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Entry version 171 (16 Oct 2019)
Sequence version 2 (02 May 2002)
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Protein

Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic

Gene

GAPC1

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

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. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism. Required for full fertility (PubMed:18820081). Involved in response to oxidative stress by mediating plant responses to abscisic acid (ABA) and water deficits through the activation of PLDDELTA and production of phosphatidic acid (PA), a multifunctional stress signaling lipid in plants (PubMed:22589465). Associates with FBA6 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress (PubMed:23316205). Binds DNA in vitro.3 Publications

Miscellaneous

Plants contain three types of GAPDH: NAD-dependent cytosolic forms which participate in glycolysis, NAD-dependent chloroplastic forms which participate in plastidic glycolysis and NADP-dependent chloroplastic forms which participate in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). All the forms are encoded by distinct genes.

<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

Inhibition by oxidized glutathione (GSSG), S-nitrosoglutathione (GSNO), hydrogen peroxide and sodium nitroprusside (SNP).4 Publications

<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 GAPC2, cytosolic (GAPC2), Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic (GAPC1)
  2. Phosphoglycerate kinase 3, cytosolic (PGK3)
  3. Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 (At3g08590), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (PGM1)
  4. Enolase 1, chloroplastic (ENO1), Bifunctional enolase 2/transcriptional activator (ENO2), Cytosolic enolase 3 (ENO3)
  5. Pyruvate kinase (AXX17_At5g51800), Pyruvate kinase (AXX17_At3g24740), Pyruvate kinase (AXX17_At3g50280), Pyruvate kinase (AXX17_ATUG04870), Pyruvate kinase (MAH20.13), Pyruvate kinase (MCD7.8), Pyruvate kinase (AXX17_At5g63250), Pyruvate kinase (MBK5.16), Pyruvate kinase (At3g25960), Pyruvate kinase (F1I16_60), Pyruvate kinase (AXX17_At3g50440), Pyruvate kinase (At3g52990), Plastidial pyruvate kinase 3, chloroplastic (PKP3), Pyruvate kinase (AXX17_At5g55530), Pyruvate kinase (AXX17_At3g28070), Pyruvate kinase (At2g36580), Pyruvate kinase (AXX17_At3g47400), Pyruvate kinase, Pyruvate kinase (AXX17_At5g08490), Pyruvate kinase (F8J2_160), Probable pyruvate kinase, cytosolic isozyme (At4g26390), Pyruvate kinase (At3g52990), Pyruvate kinase (AXX17_At3g03460), Pyruvate kinase (AXX17_At2g33300), Plastidial pyruvate kinase 2 (PKP2), Pyruvate kinase (At3g04050), Pyruvate kinase (AXX17_At4g30430), Pyruvate kinase (F1I16_220), Plastidial pyruvate kinase 1, chloroplastic (PKP1), Pyruvate kinase (AXX17_At1g33230), Pyruvate kinase (At5g63680), Pyruvate kinase, Plastidial pyruvate kinase 4, chloroplastic (PKP4)
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 sitei37NADBy similarity1
Binding sitei84NAD; via carbonyl oxygenBy 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 sitei156Nucleophile1 Publication1
<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>Sitei183Activates thiol group during catalysisBy similarity1
Binding sitei186Glyceraldehyde 3-phosphateBy similarity1
Binding sitei238Glyceraldehyde 3-phosphateBy similarity1
Binding sitei320NADBy similarity1

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 bindingi15 – 16NADBy 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

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 functionDNA-binding, Oxidoreductase
Biological processGlycolysis, Stress response
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.12 399

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

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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_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 GAPC1, cytosolic (EC:1.2.1.12)
Alternative name(s):
NAD-dependent glyceraldehydephosphate dehydrogenase C subunit 1
<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:GAPC1
Synonyms:GAPC, GAPDH
Ordered Locus Names:At3g04120
ORF Names:T6K12.26
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<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
  • UP000006548 <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 3

Organism-specific databases

Arabidopsis Information Portal

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Araporti
AT3G04120

The Arabidopsis Information Resource

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TAIRi
locus:2103085 AT3G04120

<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 Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Delayed growth, small siliques with defects in fertility, and alterations of seed and fruit development. Reduced respiratory rates, pyruvate levels and Krebs cycle intermediates. Increased reactive oxygen species levels.1 Publication

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>Mutagenesisi156C → S: Loss of activity. Loss of glutathionylation. 1 Publication1
Mutagenesisi160C → S: No effect on the activity. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001455941 – 338Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolicAdd BLAST338

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 residuei156S-glutathionyl cysteine; transient; alternate1 Publication1
Modified residuei156S-nitrosocysteine; transient; alternateBy similarity1
Modified residuei160S-nitrosocysteine; transientBy similarity1

<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-glutathionylation at Cys-156 in the presence of oxidized glutathione (GSSG). S-nitrosylation in the presence of S-nitrosoglutathione (GSNO) or sodium nitroprusside (SNP). These reactions may be both a protective mechanism against irreversible oxidation and a mean to store inhibited enzyme in a recoverable form. Glutathionylation is reversed by both glutaredoxins and thioredoxins in vitro.1 Publication

Keywords - PTMi

Glutathionylation, S-nitrosylation

Proteomic databases

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

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PaxDbi
P25858

PRoteomics IDEntifications database

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PRIDEi
P25858

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P25858

<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

Expressed in leaves, stems and siliques and at lower levels in roots and flowers.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

Not repressed by darkness or sucrose.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P25858 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P25858 AT

<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 (By similarity).

Interacts with PLDDELTA (PubMed:22589465).

Interacts with FBA6 and VDAC3 (PubMed:23316205).

By similarity2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
4902, 11 interactors

Protein interaction database and analysis system

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IntActi
P25858, 2 interactors

Molecular INTeraction database

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MINTi
P25858

STRING: functional protein association networks

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STRINGi
3702.AT3G04120.1

<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

1338
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
P25858

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...

<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>Regioni155 – 157Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni215 – 216Glyceraldehyde 3-phosphate bindingBy similarity2

<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
KOG0657 Eukaryota
COG0057 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000071678

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P25858

KEGG Orthology (KO)

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KOi
K00134

Identification of Orthologs from Complete Genome Data

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OMAi
DSTHGHF

Database of Orthologous Groups

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OrthoDBi
945145at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P25858

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR10836 PTHR10836, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000149 GAP_DH, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00078 G3PDHDRGNASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00846 Gp_dh_N, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01534 GAPDH-I, 1 hit

PROSITE; a protein domain and family database

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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>Sequencei

<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.

P25858-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK
60 70 80 90 100
YDSVHGQWKH NELKIKDEKT LLFGEKPVTV FGIRNPEDIP WAEAGADYVV
110 120 130 140 150
ESTGVFTDKD KAAAHLKGGA KKVVISAPSK DAPMFVVGVN EHEYKSDLDI
160 170 180 190 200
VSNASCTTNC LAPLAKVIND RFGIVEGLMT TVHSITATQK TVDGPSMKDW
210 220 230 240 250
RGGRAASFNI IPSSTGAAKA VGKVLPALNG KLTGMSFRVP TVDVSVVDLT
260 270 280 290 300
VRLEKAATYD EIKKAIKEES EGKLKGILGY TEDDVVSTDF VGDNRSSIFD
310 320 330
AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA
Length:338
Mass (Da):36,914
Last modified:May 2, 2002 - v2
<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:i4186F65E1F1EE96F
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 conflicti127A → E in AAA32794 (PubMed:1916285).Curated1
Sequence conflicti127A → E in AAA32796 (PubMed:1916285).Curated1
Sequence conflicti136V → F in AAM65189 (Ref. 6) Curated1
Sequence conflicti260D → E in AAA32794 (PubMed:1916285).Curated1
Sequence conflicti260D → E in AAA32796 (PubMed:1916285).Curated1
Sequence conflicti325S → N in AAM65189 (Ref. 6) Curated1

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
M64116 mRNA Translation: AAA32794.1
M64119 Genomic DNA Translation: AAA32796.1
AC016829 Genomic DNA Translation: AAF26801.1
CP002686 Genomic DNA Translation: AEE74039.1
AY052267 mRNA Translation: AAK97737.1
AY060521 mRNA Translation: AAL31134.1
AY140084 mRNA Translation: AAM98225.1
AK226804 mRNA Translation: BAE98901.1
AY087651 mRNA Translation: AAM65189.1
F20074 mRNA Translation: CAA23391.1

Protein sequence database of the Protein Information Resource

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PIRi
JQ1287

NCBI Reference Sequences

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RefSeqi
NP_187062.1, NM_111283.4

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT3G04120.1; AT3G04120.1; AT3G04120

Database of genes from NCBI RefSeq genomes

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GeneIDi
819567

Gramene; a comparative resource for plants

More...
Gramenei
AT3G04120.1; AT3G04120.1; AT3G04120

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT3G04120

<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
M64116 mRNA Translation: AAA32794.1
M64119 Genomic DNA Translation: AAA32796.1
AC016829 Genomic DNA Translation: AAF26801.1
CP002686 Genomic DNA Translation: AEE74039.1
AY052267 mRNA Translation: AAK97737.1
AY060521 mRNA Translation: AAL31134.1
AY140084 mRNA Translation: AAM98225.1
AK226804 mRNA Translation: BAE98901.1
AY087651 mRNA Translation: AAM65189.1
F20074 mRNA Translation: CAA23391.1
PIRiJQ1287
RefSeqiNP_187062.1, NM_111283.4

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
4Z0HX-ray2.30O/R5-338[»]
SMRiP25858
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4902, 11 interactors
IntActiP25858, 2 interactors
MINTiP25858
STRINGi3702.AT3G04120.1

PTM databases

iPTMnetiP25858

Proteomic databases

PaxDbiP25858
PRIDEiP25858

Genome annotation databases

EnsemblPlantsiAT3G04120.1; AT3G04120.1; AT3G04120
GeneIDi819567
GrameneiAT3G04120.1; AT3G04120.1; AT3G04120
KEGGiath:AT3G04120

Organism-specific databases

AraportiAT3G04120
TAIRilocus:2103085 AT3G04120

Phylogenomic databases

eggNOGiKOG0657 Eukaryota
COG0057 LUCA
HOGENOMiHOG000071678
InParanoidiP25858
KOiK00134
OMAiDSTHGHF
OrthoDBi945145at2759
PhylomeDBiP25858

Enzyme and pathway databases

UniPathwayiUPA00109;UER00184
BRENDAi1.2.1.12 399

Miscellaneous databases

Protein Ontology

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PROi
PR:P25858

Gene expression databases

ExpressionAtlasiP25858 baseline and differential
GenevisibleiP25858 AT

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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiG3PC1_ARATH
<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: P25858
Secondary accession number(s): Q0WVE7
, Q42352, Q8LAS0, Q9M8W8
<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: May 1, 1992
Last sequence update: May 2, 2002
Last modified: October 16, 2019
This is version 171 of the entry and version 2 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 programPlant 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, Complete proteome, 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. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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