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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 (HEL-S-30), Pyruvate kinase (PKM), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351NAD2 Publications
Binding sitei80 – 801NAD; via carbonyl oxygen2 Publications
Binding sitei122 – 1221NAD2 Publications
Active sitei152 – 1521Nucleophile
Sitei179 – 1791Activates thiol group during catalysis
Binding sitei182 – 1821Glyceraldehyde 3-phosphateBy similarity
Binding sitei234 – 2341Glyceraldehyde 3-phosphateBy similarity
Binding sitei316 – 3161NAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 142NAD2 Publications

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461M → L: Drastic reduction of the extent and significant prolongation of the lag phase of free radical-induced aggregation. 1 Publication
Mutagenesisi105 – 1051M → L: Increased resistance to free radical-induced aggregation. 1 Publication
Mutagenesisi152 – 1521C → 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 Publication
Mutagenesisi156 – 1561C → 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 Publication
Mutagenesisi196 – 1961W → F: Increased free radical-induced aggregation. 1 Publication
Mutagenesisi245 – 2451L → M: Inhibits S-nitrosylation of Cys-247; when associated with M-250. 1 Publication
Mutagenesisi247 – 2471C → 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 Publication
Mutagenesisi250 – 2501E → M: Inhibits S-nitrosylation of Cys-247; when associated with M-245. 1 Publication
Mutagenesisi320 – 3201Y → F: No effect on free radical-induced aggregation. 1 Publication

Organism-specific databases

PharmGKBiPA28554.

Chemistry

ChEMBLiCHEMBL2284.

Polymorphism and mutation databases

BioMutaiGAPDH.
DMDMi120649.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 335334Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145486Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6-dimethyllysine1 Publication
Modified residuei9 – 91Deamidated asparagine1 Publication
Modified residuei42 – 421PhosphotyrosineCombined sources
Modified residuei46 – 461Methionine sulfoxide; in vitro1 Publication
Modified residuei61 – 611N6-acetyllysineCombined sources
Modified residuei64 – 641Deamidated asparagine1 Publication
Modified residuei66 – 661N6,N6-dimethyllysine1 Publication
Modified residuei70 – 701Deamidated asparagine1 Publication
Modified residuei75 – 751PhosphothreonineCombined sources1 Publication
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei148 – 1481Phosphoserine1 Publication
Modified residuei149 – 1491Deamidated asparagine1 Publication
Modified residuei151 – 1511PhosphoserineCombined sources
Modified residuei152 – 1521ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity
Modified residuei152 – 1521Cysteine persulfideBy similarity
Modified residuei152 – 1521S-nitrosocysteine; in reversibly inhibited formBy similarity
Modified residuei153 – 1531PhosphothreonineCombined sources
Modified residuei155 – 1551Deamidated asparagine1 Publication
Modified residuei177 – 1771PhosphothreonineCombined sources
Modified residuei182 – 1821PhosphothreonineCombined sources
Modified residuei184 – 1841PhosphothreonineCombined sources
Modified residuei194 – 1941N6,N6-dimethyllysine; alternate1 Publication
Modified residuei194 – 1941N6-acetyllysine; alternateCombined sources
Modified residuei194 – 1941N6-malonyllysine; alternate1 Publication
Modified residuei211 – 2111PhosphothreonineCombined sources
Modified residuei215 – 2151N6,N6-dimethyllysine; alternate1 Publication
Modified residuei215 – 2151N6-malonyllysine; alternate1 Publication
Modified residuei219 – 2191N6-acetyllysineCombined sources
Modified residuei225 – 2251Deamidated asparagine1 Publication
Modified residuei227 – 2271N6,N6-dimethyllysine; alternate1 Publication
Modified residuei227 – 2271N6-acetyllysine; alternateCombined sources
Modified residuei229 – 2291PhosphothreonineCombined sources1 Publication
Modified residuei237 – 2371Phosphothreonine1 Publication
Modified residuei241 – 2411PhosphoserineCombined sources
Modified residuei247 – 2471S-nitrosocysteine2 Publications
Modified residuei254 – 2541N6-acetyllysineCombined sources
Modified residuei260 – 2601N6,N6-dimethyllysine1 Publication
Modified residuei263 – 2631N6,N6-dimethyllysine1 Publication
Modified residuei312 – 3121PhosphoserineCombined sources1 Publication
Modified residuei316 – 3161Deamidated asparagine1 Publication
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei334 – 3341N6,N6-dimethyllysine1 Publication

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.
MaxQBiP04406.
PaxDbiP04406.
PeptideAtlasiP04406.
PRIDEiP04406.
TopDownProteomicsiP04406-1. [P04406-1]

2D gel databases

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

PTM databases

iPTMnetiP04406.
PhosphoSiteiP04406.
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

  • identical protein binding Source: IntAct
  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

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

Chemistry

BindingDBiP04406.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi13 – 2513Combined sources
Beta strandi27 – 348Combined sources
Beta strandi36 – 383Combined sources
Helixi40 – 489Combined sources
Turni51 – 533Combined sources
Beta strandi60 – 634Combined sources
Beta strandi66 – 694Combined sources
Beta strandi72 – 776Combined sources
Helixi82 – 843Combined sources
Turni87 – 915Combined sources
Beta strandi94 – 974Combined sources
Beta strandi99 – 1013Combined sources
Helixi105 – 1084Combined sources
Helixi109 – 1146Combined sources
Beta strandi117 – 1237Combined sources
Beta strandi126 – 1283Combined sources
Turni133 – 1353Combined sources
Helixi137 – 1393Combined sources
Beta strandi145 – 1484Combined sources
Helixi152 – 16817Combined sources
Beta strandi170 – 18011Combined sources
Beta strandi185 – 1895Combined sources
Helixi196 – 1994Combined sources
Turni202 – 2043Combined sources
Beta strandi207 – 2104Combined sources
Turni213 – 2164Combined sources
Helixi217 – 2204Combined sources
Helixi222 – 2243Combined sources
Beta strandi227 – 23610Combined sources
Beta strandi241 – 25111Combined sources
Helixi255 – 26713Combined sources
Turni268 – 2736Combined sources
Beta strandi274 – 2774Combined sources
Helixi283 – 2864Combined sources
Beta strandi292 – 2965Combined sources
Turni297 – 2993Combined sources
Beta strandi301 – 3044Combined sources
Beta strandi307 – 3148Combined sources
Helixi318 – 33316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04406.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 148147Interaction with WARSAdd
BLAST
Regioni151 – 1533Glyceraldehyde 3-phosphate bindingBy similarity
Regioni211 – 2122Glyceraldehyde 3-phosphate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi245 – 2506[IL]-x-C-x-x-[DE] motif1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251N → D in CAA25833 (PubMed:6096821).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221A → G.1 Publication
Corresponds to variant rs45541435 [ dbSNP | Ensembl ].
VAR_018889
Natural varianti251 – 2511K → N.
Corresponds to variant rs1062429 [ dbSNP | Ensembl ].
VAR_049218

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4242Missing in isoform 2. CuratedVSP_047289Add
BLAST

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
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. Positions 3-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP04406.
ChEMBLiCHEMBL2284.

PTM databases

iPTMnetiP04406.
PhosphoSiteiP04406.
SwissPalmiP04406.

Polymorphism and mutation databases

BioMutaiGAPDH.
DMDMi120649.

2D gel databases

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

Proteomic databases

EPDiP04406.
MaxQBiP04406.
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.
GeneCardsiGAPDH.
H-InvDBHIX0000949.
HIX0024996.
HGNCiHGNC:4141. GAPDH.
HPAiCAB005197.
CAB016392.
HPA040067.
HPA061280.
MIMi138400. gene.
neXtProtiNX_P04406.
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.
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: September 7, 2016
This is version 217 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.