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Beta-hexosaminidase subunit beta (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit beta) (Hexosaminidase subunit B) (Cervical cancer proto-oncogene 7 protein) (HCC-7) (N-acetyl-beta-glucosaminidase subunit beta) [Cleaved into: Beta-hexosaminidase subunit beta chain B; Beta-hexosaminidase subunit beta chain A]

 HEXB_HUMAN              Reviewed;         556 AA.
P07686;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 3.
27-SEP-2017, entry version 193.
RecName: Full=Beta-hexosaminidase subunit beta;
EC=3.2.1.52;
AltName: Full=Beta-N-acetylhexosaminidase subunit beta;
Short=Hexosaminidase subunit B;
AltName: Full=Cervical cancer proto-oncogene 7 protein;
Short=HCC-7;
AltName: Full=N-acetyl-beta-glucosaminidase subunit beta;
Contains:
RecName: Full=Beta-hexosaminidase subunit beta chain B;
Contains:
RecName: Full=Beta-hexosaminidase subunit beta chain A;
Flags: Precursor;
Name=HEXB; ORFNames=HCC7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3013851;
Korneluk R.G., Mahuran D.J., Neote K., Klavins M.H., O'Dowd B.F.,
Tropak M., Willard H.F., Anderson M.-J., Lowden J.A., Gravel R.A.;
"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.";
J. Biol. Chem. 261:8407-8413(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2977375; DOI=10.1016/0888-7543(88)90116-4;
Neote K., Bapat B., Dumbrille-Ross A., Troxel C., Schuster S.M.,
Mahuran D.J., Gravel R.A.;
"Characterization of the human HEXB gene encoding lysosomal beta-
hexosaminidase.";
Genomics 3:279-286(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2964638; DOI=10.1073/pnas.85.6.1883;
Proia R.L.;
"Gene encoding the human beta-hexosaminidase beta chain: extensive
homology of intron placement in the alpha- and beta-chain genes.";
Proc. Natl. Acad. Sci. U.S.A. 85:1883-1887(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a new proto-oncogene in human cancers.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-67.
PubMed=2971039;
Sonderfeld-Fresko S., Proia R.L.;
"Synthesis and assembly of a catalytically active lysosomal enzyme,
beta-hexosaminidase B, in a cell-free system.";
J. Biol. Chem. 263:13463-13469(1988).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
PubMed=2147427;
Neote K., Brown C.A., Mahuran D.J., Gravel R.A.;
"Translation initiation in the HEXB gene encoding the beta-subunit of
human beta-hexosaminidase.";
J. Biol. Chem. 265:20799-20806(1990).
[10]
PROTEIN SEQUENCE OF 43-57 AND 122-151.
PubMed=2966076; DOI=10.1016/0014-5793(88)80699-9;
Stirling J., Leung A., Gravel R.A., Mahuran D.;
"Localization of the pro-sequence within the total deduced primary
structure of human beta-hexosaminidase B.";
FEBS Lett. 231:47-50(1988).
[11]
PROTEIN SEQUENCE OF 45-54 AND 315-324.
PubMed=2139028;
Mahuran D.J.;
"Characterization of human placental beta-hexosaminidase I2.
Proteolytic processing intermediates of hexosaminidase A.";
J. Biol. Chem. 265:6794-6799(1990).
[12]
PROTEIN SEQUENCE OF 50-59.
PubMed=2525487; DOI=10.1016/0014-5793(89)80649-0;
Hubbes M., Callahan J., Gravel R., Mahuran D.;
"The amino-terminal sequences in the pro-alpha and -beta polypeptides
of human lysosomal beta-hexosaminidase A and B are retained in the
mature isozymes.";
FEBS Lett. 249:316-320(1989).
[13]
PROTEIN SEQUENCE OF 122-151 AND 315-340.
PubMed=2965147;
Mahuran D.J., Neote K., Klavins M.H., Leung A., Gravel R.A.;
"Proteolytic processing of pro-alpha and pro-beta precursors from
human beta-hexosaminidase. Generation of the mature alpha and beta a
beta b subunits.";
J. Biol. Chem. 263:4612-4618(1988).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 226-283.
PubMed=2579389; DOI=10.1073/pnas.82.4.1184;
O'Dowd B.F., Quan F., Willard H.F., Lamhonwah A.-M., Korneluk R.G.,
Lowden J.A., Gravel R.A., Mahuran D.J.;
"Isolation of cDNA clones coding for the beta subunit of human beta-
hexosaminidase.";
Proc. Natl. Acad. Sci. U.S.A. 82:1184-1188(1985).
[15]
STRUCTURE OF CARBOHYDRATES.
PubMed=2971395; DOI=10.1021/bi00414a041;
O'Dowd B.F., Cumming D.A., Gravel R.A., Mahuran D.J.;
"Oligosaccharide structure and amino acid sequence of the major
glycopeptides of mature human beta-hexosaminidase.";
Biochemistry 27:5216-5226(1988).
[16]
GLYCOSYLATION AT ASN-327.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[17]
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-84; ASN-142; ASN-190 AND
ASN-327.
PubMed=11447134; DOI=10.1093/glycob/11.7.549;
Schuette C.G., Weisgerber J., Sandhoff K.;
"Complete analysis of the glycosylation and disulfide bond pattern of
human beta-hexosaminidase B by MALDI-MS.";
Glycobiology 11:549-556(2001).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-323 AND ASN-327.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
3D-STRUCTURE MODELING.
PubMed=8673609; DOI=10.1038/nsb0796-638;
Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S.,
Vorgias C.E.;
"Bacterial chitobiase structure provides insight into catalytic
mechanism and the basis of Tay-Sachs disease.";
Nat. Struct. Biol. 3:638-648(1996).
[23]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 50-556, AND DISULFIDE BONDS.
PubMed=12662933; DOI=10.1016/S0022-2836(03)00216-X;
Mark B.L., Mahuran D.J., Cherney M.M., Zhao D., Knapp S., James M.N.;
"Crystal structure of human beta-hexosaminidase B: understanding the
molecular basis of Sandhoff and Tay-Sachs disease.";
J. Mol. Biol. 327:1093-1109(2003).
[24]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 42-556, AND DISULFIDE BONDS.
PubMed=12706724; DOI=10.1016/S0022-2836(03)00311-5;
Maier T., Strater N., Schuette C.G., Klingenstein R., Sandhoff K.,
Saenger W.;
"The X-ray crystal structure of human beta-hexosaminidase B provides
new insights into Sandhoff disease.";
J. Mol. Biol. 328:669-681(2003).
[25]
REVIEW ON VARIANTS.
PubMed=1825792; DOI=10.1016/0925-4439(91)90044-A;
Mahuran D.J.;
"The biochemistry of HEXA and HEXB gene mutations causing GM2
gangliosidosis.";
Biochim. Biophys. Acta 1096:87-94(1991).
[26]
VARIANT GM2G2 SER-456, AND VARIANT VAL-207.
PubMed=1720305; DOI=10.1016/S0006-291X(05)81388-9;
Banerjee P., Siciliano L., Oliveri D., McCabe N.R., Boyers M.J.,
Horwitz A.L., Li S.-C., Dawson G.;
"Molecular basis of an adult form of beta-hexosaminidase B deficiency
with motor neuron disease.";
Biochem. Biophys. Res. Commun. 181:108-115(1991).
[27]
VARIANT GM2G2 LEU-417.
PubMed=1531140;
Wakamatsu N., Kobayashi H., Miyatake T., Tsuji S.;
"A novel exon mutation in the human beta-hexosaminidase beta subunit
gene affects 3' splice site selection.";
J. Biol. Chem. 267:2406-2413(1992).
[28]
VARIANT GM2G2 GLN-505.
PubMed=8357844; DOI=10.1016/0925-4439(93)90134-M;
Bolhuis P.A., Ponne N.J., Bikker H., Baas F., Vianney de Jong J.M.B.;
"Molecular basis of an adult form of Sandhoff disease: substitution of
glutamine for arginine at position 505 of the beta-chain of beta-
hexosaminidase results in a labile enzyme.";
Biochim. Biophys. Acta 1182:142-146(1993).
[29]
VARIANT GM2G2 TYR-534.
PubMed=7626071; DOI=10.1006/bbrc.1995.2007;
Kuroki Y., Itoh K., Nadaoka Y., Tanaka T., Sakuraba H.;
"A novel missense mutation (C522Y) is present in the beta-
hexosaminidase beta-subunit gene of a Japanese patient with infantile
Sandhoff disease.";
Biochem. Biophys. Res. Commun. 212:564-571(1995).
[30]
VARIANTS GM2G2 TYR-309 AND LEU-417.
PubMed=7557963; DOI=10.1007/BF00191799;
Gomez-Lira M., Sangalli A., Mottes M., Perusi C., Pignatti P.F.,
Rizzuto N., Salviati A.;
"A common beta hexosaminidase gene mutation in adult Sandhoff disease
patients.";
Hum. Genet. 96:417-422(1995).
[31]
VARIANT GM2G2 LEU-62.
PubMed=7633435; DOI=10.1093/hmg/4.4.777;
Zhang Z.-X., Wakamatsu N., Akerman B.R., Mules E.H., Thomas G.H.,
Gravel R.A.;
"A second, large deletion in the HEXB gene in a patient with infantile
Sandhoff disease.";
Hum. Mol. Genet. 4:777-780(1995).
[32]
VARIANT GM2G2 GLN-505, AND VARIANT VAL-207.
PubMed=8950198; DOI=10.1016/S0925-4439(96)00044-0;
Redonnet-Vernhet I., Mahuran D.J., Salvayre R., Dubas F., Levade T.;
"Significance of two point mutations present in each HEXB allele of
patients with adult GM2 gangliosidosis (Sandhoff disease) homozygosity
for the Ile207-->Val substitution is not associated with a clinical or
biochemical phenotype.";
Biochim. Biophys. Acta 1317:127-133(1996).
[33]
VARIANT GM2G2 THR-543.
PubMed=9401004;
DOI=10.1002/(SICI)1098-1004(1997)10:6<424::AID-HUMU2>3.3.CO;2-Y;
Narkis G., Adam A., Jaber L., Pennybacker M., Proia R.L., Navon R.;
"Molecular basis of heat labile hexosaminidase B among Jews and
Arabs.";
Hum. Mutat. 10:424-429(1997).
[34]
VARIANT GM2G2 ARG-255.
PubMed=9856491; DOI=10.1007/s004390050851;
Fujimaru M., Tanaka A., Choeh K., Wakamatsu N., Sakuraba H.,
Isshiki G.;
"Two mutations remote from an exon/intron junction in the beta-
hexosaminidase beta-subunit gene affect 3'-splice site selection and
cause Sandhoff disease.";
Hum. Genet. 103:462-469(1998).
[35]
VARIANT GM2G2 SER-504.
PubMed=9694901; DOI=10.1074/jbc.273.33.21386;
Hou Y., McInnes B., Hinek A., Karpati G., Mahuran D.;
"A Pro504 --> Ser substitution in the beta-subunit of beta-
hexosaminidase A inhibits alpha-subunit hydrolysis of GM2 ganglioside,
resulting in chronic Sandhoff disease.";
J. Biol. Chem. 273:21386-21392(1998).
-!- FUNCTION: Responsible for the degradation of GM2 gangliosides, and
a variety of other molecules containing terminal N-acetyl
hexosamines, in the brain and other tissues.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
-!- SUBUNIT: There are 3 forms of beta-hexosaminidase: hexosaminidase
A is a trimer composed of one subunit alpha, one subunit beta
chain A and one subunit beta chain B; hexosaminidase B is a
tetramer of two subunit beta chains A and two subunit beta chains
B; hexosaminidase S is a homodimer of two alpha subunits. The two
beta chains are derived from the cleavage of the beta subunit.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- PTM: N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-
GlcNAc(2) and Man(5 to 7)-GlcNAc(2), respectively.
{ECO:0000269|PubMed:11447134, ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
-!- PTM: The beta-A and beta-B chains are produced by proteolytic
processing of the precursor beta chain.
-!- DISEASE: GM2-gangliosidosis 2 (GM2G2) [MIM:268800]: An autosomal
recessive lysosomal storage disease marked by the accumulation of
GM2 gangliosides in the neuronal cells. 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.
{ECO:0000269|PubMed:1531140, ECO:0000269|PubMed:1720305,
ECO:0000269|PubMed:7557963, ECO:0000269|PubMed:7626071,
ECO:0000269|PubMed:7633435, ECO:0000269|PubMed:8357844,
ECO:0000269|PubMed:8950198, ECO:0000269|PubMed:9401004,
ECO:0000269|PubMed:9694901, ECO:0000269|PubMed:9856491}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA51828.1; Type=Frameshift; Positions=21; Evidence={ECO:0000305};
Sequence=AAA68620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=HEXBdb; Note=HEXB mutation database;
URL="http://www.hexdb.mcgill.ca/?Topic=HEXBdb";
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EMBL; M13519; AAA51828.1; ALT_FRAME; mRNA.
EMBL; M23294; AAA52645.1; -; Genomic_DNA.
EMBL; M23282; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23283; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23284; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23285; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23286; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23287; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23288; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23290; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23291; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23292; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M23293; AAA52645.1; JOINED; Genomic_DNA.
EMBL; M19735; AAA68620.1; ALT_INIT; mRNA.
EMBL; AF378118; AAM46114.1; -; mRNA.
EMBL; BT009919; AAP88921.1; -; mRNA.
EMBL; AC026405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017378; AAH17378.1; -; mRNA.
EMBL; M34906; AAA51829.1; -; mRNA.
CCDS; CCDS4022.1; -.
PIR; A31250; A31250.
RefSeq; NP_000512.1; NM_000521.3.
RefSeq; NP_001278933.1; NM_001292004.1.
UniGene; Hs.69293; -.
PDB; 1NOU; X-ray; 2.40 A; A/B=50-556.
PDB; 1NOW; X-ray; 2.20 A; A/B=50-556.
PDB; 1NP0; X-ray; 2.50 A; A/B=50-556.
PDB; 1O7A; X-ray; 2.25 A; A/B/C/D/E/F=42-556.
PDB; 1QBD; Model; -; A=122-556.
PDB; 2GJX; X-ray; 2.80 A; B/C/F/G=50-556.
PDB; 2GK1; X-ray; 3.25 A; B/D/F/H=50-552.
PDB; 3LMY; X-ray; 2.80 A; A/B=1-556.
PDB; 5BRO; X-ray; 2.40 A; A=43-556.
PDBsum; 1NOU; -.
PDBsum; 1NOW; -.
PDBsum; 1NP0; -.
PDBsum; 1O7A; -.
PDBsum; 1QBD; -.
PDBsum; 2GJX; -.
PDBsum; 2GK1; -.
PDBsum; 3LMY; -.
PDBsum; 5BRO; -.
ProteinModelPortal; P07686; -.
SMR; P07686; -.
BioGrid; 109323; 35.
CORUM; P07686; -.
ELM; P07686; -.
IntAct; P07686; 10.
MINT; MINT-4528380; -.
STRING; 9606.ENSP00000261416; -.
BindingDB; P07686; -.
ChEMBL; CHEMBL5877; -.
CAZy; GH20; Glycoside Hydrolase Family 20.
iPTMnet; P07686; -.
PhosphoSitePlus; P07686; -.
SwissPalm; P07686; -.
UniCarbKB; P07686; -.
BioMuta; HEXB; -.
DMDM; 123081; -.
UCD-2DPAGE; P07686; -.
EPD; P07686; -.
MaxQB; P07686; -.
PaxDb; P07686; -.
PeptideAtlas; P07686; -.
PRIDE; P07686; -.
TopDownProteomics; P07686; -.
DNASU; 3074; -.
Ensembl; ENST00000261416; ENSP00000261416; ENSG00000049860.
GeneID; 3074; -.
KEGG; hsa:3074; -.
UCSC; uc003kdf.4; human.
CTD; 3074; -.
DisGeNET; 3074; -.
EuPathDB; HostDB:ENSG00000049860.13; -.
GeneCards; HEXB; -.
HGNC; HGNC:4879; HEXB.
HPA; HPA055409; -.
HPA; HPA056010; -.
MalaCards; HEXB; -.
MIM; 268800; phenotype.
MIM; 606873; gene.
neXtProt; NX_P07686; -.
Orphanet; 309169; Sandhoff disease, adult form.
Orphanet; 309155; Sandhoff disease, infantile form.
Orphanet; 309162; Sandhoff disease, juvenile form.
PharmGKB; PA29257; -.
eggNOG; KOG2499; Eukaryota.
eggNOG; COG3525; LUCA.
HOGENOM; HOG000157972; -.
HOVERGEN; HBG005961; -.
InParanoid; P07686; -.
KO; K12373; -.
OrthoDB; EOG091G04NA; -.
PhylomeDB; P07686; -.
TreeFam; TF313036; -.
BioCyc; MetaCyc:HS00629-MONOMER; -.
BRENDA; 3.2.1.52; 2681.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-2022857; Keratan sulfate degradation.
Reactome; R-HSA-2024101; CS/DS degradation.
Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P07686; -.
ChiTaRS; HEXB; human.
EvolutionaryTrace; P07686; -.
GeneWiki; HEXB; -.
GenomeRNAi; 3074; -.
PRO; PR:P07686; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000049860; -.
CleanEx; HS_HEXB; -.
ExpressionAtlas; P07686; baseline and differential.
Genevisible; P07686; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; TAS:Reactome.
GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0043615; P:astrocyte cell migration; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; IEA:Ensembl.
GO; GO:0030207; P:chondroitin sulfate catabolic process; TAS:Reactome.
GO; GO:0006689; P:ganglioside catabolic process; IEA:Ensembl.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0030214; P:hyaluronan catabolic process; TAS:Reactome.
GO; GO:0042340; P:keratan sulfate catabolic process; TAS:Reactome.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
GO; GO:0008049; P:male courtship behavior; IEA:Ensembl.
GO; GO:0042552; P:myelination; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0009313; P:oligosaccharide catabolic process; IEA:Ensembl.
GO; GO:0048477; P:oogenesis; IEA:Ensembl.
GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
InterPro; IPR029018; Chitobiase/Hex_dom_2-like.
InterPro; IPR015883; Glyco_hydro_20_cat.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR029019; HEX_eukaryotic_N.
Pfam; PF00728; Glyco_hydro_20; 1.
Pfam; PF14845; Glycohydro_20b2; 1.
PIRSF; PIRSF001093; B-hxosamndse_ab_euk_; 1.
PRINTS; PR00738; GLHYDRLASE20.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF55545; SSF55545; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Gangliosidosis; Glycoprotein;
Glycosidase; Hydrolase; Lysosome; Neurodegeneration; Polymorphism;
Reference proteome; Signal; Zymogen.
SIGNAL 1 42 {ECO:0000255}.
PROPEP 43 121 {ECO:0000269|PubMed:2965147,
ECO:0000269|PubMed:2966076}.
/FTId=PRO_0000012002.
CHAIN 122 556 Beta-hexosaminidase subunit beta.
/FTId=PRO_0000012003.
CHAIN 122 311 Beta-hexosaminidase subunit beta chain B.
/FTId=PRO_0000012004.
CHAIN 315 556 Beta-hexosaminidase subunit beta chain A.
/FTId=PRO_0000012005.
ACT_SITE 355 355 Proton donor. {ECO:0000250}.
SITE 497 497 Not glycosylated.
{ECO:0000269|PubMed:11447134}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11447134,
ECO:0000269|PubMed:19159218}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11447134}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11447134}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11447134,
ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
DISULFID 91 137
DISULFID 309 360
DISULFID 534 551
VARIANT 62 62 S -> L (in GM2G2; dbSNP:rs820878).
{ECO:0000269|PubMed:7633435}.
/FTId=VAR_003247.
VARIANT 121 121 K -> R (in dbSNP:rs11556045).
/FTId=VAR_003248.
VARIANT 207 207 I -> V (probable polymorphism;
dbSNP:rs10805890).
{ECO:0000269|PubMed:1720305,
ECO:0000269|PubMed:8950198}.
/FTId=VAR_003249.
VARIANT 255 255 S -> R (in GM2G2).
{ECO:0000269|PubMed:9856491}.
/FTId=VAR_011704.
VARIANT 309 309 C -> Y (in GM2G2; adult type; severe).
{ECO:0000269|PubMed:7557963}.
/FTId=VAR_003250.
VARIANT 417 417 P -> L (in GM2G2; dbSNP:rs28942073).
{ECO:0000269|PubMed:1531140,
ECO:0000269|PubMed:7557963}.
/FTId=VAR_003251.
VARIANT 456 456 Y -> S (in GM2G2).
{ECO:0000269|PubMed:1720305}.
/FTId=VAR_003252.
VARIANT 504 504 P -> S (in GM2G2).
{ECO:0000269|PubMed:9694901}.
/FTId=VAR_011705.
VARIANT 505 505 R -> Q (in GM2G2).
{ECO:0000269|PubMed:8357844,
ECO:0000269|PubMed:8950198}.
/FTId=VAR_003253.
VARIANT 534 534 C -> Y (in GM2G2; infantile type).
{ECO:0000269|PubMed:7626071}.
/FTId=VAR_003254.
VARIANT 543 543 A -> T (in GM2G2).
{ECO:0000269|PubMed:9401004}.
/FTId=VAR_011706.
STRAND 61 71 {ECO:0000244|PDB:1NOW}.
HELIX 74 76 {ECO:0000244|PDB:1NOW}.
STRAND 78 81 {ECO:0000244|PDB:1NOW}.
STRAND 83 86 {ECO:0000244|PDB:1O7A}.
HELIX 92 105 {ECO:0000244|PDB:1NOW}.
STRAND 126 131 {ECO:0000244|PDB:1NOW}.
STRAND 149 153 {ECO:0000244|PDB:1NOW}.
STRAND 155 164 {ECO:0000244|PDB:1NOW}.
HELIX 165 178 {ECO:0000244|PDB:1NOW}.
STRAND 187 196 {ECO:0000244|PDB:1NOW}.
STRAND 201 212 {ECO:0000244|PDB:1NOW}.
HELIX 216 228 {ECO:0000244|PDB:1NOW}.
STRAND 233 237 {ECO:0000244|PDB:1NOW}.
HELIX 253 258 {ECO:0000244|PDB:1NOW}.
STRAND 259 261 {ECO:0000244|PDB:1NOW}.
STRAND 262 264 {ECO:0000244|PDB:2GJX}.
HELIX 268 280 {ECO:0000244|PDB:1NOW}.
STRAND 284 294 {ECO:0000244|PDB:1NOW}.
HELIX 298 301 {ECO:0000244|PDB:1NOW}.
STRAND 306 308 {ECO:0000244|PDB:1NOW}.
STRAND 318 322 {ECO:0000244|PDB:1NOW}.
HELIX 327 343 {ECO:0000244|PDB:1NOW}.
STRAND 346 352 {ECO:0000244|PDB:1NOW}.
HELIX 359 362 {ECO:0000244|PDB:1NOW}.
HELIX 365 373 {ECO:0000244|PDB:1NOW}.
HELIX 380 397 {ECO:0000244|PDB:1NOW}.
STRAND 401 405 {ECO:0000244|PDB:1NOW}.
HELIX 406 410 {ECO:0000244|PDB:1NOW}.
STRAND 420 423 {ECO:0000244|PDB:1NOW}.
HELIX 429 438 {ECO:0000244|PDB:1NOW}.
STRAND 443 445 {ECO:0000244|PDB:1NOW}.
HELIX 447 449 {ECO:0000244|PDB:3LMY}.
STRAND 450 453 {ECO:0000244|PDB:2GK1}.
STRAND 455 457 {ECO:0000244|PDB:2GJX}.
HELIX 460 465 {ECO:0000244|PDB:1NOW}.
HELIX 475 479 {ECO:0000244|PDB:1NOW}.
STRAND 481 488 {ECO:0000244|PDB:1NOW}.
HELIX 490 492 {ECO:0000244|PDB:3LMY}.
TURN 495 497 {ECO:0000244|PDB:1NOW}.
HELIX 498 502 {ECO:0000244|PDB:1NOW}.
HELIX 505 514 {ECO:0000244|PDB:1NOW}.
HELIX 522 538 {ECO:0000244|PDB:1NOW}.
STRAND 546 548 {ECO:0000244|PDB:1NOW}.
SEQUENCE 556 AA; 63111 MW; B3A0A36594F62536 CRC64;
MELCGLGLPR PPMLLALLLA TLLAAMLALL TQVALVVQVA EAARAPSVSA KPGPALWPLP
LSVKMTPNLL HLAPENFYIS HSPNSTAGPS CTLLEEAFRR YHGYIFGFYK WHHEPAEFQA
KTQVQQLLVS ITLQSECDAF PNISSDESYT LLVKEPVAVL KANRVWGALR GLETFSQLVY
QDSYGTFTIN ESTIIDSPRF SHRGILIDTS RHYLPVKIIL KTLDAMAFNK FNVLHWHIVD
DQSFPYQSIT FPELSNKGSY SLSHVYTPND VRMVIEYARL RGIRVLPEFD TPGHTLSWGK
GQKDLLTPCY SRQNKLDSFG PINPTLNTTY SFLTTFFKEI SEVFPDQFIH LGGDEVEFKC
WESNPKIQDF MRQKGFGTDF KKLESFYIQK VLDIIATINK GSIVWQEVFD DKAKLAPGTI
VEVWKDSAYP EELSRVTASG FPVILSAPWY LDLISYGQDW RKYYKVEPLD FGGTQKQKQL
FIGGEACLWG EYVDATNLTP RLWPRASAVG ERLWSSKDVR DMDDAYDRLT RHRCRMVERG
IAAQPLYAGY CNHENM


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