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Entry version 247 (16 Oct 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

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

Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.By similarity3 Publications

<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 <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

Glyceraldehyde-3-phosphate dehydrogenase activity is inhibited by fumarate, via the formation of S-(2-succinyl)cysteine residues.By similarity

<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: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-278), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
  2. Phosphoglycerate kinase, Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase, Phosphoglycerate kinase (HEL-S-68p), Phosphoglycerate kinase 1 (PGK1), Phosphoglycerate kinase (HEL-S-272), Phosphoglycerate kinase, Phosphoglycerate kinase
  3. no protein annotated in this organism
  4. Alpha-enolase (ENO1), Beta-enolase (ENO3), Enolase 4 (ENO4), Gamma-enolase (ENO2)
  5. Pyruvate kinase, Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKLR), Pyruvate kinase (PKM2), Pyruvate kinase (HEL-S-30), Pyruvate kinase (PKM), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase, Pyruvate kinase (PKM)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

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 sitei35NAD2 Publications1
Binding sitei80NAD; via carbonyl oxygen2 Publications1
Binding sitei122NAD2 Publications1
<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 sitei152Nucleophile1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei179Activates thiol group during catalysis1
Binding sitei182Glyceraldehyde 3-phosphateBy similarity1
Binding sitei234Glyceraldehyde 3-phosphateBy similarity1
Binding sitei316NAD2 Publications1

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 bindingi13 – 14NAD2 Publications2

<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 functionOxidoreductase, Transferase
Biological processApoptosis, Glycolysis, Translation regulation
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS03433-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.2.1.12 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-70171 Glycolysis
R-HSA-70263 Gluconeogenesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P04406

SIGNOR Signaling Network Open Resource

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SIGNORi
P04406

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

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UniPathwayi
UPA00109;UER00184

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P04406 Curated

MoonProt database of moonlighting proteins

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MoonProti
P04406

<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:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
Short name:
GAPDH
Alternative name(s):
Peptidyl-cysteine S-nitrosylase GAPDH (EC:2.6.99.-)
<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:GAPDH
Synonyms:GAPD
ORF Names:CDABP0047, OK/SW-cl.12
<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 12

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:4141 GAPDH

Online Mendelian Inheritance in Man (OMIM)

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MIMi
138400 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P04406

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

<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

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>Mutagenesisi46M → L: Drastic reduction of the extent and significant prolongation of the lag phase of free radical-induced aggregation. 1 Publication1
Mutagenesisi105M → L: Increased resistance to free radical-induced aggregation. 1 Publication1
Mutagenesisi152C → S: Markedly reduced glycolytic activity; when associated with S-156 and S-247. Forms free radical-induced aggregates, but to a lesser extent than wild-type protein; when associated with S-156 and S-247. 1 Publication1
Mutagenesisi156C → S: Markedly reduced glycolytic activity; when associated with S-152 and S-247. Forms free radical-induced aggregates, but to a lesser extent than wild-type protein; when associated with S-156 and S-247. 1 Publication1
Mutagenesisi196W → F: Increased free radical-induced aggregation. 1 Publication1
Mutagenesisi245L → M: Inhibits S-nitrosylation of Cys-247; when associated with M-250. 1 Publication1
Mutagenesisi247C → S: Markedly reduced glycolytic activity; when associated with S-152 and S-156. Forms free radical-induced aggregates, but to a lesser extent than wild-type protein; when associated with S-156 and S-247. 1 Publication1
Mutagenesisi250E → M: Inhibits S-nitrosylation of Cys-247; when associated with M-245. 1 Publication1
Mutagenesisi320Y → F: No effect on free radical-induced aggregation. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
2597

Open Targets

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OpenTargetsi
ENSG00000111640

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28554

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P04406

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2284

Drug and drug target database

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DrugBanki
DB07347 4-(2-Aminoethyl)Benzenesulfonyl Fluoride
DB02059 Adenosine-5-Diphosphoribose
DB11638 Artenimol
DB09130 Copper
DB00157 NADH
DB03893 Thionicotinamide-Adenine-Dinucleotide
DB09092 Xanthinol

DrugCentral

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DrugCentrali
P04406

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
GAPDH

Domain mapping of disease mutations (DMDM)

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DMDMi
120649

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001454862 – 335Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST334

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 residuei5N6,N6-dimethyllysine1 Publication1
Modified residuei9Deamidated asparagine1 Publication1
Modified residuei42PhosphotyrosineCombined sources1
Modified residuei46Methionine sulfoxide; in vitro1 Publication1
Modified residuei61N6-acetyllysineCombined sources1
Modified residuei64Deamidated asparagine1 Publication1
Modified residuei66N6,N6-dimethyllysine1 Publication1
Modified residuei70Deamidated asparagine1 Publication1
Modified residuei75PhosphothreonineCombined sources1 Publication1
Modified residuei83PhosphoserineCombined sources1
Modified residuei122Phosphoserine1 Publication1
Modified residuei148Phosphoserine1 Publication1
Modified residuei149Deamidated asparagine1 Publication1
Modified residuei151PhosphoserineCombined sources1
Modified residuei152ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity1
Modified residuei152Cysteine persulfideBy similarity1
Modified residuei152S-(2-succinyl)cysteineBy similarity1
Modified residuei152S-nitrosocysteine; in reversibly inhibited formBy similarity1
Modified residuei153PhosphothreonineCombined sources1
Modified residuei155Deamidated asparagine1 Publication1
Modified residuei177PhosphothreonineCombined sources1
Modified residuei182PhosphothreonineCombined sources1
Modified residuei184PhosphothreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei194N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei194N6-acetyllysine; alternateCombined sources1
Modified residuei194N6-malonyllysine; alternate1 Publication1
Modified residuei211PhosphothreonineCombined sources1
Modified residuei215N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei215N6-malonyllysine; alternate1 Publication1
Modified residuei219N6-acetyllysineCombined sources1
Modified residuei225Deamidated asparagine1 Publication1
Modified residuei227N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei227N6-acetyllysine; alternateCombined sources1
Modified residuei229PhosphothreonineCombined sources1 Publication1
Modified residuei237Phosphothreonine1 Publication1
Modified residuei241PhosphoserineCombined sources1
Modified residuei247S-(2-succinyl)cysteineBy similarity1
Modified residuei247S-nitrosocysteine2 Publications1
Modified residuei254N6-acetyllysineCombined sources1
Modified residuei260N6,N6-dimethyllysine1 Publication1
Modified residuei263N6,N6-dimethyllysine1 Publication1
Modified residuei312PhosphoserineCombined sources1 Publication1
Modified residuei316Deamidated asparagine1 Publication1
Modified residuei333PhosphoserineCombined sources1
Modified residuei334N6,N6-dimethyllysine1 Publication1

<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

S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus (By similarity). S-nitrosylation of Cys-247 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity.By similarity2 Publications
ISGylated.1 Publication
Sulfhydration at Cys-152 increases catalytic activity.By similarity
Oxidative stress can promote the formation of high molecular weight disulfide-linked GAPDH aggregates, through a process called nucleocytoplasmic coagulation. Such aggregates can be observed in vivo in the affected tissues of patients with Alzheimer disease or alcoholic liver cirrhosis, or in cell cultures during necrosis. Oxidation at Met-46 may play a pivotal role in the formation of these insoluble structures. This modification has been detected in vitro following treatment with free radical donor (+/-)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide. It has been proposed to destabilize nearby residues, increasing the likelihood of secondary oxidative damages, including oxidation of Tyr-45 and Met-105. This cascade of oxidations may augment GAPDH misfolding, leading to intermolecular disulfide cross-linking and aggregation.1 Publication
Succination of Cys-152 and Cys-247 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits glyceraldehyde-3-phosphate dehydrogenase activity. Fumarate concentration as well as succination of cysteine residues in GAPDH is significantly increased in muscle of diabetic mammals. It was proposed that the S-(2-succinyl)cysteine chemical modification may be a useful biomarker of mitochondrial and oxidative stress in diabetes and that succination of GAPDH and other thiol proteins by fumarate may contribute to the metabolic changes underlying the development of diabetes complications.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Methylation, Oxidation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P04406

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P04406

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P04406

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

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PaxDbi
P04406

PeptideAtlas

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PeptideAtlasi
P04406

PRoteomics IDEntifications database

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PRIDEi
P04406

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
18491
51703 [P04406-1]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P04406-1 [P04406-1]

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P04406

USC-OGP 2-DE database

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OGPi
P04406

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00219018
P04406

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P04406

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P04406

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1941

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P04406

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

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PhosphoSitePlusi
P04406

SwissPalm database of S-palmitoylation events

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SwissPalmi
P04406

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000111640 Expressed in 236 organ(s), highest expression level in smooth muscle tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P04406 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04406 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB005197
CAB016392
HPA040067
HPA061280

<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

Homotetramer.

Interacts with TPPP; the interaction is direct.

Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation.

Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation.

Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules. Associates with microtubules (By similarity).

Interacts with EIF1AD, USP25, PRKCI and WARS.

Interacts with phosphorylated RPL13A; inhibited by oxidatively-modified low-densitity lipoprotein (LDL(ox)).

Component of the GAIT complex.

Interacts with FKBP6; leading to inhibit GAPDH catalytic activity.

By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108868, 253 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P04406

Database of interacting proteins

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DIPi
DIP-32521N

Protein interaction database and analysis system

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IntActi
P04406, 159 interactors

Molecular INTeraction database

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MINTi
P04406

STRING: functional protein association networks

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STRINGi
9606.ENSP00000229239

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P04406

<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

1335
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
P04406

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
P04406

<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>Regioni2 – 148Interaction with WARS1 PublicationAdd BLAST147
Regioni151 – 153Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni211 – 212Glyceraldehyde 3-phosphate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi245 – 250[IL]-x-C-x-x-[DE] motif1 Publication6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.1 Publication

<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

More...
eggNOGi
KOG0657 Eukaryota
COG0057 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153298

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000071678

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P04406

KEGG Orthology (KO)

More...
KOi
K00134

Identification of Orthologs from Complete Genome Data

More...
OMAi
DSTHGHF

Database of Orthologous Groups

More...
OrthoDBi
945145at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P04406

TreeFam database of animal gene trees

More...
TreeFami
TF300533

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR020831 GlycerAld/Erythrose_P_DH
IPR020830 GlycerAld_3-P_DH_AS
IPR020829 GlycerAld_3-P_DH_cat
IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
IPR006424 Glyceraldehyde-3-P_DH_1
IPR036291 NAD(P)-bd_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10836 PTHR10836, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02800 Gp_dh_C, 1 hit
PF00044 Gp_dh_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000149 GAP_DH, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00078 G3PDHDRGNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00846 Gp_dh_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01534 GAPDH-I, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00071 GAPDH, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P04406-1) [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
MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD
60 70 80 90 100
STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG
110 120 130 140 150
VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA
160 170 180 190 200
SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR
210 220 230 240 250
GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE
260 270 280 290 300
KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG
310 320 330
IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE
Length:335
Mass (Da):36,053
Last modified:January 23, 2007 - 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:iC9C135E8AE3E8744
GO
Isoform 2 (identifier: P04406-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:293
Mass (Da):31,548
Checksum:i6705C1F127BB6C09
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EUT5E7EUT5_HUMAN
Glyceraldehyde-3-phosphate dehydrog...
GAPDH
260Annotation score:

Annotation score:2 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 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 conflicti225N → D in CAA25833 (PubMed:6096821).Curated1

Natural variant

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_01888922A → G1 PublicationCorresponds to variant dbSNP:rs45541435Ensembl.1
Natural variantiVAR_049218251K → N. Corresponds to variant dbSNP:rs1062429Ensembl.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_0472891 – 42Missing in isoform 2. CuratedAdd BLAST42

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X01677 mRNA Translation: CAA25833.1
M17851 mRNA Translation: AAA86283.1
M33197 mRNA Translation: AAA52518.1
J02642 mRNA Translation: AAA52496.1
J04038 Genomic DNA Translation: AAA53191.1
X53778 mRNA Translation: CAA37794.1
AF261085 mRNA Translation: AAF99678.1
AY007133 mRNA Translation: AAG01996.1
AB062273 mRNA Translation: BAB93466.1
BT006893 mRNA Translation: AAP35539.1
AY340484 Genomic DNA Translation: AAP88932.1
CR407671 mRNA Translation: CAG28599.1
AC006064 Genomic DNA No translation available.
CH471116 Genomic DNA Translation: EAW88787.1
BC001601 mRNA Translation: AAH01601.1
BC004109 mRNA Translation: AAH04109.1
BC009081 mRNA Translation: AAH09081.1
BC013310 mRNA Translation: AAH13310.1
BC023632 mRNA Translation: AAH23632.1
BC025925 mRNA Translation: AAH25925.1
BC026907 mRNA Translation: AAH26907.1
BC029618 mRNA Translation: AAH29618.1
BC083511 mRNA Translation: AAH83511.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS58201.1 [P04406-2]
CCDS8549.1 [P04406-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A31988 DEHUG3

NCBI Reference Sequences

More...
RefSeqi
NP_001243728.1, NM_001256799.2 [P04406-2]
NP_001276674.1, NM_001289745.1 [P04406-1]
NP_001276675.1, NM_001289746.1 [P04406-1]
NP_002037.2, NM_002046.5 [P04406-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000229239; ENSP00000229239; ENSG00000111640 [P04406-1]
ENST00000396858; ENSP00000380067; ENSG00000111640 [P04406-2]
ENST00000396859; ENSP00000380068; ENSG00000111640 [P04406-1]
ENST00000396861; ENSP00000380070; ENSG00000111640 [P04406-1]
ENST00000619601; ENSP00000478864; ENSG00000111640 [P04406-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2597

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2597

UCSC genome browser

More...
UCSCi
uc031qfw.3 human [P04406-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
Wikipedia

Glyceraldehyde 3-phosphate dehydrogenase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01677 mRNA Translation: CAA25833.1
M17851 mRNA Translation: AAA86283.1
M33197 mRNA Translation: AAA52518.1
J02642 mRNA Translation: AAA52496.1
J04038 Genomic DNA Translation: AAA53191.1
X53778 mRNA Translation: CAA37794.1
AF261085 mRNA Translation: AAF99678.1
AY007133 mRNA Translation: AAG01996.1
AB062273 mRNA Translation: BAB93466.1
BT006893 mRNA Translation: AAP35539.1
AY340484 Genomic DNA Translation: AAP88932.1
CR407671 mRNA Translation: CAG28599.1
AC006064 Genomic DNA No translation available.
CH471116 Genomic DNA Translation: EAW88787.1
BC001601 mRNA Translation: AAH01601.1
BC004109 mRNA Translation: AAH04109.1
BC009081 mRNA Translation: AAH09081.1
BC013310 mRNA Translation: AAH13310.1
BC023632 mRNA Translation: AAH23632.1
BC025925 mRNA Translation: AAH25925.1
BC026907 mRNA Translation: AAH26907.1
BC029618 mRNA Translation: AAH29618.1
BC083511 mRNA Translation: AAH83511.1
CCDSiCCDS58201.1 [P04406-2]
CCDS8549.1 [P04406-1]
PIRiA31988 DEHUG3
RefSeqiNP_001243728.1, NM_001256799.2 [P04406-2]
NP_001276674.1, NM_001289745.1 [P04406-1]
NP_001276675.1, NM_001289746.1 [P04406-1]
NP_002037.2, NM_002046.5 [P04406-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U8FX-ray1.75O/P/Q/R1-335[»]
1ZNQX-ray2.50O/P/Q/R1-335[»]
2FEHmodel-O/P/Q/R1-335[»]
3GPDX-ray3.50G/R2-335[»]
4WNCX-ray1.99A/B/C/D/E/F/G/O1-335[»]
4WNIX-ray2.30A/B/C/O1-335[»]
6ADEX-ray3.15A/B/C1-335[»]
6IQ6X-ray2.29A/B/C/D/E/F/G/H1-335[»]
SMRiP04406
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi108868, 253 interactors
CORUMiP04406
DIPiDIP-32521N
IntActiP04406, 159 interactors
MINTiP04406
STRINGi9606.ENSP00000229239

Chemistry databases

BindingDBiP04406
ChEMBLiCHEMBL2284
DrugBankiDB07347 4-(2-Aminoethyl)Benzenesulfonyl Fluoride
DB02059 Adenosine-5-Diphosphoribose
DB11638 Artenimol
DB09130 Copper
DB00157 NADH
DB03893 Thionicotinamide-Adenine-Dinucleotide
DB09092 Xanthinol
DrugCentraliP04406

Protein family/group databases

MoonDBiP04406 Curated
MoonProtiP04406

PTM databases

GlyConnecti1941
iPTMnetiP04406
PhosphoSitePlusiP04406
SwissPalmiP04406

Polymorphism and mutation databases

BioMutaiGAPDH
DMDMi120649

2D gel databases

DOSAC-COBS-2DPAGEiP04406
OGPiP04406
REPRODUCTION-2DPAGEiIPI00219018
P04406
SWISS-2DPAGEiP04406
UCD-2DPAGEiP04406

Proteomic databases

EPDiP04406
jPOSTiP04406
MassIVEiP04406
PaxDbiP04406
PeptideAtlasiP04406
PRIDEiP04406
ProteomicsDBi18491
51703 [P04406-1]
TopDownProteomicsiP04406-1 [P04406-1]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P04406

The DNASU plasmid repository

More...
DNASUi
2597

Genome annotation databases

EnsembliENST00000229239; ENSP00000229239; ENSG00000111640 [P04406-1]
ENST00000396858; ENSP00000380067; ENSG00000111640 [P04406-2]
ENST00000396859; ENSP00000380068; ENSG00000111640 [P04406-1]
ENST00000396861; ENSP00000380070; ENSG00000111640 [P04406-1]
ENST00000619601; ENSP00000478864; ENSG00000111640 [P04406-2]
GeneIDi2597
KEGGihsa:2597
UCSCiuc031qfw.3 human [P04406-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2597
DisGeNETi2597

GeneCards: human genes, protein and diseases

More...
GeneCardsi
GAPDH
HGNCiHGNC:4141 GAPDH
HPAiCAB005197
CAB016392
HPA040067
HPA061280
MIMi138400 gene
neXtProtiNX_P04406
OpenTargetsiENSG00000111640
PharmGKBiPA28554

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0657 Eukaryota
COG0057 LUCA
GeneTreeiENSGT00940000153298
HOGENOMiHOG000071678
InParanoidiP04406
KOiK00134
OMAiDSTHGHF
OrthoDBi945145at2759
PhylomeDBiP04406
TreeFamiTF300533

Enzyme and pathway databases

UniPathwayiUPA00109;UER00184
BioCyciMetaCyc:HS03433-MONOMER
BRENDAi1.2.1.12 2681
ReactomeiR-HSA-70171 Glycolysis
R-HSA-70263 Gluconeogenesis
SABIO-RKiP04406
SIGNORiP04406

Miscellaneous databases

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

More...
ChiTaRSi
GAPDH human
EvolutionaryTraceiP04406

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Glyceraldehyde_3-phosphate_dehydrogenase

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

More...
GenomeRNAii
2597
PharosiP04406

Protein Ontology

More...
PROi
PR:P04406

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000111640 Expressed in 236 organ(s), highest expression level in smooth muscle tissue
ExpressionAtlasiP04406 baseline and differential
GenevisibleiP04406 HS

Family and domain databases

InterProiView protein in InterPro
IPR020831 GlycerAld/Erythrose_P_DH
IPR020830 GlycerAld_3-P_DH_AS
IPR020829 GlycerAld_3-P_DH_cat
IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
IPR006424 Glyceraldehyde-3-P_DH_1
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR10836 PTHR10836, 1 hit
PfamiView protein in Pfam
PF02800 Gp_dh_C, 1 hit
PF00044 Gp_dh_N, 1 hit
PIRSFiPIRSF000149 GAP_DH, 1 hit
PRINTSiPR00078 G3PDHDRGNASE
SMARTiView protein in SMART
SM00846 Gp_dh_N, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01534 GAPDH-I, 1 hit
PROSITEiView protein in PROSITE
PS00071 GAPDH, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiG3P_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: P04406
Secondary accession number(s): E7EUT4, P00354, Q53X65
<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: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 247 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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