Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P00355 (G3P_PIG)

Entry version 162 (02 Dec 2020)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

Organism
Sus scrofa (Pig)
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. 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. 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. Also 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. 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 similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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%5Fsection">'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 (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
  2. Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase, Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase 1 (PGK1), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase (PGK1)
  3. no protein annotated in this organism
  4. 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO4), Beta-enolase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO2), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO2), 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO3), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase (ENO1), 2-phospho-D-glycerate hydro-lyase (ENO2), 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (ENO4), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase
  5. Pyruvate kinase (PKLR), Pyruvate kinase (PKM), Multifunctional fusion protein (PKM), Multifunctional fusion protein (PKM), Multifunctional fusion protein (PKM), Pyruvate kinase, Multifunctional fusion protein (PKM), Pyruvate kinase (PKLR), Pyruvate kinase, Multifunctional fusion protein (PKM), Pyruvate kinase, Multifunctional fusion protein (PKM), Pyruvate kinase (PKLR), Multifunctional fusion protein (PKM), Pyruvate kinase (PKM), Pyruvate kinase (PKM), Pyruvate kinase (PKLR), Multifunctional fusion protein (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase (PKM), Pyruvate kinase, Multifunctional fusion protein (PKM), Multifunctional fusion protein (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%5Fsection">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 sitei33NADBy similarity1
Binding sitei78NAD; via carbonyl oxygenBy similarity1
Binding sitei120NADBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei150NucleophilePROSITE-ProRule annotation1
<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>Sitei177Activates thiol group during catalysisBy similarity1
Binding sitei180Glyceraldehyde 3-phosphateBy similarity1
Binding sitei232Glyceraldehyde 3-phosphateBy similarity1
Binding sitei314NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi11 – 12NADBy similarity2

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

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

More...UniPathwayi		UPA00109;UER00184

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000314985 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 5
  • UP000008227 Componenti: Unplaced

<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, 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

Protein family/group databases

Allergome; a platform for allergen knowledge

More...Allergomei		12129, Sus s GAPDH

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001454912 – 333Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST332

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 residuei3N6,N6-dimethyllysineBy similarity1
Modified residuei7Deamidated asparagineBy similarity1
Modified residuei40PhosphotyrosineBy similarity1
Modified residuei59N6-acetyllysineBy similarity1
Modified residuei62Deamidated asparagineBy similarity1
Modified residuei64N6,N6-dimethyllysineBy similarity1
Modified residuei68Deamidated asparagineBy similarity1
Modified residuei73PhosphothreonineBy similarity1
Modified residuei120PhosphoserineBy similarity1
Modified residuei146PhosphoserineBy similarity1
Modified residuei147Deamidated asparagineBy similarity1
Modified residuei149PhosphoserineBy similarity1
Modified residuei150ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity1
Modified residuei150Cysteine persulfideBy similarity1
Modified residuei150S-(2-succinyl)cysteineBy similarity1
Modified residuei150S-nitrosocysteine; in reversibly inhibited formBy similarity1
Modified residuei151PhosphothreonineBy similarity1
Modified residuei153Deamidated asparagineBy similarity1
Modified residuei175PhosphothreonineBy similarity1
Modified residuei180PhosphothreonineBy similarity1
Modified residuei182PhosphothreonineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki184Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei192N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei192N6-acetyllysine; alternateBy similarity1
Modified residuei192N6-malonyllysine; alternateBy similarity1
Modified residuei209PhosphothreonineBy similarity1
Modified residuei213N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei213N6-malonyllysine; alternateBy similarity1
Modified residuei217N6-acetyllysineBy similarity1
Modified residuei223Deamidated asparagineBy similarity1
Modified residuei225N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei225N6-acetyllysine; alternateBy similarity1
Modified residuei227PhosphothreonineBy similarity1
Modified residuei235PhosphothreonineBy similarity1
Modified residuei239PhosphoserineBy similarity1
Modified residuei245S-(2-succinyl)cysteineBy similarity1
Modified residuei245S-nitrosocysteineBy similarity1
Modified residuei252N6-acetyllysineBy similarity1
Modified residuei258N6,N6-dimethyllysineBy similarity1
Modified residuei261N6,N6-dimethyllysineBy similarity1
Modified residuei310PhosphoserineBy similarity1
Modified residuei314Deamidated asparagineBy similarity1
Modified residuei331PhosphoserineBy similarity1
Modified residuei332N6,N6-dimethyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

ISGylated.By similarity
S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus. S-nitrosylation of Cys-245 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 similarity).By similarity
Sulfhydration at Cys-150 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.By similarity

Keywords - PTMi

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

Proteomic databases

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

More...PaxDbi		P00355

PeptideAtlas

More...PeptideAtlasi		P00355

PRoteomics IDEntifications database

More...PRIDEi		P00355

<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

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P00355, baseline and differential

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

Interacts with EIF1AD, USP25, PRKCI and WARS1.

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.

Interacts with phosphorylated RPL13A (By similarity).

Component of the GAIT complex.

Interacts with FKBP6; leading to inhibit GAPDH catalytic activity (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P00355, 1 interactor

STRING: functional protein association networks

More...STRINGi		9823.ENSSSCP00000000740

<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

1333
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

More...SMRi		P00355

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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 – 146Interaction with WARS1By similarityAdd BLAST145
Regioni149 – 151Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni209 – 210Glyceraldehyde 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>Motifi243 – 248[IL]-x-C-x-x-[DE] motifBy similarity6

<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.By similarity

<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

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0657, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00355

Identification of Orthologs from Complete Genome Data

More...OMAi		HETYKGE

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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P00355-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVKVGVNGFG RIGRLVTRAA FNSGKVDIVA INDPFIDLHY MVYMFQYDST 
        60         70         80         90        100
HGKFHGTVKA ENGKLVINGK AITIFQERDP ANIKWGDAGA TYVVESTGVF 
       110        120        130        140        150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC 
       160        170        180        190        200
TTNCLAPLAK VIHDHFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA 
       210        220        230        240        250
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP 
       260        270        280        290        300
AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDTHS STFDAGAGIA 
       310        320        330 
LNDHFVKLIS WYDNEFGYSN RVVDLMVHMA SKE
Length:333
Mass (Da):35,836
Last modified:January 23, 2007 - v4
<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:i5F29175285D897BB
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 conflicti7N → D AA sequence (PubMed:4299800).Curated1
Sequence conflicti62N → D AA sequence (PubMed:4299800).Curated1
Sequence conflicti68N → D AA sequence (PubMed:4299800).Curated1
Sequence conflicti70 – 71KA → NP in AAB94053 (Ref. 1) Curated2
Sequence conflicti82N → K in AAB94053 (Ref. 1) Curated1
Sequence conflicti90 – 91AT → TA AA sequence (PubMed:4299800).Curated2
Sequence conflicti91T → E in AAB94053 (Ref. 1) Curated1
Sequence conflicti133V → M in AAB94053 (Ref. 1) Curated1
Sequence conflicti145V → I in AAB94053 (Ref. 1) Curated1
Sequence conflicti165H → N in AAB94053 (Ref. 1) Curated1
Sequence conflicti201A → L in AAB94053 (Ref. 1) Curated1
Sequence conflicti223N → D AA sequence (PubMed:4299800).Curated1
Sequence conflicti236P → A in AAB94053 (Ref. 1) Curated1
Sequence conflicti277D → H in AAB94053 (Ref. 1) Curated1
Sequence conflicti282C → S in AAB94053 (Ref. 1) Curated1
Sequence conflicti286 – 287SD → DS AA sequence (PubMed:4299800).Curated2
Sequence conflicti311W → S in AAB94053 (Ref. 1) Curated1
Sequence conflicti321R → W in AAB40155 (PubMed:9241041).Curated1

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
AF017079 mRNA Translation: AAB94053.1
Z84063 mRNA Translation: CAB06323.1
U48832 mRNA Translation: AAA91804.1
U82261 mRNA Translation: AAB40155.1
X94251 mRNA Translation: CAA63935.1

Protein sequence database of the Protein Information Resource

More...PIRi		B12055

NCBI Reference Sequences

More...RefSeqi		NP_001193288.1, NM_001206359.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSSSCT00005060912; ENSSSCP00005037648; ENSSSCG00005037806
ENSSSCT00015092759; ENSSSCP00015037932; ENSSSCG00015069184
ENSSSCT00035111381; ENSSSCP00035048787; ENSSSCG00035081064
ENSSSCT00035111396; ENSSSCP00035048801; ENSSSCG00035081064
ENSSSCT00040088131; ENSSSCP00040038735; ENSSSCG00040064450
ENSSSCT00045030090; ENSSSCP00045020842; ENSSSCG00045017499
ENSSSCT00055060969; ENSSSCP00055048878; ENSSSCG00055030580
ENSSSCT00060058387; ENSSSCP00060024997; ENSSSCG00060043031
ENSSSCT00065107183; ENSSSCP00065047768; ENSSSCG00065077443
ENSSSCT00070038969; ENSSSCP00070032633; ENSSSCG00070019692
ENSSSCT00070038975; ENSSSCP00070032639; ENSSSCG00070019692

Database of genes from NCBI RefSeq genomes

More...GeneIDi		396823

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ssc:396823

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017079 mRNA Translation: AAB94053.1
Z84063 mRNA Translation: CAB06323.1
U48832 mRNA Translation: AAA91804.1
U82261 mRNA Translation: AAB40155.1
X94251 mRNA Translation: CAA63935.1
PIRiB12055
RefSeqiNP_001193288.1, NM_001206359.1

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
5DDIX-ray2.40P/R/S2-333[»]
5TSOX-ray1.90P/R/S1-333[»]
SMRiP00355
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP00355, 1 interactor
STRINGi9823.ENSSSCP00000000740

Protein family/group databases

Allergomei12129, Sus s GAPDH

Proteomic databases

PaxDbiP00355
PeptideAtlasiP00355
PRIDEiP00355

Genome annotation databases

EnsembliENSSSCT00005060912; ENSSSCP00005037648; ENSSSCG00005037806
ENSSSCT00015092759; ENSSSCP00015037932; ENSSSCG00015069184
ENSSSCT00035111381; ENSSSCP00035048787; ENSSSCG00035081064
ENSSSCT00035111396; ENSSSCP00035048801; ENSSSCG00035081064
ENSSSCT00040088131; ENSSSCP00040038735; ENSSSCG00040064450
ENSSSCT00045030090; ENSSSCP00045020842; ENSSSCG00045017499
ENSSSCT00055060969; ENSSSCP00055048878; ENSSSCG00055030580
ENSSSCT00060058387; ENSSSCP00060024997; ENSSSCG00060043031
ENSSSCT00065107183; ENSSSCP00065047768; ENSSSCG00065077443
ENSSSCT00070038969; ENSSSCP00070032633; ENSSSCG00070019692
ENSSSCT00070038975; ENSSSCP00070032639; ENSSSCG00070019692
GeneIDi396823
KEGGissc:396823

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2597

Phylogenomic databases

eggNOGiKOG0657, Eukaryota
InParanoidiP00355
OMAiHETYKGE

Enzyme and pathway databases

UniPathwayiUPA00109;UER00184

Gene expression databases

ExpressionAtlasiP00355, baseline and differential

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_PIG
<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: P00355
Secondary accession number(s): O18816
, P79299, P79317, Q29546
<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%5Fand%5Fisoforms">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: December 2, 2020
This is version 162 of the entry and version 4 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again