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Protein

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Gene

Pck1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Enzyme regulationi

Enzyme activity is enhanced by acetylation.By similarity

Pathwayi

Sites

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

Regions

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

GO - Molecular functioni

GO - Biological processi

  • cellular response to potassium ion starvation Source: MGI
  • gluconeogenesis Source: MGI
  • glucose homeostasis Source: Ensembl
  • glucose metabolic process Source: MGI
  • glycerol biosynthetic process from pyruvate Source: MGI
  • internal protein amino acid acetylation Source: UniProtKB
  • lipid metabolic process Source: MGI
  • oxaloacetate metabolic process Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter in response to acidic pH Source: MGI
  • response to activity Source: Ensembl
  • response to insulin Source: MGI
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_308431. Gluconeogenesis.
REACT_329645. 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 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97501. Pck1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]PRO_0000103628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei70 – 701N6-acetyllysine; by p300/EP300By similarity
Modified residuei71 – 711N6-acetyllysine; by p300/EP300By similarity
Modified residuei286 – 2861PhosphoserineBy 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).By similarity
Ubiquitination by UBR5 leads to proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1274.
GeneTreeiENSGT00390000001912.
HOGENOMiHOG000191700.
HOVERGENiHBG053651.
InParanoidiQ9Z2V4.
KOiK01596.
OMAiHIHICDG.
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

        10         20         30         40         50
MPPQLHNGLD FSAKVIQGSL DSLPQAVRKF VEGNAQLCQP EYIHICDGSE
60 70 80 90 100
EEYGQLLAHM QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR
110 120 130 140 150
DTVPIPKTGL SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG
160 170 180 190 200
SPLAKIGIEL TDSPYVVASM RIMTRMGISV LEALGDGEFI KCLHSVGCPL
210 220 230 240 250
PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRI
260 270 280 290 300
ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPSL
310 320 330 340 350
PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT
360 370 380 390 400
IQKNTIFTNV AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDAEPCA
410 420 430 440 450
HPNSRFCTPA SQCPIIDPAW ESPEGVPIEG IIFGGRRPEG VPLVYEALSW
460 470 480 490 500
QHGVFVGAAM RSEATAAAEH KGKIIMHDPF AMRPFFGYNF GKYLAHWLSM
510 520 530 540 550
AHRPAAKLPK IFHVNWFRKD KDGKFLWPGF GENSRVLEWM FGRIEGEDSA
560 570 580 590 600
KLTPIGYIPK ENALNLKGLG GVNVEELFGI SKEFWEKEVE EIDRYLEDQV
610 620
NTDLPYEIER ELRALKQRIS QM
Length:622
Mass (Da):69,355
Last modified:May 1, 1999 - v1
Checksum:i9D94738B4A0EE196
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9Z2V4.
SMRiQ9Z2V4. Positions 1-622.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9Z2V4.

Proteomic databases

MaxQBiQ9Z2V4.
PaxDbiQ9Z2V4.
PRIDEiQ9Z2V4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5105.
MGIiMGI:97501. Pck1.

Phylogenomic databases

eggNOGiCOG1274.
GeneTreeiENSGT00390000001912.
HOGENOMiHOG000191700.
HOVERGENiHBG053651.
InParanoidiQ9Z2V4.
KOiK01596.
OMAiHIHICDG.
OrthoDBiEOG7KSX81.
PhylomeDBiQ9Z2V4.
TreeFamiTF314402.

Enzyme and pathway databases

UniPathwayiUPA00138.
ReactomeiREACT_308431. Gluconeogenesis.
REACT_329645. Abacavir metabolism.
SABIO-RKQ9Z2V4.

Miscellaneous databases

ChiTaRSiPck1. mouse.
NextBioi294300.
PROiQ9Z2V4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2V4.
CleanExiMM_PCK1.
GenevestigatoriQ9Z2V4.

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.