Skip Header

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

Glyceraldehyde-3-phosphate dehydrogenase

Gene

Gapdh

Organism
Rattus norvegicus (Rat)
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. 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 similarity4 Publications

Catalytic activityi

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

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, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (Gapdh-ps2), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (RGD1562758)
  2. Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Alpha-enolase (Eno1), Beta-enolase (Eno3), Gamma-enolase (Eno2)
  5. Pyruvate kinase PKLR (Pklr), Pyruvate kinase PKM (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (LOC100362738), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pkm)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NADBy similarity
Binding sitei78 – 781NAD; via carbonyl oxygenBy similarity
Binding sitei120 – 1201NADBy similarity
Active sitei150 – 1501NucleophilePROSITE-ProRule annotation1 Publication
Sitei177 – 1771Activates thiol group during catalysisBy similarity
Binding sitei180 – 1801Glyceraldehyde 3-phosphateBy similarity
Binding sitei232 – 2321Glyceraldehyde 3-phosphateBy similarity
Binding sitei314 – 3141NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NADBy similarity

GO - Molecular functioni

  • glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • NAD binding Source: InterPro
  • NADP binding Source: InterPro
  • peptidyl-cysteine S-nitrosylase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: RGD
  • carbohydrate metabolic process Source: RGD
  • gluconeogenesis Source: RGD
  • glycolytic process Source: RGD
  • microtubule cytoskeleton organization Source: UniProtKB
  • neuron apoptotic process Source: UniProtKB
  • peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of translation Source: UniProtKB-KW
  • response to ammonium ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Apoptosis, Glycolysis, Translation regulation

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.12. 5301.
SABIO-RKP04797.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
Short name:
GAPDH
Alternative name(s):
38 kDa BFA-dependent ADP-ribosylation substrate
BARS-38
Peptidyl-cysteine S-nitrosylase GAPDH (EC:2.6.99.-)
Gene namesi
Name:Gapdh
Synonyms:Gapd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2661. Gapdh.

Subcellular locationi

  • Cytoplasmcytosol
  • Cytoplasmcytoskeleton
  • Nucleus

  • Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with CHP1 to small punctate structures along the microtubules tracks.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • GAIT complex Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi149 – 1491S → A: Does not affect interaction with SIRT1. 1 Publication
Mutagenesisi150 – 1501C → S: Abolishes S-nitrosylation and subsequent nuclear translocation. 2 Publications
Mutagenesisi151 – 1511T → A: Does not affect interaction with SIRT1. 1 Publication
Mutagenesisi152 – 1521T → A: Abolishes interaction and subsequent nitrosylation of SIRT1. 1 Publication
Mutagenesisi225 – 2251K → A: Abolishes interaction with SIAH1. 1 Publication
Mutagenesisi234 – 2341P → A: Does not affect interaction with SIAH1. 1 Publication
Mutagenesisi235 – 2351T → A: Does not affect interaction with SIAH1. 1 Publication

Chemistry

ChEMBLiCHEMBL2176832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 333332Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N6,N6-dimethyllysineBy similarity
Modified residuei7 – 71Deamidated asparagineBy similarity
Modified residuei40 – 401PhosphotyrosineBy similarity
Modified residuei59 – 591N6-acetyllysineBy similarity
Modified residuei62 – 621Deamidated asparagineBy similarity
Modified residuei64 – 641N6,N6-dimethyllysineBy similarity
Modified residuei68 – 681Deamidated asparagineBy similarity
Modified residuei73 – 731PhosphothreonineBy similarity
Modified residuei120 – 1201PhosphoserineBy similarity
Modified residuei146 – 1461PhosphoserineBy similarity
Modified residuei147 – 1471Deamidated asparagineBy similarity
Modified residuei149 – 1491PhosphoserineBy similarity
Modified residuei150 – 1501ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form1 Publication
Modified residuei150 – 1501Cysteine persulfideBy similarity
Modified residuei150 – 1501S-nitrosocysteine; in reversibly inhibited form3 Publications
Modified residuei151 – 1511PhosphothreonineBy similarity
Modified residuei153 – 1531Deamidated asparagineBy similarity
Modified residuei175 – 1751PhosphothreonineBy similarity
Modified residuei180 – 1801PhosphothreonineBy similarity
Modified residuei182 – 1821PhosphothreonineBy similarity
Modified residuei192 – 1921N6,N6-dimethyllysine; alternateBy similarity
Modified residuei192 – 1921N6-acetyllysine; alternateBy similarity
Modified residuei192 – 1921N6-malonyllysine; alternateBy similarity
Modified residuei209 – 2091PhosphothreonineBy similarity
Modified residuei213 – 2131N6,N6-dimethyllysine; alternateBy similarity
Modified residuei213 – 2131N6-malonyllysine; alternateBy similarity
Modified residuei217 – 2171N6-acetyllysineBy similarity
Modified residuei223 – 2231Deamidated asparagineBy similarity
Modified residuei225 – 2251N6,N6-dimethyllysine; alternateBy similarity
Modified residuei225 – 2251N6-acetyllysine; alternateBy similarity
Modified residuei227 – 2271PhosphothreonineBy similarity
Modified residuei235 – 2351PhosphothreonineBy similarity
Modified residuei239 – 2391PhosphoserineBy similarity
Modified residuei245 – 2451S-nitrosocysteineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei258 – 2581N6,N6-dimethyllysineBy similarity
Modified residuei261 – 2611N6,N6-dimethyllysineBy similarity
Modified residuei310 – 3101PhosphoserineBy similarity
Modified residuei314 – 3141Deamidated asparagineBy similarity
Modified residuei331 – 3311PhosphoserineBy similarity
Modified residuei332 – 3321N6,N6-dimethyllysineBy similarity

Post-translational modificationi

S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus. The effect of S-nitrosylation on enzymatic activity is unclear: according to some authors, it inhibits enzymatic activity and increases endogenous ADP-ribosylation, inhibiting the enzyme in a non-reversible manner (PubMed:8626764). According to others, it does not affect glycolysis (PubMed:15951807). ADP-ribosylation is likely to be a pathophysiological event associated with inhibition of gluconeogenesis. 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 similarity4 Publications
ISGylated.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei154 – 1541Not nitrosylated

Keywords - PTMi

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

Proteomic databases

PaxDbiP04797.
PRIDEiP04797.

2D gel databases

World-2DPAGE0004:P04797.

PTM databases

iPTMnetiP04797.
PhosphoSiteiP04797.

Expressioni

Tissue specificityi

High levels in skeletal muscle and heart, low levels in liver, brain, and kidney.1 Publication

Gene expression databases

GenevisibleiP04797. RN.

Interactioni

Subunit structurei

Homotetramer. Interacts with EIF1AD, USP25, PRKCI and WARS. Interacts with TPPP; the interaction is direct (By similarity). 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. Interacts with phosphorylated RPL13A (By similarity). Associates with microtubules. Component of the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Akt1P471963EBI-349219,EBI-7204362
Chp1P610233EBI-349219,EBI-917838
Ppm1eQ80Z305EBI-349219,EBI-7473061
Slc2a4P193572EBI-349219,EBI-915426

GO - Molecular functioni

  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi246554. 6 interactions.
IntActiP04797. 8 interactions.
MINTiMINT-1775142.
STRINGi10116.ENSRNOP00000040878.

Structurei

3D structure databases

ProteinModelPortaliP04797.
SMRiP04797. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 146145Interaction with WARSBy similarityAdd
BLAST
Regioni149 – 1513Glyceraldehyde 3-phosphate bindingBy similarity
Regioni209 – 2102Glyceraldehyde 3-phosphate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi243 – 2486[IL]-x-C-x-x-[DE] motifBy similarity

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiP04797.
KOiK00134.
OMAiSTDFIHD.
OrthoDBiEOG7Q5HDF.
PhylomeDBiP04797.
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]

Sequencei

Sequence statusi: Complete.

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

P04797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKVGVNGFG RIGRLVTRAA FSCDKVDIVA INDPFIDLNY MVYMFQYDST
60 70 80 90 100
HGKFNGTVKA ENGKLVINGK PITIFQERDP ANIKWGDAGA EYVVESTGVF
110 120 130 140 150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC
160 170 180 190 200
TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA
210 220 230 240 250
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP
260 270 280 290 300
AKYDDIKKVV KQAAEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA
310 320 330
LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE
Length:333
Mass (Da):35,828
Last modified:January 23, 2007 - v3
Checksum:iD9E5ED4F38544C77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 822AN → VK in AAA41193 (PubMed:2987824).Curated
Sequence conflicti129 – 1291F → L in AAH87743 (PubMed:15489334).Curated
Sequence conflicti305 – 3051F → I in AAA41193 (PubMed:2987824).Curated
Sequence conflicti305 – 3051F → I in CAA26150 (PubMed:6548307).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02231 mRNA. Translation: CAA26150.1.
M17701 mRNA. Translation: AAA41193.1.
AB017801 mRNA. Translation: BAB11748.1.
AF106860 mRNA. Translation: AAD08929.2.
BC059110 mRNA. Translation: AAH59110.1.
BC087743 mRNA. Translation: AAH87743.1.
M29341 mRNA. Translation: AAA40814.1.
M11561 mRNA. Translation: AAA41795.1.
PIRiA23013. DERTG.
RefSeqiNP_058704.1. NM_017008.4.
UniGeneiRn.129558.
Rn.91450.

Genome annotation databases

EnsembliENSRNOT00000050443; ENSRNOP00000040878; ENSRNOG00000018630.
GeneIDi24383.
KEGGirno:24383.
UCSCiRGD:2661. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02231 mRNA. Translation: CAA26150.1.
M17701 mRNA. Translation: AAA41193.1.
AB017801 mRNA. Translation: BAB11748.1.
AF106860 mRNA. Translation: AAD08929.2.
BC059110 mRNA. Translation: AAH59110.1.
BC087743 mRNA. Translation: AAH87743.1.
M29341 mRNA. Translation: AAA40814.1.
M11561 mRNA. Translation: AAA41795.1.
PIRiA23013. DERTG.
RefSeqiNP_058704.1. NM_017008.4.
UniGeneiRn.129558.
Rn.91450.

3D structure databases

ProteinModelPortaliP04797.
SMRiP04797. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246554. 6 interactions.
IntActiP04797. 8 interactions.
MINTiMINT-1775142.
STRINGi10116.ENSRNOP00000040878.

Chemistry

ChEMBLiCHEMBL2176832.

PTM databases

iPTMnetiP04797.
PhosphoSiteiP04797.

2D gel databases

World-2DPAGE0004:P04797.

Proteomic databases

PaxDbiP04797.
PRIDEiP04797.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000050443; ENSRNOP00000040878; ENSRNOG00000018630.
GeneIDi24383.
KEGGirno:24383.
UCSCiRGD:2661. rat.

Organism-specific databases

CTDi2597.
RGDi2661. Gapdh.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiP04797.
KOiK00134.
OMAiSTDFIHD.
OrthoDBiEOG7Q5HDF.
PhylomeDBiP04797.
TreeFamiTF300533.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BRENDAi1.2.1.12. 5301.
SABIO-RKP04797.

Miscellaneous databases

PROiP04797.

Gene expression databases

GenevisibleiP04797. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family."
    Fort P., Marty L., Piechaczyk M., el Sabrouty S., Dani C., Jeanteur P., Blanchard J.-M.
    Nucleic Acids Res. 13:1431-1442(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Muscle.
  2. "Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene."
    Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.
    Nucleic Acids Res. 13:2485-2502(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs."
    Tajima H., Tsuchiya K., Yamada M., Kondo K., Katsube N., Ishitani R.
    NeuroReport 10:2029-2033(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: Sprague-Dawley.
    Tissue: Cerebellum.
  4. "Isolation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH) cDNA isoform from rat brain by a rapid PCR-based cloning method and its expression by RT-PCR."
    Zheng J., Ramirez V.D.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Pituitary anterior lobe.
  6. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 65-105; 116-137; 144-184; 233-246 AND 308-321, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  7. "Trifluoperazine activates and releases latent ATP-generating enzymes associated with the synaptic plasma membrane."
    Leung T.K.C., Hall C., Monfries C., Lim L.
    J. Neurochem. 49:232-238(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 235-333.
    Tissue: Brain.
  8. "Post-transcriptional regulation of glyceraldehyde-3-phosphate-dehydrogenase gene expression in rat tissues."
    Piechaczyk M., Blanchard J.-M., Marty L., Dani C., Panabieres F., el Sabrouty S., Fort P., Jeanteur P.
    Nucleic Acids Res. 12:6951-6963(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 261-323, TISSUE SPECIFICITY.
    Tissue: Glial tumor.
  9. "1.5 kb mRNA abundantly expressed in rat tumors encodes a 37 kilodalton protein in vitro."
    Maehara Y., Fujiyoshi T., Takahashi K., Yamamoto M., Endo H.
    Biochem. Biophys. Res. Commun. 131:800-805(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 267-333.
  10. "Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation."
    Molina y Vedia L., McDonald B., Reep B., Brune B., Di Silvio M., Billiar T.R., Lapetina E.G.
    J. Biol. Chem. 267:24929-24932(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION.
  11. "Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment."
    Mohr S., Stamler J.S., Brune B.
    J. Biol. Chem. 271:4209-4214(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-150, ADP-RIBOSYLATION AT CYS-150, ABSENCE OF S-NITROSYLATION AT CYS-154, ACTIVE SITE.
  12. "Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules."
    Andrade J., Pearce S.T., Zhao H., Barroso M.
    Biochem. J. 384:327-336(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHP1, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION.
  13. "S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding."
    Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y., Takahashi M., Cheah J.H., Tankou S.K., Hester L.D., Ferris C.D., Hayward S.D., Snyder S.H., Sawa A.
    Nat. Cell Biol. 7:665-674(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIAH1, S-NITROSYLATION AT CYS-150, MUTAGENESIS OF CYS-150; LYS-225; PRO-234 AND THR-235.
  14. "GOSPEL: a neuroprotective protein that binds to GAPDH upon S-nitrosylation."
    Sen N., Hara M.R., Ahmad A.S., Cascio M.B., Kamiya A., Ehmsen J.T., Agrawal N., Hester L., Dore S., Snyder S.H., Sawa A.
    Neuron 63:81-91(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RILPL1 AND SIAH1.
  15. Cited for: FUNCTION AS NITROSYLASE, SUBCELLULAR LOCATION, INTERACTION WITH SIRT1, S-NITROSYLATION AT CYS-150, MUTAGENESIS OF SER-149; CYS-150; THR-151 AND THR-152.

Entry informationi

Entry nameiG3P_RAT
AccessioniPrimary (citable) accession number: P04797
Secondary accession number(s): P09328, Q5M916, Q9QWU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.