Glyceraldehyde 3-phosphate dehydrogenase

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
	determinants of enzyme thermostability observed in the molecular structure of thermus aquaticus d-glyceraldehyde-3-phosphate dehydrogenase at 2.5 angstroms resolution
Identifiers
Symbol	Gp_dh_N
Pfam	PF00044
Pfam clan	CL0063
InterPro	IPR020828
PROSITE	PDOC00069
SCOP2	1gd1 / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

GAPDH
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1U8F, 1ZNQ, 3GPD, 4WNC, 4WNI
Identifiers
Aliases	GAPDH, GAPD, G3PD, HEL-S-162eP, glyceraldehyde-3-phosphate dehydrogenase
External IDs	OMIM: 138400; MGI: 5434255; HomoloGene: 107053; GeneCards: GAPDH; OMA:GAPDH - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	6,538,374 bp
RNA expression pattern
	Top expressed in
	frontal pole; ; pons; ; paraflocculus of cerebellum; ; Brodmann area 10; ; triceps brachii muscle; ; deltoid muscle; ; Skeletal muscle tissue of biceps brachii; ; Brodmann area 46; ; lateral nuclear group of thalamus; ; body of tongue;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity; microtubule binding; NAD binding; oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; protein binding; peptidyl-cysteine S-nitrosylase activity; NADP binding; identical protein binding; oxidoreductase activity; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; aspartic-type endopeptidase inhibitor activity; disordered domain specific binding;
Cellular component	vesicle; nuclear membrane; membrane; intracellular membrane-bounded organelle; microtubule cytoskeleton; lipid droplet; plasma membrane; perinuclear region of cytoplasm; GAIT complex; cytoskeleton; extracellular exosome; cytosol; nucleus; extracellular matrix; cytoplasm; ribonucleoprotein complex;
Biological process	peptidyl-cysteine S-trans-nitrosylation; neuron apoptotic process; gluconeogenesis; negative regulation of translation; glycolytic process; canonical glycolysis; protein stabilization; cellular response to interferon-gamma; regulation of translation; microtubule cytoskeleton organization; regulation of macroautophagy; apoptotic process; glucose metabolic process; negative regulation of endopeptidase activity; antimicrobial humoral immune response mediated by antimicrobial peptide;
	Sources:Amigo / QuickGO
Orthologs
	2597
	100042025
	ENSG00000111640
	n/a
	P04406
	P16858
NM_002046; NM_001256799; NM_001289745; NM_001289746; NM_001357938;
	NM_001357943; NM_001357944
	XM_001476707
	NP_001243728; NP_001276674; NP_001276675; NP_002037; NP_001344872
	NP_001276655; NP_032110
	Wikidata
View/Edit Human	View/Edit Mouse

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain

crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pyrococcus horikoshii ot3

Identifiers

Symbol

Gp_dh_C

Pfam clan

1gd1 / SCOPe / SUPFAM

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Glyceraldehyde 3-phosphate dehydrogenase (abbreviated GAPDH) (EC 1.2.1.12) is an enzyme of about 37kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In addition to this long established metabolic function, GAPDH has recently been implicated in several non-metabolic processes, including transcription activation, initiation of apoptosis,^[4] ER-to-Golgi vesicle shuttling, and fast axonal, or axoplasmic transport.^[5] In sperm, a testis-specific isoenzyme GAPDHS is expressed.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000111640 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Tarze A, Deniaud A, Le Bras M, Maillier E, Molle D, Larochette N, Zamzami N, Jan G, Kroemer G, Brenner C (April 2007). "GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilization". Oncogene. 26 (18): 2606–2620. doi:10.1038/sj.onc.1210074. PMID 17072346. S2CID 20291542.
^ Zala D, Hinckelmann MV, Yu H, Lyra da Cunha MM, Liot G, Cordelières FP, Marco S, Saudou F (January 2013). "Vesicular glycolysis provides on-board energy for fast axonal transport". Cell. 152 (3): 479–491. doi:10.1016/j.cell.2012.12.029. PMID 23374344.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000111640 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[Tarze_2007-4] Tarze A, Deniaud A, Le Bras M, Maillier E, Molle D, Larochette N, Zamzami N, Jan G, Kroemer G, Brenner C (April 2007). "GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilization". Oncogene. 26 (18): 2606–2620. doi:10.1038/sj.onc.1210074. PMID 17072346. S2CID 20291542.

[Zala_2013-5] Zala D, Hinckelmann MV, Yu H, Lyra da Cunha MM, Liot G, Cordelières FP, Marco S, Saudou F (January 2013). "Vesicular glycolysis provides on-board energy for fast axonal transport". Cell. 152 (3): 479–491. doi:10.1016/j.cell.2012.12.029. PMID 23374344.

[1]

[2]

[3]

[4]

[5]