HUMAN:G3P

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	GAPDH (synonyms: GAPD)
Protein Name(s)	Glyceraldehyde-3-phosphate dehydrogenase GAPDH Peptidyl-cysteine S-nitrosylase GAPDH
External Links
UniProt	P04406
EMBL	X01677 M17851 M33197 J02642 J04038 X53778 AF261085 AY007133 AB062273 BT006893 AY340484 CR407671 AC006064 CH471116 BC001601 BC004109 BC009081 BC013310 BC023632 BC025925 BC026907 BC029618 BC083511
CCDS	CCDS58201.1 CCDS8549.1
PIR	A31988
RefSeq	NP_001243728.1 NP_001276674.1 NP_001276675.1 NP_002037.2
UniGene	Hs.544577 Hs.592355 Hs.598320
PDB	1U8F 1ZNQ 2FEH 3GPD 4WNC 4WNI
PDBsum	1U8F 1ZNQ 2FEH 3GPD 4WNC 4WNI
ProteinModelPortal	P04406
SMR	P04406
BioGrid	108868
DIP	DIP-32521N
IntAct	P04406
MINT	MINT-1150338
STRING	9606.ENSP00000229239
BindingDB	P04406
ChEMBL	CHEMBL2284
DrugBank	DB07347 DB02059 DB00157 DB03893
iPTMnet	P04406
PhosphoSitePlus	P04406
SwissPalm	P04406
BioMuta	GAPDH
DMDM	120649
DOSAC-COBS-2DPAGE	P04406
OGP	P04406
REPRODUCTION-2DPAGE	IPI00219018 P04406
SWISS-2DPAGE	P04406
UCD-2DPAGE	P04406
EPD	P04406
PaxDb	P04406
PeptideAtlas	P04406
PRIDE	P04406
TopDownProteomics	P04406-1
DNASU	2597
Ensembl	ENST00000229239 ENST00000396858 ENST00000396859 ENST00000396861 ENST00000619601
GeneID	2597
KEGG	hsa:2597
UCSC	uc031qfw.3
CTD	2597
DisGeNET	2597
GeneCards	GAPDH
H-InvDB	HIX0000949 HIX0024996
HGNC	HGNC:4141
HPA	CAB005197 CAB016392 HPA040067 HPA061280
MIM	138400
neXtProt	NX_P04406
OpenTargets	ENSG00000111640
PharmGKB	PA28554
eggNOG	KOG0657 COG0057
GeneTree	ENSGT00760000119172
HOGENOM	HOG000071678
HOVERGEN	HBG000227
InParanoid	P04406
KO	K00134
OMA	KWGEVGA
OrthoDB	EOG091G0B1Y
PhylomeDB	P04406
TreeFam	TF300533
BioCyc	MetaCyc:HS03433-MONOMER
BRENDA	1.2.1.12
Reactome	[www.reactome.org/content/detail/R-HSA-70171 R-HSA-70171] [www.reactome.org/content/detail/R-HSA-70263 R-HSA-70263]
SABIO-RK	P04406
UniPathway	UPA00109
ChiTaRS	GAPDH
EvolutionaryTrace	P04406
GeneWiki	Glyceraldehyde_3-phosphate_dehydrogenase
GenomeRNAi	2597
PRO	PR:P04406
Proteomes	UP000005640
Bgee	ENSG00000111640
CleanEx	HS_GAPDH
ExpressionAtlas	P04406
Genevisible	P04406
GO	GO:0005737 GO:0005829 GO:0070062 GO:0031012 GO:0097452 GO:0043231 GO:0030529 GO:0005811 GO:0016020 GO:0015630 GO:0031965 GO:0005634 GO:0048471 GO:0005886 GO:0031982 GO:0004365 GO:0042802 GO:0008017 GO:0051287 GO:0050661 GO:0035605 GO:0061621 GO:0071346 GO:0006094 GO:0000226 GO:0017148 GO:0051402 GO:0035606 GO:0050821 GO:0016241
Gene3D	3.40.50.720
InterPro	IPR020831 IPR020830 IPR020829 IPR020828 IPR006424 IPR016040
PANTHER	PTHR10836
Pfam	PF02800 PF00044
PIRSF	PIRSF000149
PRINTS	PR00078
SMART	SM00846
SUPFAM	SSF51735
TIGRFAMs	TIGR01534
PROSITE	PS00071

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0005737	cytoplasm	PMID:11785981^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:11785981^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21758	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24507776^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0050715	positive regulation of cytokine secretion	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0052501	positive regulation by organism of apoptotic process in other organism involved in symbiotic interaction	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050832	defense response to fungus	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010951	negative regulation of endopeptidase activity	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019828	aspartic-type endopeptidase inhibitor activity	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051873	killing by host of symbiont cells	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
	GO:0005634	nucleus	PMID:28404743^[4]	ECO:0000314			C		HUMAN G3P (GAPDH) // GAPDH was localized in the nucleus of SMCs in both the control cells and the H2O2 treated cells (Fig 3D).	complete CACAO 12689
involved_in	GO:0031640	killing of cells of other organism	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
	GO:0005829	cytosol	PMID:28404743^[4]	ECO:0000314			C		HUMAN G3P (GAPDH) // GADPH was evident in the cytosol of both control cells as well as cells treated with H2O2 (Fig 3C).	complete CACAO 12690
involved_in	GO:0061844	antimicrobial humoral immune response mediated by antimicrobial peptide	PMID:22832495^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:19190083^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002202)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:11487543^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	produced_by:(CL:0002563)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:12519789^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	produced_by:(CL:0000236)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
part_of	GO:0097452	GAIT complex	PMID:23071094^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097452	GAIT complex	PMID:15479637^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071346	cellular response to interferon-gamma	PMID:15479637^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21362503^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002367)	Seeded From UniProt	complete
involved_in	GO:0051402	neuron apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	P		Seeded From UniProt	complete
involved_in	GO:0035606	peptidyl-cysteine S-trans-nitrosylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	P		Seeded From UniProt	complete
enables	GO:0035605	peptidyl-cysteine S-nitrosylase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	F		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:15479637^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:15479637^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:23071094^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0015630	microtubule cytoskeleton	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	C		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	C		Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	PMID:14741744^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0002107)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	C		Seeded From UniProt	complete
enables	GO:0004365	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity	PMID:3170585^[18]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004365	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity	PMID:7030790^[19]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004365	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	F		Seeded From UniProt	complete
involved_in	GO:0000226	microtubule cytoskeleton organization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P04797	P		Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10367 FB:FBgn0001091 FB:FBgn0001092 MGI:MGI:95653 PANTHER:PTN000089473 RGD:2661 SGD:S000003424 SGD:S000003588 SGD:S000003769 TAIR:locus:2103085	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10367 MGI:MGI:95640 PANTHER:PTN000089473 RGD:2661 SGD:S000003424 SGD:S000003588 SGD:S000003769 TAIR:locus:2103085 UniProtKB:M0R590 UniProtKB:P04406 UniProtKB:Q8IKK7 UniProtKB:Q9FX54	C		Seeded From UniProt	complete
enables	GO:0004365	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10367 FB:FBgn0001091 FB:FBgn0001092 MGI:MGI:95640 MGI:MGI:95653 PANTHER:PTN000089473 RGD:2661 SGD:S000003424 SGD:S000003588 SGD:S000003769 TAIR:locus:2032810 TAIR:locus:2206435 UniProtKB:M0R590 UniProtKB:O14556 UniProtKB:P04406 UniProtKB:P20445 UniProtKB:Q9FX54	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:24101517^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21988832^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04406	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20392205^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04406	F		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006006	glucose metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006424	P		Seeded From UniProt	complete
enables	GO:0016620	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006424 InterPro:IPR020828 InterPro:IPR020829 InterPro:IPR020830 InterPro:IPR020831	F		Seeded From UniProt	complete
enables	GO:0050661	NADP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006424	F		Seeded From UniProt	complete
enables	GO:0051287	NAD binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006424	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006424 InterPro:IPR020828 InterPro:IPR020829 InterPro:IPR020830 InterPro:IPR020831	P		Seeded From UniProt	complete
enables	GO:0004365	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.2.1.12	F		Seeded From UniProt	complete
involved_in	GO:0016241	regulation of macroautophagy	PMID:26626483^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061621	canonical glycolysis	Reactome:R-HSA-70171	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006094	gluconeogenesis	Reactome:R-HSA-70263	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-70482 Reactome:R-HSA-70449	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0324 UniPathway:UPA00109	P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
involved_in	GO:0006417	regulation of translation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0810	P		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472 UniProtKB-SubCell:SL-0162	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Nakamura, T et al. (2002) HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. Biochem. Biophys. Res. Commun. 290 858-64 PubMed GONUTS page
↑ Tummala, H et al. (2014) ERCC6L2 mutations link a distinct bone-marrow-failure syndrome to DNA repair and mitochondrial function. Am. J. Hum. Genet. 94 246-56 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Wagener, J et al. (2013) A peptide derived from the highly conserved protein GAPDH is involved in tissue protection by different antifungal strategies and epithelial immunomodulation. J. Invest. Dermatol. 133 144-53 PubMed GONUTS page
↑ ^4.0 ^4.1 Hou, X et al. (2017) Nuclear complex of glyceraldehyde-3-phosphate dehydrogenase and DNA repair enzyme apurinic/apyrimidinic endonuclease I protect smooth muscle cells against oxidant-induced cell death. FASEB J. PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ van Niel, G et al. (2001) Intestinal epithelial cells secrete exosome-like vesicles. Gastroenterology 121 337-49 PubMed GONUTS page
↑ Wubbolts, R et al. (2003) Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation. J. Biol. Chem. 278 10963-72 PubMed GONUTS page
↑ ^12.0 ^12.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ ^14.0 ^14.1 Arif, A et al. (2012) Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages. Mol. Cell. Biol. 32 5046-55 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 Sampath, P et al. (2004) Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Cell 119 195-208 PubMed GONUTS page
↑ Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page
↑ Fujimoto, Y et al. (2004) Identification of major proteins in the lipid droplet-enriched fraction isolated from the human hepatocyte cell line HuH7. Biochim. Biophys. Acta 1644 47-59 PubMed GONUTS page
↑ Ercolani, L et al. (1988) Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene. J. Biol. Chem. 263 15335-41 PubMed GONUTS page
↑ Nowak, K et al. (1981) The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase. FEBS Lett. 134 143-6 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Zhuang, J et al. (2013) Mitochondrial disulfide relay mediates translocation of p53 and partitions its subcellular activity. Proc. Natl. Acad. Sci. U.S.A. 110 17356-61 PubMed GONUTS page
↑ Wang, J et al. (2011) Toward an understanding of the protein interaction network of the human liver. Mol. Syst. Biol. 7 536 PubMed GONUTS page
↑ Tomokuni, Y et al. (2010) Loose interaction between glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase revealed by fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy in living cells. FEBS J. 277 1310-8 PubMed GONUTS page
↑ Chang, C et al. (2015) AMPK-Dependent Phosphorylation of GAPDH Triggers Sirt1 Activation and Is Necessary for Autophagy upon Glucose Starvation. Mol. Cell 60 930-40 PubMed GONUTS page

[PMID:11785981-1] 1.0 ^1.1 Nakamura, T et al. (2002) HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. Biochem. Biophys. Res. Commun. 290 858-64 PubMed GONUTS page

[PMID:24507776-2] Tummala, H et al. (2014) ERCC6L2 mutations link a distinct bone-marrow-failure syndrome to DNA repair and mitochondrial function. Am. J. Hum. Genet. 94 246-56 PubMed GONUTS page

[PMID:22832495-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Wagener, J et al. (2013) A peptide derived from the highly conserved protein GAPDH is involved in tissue protection by different antifungal strategies and epithelial immunomodulation. J. Invest. Dermatol. 133 144-53 PubMed GONUTS page

[PMID:28404743-4] 4.0 ^4.1 Hou, X et al. (2017) Nuclear complex of glyceraldehyde-3-phosphate dehydrogenase and DNA repair enzyme apurinic/apyrimidinic endonuclease I protect smooth muscle cells against oxidant-induced cell death. FASEB J. PubMed GONUTS page

[PMID:23533145-5] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19190083-6] Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page

[PMID:19946888-7] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

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HUMAN:G3P

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