HEXA

HEXA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2GJX, 2GK1
Identifiers
Aliases	HEXA, TSD, hexosaminidase subunit alpha
External IDs	OMIM: 606869; MGI: 96073; HomoloGene: 20146; GeneCards: HEXA; OMA:HEXA - orthologs
Gene location (Human)
Chr.	Chromosome 15 (human)
End	72,376,420 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	59,472,392 bp
RNA expression pattern
	Top expressed in
	beta cell; ; gallbladder; ; stromal cell of endometrium; ; right adrenal cortex; ; left lobe of thyroid gland; ; right coronary artery; ; granulocyte; ; right lobe of thyroid gland; ; left adrenal gland; ; tendon of biceps brachii;
	Top expressed in
	stroma of bone marrow; ; calvaria; ; decidua; ; body of femur; ; vestibular membrane of cochlear duct; ; mesenteric lymph nodes; ; iris; ; aortic valve; ; crypt of lieberkuhn of small intestine; ; ascending aorta;
	More reference expression data
	n/a
Gene ontology
Molecular function	acetylglucosaminyltransferase activity; protein heterodimerization activity; hydrolase activity, hydrolyzing O-glycosyl compounds; hydrolase activity; hydrolase activity, acting on glycosyl bonds; beta-N-acetylhexosaminidase activity; N-acetyl-beta-D-galactosaminidase activity; protein binding;
Cellular component	extracellular exosome; membrane; lysosome; lysosomal lumen; azurophil granule;
Biological process	hyaluronan catabolic process; glycosaminoglycan biosynthetic process; metabolism; glycosphingolipid metabolic process; chondroitin sulfate catabolic process; keratan sulfate catabolic process; carbohydrate metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	3073
	15211
	ENSG00000213614
	ENSMUSG00000025232
	P06865
	P29416
	NM_000520; NM_001318825
	NM_010421
	NP_000511; NP_001305754
	NP_034551
	Wikidata
View/Edit Human	View/Edit Mouse

Hexosaminidase A (alpha polypeptide), also known as HEXA, is an enzyme that in humans is encoded by the HEXA gene, located on the 15th chromosome.^[5]^[6]

Hexosaminidase A and the cofactor G_M2 activator protein catalyze the degradation of the G_M2 gangliosides and other molecules containing terminal N-acetyl hexosamines.^[7] Hexosaminidase A is a heterodimer composed of an alpha subunit (this protein) and a beta subunit. The alpha subunit polypeptide is encoded by the HEXA gene while the beta subunit is encoded by the HEXB gene. Gene mutations in the gene encoding the beta subunit (HEXB) often result in Sandhoff disease; whereas, mutations in the gene encoding the alpha subunit (HEXA, this gene) decrease the hydrolysis of G_M2 gangliosides, which is the main cause of Tay–Sachs disease.^[8]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000213614 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025232 – 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.
^ Korneluk RG, Mahuran DJ, Neote K, Klavins MH, O'Dowd BF, Tropak M, Willard HF, Anderson MJ, Lowden JA, Gravel RA (June 1986). "Isolation of cDNA clones coding for the alpha-subunit of human beta-hexosaminidase. Extensive homology between the alpha- and beta-subunits and studies on Tay-Sachs disease". The Journal of Biological Chemistry. 261 (18): 8407–13. doi:10.1016/S0021-9258(19)83927-3. PMID 3013851.
^ Proia RL, Soravia E (April 1987). "Organization of the gene encoding the human beta-hexosaminidase alpha-chain". The Journal of Biological Chemistry. 262 (12): 5677–81. doi:10.1016/S0021-9258(18)45628-1. PMID 2952641.
^ Knapp S, Vocadlo D, Gao Z, Kirk B, Lou J, Withers SG (1996). "NAG-thiazoline, an N-acetylbeta-hexosaminidase inhibitor that implicates acetamido participation". J. Am. Chem. Soc. 118 (28): 6804–6805. doi:10.1021/ja960826u.
^ Mark BL, Mahuran DJ, Cherney MM, Zhao D, Knapp S, James MN (April 2003). "Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease". Journal of Molecular Biology. 327 (5): 1093–109. doi:10.1016/S0022-2836(03)00216-X. PMC 2910754. PMID 12662933.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000213614 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025232 – Ensembl, May 2017

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

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

[pmid3013851-5] Korneluk RG, Mahuran DJ, Neote K, Klavins MH, O'Dowd BF, Tropak M, Willard HF, Anderson MJ, Lowden JA, Gravel RA (June 1986). "Isolation of cDNA clones coding for the alpha-subunit of human beta-hexosaminidase. Extensive homology between the alpha- and beta-subunits and studies on Tay-Sachs disease". The Journal of Biological Chemistry. 261 (18): 8407–13. doi:10.1016/S0021-9258(19)83927-3. PMID 3013851.

[pmid2952641-6] Proia RL, Soravia E (April 1987). "Organization of the gene encoding the human beta-hexosaminidase alpha-chain". The Journal of Biological Chemistry. 262 (12): 5677–81. doi:10.1016/S0021-9258(18)45628-1. PMID 2952641.

[7] Knapp S, Vocadlo D, Gao Z, Kirk B, Lou J, Withers SG (1996). "NAG-thiazoline, an N-acetylbeta-hexosaminidase inhibitor that implicates acetamido participation". J. Am. Chem. Soc. 118 (28): 6804–6805. doi:10.1021/ja960826u.

[pmid12662933-8] Mark BL, Mahuran DJ, Cherney MM, Zhao D, Knapp S, James MN (April 2003). "Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease". Journal of Molecular Biology. 327 (5): 1093–109. doi:10.1016/S0022-2836(03)00216-X. PMC 2910754. PMID 12662933.

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