. carboxylic acid binding Source: Ensembl
  2. GDP binding Source: Ensembl
  3. GTP binding Source: UniProtKB-KW
  4. magnesium ion binding Source: Ensembl
  5. manganese ion binding Source: Ensembl
  6. phosphoenolpyruvate carboxykinase (GTP) activity Source: UniProtKB-EC
  7. phosphoenolpyruvate carboxykinase activity Source: MGI

GO - Biological processi

  1. gluconeogenesis Source: MGI
  2. glucose homeostasis Source: Ensembl
  3. glycerol biosynthetic process from pyruvate Source: MGI
  4. internal protein amino acid acetylation Source: UniProtKB
  5. lipid metabolic process Source: MGI
  6. oxaloacetate metabolic process Source: Ensembl
  7. response to activity Source: Ensembl
  8. response to insulin Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_196553. Abacavir metabolism.
SABIO-RKQ9Z2V4.
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:Pepck
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:97501. Pck1.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]UniRule annotationPRO_0000103628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; by p300/EP300 By similarity
Modified residuei71 – 711N6-acetyllysine; by p300/EP300 By similarity

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 By similarity.UniRule annotation
Ubiquitination by UBR5 leads to proteasomal degradation By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ9Z2V4.
PaxDbiQ9Z2V4.
PRIDEiQ9Z2V4.

PTM databases

PhosphoSiteiQ9Z2V4.

Expressioni

Inductioni

Regulated by glucocortinoids and insulin.1 Publication

Gene expression databases

BgeeiQ9Z2V4.
CleanExiMM_PCK1.
GenevestigatoriQ9Z2V4.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiQ9Z2V4. 1 interaction.
MINTiMINT-1869570.
STRINGi10090.ENSMUSP00000029017.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2V4.
SMRiQ9Z2V4. Positions 1-622.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1274.
GeneTreeiENSGT00390000001912.
HOGENOMiHOG000191700.
HOVERGENiHBG053651.
InParanoidiQ9Z2V4.
KOiK01596.
OMAiPDHIHIC.
OrthoDBiEOG7KSX81.
PhylomeDBiQ9Z2V4.
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.

Q9Z2V4-1 [UniParc]FASTAAdd to Basket

« Hide

MPPQLHNGLD FSAKVIQGSL DSLPQAVRKF VEGNAQLCQP EYIHICDGSE    50
EEYGQLLAHM QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR 100
DTVPIPKTGL SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG 150
SPLAKIGIEL TDSPYVVASM RIMTRMGISV LEALGDGEFI KCLHSVGCPL 200
PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRI 250
ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPSL 300
PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT 350
IQKNTIFTNV AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDAEPCA 400
HPNSRFCTPA SQCPIIDPAW ESPEGVPIEG IIFGGRRPEG VPLVYEALSW 450
QHGVFVGAAM RSEATAAAEH KGKIIMHDPF AMRPFFGYNF GKYLAHWLSM 500
AHRPAAKLPK IFHVNWFRKD KDGKFLWPGF GENSRVLEWM FGRIEGEDSA 550
KLTPIGYIPK ENALNLKGLG GVNVEELFGI SKEFWEKEVE EIDRYLEDQV 600
NTDLPYEIER ELRALKQRIS QM 622
Length:622
Mass (Da):69,355
Last modified:May 1, 1999 - v1
Checksum:i9D94738B4A0EE196
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF009605 Genomic DNA. Translation: AAD01427.1.
AK028046 mRNA. Translation: BAC25718.1.
AK133496 mRNA. Translation: BAE21687.1.
AK149525 mRNA. Translation: BAE28938.1.
CCDSiCCDS17141.1.
RefSeqiNP_035174.1. NM_011044.2.
UniGeneiMm.266867.

Genome annotation databases

EnsembliENSMUST00000029017; ENSMUSP00000029017; ENSMUSG00000027513.
GeneIDi18534.
KEGGimmu:18534.
UCSCiuc008odm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF009605 Genomic DNA. Translation: AAD01427.1 .
AK028046 mRNA. Translation: BAC25718.1 .
AK133496 mRNA. Translation: BAE21687.1 .
AK149525 mRNA. Translation: BAE28938.1 .
CCDSi CCDS17141.1.
RefSeqi NP_035174.1. NM_011044.2.
UniGenei Mm.266867.

3D structure databases

ProteinModelPortali Q9Z2V4.
SMRi Q9Z2V4. Positions 1-622.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9Z2V4. 1 interaction.
MINTi MINT-1869570.
STRINGi 10090.ENSMUSP00000029017.

PTM databases

PhosphoSitei Q9Z2V4.

Proteomic databases

MaxQBi Q9Z2V4.
PaxDbi Q9Z2V4.
PRIDEi Q9Z2V4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029017 ; ENSMUSP00000029017 ; ENSMUSG00000027513 .
GeneIDi 18534.
KEGGi mmu:18534.
UCSCi uc008odm.1. mouse.

Organism-specific databases

CTDi 5105.
MGIi MGI:97501. Pck1.

Phylogenomic databases

eggNOGi COG1274.
GeneTreei ENSGT00390000001912.
HOGENOMi HOG000191700.
HOVERGENi HBG053651.
InParanoidi Q9Z2V4.
KOi K01596.
OMAi PDHIHIC.
OrthoDBi EOG7KSX81.
PhylomeDBi Q9Z2V4.
TreeFami TF314402.

Enzyme and pathway databases

UniPathwayi UPA00138 .
Reactomei REACT_196553. Abacavir metabolism.
SABIO-RK Q9Z2V4.

Miscellaneous databases

ChiTaRSi PCK1. mouse.
NextBioi 294300.
PROi Q9Z2V4.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z2V4.
CleanExi MM_PCK1.
Genevestigatori Q9Z2V4.

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

« Hide 'large scale' publications
  1. "Isolation and characterization of the mouse cytosolic phosphoenolpyruvate carboxykinase (GTP) gene: evidence for tissue-specific hypersensitive sites."
    Williams C.P., Postic C., Robin D., Robin P., Parrinello J., Shelton K., Printz R.L., Magnuson M.A., Granner D.K., Forest C., Chalkley R.
    Mol. Cell. Endocrinol. 148:67-77(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  2. "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: Liver and Ovary.
  3. "Glucocorticoids regulate transcription of the gene for phosphoenolpyruvate carboxykinase in the liver via an extended glucocorticoid regulatory unit."
    Cassuto H., Kochan K., Chakravarty K., Cohen H., Blum B., Olswang Y., Hakimi P., Xu C., Massillon D., Hanson R.W., Reshef L.
    J. Biol. Chem. 280:33873-33884(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiPCKGC_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2V4
Secondary accession number(s): Q3UEH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 121 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

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