Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-8355-00725
Entry Name
UniProt Accession
Theoretical PI
7.59
Molecular Weight
35697.78
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Glyceraldehyde-3-phosphate dehydrogenase
Protein Synonyms/Alias
GAPDH; 1.2.1.12; Peptidyl-cysteine S-nitrosylase GAPDH; 2.6.99.-;
Gene Name
gapdh
Gene Synonyms/Alias
gapd;
Created Date
01-OCT-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
245
Canonical
VSVVDLTCRLQKPAK
[1]
S-Palmitoylation
Organism
Xenopus laevis (African clawed frog)
NCBI Taxa ID
8355
Reference
[1] Yang J, Gibson B, Snider J, Jenkins CM, Han X, Gross RW. Submicromolarconcentrations of palmitoyl-CoA specifically thioesterify cysteine 244 inglyceraldehyde-3-phosphate dehydrogenase inhibiting enzyme activity: a novelmechanism potentially underlying fatty acid induced insulin resistance.Biochemistry. 2005 Sep 6;44(35):11903-12.[PMID:16128592]
Functional Description
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. 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 (By similarity).
Sequence Annotation
Nucleotide-binding: 11 12 NAD.
Region: 149 151 Glyceraldehyde 3-phosphate binding.
Region: 209 210 Glyceraldehyde 3-phosphate binding.
Active site: 150 150 Nucleophile.
Binding site: 33 33 NAD.
Binding site: 78 78 NAD; via carbonyl oxygen.
Binding site: 180 180 Glyceraldehyde 3-phosphate.
Binding site: 232 232 Glyceraldehyde 3-phosphate.
Binding site: 314 314 NAD.
Functional site: 177 177 Activates thiol group during catalysis.
Modified residue: 150 150 S-nitrosocysteine.
Protein Length
333 AA.
Protein Sequence
(Canonical)
MVKVGINGFG CIGRLVTRAA FDSGKVQVVA INDPFIDLDY MVYMFKYDST HGRFKGTVKA  60
ENGKLIINDQ VITVFQERDP SSIKWGDAGA VYVVESTGVF TTTEKASLHL KGGAKRVVIS  120
APSADAPMFV VGVNHEKYEN SLKVVSNASC TTNCLAPLAK VINDNFGIVE GLMTTVHAFT  180
ATQKTVDGPS GKLWRDGRGA GQNIIPASTG AAKAVGKVIP ELNGKITGMA FRVPTPNVSV  240
VDLTCRLQKP AKYDDIKAAI KTASEGPMKG ILGYTQDQVV STDFNGDTHS SIFDADAGIA  300
LNENFVKLVS WYDNECGYSN RVVDLVCHMA SKE                               333
FASTA
(Canonical)
>LipidDB-8355-00725|P51469
MVKVGINGFGCIGRLVTRAAFDSGKVQVVAINDPFIDLDYMVYMFKYDSTHGRFKGTVKA
ENGKLIINDQVITVFQERDPSSIKWGDAGAVYVVESTGVFTTTEKASLHLKGGAKRVVIS
APSADAPMFVVGVNHEKYENSLKVVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHAFT
ATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKITGMAFRVPTPNVSV
VDLTCRLQKPAKYDDIKAAIKTASEGPMKGILGYTQDQVVSTDFNGDTHSSIFDADAGIA
LNENFVKLVSWYDNECGYSNRVVDLVCHMASKE
Gene Ontology
GO:0005737; C:cytoplasm; ISS:UniProtKB
GO:0005829; C:cytosol; ISS:UniProtKB
GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB
GO:0005634; C:nucleus; ISS:UniProtKB
GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB
GO:0008017; F:microtubule binding; ISS:UniProtKB
GO:0051287; F:NAD binding; IEA:InterPro
GO:0050661; F:NADP binding; IEA:InterPro
GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB
GO:0006006; P:glucose metabolic process; IEA:InterPro
GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway
GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB
GO:0051402; P:neuron apoptotic process; ISS:UniProtKB
GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB
GO:0050821; P:protein stabilization; ISS:UniProtKB
Interpro
InterPro; IPR020831; GlycerAld/Erythrose_P_DH
InterPro; IPR020830; GlycerAld_3-P_DH_AS
InterPro; IPR020829; GlycerAld_3-P_DH_cat
InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd
InterPro; IPR006424; Glyceraldehyde-3-P_DH_1
InterPro; IPR016040; NAD(P)-bd_dom
Pfam
Pfam; PF02800; Gp_dh_C;
Pfam; PF00044; Gp_dh_N;
SMART
SMART; SM00846; Gp_dh_N;
PROSITE
PROSITE; PS00071; GAPDH;
PRINTS
PRINTS; PR00078; G3PDHDRGNASE;