IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ lemieux-2006-1 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Lemieux MJ., Mark BL., Cherney MM., Withers SG., Mahuran DJ., James MN. michael.james@ualberta.ca Journal of molecular biology 2006 Only protein-protein interactions imex curation imex curation hexb_human Beta-hexosaminidase subunit beta HEXB HCC7 N-acetyl-beta-glucosaminidase subunit beta Beta-N-acetylhexosaminidase subunit beta Cervical cancer proto-oncogene 7 protein protein protein human Homo sapiens Human MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLSVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:268800]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula mint homomint Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues hexa_human Beta-hexosaminidase subunit alpha N-acetyl-beta-glucosaminidase subunit alpha Beta-N-acetylhexosaminidase subunit alpha HEXA protein protein human Homo sapiens Human MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT nag-thiazoline NGT small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) hexa-hexb-1 2846294 N/A 2846295 unspecified role unspecified role neutral component neutral component purified purified region glycores glycosylated residue GlycoRes undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-placenta Homo sapiens placenta placenta Stoichiometry: 4.0 N/A 2846296 unspecified role unspecified role neutral component neutral component purified purified region glycores glycosylated residue GlycoRes undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-placenta Homo sapiens placenta placenta Stoichiometry: 4.0 direct interaction direct interaction false false false Table 1 2.8A Rw = 0.269 Rfree = 0.288 Both subunits have many N-linked glycosyl residues and there are oligosaccharides bound at most of the known glycosylation sites. hexa-hexb-2 2846294 N/A 2846295 unspecified role unspecified role neutral component neutral component purified purified region glycores glycosylated residue GlycoRes undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-placenta Homo sapiens placenta placenta Stoichiometry: 4.0 N/A 2846296 unspecified role unspecified role neutral component neutral component purified purified region glycores glycosylated residue GlycoRes undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-placenta Homo sapiens placenta placenta Stoichiometry: 4.0 N/A 2846297 unspecified role unspecified role neutral component neutral component purified purified chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction false false false Table 1i 3.25A Rw = 0.274 Rfree = 0.322 Both subunits have many N-linked glycosyl residues and there are oligosaccharides bound at most of the known glycosylation sites.