Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:3170585, PubMed:11724794).
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 (PubMed:3170585, PubMed:11724794).
Modulates the organization and assembly of the cytoskeleton (By similarity).
Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity).
Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094).
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 (PubMed:23071094).
Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501).
Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity).
Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).

Homotetramer (PubMed:16239728, PubMed:16510976).
Interacts with TPPP; the interaction is direct (By similarity).
Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation (By similarity).
Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation (By similarity).
Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules (By similarity).
Associates with microtubules (By similarity).
Interacts with EIF1AD, USP25, PRKCI and WARS1 (PubMed:11724794, PubMed:16501887, PubMed:15628863, PubMed:20644585).
Interacts with phosphorylated RPL13A; inhibited by oxidatively-modified low-densitity lipoprotein (LDL(ox)) (PubMed:22771119).
Component of the GAIT complex (PubMed:15479637).
Interacts with FKBP6; leading to inhibit GAPDH catalytic activity (PubMed:19001379).
Interacts with TRAF2, promoting TRAF2 ubiquitination (PubMed:23332158).
Interacts with TRAF3, promoting TRAF3 ubiquitination (PubMed:27387501).

Cytoplasm, cytosol. Nucleus. Cytoplasm, perinuclear region. Membrane. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Postnuclear and Perinuclear regions.

#Acetylation

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Entrez Gene: 374193 Chicken

Entrez Gene: 2597 Human

Entrez Gene: 100042025 Mouse

Entrez Gene: 14433 Mouse

Entrez Gene: 24383 Rat

Entrez Gene: 685186 Rat

Entrez Gene: 317743 Zebrafish

Omim: 138400 Human

SwissProt: P00356 Chicken

SwissProt: P04406 Human

SwissProt: P16858 Mouse

SwissProt: P04797 Rat

SwissProt: Q5XJ10 Zebrafish

oading Control
Glyceraldehyde 3 phosphate dehydrogenase (GAPDH) is well known as one of the key enzymes involved in glycolysis. As well as functioning as a glycolytic enzyme in cytoplasm, recent evidence suggests that mammalian GAPDH is also involved in a great number of intracellular proceses such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. During the last decade a lot of data appeared concerning the role of GAPDH in different pathologies including prostate cancer progression, programmed neuronal cell death, age related neuronal diseases, such as Alzheimer's and Huntington's disease. GAPDH is expressed in all cells. It is constitutively expressed in almost all tissues at high levels. There are however some physiological factors such as hypoxia and diabetes that increase GAPDH expression in certain cell types. GAPDH molecule is composed of four 36kDa subunits.