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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-Experimental evidence at protein leveli

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

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation1 Publication

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, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-278), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase 1 (PGK1)
  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 PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (HEL-S-30), Pyruvate kinase (PKM2)
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
Binding sitei35NAD2 Publications1
Binding sitei80NAD; via carbonyl oxygen2 Publications1
Binding sitei122NAD2 Publications1
Active sitei152Nucleophile1
Sitei179Activates thiol group during catalysis1
Binding sitei182Glyceraldehyde 3-phosphateBy similarity1
Binding sitei234Glyceraldehyde 3-phosphateBy similarity1
Binding sitei316NAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 14NAD2 Publications2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Apoptosis, Glycolysis, Translation regulation

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS03433-MONOMER.
ZFISH:HS03433-MONOMER.
BRENDAi1.2.1.12. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP04406.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

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.-)
Gene namesi
Name:GAPDH
Synonyms:GAPD
ORF Names:CDABP0047, OK/SW-cl.12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:4141. GAPDH.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • GAIT complex Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • lipid particle Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • nuclear membrane Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: HPA
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi2597.
OpenTargetsiENSG00000111640.
PharmGKBiPA28554.

Chemistry databases

ChEMBLiCHEMBL2284.

Polymorphism and mutation databases

BioMutaiGAPDH.
DMDMi120649.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001454862 – 335Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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-nitrosocysteine; in reversibly inhibited formBy similarity1
Modified residuei153PhosphothreonineCombined sources1
Modified residuei155Deamidated asparagine1 Publication1
Modified residuei177PhosphothreonineCombined sources1
Modified residuei182PhosphothreonineCombined sources1
Modified residuei184PhosphothreonineCombined sources1
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-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

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

Keywords - PTMi

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

Proteomic databases

EPDiP04406.
PaxDbiP04406.
PeptideAtlasiP04406.
PRIDEiP04406.
TopDownProteomicsiP04406-1. [P04406-1]

2D gel databases

DOSAC-COBS-2DPAGEP04406.
OGPiP04406.
REPRODUCTION-2DPAGEIPI00219018.
P04406.
SWISS-2DPAGEP04406.
UCD-2DPAGEP04406.

PTM databases

iPTMnetiP04406.
PhosphoSitePlusiP04406.
SwissPalmiP04406.

Expressioni

Gene expression databases

BgeeiENSG00000111640.
CleanExiHS_GAPDH.
ExpressionAtlasiP04406. baseline and differential.
GenevisibleiP04406. HS.

Organism-specific databases

HPAiCAB005197.
CAB016392.
HPA040067.
HPA061280.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-354056,EBI-354056
Akt2Q608232EBI-354056,EBI-400263From a different organism.
EGFRP005336EBI-354056,EBI-297353
NOS2P352288EBI-354056,EBI-6662224
PCNAP120043EBI-354056,EBI-358311
PGK1P005582EBI-354056,EBI-709599
PREPP481475EBI-354056,EBI-1049962
RPA2P159272EBI-354056,EBI-621404
S100A8P051096EBI-354056,EBI-355281
TINF2Q9BSI42EBI-354056,EBI-717399

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108868. 202 interactors.
DIPiDIP-32521N.
IntActiP04406. 94 interactors.
MINTiMINT-1150338.
STRINGi9606.ENSP00000229239.

Chemistry databases

BindingDBiP04406.

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi13 – 25Combined sources13
Beta strandi27 – 34Combined sources8
Beta strandi36 – 38Combined sources3
Helixi40 – 48Combined sources9
Turni51 – 53Combined sources3
Beta strandi60 – 63Combined sources4
Beta strandi66 – 69Combined sources4
Beta strandi72 – 77Combined sources6
Helixi82 – 84Combined sources3
Turni87 – 91Combined sources5
Beta strandi94 – 97Combined sources4
Beta strandi99 – 101Combined sources3
Helixi105 – 108Combined sources4
Helixi109 – 114Combined sources6
Beta strandi117 – 123Combined sources7
Beta strandi126 – 128Combined sources3
Turni133 – 135Combined sources3
Helixi137 – 139Combined sources3
Beta strandi145 – 148Combined sources4
Helixi152 – 168Combined sources17
Beta strandi170 – 180Combined sources11
Beta strandi185 – 189Combined sources5
Helixi196 – 199Combined sources4
Turni202 – 204Combined sources3
Beta strandi207 – 210Combined sources4
Turni213 – 216Combined sources4
Helixi217 – 220Combined sources4
Helixi222 – 224Combined sources3
Beta strandi227 – 236Combined sources10
Beta strandi241 – 251Combined sources11
Helixi255 – 267Combined sources13
Turni268 – 273Combined sources6
Beta strandi274 – 277Combined sources4
Helixi283 – 286Combined sources4
Beta strandi292 – 296Combined sources5
Turni297 – 299Combined sources3
Beta strandi301 – 304Combined sources4
Beta strandi307 – 314Combined sources8
Helixi318 – 333Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP04406.
SMRiP04406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04406.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 148Interaction with WARS1 PublicationAdd BLAST147
Regioni151 – 153Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni211 – 212Glyceraldehyde 3-phosphate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi245 – 250[IL]-x-C-x-x-[DE] motif1 Publication6

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiP04406.
KOiK00134.
OMAiKWGEVGA.
OrthoDBiEOG091G0B1Y.
PhylomeDBiP04406.
TreeFamiTF300533.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P04406-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti225N → D in CAA25833 (PubMed:6096821).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01888922A → G.1 PublicationCorresponds to variant rs45541435dbSNPEnsembl.1
Natural variantiVAR_049218251K → N.Corresponds to variant rs1062429dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0472891 – 42Missing in isoform 2. CuratedAdd BLAST42

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]
UniGeneiHs.544577.
Hs.592355.
Hs.598320.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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]
UniGeneiHs.544577.
Hs.592355.
Hs.598320.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP04406.
SMRiP04406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108868. 202 interactors.
DIPiDIP-32521N.
IntActiP04406. 94 interactors.
MINTiMINT-1150338.
STRINGi9606.ENSP00000229239.

Chemistry databases

BindingDBiP04406.
ChEMBLiCHEMBL2284.

PTM databases

iPTMnetiP04406.
PhosphoSitePlusiP04406.
SwissPalmiP04406.

Polymorphism and mutation databases

BioMutaiGAPDH.
DMDMi120649.

2D gel databases

DOSAC-COBS-2DPAGEP04406.
OGPiP04406.
REPRODUCTION-2DPAGEIPI00219018.
P04406.
SWISS-2DPAGEP04406.
UCD-2DPAGEP04406.

Proteomic databases

EPDiP04406.
PaxDbiP04406.
PeptideAtlasiP04406.
PRIDEiP04406.
TopDownProteomicsiP04406-1. [P04406-1]

Protocols and materials databases

DNASUi2597.
Structural Biology KnowledgebaseSearch...

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

CTDi2597.
DisGeNETi2597.
GeneCardsiGAPDH.
H-InvDBHIX0000949.
HIX0024996.
HGNCiHGNC:4141. GAPDH.
HPAiCAB005197.
CAB016392.
HPA040067.
HPA061280.
MIMi138400. gene.
neXtProtiNX_P04406.
OpenTargetsiENSG00000111640.
PharmGKBiPA28554.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiP04406.
KOiK00134.
OMAiKWGEVGA.
OrthoDBiEOG091G0B1Y.
PhylomeDBiP04406.
TreeFamiTF300533.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BioCyciMetaCyc:HS03433-MONOMER.
ZFISH:HS03433-MONOMER.
BRENDAi1.2.1.12. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP04406.

Miscellaneous databases

ChiTaRSiGAPDH. human.
EvolutionaryTraceiP04406.
GeneWikiiGlyceraldehyde_3-phosphate_dehydrogenase.
GenomeRNAii2597.
PROiP04406.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111640.
CleanExiHS_GAPDH.
ExpressionAtlasiP04406. baseline and differential.
GenevisibleiP04406. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG3P_HUMAN
AccessioniPrimary (citable) accession number: P04406
Secondary accession number(s): E7EUT4, P00354, Q53X65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 219 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.