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Entry version 211 (29 Sep 2021)
Sequence version 3 (07 Mar 2006)
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Protein

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Gene

PCK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:30193097, PubMed:24863970, PubMed:26971250, PubMed:28216384).

Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (PubMed:30193097, PubMed:24863970, PubMed:26971250, PubMed:28216384).

At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate 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 (PubMed:30193097).

At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (PubMed:30193097).

Acts as a regulator of formation and maintenance of memory CD8+ T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity).

The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8+ T-cells homeostasis (By similarity).

In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (PubMed:32322062).

The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (PubMed:32322062).

By similarity5 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+3 PublicationsNote: Binds 1 Mn2+ ion per subunit.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phosphoenolpyruvate carboxykinase activity is regulated by acetylation and glucose levels (PubMed:20167786, PubMed:30193097). The anaplerotic conversion of phosphoenolpyruvate to oxaloacetate is improved by PCK1 acetylation on Lys-91 (K91ac), Lys-473 (K473ac) and Lys-521 (K521ac) (By similarity). High glucose concentrations favor PCK1 anaplerotic activity by triggering acetylation on Lys-91 (K91ac). At low glucose levels, SIRT1-mediated deacetylation of Lys-91 promotes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PubMed:30193097). Phosphorylation at Ser-90 reduces the binding affinity to oxaloacetate and converts the enzyme into an atypical protein kinase using GTP as donor (PubMed:32322062).By similarity3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 33 sec(-1) with oxaloacetate as substrate (for the enzyme purified from cells exposed to 10 mM glucose) (PubMed:30193097). Kcat is 21 sec(-1) with oxaloacetate as substrate (for the enzyme purified from cells exposed to 15 mM glucose) (PubMed:30193097). Kcat is 17 sec(-1) with phosphoenolpyruvate as substrate (for the enzyme purified from cells exposed to 10 mM glucose) (PubMed:30193097). Kcat is 11 sec(-1)with phosphoenolpyruvate as substrate (for the enzyme purified from cells exposed to 15 mM glucose) (PubMed:30193097). Kcat is 40 sec(-1) with GTP as substrate (for the enzyme purified from cells exposed to 10 mM glucose) (PubMed:30193097). Kcat is 22 sec(-1) with GTP as substrate (for the enzyme purified from cells exposed to 15 mM glucose) (PubMed:30193097). Kcat is 16 sec(-1) with GDP as substrate (for the enzyme purified from cells exposed to 10 mM glucose) (PubMed:30193097). Kcat is 11 sec(-1) with GDP as substrate (for the enzyme purified from cells exposed to 15 mM glucose) (PubMed:30193097).1 Publication
  1. KM=35 µM for oxaloacetate (for the enzyme purified from cells exposed to 10 mM glucose)1 Publication
  2. KM=46 µM for oxaloacetate (for the enzyme purified from cells exposed to 15 mM glucose)1 Publication
  3. KM=170 µM for GTP (for the enzyme purified from cells exposed to 10 mM glucose)1 Publication
  4. KM=151 µM for GTP (for the enzyme purified from cells exposed to 15 mM glucose)1 Publication
  5. KM=208 µM for phosphoenolpyruvate (for the enzyme purified from cells exposed to 10 mM glucose)1 Publication
  6. KM=87 µM for phosphoenolpyruvate (for the enzyme purified from cells exposed to 15 mM glucose)1 Publication
  7. KM=63 µM for GDP (for the enzyme purified from cells exposed to 10 mM glucose)1 Publication
  8. KM=29 µM for GDP (for the enzyme purified from cells exposed to 15 mM glucose)1 Publication
  9. KM=1.15 mM for GTP (in a protein kinase activity assay when not phosphorylated at Ser-90)1 Publication
  10. KM=0.21 mM for GTP (in a protein kinase activity assay when using a phosphomimetic mutant at Ser-90)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.4 Publications
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei87Substrate3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi244Manganese3 Publications1
Metal bindingi264Manganese; via tele nitrogen3 Publications1
Binding sitei286SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2881 Publication1 Publication1
Metal bindingi311Manganese3 Publications1
Binding sitei405GTP1 Publication1
Binding sitei436GTP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi287 – 292GTP1 Publication6
Nucleotide bindingi530 – 533GTP3 Publications4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDecarboxylase, Kinase, Lyase, Transferase
Biological processGluconeogenesis
LigandGTP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS04751-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
4.1.1.32, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P35558

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2161541, Abacavir metabolism
R-HSA-381340, Transcriptional regulation of white adipocyte differentiation
R-HSA-70263, Gluconeogenesis
R-HSA-9615017, FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
R-HSA-9632974, NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P35558

SIGNOR Signaling Network Open Resource

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SIGNORi
P35558

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00138

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase, cytosolic [GTP]Curated (EC:4.1.1.324 Publications)
Short name:
PEPCK-C
Alternative name(s):
Serine-protein kinase PCK1Curated (EC:2.7.11.-1 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PCK11 PublicationImported
Synonyms:PEPCK11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:8724, PCK1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
614168, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P35558

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000124253

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Phosphoenolpyruvate carboxykinase deficiency, cytosolic (PCKDC)3 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive metabolic disorder characterized by impaired gluconeogenesis, hypoglycemia, hypotonia, hepatomegaly, hepatic dysfunction, failure to thrive, lactic acidosis, and elevated tricarboxylic acid intermediates, particularly fumarate, in urine.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07963345I → T in PCKDC; decreased stability; no effect on phosphoenolpyruvate carboxykinase activity. 1 PublicationCorresponds to variant dbSNP:rs202197769EnsemblClinVar.1
Natural variantiVAR_079634309G → R in PCKDC; unknown pathological significance; decreased phosphoenolpyruvate carboxykinase activity. 1 PublicationCorresponds to variant dbSNP:rs201186470EnsemblClinVar.1
Natural variantiVAR_079635440 – 443Missing in PCKDC; decreased phosphoenolpyruvate carboxykinase activity. 1 Publication4

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi70K → R: Abolishes acetylation and increases protein stability; when associated with R-71 and R-594. 1 Publication1
Mutagenesisi71K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-594. 1 Publication1
Mutagenesisi90S → A: Abolished phosphorylation by AKT1, interaction with INSIG proteins (INSIG1 and INSIG2) and ability to regulate lipogenesis. 1 Publication1
Mutagenesisi90S → E: Phosphomimetic mutant, promotes the serine protein kinase activity by reducing the binding affinity to oxaloacetate. 1 Publication1
Mutagenesisi288C → S: Abolished both phosphoenolpyruvate carboxykinase and protein kinase activities. 1 Publication1
Mutagenesisi594K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-71. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
5105

MalaCards human disease database

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MalaCardsi
PCK1
MIMi261680, phenotype

Open Targets

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OpenTargetsi
ENSG00000124253

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2880, Phosphoenolpyruvate carboxykinase deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33069

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P35558, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2911

Drug and drug target database

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DrugBanki
DB02008, 1-(2-Fluorobenzyl)-3-Butyl-8-(N-Acetyl-4-Aminobenzyl)-Xanthine
DB03267, 1-Allyl-3-Butyl-8-(N-Acetyl-4-Aminobenzyl)-Xanthine
DB03725, 5'-Guanylylmethylenebisphosphonate
DB00787, Acyclovir
DB09338, Mersalyl
DB01819, Phosphoenolpyruvate

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PCK1

Domain mapping of disease mutations (DMDM)

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DMDMi
93138710

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001036271 – 622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]Add BLAST622

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19PhosphoserineCombined sources1
Modified residuei70N6-acetyllysine; by p300/EP3002 Publications1
Modified residuei71N6-acetyllysine; by p300/EP3002 Publications1
Modified residuei90Phosphoserine; by PKB/AKT11 Publication1
Modified residuei91N6-acetyllysine; by p300/EP3001 Publication1
Modified residuei118PhosphoserineBy similarity1
Modified residuei178PhosphothreonineBy similarity1
Modified residuei286PhosphoserineBy similarity1
Modified residuei473N6-acetyllysineBy similarity1
Modified residuei521N6-acetyllysineBy similarity1
Modified residuei524N6-acetyllysineBy similarity1
Modified residuei594N6-acetyllysine; by p300/EP3002 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated. Lysine acetylation by p300/EP300 is increased on high glucose conditions (PubMed:20167786, PubMed:21726808, PubMed:30193097). Lysine acetylation promotes ubiquitination by UBR5 (PubMed:21726808). Acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2. Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels (PubMed:30193097).3 Publications
Phosphorylated in a GSK3B-mediated pathway; phosphorylation affects the efficiency of SIRT1-mediated deacetylation, and regulates PCK1 ubiquitination and degradation (PubMed:30193097). Phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity: phosphorylated PCK1 translocates to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2 (PubMed:32322062).2 Publications
Ubiquitination by UBR5 leads to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P35558

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P35558

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P35558

MaxQB - The MaxQuant DataBase

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MaxQBi
P35558

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P35558

PeptideAtlas

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PeptideAtlasi
P35558

PRoteomics IDEntifications database

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PRIDEi
P35558

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
5077
55087 [P35558-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35558

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P35558

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Major sites of expression are liver, kidney and adipocytes.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Regulated by cAMP and insulin.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000124253, Expressed in cortex of kidney and 172 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35558, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000124253, Tissue enriched (liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
111136, 81 interactors

Protein interaction database and analysis system

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IntActi
P35558, 5 interactors

Molecular INTeraction database

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MINTi
P35558

STRING: functional protein association networks

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STRINGi
9606.ENSP00000319814

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35558

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P35558, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1622
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P35558

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P35558

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni235 – 237Substrate binding3 Publications3
Regioni403 – 405Substrate binding3 Publications3
Regioni457 – 487Omega-loopBy similarityAdd BLAST31

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3749, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000001912

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_028872_1_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35558

Identification of Orthologs from Complete Genome Data

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OMAi
GPTNNWV

Database of Orthologous Groups

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OrthoDBi
286671at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35558

TreeFam database of animal gene trees

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TreeFami
TF314402

Family and domain databases

Conserved Domains Database

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CDDi
cd00819, PEPCK_GTP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.449.10, 1 hit
3.90.228.20, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00452, PEPCK_GTP, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR018091, PEP_carboxykin_GTP_CS
IPR013035, PEP_carboxykinase_C
IPR008209, PEP_carboxykinase_GTP
IPR035077, PEP_carboxykinase_GTP_C
IPR035078, PEP_carboxykinase_GTP_N
IPR008210, PEP_carboxykinase_N

The PANTHER Classification System

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PANTHERi
PTHR11561, PTHR11561, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00821, PEPCK_GTP, 1 hit
PF17297, PEPCK_N, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001348, PEP_carboxykinase_GTP, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF68923, SSF68923, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00505, PEPCK_GTP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P35558-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MPPQLQNGLN LSAKVVQGSL DSLPQAVREF LENNAELCQP DHIHICDGSE
60 70 80 90 100
EENGRLLGQM EEEGILRRLK KYDNCWLALT DPRDVARIES KTVIVTQEQR
110 120 130 140 150
DTVPIPKTGL SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG
160 170 180 190 200
SPLSKIGIEL TDSPYVVASM RIMTRMGTPV LEAVGDGEFV KCLHSVGCPL
210 220 230 240 250
PLQKPLVNNW PCNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRM
260 270 280 290 300
ASRLAKEEGW LAEHMLILGI TNPEGEKKYL AAAFPSACGK TNLAMMNPSL
310 320 330 340 350
PGWKVECVGD DIAWMKFDAQ GHLRAINPEN GFFGVAPGTS VKTNPNAIKT
360 370 380 390 400
IQKNTIFTNV AETSDGGVYW EGIDEPLASG VTITSWKNKE WSSEDGEPCA
410 420 430 440 450
HPNSRFCTPA SQCPIIDAAW ESPEGVPIEG IIFGGRRPAG VPLVYEALSW
460 470 480 490 500
QHGVFVGAAM RSEATAAAEH KGKIIMHDPF AMRPFFGYNF GKYLAHWLSM
510 520 530 540 550
AQHPAAKLPK IFHVNWFRKD KEGKFLWPGF GENSRVLEWM FNRIDGKAST
560 570 580 590 600
KLTPIGYIPK EDALNLKGLG HINMMELFSI SKEFWEKEVE DIEKYLEDQV
610 620
NADLPCEIER EILALKQRIS QM
Length:622
Mass (Da):69,195
Last modified:March 7, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i78D309E0845CC181
GO
Isoform 2 (identifier: P35558-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MPP → MTT
     4-320: Missing.

Show »
Length:305
Mass (Da):34,156
Checksum:i2FDE6275A0F15D6C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti250M → N in AAA02558 (PubMed:8325643).Curated1
Sequence conflicti256K → E in AAA60084 (PubMed:8490617).Curated1
Sequence conflicti291T → S in AAA02558 (PubMed:8325643).Curated1
Sequence conflicti551 – 552KL → NV in AAA60084 (PubMed:8490617).Curated2
Sequence conflicti597E → V in AAA60084 (PubMed:8490617).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07963345I → T in PCKDC; decreased stability; no effect on phosphoenolpyruvate carboxykinase activity. 1 PublicationCorresponds to variant dbSNP:rs202197769EnsemblClinVar.1
Natural variantiVAR_02107255R → Q1 PublicationCorresponds to variant dbSNP:rs28383585Ensembl.1
Natural variantiVAR_02107360M → T1 PublicationCorresponds to variant dbSNP:rs28383586EnsemblClinVar.1
Natural variantiVAR_021074138T → I1 PublicationCorresponds to variant dbSNP:rs28359542EnsemblClinVar.1
Natural variantiVAR_021075184V → L5 PublicationsCorresponds to variant dbSNP:rs707555EnsemblClinVar.1
Natural variantiVAR_015575267I → V2 PublicationsCorresponds to variant dbSNP:rs8192708EnsemblClinVar.1
Natural variantiVAR_021076276E → K1 PublicationCorresponds to variant dbSNP:rs11552145EnsemblClinVar.1
Natural variantiVAR_079634309G → R in PCKDC; unknown pathological significance; decreased phosphoenolpyruvate carboxykinase activity. 1 PublicationCorresponds to variant dbSNP:rs201186470EnsemblClinVar.1
Natural variantiVAR_021077368V → I1 PublicationCorresponds to variant dbSNP:rs1804160EnsemblClinVar.1
Natural variantiVAR_021078427P → S1 PublicationCorresponds to variant dbSNP:rs28359550EnsemblClinVar.1
Natural variantiVAR_079635440 – 443Missing in PCKDC; decreased phosphoenolpyruvate carboxykinase activity. 1 Publication4
Natural variantiVAR_042444586E → D1 PublicationCorresponds to variant dbSNP:rs1042529Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0570731 – 3MPP → MTT in isoform 2. 1 Publication3
Alternative sequenceiVSP_0570744 – 320Missing in isoform 2. 1 PublicationAdd BLAST317

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L05144 mRNA Translation: AAA60084.1
L12760 Genomic DNA Translation: AAA02558.1
AY794987 Genomic DNA Translation: AAV50001.1
AK290802 mRNA Translation: BAF83491.1
AK300072 mRNA Translation: BAG61876.1
AL035541 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75514.1
BC023978 mRNA Translation: AAH23978.1
U31519 Genomic DNA Translation: AAA91026.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS13460.1 [P35558-1]

Protein sequence database of the Protein Information Resource

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PIRi
A45746

NCBI Reference Sequences

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RefSeqi
NP_002582.3, NM_002591.3 [P35558-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000319441; ENSP00000319814; ENSG00000124253 [P35558-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5105

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5105

UCSC genome browser

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UCSCi
uc002xyn.5, human [P35558-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Protein Spotlight

On a tangent - Issue 233 of February 2021

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05144 mRNA Translation: AAA60084.1
L12760 Genomic DNA Translation: AAA02558.1
AY794987 Genomic DNA Translation: AAV50001.1
AK290802 mRNA Translation: BAF83491.1
AK300072 mRNA Translation: BAG61876.1
AL035541 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75514.1
BC023978 mRNA Translation: AAH23978.1
U31519 Genomic DNA Translation: AAA91026.1
CCDSiCCDS13460.1 [P35558-1]
PIRiA45746
RefSeqiNP_002582.3, NM_002591.3 [P35558-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
SMRiP35558
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111136, 81 interactors
IntActiP35558, 5 interactors
MINTiP35558
STRINGi9606.ENSP00000319814

Chemistry databases

BindingDBiP35558
ChEMBLiCHEMBL2911
DrugBankiDB02008, 1-(2-Fluorobenzyl)-3-Butyl-8-(N-Acetyl-4-Aminobenzyl)-Xanthine
DB03267, 1-Allyl-3-Butyl-8-(N-Acetyl-4-Aminobenzyl)-Xanthine
DB03725, 5'-Guanylylmethylenebisphosphonate
DB00787, Acyclovir
DB09338, Mersalyl
DB01819, Phosphoenolpyruvate

PTM databases

iPTMnetiP35558
PhosphoSitePlusiP35558

Genetic variation databases

BioMutaiPCK1
DMDMi93138710

Proteomic databases

EPDiP35558
jPOSTiP35558
MassIVEiP35558
MaxQBiP35558
PaxDbiP35558
PeptideAtlasiP35558
PRIDEiP35558
ProteomicsDBi5077
55087 [P35558-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
1643, 603 antibodies

The DNASU plasmid repository

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DNASUi
5105

Genome annotation databases

EnsembliENST00000319441; ENSP00000319814; ENSG00000124253 [P35558-1]
GeneIDi5105
KEGGihsa:5105
UCSCiuc002xyn.5, human [P35558-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5105
DisGeNETi5105

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PCK1
HGNCiHGNC:8724, PCK1
HPAiENSG00000124253, Tissue enriched (liver)
MalaCardsiPCK1
MIMi261680, phenotype
614168, gene
neXtProtiNX_P35558
OpenTargetsiENSG00000124253
Orphaneti2880, Phosphoenolpyruvate carboxykinase deficiency
PharmGKBiPA33069
VEuPathDBiHostDB:ENSG00000124253

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3749, Eukaryota
GeneTreeiENSGT00390000001912
HOGENOMiCLU_028872_1_1_1
InParanoidiP35558
OMAiGPTNNWV
OrthoDBi286671at2759
PhylomeDBiP35558
TreeFamiTF314402

Enzyme and pathway databases

UniPathwayiUPA00138
BioCyciMetaCyc:HS04751-MONOMER
BRENDAi4.1.1.32, 2681
PathwayCommonsiP35558
ReactomeiR-HSA-2161541, Abacavir metabolism
R-HSA-381340, Transcriptional regulation of white adipocyte differentiation
R-HSA-70263, Gluconeogenesis
R-HSA-9615017, FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
R-HSA-9632974, NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis
SABIO-RKiP35558
SIGNORiP35558

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
5105, 8 hits in 1007 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PCK1, human
EvolutionaryTraceiP35558

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PCK1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5105
PharosiP35558, Tbio

Protein Ontology

More...
PROi
PR:P35558
RNActiP35558, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000124253, Expressed in cortex of kidney and 172 other tissues
GenevisibleiP35558, HS

Family and domain databases

CDDicd00819, PEPCK_GTP, 1 hit
Gene3Di3.40.449.10, 1 hit
3.90.228.20, 1 hit
HAMAPiMF_00452, PEPCK_GTP, 1 hit
InterProiView protein in InterPro
IPR018091, PEP_carboxykin_GTP_CS
IPR013035, PEP_carboxykinase_C
IPR008209, PEP_carboxykinase_GTP
IPR035077, PEP_carboxykinase_GTP_C
IPR035078, PEP_carboxykinase_GTP_N
IPR008210, PEP_carboxykinase_N
PANTHERiPTHR11561, PTHR11561, 1 hit
PfamiView protein in Pfam
PF00821, PEPCK_GTP, 1 hit
PF17297, PEPCK_N, 1 hit
PIRSFiPIRSF001348, PEP_carboxykinase_GTP, 1 hit
SUPFAMiSSF68923, SSF68923, 1 hit
PROSITEiView protein in PROSITE
PS00505, PEPCK_GTP, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPCKGC_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P35558
Secondary accession number(s): A8K437
, B4DT64, Q8TCA3, Q9UJD2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 7, 2006
Last modified: September 29, 2021
This is version 211 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
  8. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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