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P35558 (PCKGC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Short name=PEPCK-C
EC=4.1.1.32
Gene names
Name:PCK1
Synonyms:PEPCK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00452

Catalytic activity

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2. HAMAP-Rule MF_00452

Cofactor

Binds 1 manganese ion per subunit. Ref.12

Enzyme regulation

Enzyme activity is enhanced by acetylation. Ref.10

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_00452

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00452.

Tissue specificity

Major sites of expression are liver, kidney and adipocytes.

Induction

Regulated by cAMP and insulin. Ref.9 Ref.10

Post-translational modification

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. Ref.10 Ref.11

Ubiquitination by UBR5 leads to proteasomal degradation. HAMAP-Rule MF_00452

Involvement in disease

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.

Miscellaneous

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

Sequence similarities

Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionDecarboxylase
Lyase
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

drug metabolic process

Traceable author statement. Source: Reactome

gluconeogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

glucose homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

glucose metabolic process

Inferred from mutant phenotype PubMed 14764811. Source: BHF-UCL

glycerol biosynthetic process from pyruvate

Inferred from sequence or structural similarity. Source: BHF-UCL

internal protein amino acid acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

oxaloacetate metabolic process

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from direct assay PubMed 14764811. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functionGDP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from direct assay Ref.12. Source: BHF-UCL

carboxylic acid binding

Inferred from direct assay Ref.12. Source: BHF-UCL

magnesium ion binding

Inferred from direct assay Ref.12. Source: BHF-UCL

manganese ion binding

Inferred from direct assay Ref.12. Source: BHF-UCL

phosphoenolpyruvate carboxykinase (GTP) activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Phosphoenolpyruvate carboxykinase, cytosolic [GTP] HAMAP-Rule MF_00452
PRO_0000103627

Regions

Nucleotide binding287 – 2926GTP HAMAP-Rule MF_00452
Nucleotide binding530 – 5334GTP HAMAP-Rule MF_00452
Region403 – 4053Substrate binding HAMAP-Rule MF_00452

Sites

Active site2881
Metal binding2441Manganese
Metal binding2641Manganese; via tele nitrogen
Metal binding3111Manganese
Binding site871Substrate
Binding site2371Substrate; via amide nitrogen
Binding site2441Substrate By similarity
Binding site2861Substrate By similarity
Binding site4051GTP
Binding site4361GTP

Amino acid modifications

Modified residue701N6-acetyllysine; by p300/EP300 Ref.10 Ref.11
Modified residue711N6-acetyllysine; by p300/EP300 Ref.10 Ref.11
Modified residue5941N6-acetyllysine; by p300/EP300 Ref.10 Ref.11

Natural variations

Natural variant551R → Q. Ref.3
Corresponds to variant rs28383585 [ dbSNP | Ensembl ].
VAR_021072
Natural variant601M → T. Ref.3
Corresponds to variant rs28383586 [ dbSNP | Ensembl ].
VAR_021073
Natural variant1381T → I. Ref.3
Corresponds to variant rs28359542 [ dbSNP | Ensembl ].
VAR_021074
Natural variant1841V → L. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7
Corresponds to variant rs707555 [ dbSNP | Ensembl ].
VAR_021075
Natural variant2671I → V. Ref.3 Ref.7
Corresponds to variant rs8192708 [ dbSNP | Ensembl ].
VAR_015575
Natural variant2761E → K. Ref.3
Corresponds to variant rs11552145 [ dbSNP | Ensembl ].
VAR_021076
Natural variant3681V → I. Ref.3
Corresponds to variant rs1804160 [ dbSNP | Ensembl ].
VAR_021077
Natural variant4271P → S. Ref.3
Corresponds to variant rs28359550 [ dbSNP | Ensembl ].
VAR_021078
Natural variant5861E → D. Ref.1
Corresponds to variant rs1042529 [ dbSNP | Ensembl ].
VAR_042444

Experimental info

Mutagenesis701K → R: Abolishes acetylation and increases protein stability; when associated with R-71 and R-594. Ref.10
Mutagenesis711K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-594. Ref.10
Mutagenesis5941K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-71. Ref.10
Sequence conflict2501M → N in AAA02558. Ref.2
Sequence conflict2561K → E in AAA60084. Ref.1
Sequence conflict2911T → S in AAA02558. Ref.2
Sequence conflict551 – 5522KL → NV in AAA60084. Ref.1
Sequence conflict5971E → V in AAA60084. Ref.1

Secondary structure

............................................................................................................................ 622
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35558 [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: 78D309E0845CC181

FASTA62269,195
        10         20         30         40         50         60 
MPPQLQNGLN LSAKVVQGSL DSLPQAVREF LENNAELCQP DHIHICDGSE EENGRLLGQM 

        70         80         90        100        110        120 
EEEGILRRLK KYDNCWLALT DPRDVARIES KTVIVTQEQR DTVPIPKTGL SQLGRWMSEE 

       130        140        150        160        170        180 
DFEKAFNARF PGCMKGRTMY VIPFSMGPLG SPLSKIGIEL TDSPYVVASM RIMTRMGTPV 

       190        200        210        220        230        240 
LEAVGDGEFV KCLHSVGCPL PLQKPLVNNW PCNPELTLIA HLPDRREIIS FGSGYGGNSL 

       250        260        270        280        290        300 
LGKKCFALRM ASRLAKEEGW LAEHMLILGI TNPEGEKKYL AAAFPSACGK TNLAMMNPSL 

       310        320        330        340        350        360 
PGWKVECVGD DIAWMKFDAQ GHLRAINPEN GFFGVAPGTS VKTNPNAIKT IQKNTIFTNV 

       370        380        390        400        410        420 
AETSDGGVYW EGIDEPLASG VTITSWKNKE WSSEDGEPCA HPNSRFCTPA SQCPIIDAAW 

       430        440        450        460        470        480 
ESPEGVPIEG IIFGGRRPAG VPLVYEALSW QHGVFVGAAM RSEATAAAEH KGKIIMHDPF 

       490        500        510        520        530        540 
AMRPFFGYNF GKYLAHWLSM AQHPAAKLPK IFHVNWFRKD KEGKFLWPGF GENSRVLEWM 

       550        560        570        580        590        600 
FNRIDGKAST KLTPIGYIPK EDALNLKGLG HINMMELFSI SKEFWEKEVE DIEKYLEDQV 

       610        620 
NADLPCEIER EILALKQRIS QM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Regulation of cellular metabolism by protein lysine acetylation."
Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L., Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L., Chin J., Yang P. expand/collapse author list , Chen X., Lei Q., Xiong Y., Guan K.L.
Science 327:1000-1004(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA45746.
RefSeqNP_002582.3. NM_002591.3.
UniGeneHs.1872.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP35558.
SMRP35558. Positions 10-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111136. 75 interactions.
IntActP35558. 1 interaction.
MINTMINT-3013923.
STRING9606.ENSP00000319814.

Chemistry

BindingDBP35558.
ChEMBLCHEMBL2911.

PTM databases

PhosphoSiteP35558.

Polymorphism databases

DMDM93138710.

Proteomic databases

PaxDbP35558.
PRIDEP35558.

Protocols and materials databases

DNASU5105.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319441; ENSP00000319814; ENSG00000124253.
GeneID5105.
KEGGhsa:5105.
UCSCuc002xyn.4. human.

Organism-specific databases

CTD5105.
GeneCardsGC20P056136.
H-InvDBHIX0015941.
HGNCHGNC:8724. PCK1.
HPACAB017027.
HPA006277.
HPA006507.
MIM261680. phenotype.
614168. gene.
neXtProtNX_P35558.
Orphanet79316. Phosphoenolpyruvate carboxykinase 1 deficiency.
PharmGKBPA33069.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1274.
HOGENOMHOG000191700.
HOVERGENHBG053651.
InParanoidP35558.
KOK01596.
OMAVNADLPC.
OrthoDBEOG7KSX81.
PhylomeDBP35558.
TreeFamTF314402.

Enzyme and pathway databases

BioCycMetaCyc:HS04751-MONOMER.
ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.
SABIO-RKP35558.
UniPathwayUPA00138.

Gene expression databases

ArrayExpressP35558.
BgeeP35558.
CleanExHS_PCK1.
GenevestigatorP35558.

Family and domain databases

Gene3D3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPMF_00452. PEPCK_GTP.
InterProIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERPTHR11561. PTHR11561. 1 hit.
PfamPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMSSF68923. SSF68923. 1 hit.
PROSITEPS00505. PEPCK_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPCK1. human.
EvolutionaryTraceP35558.
GeneWikiPCK1.
GenomeRNAi5105.
NextBio19702.
PROP35558.
SOURCESearch...

Entry information

Entry namePCKGC_HUMAN
AccessionPrimary (citable) accession number: P35558
Secondary accession number(s): A8K437, Q8TCA3, Q9UJD2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM