P07686 (HEXB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-hexosaminidase subunit beta
EC=3.2.1.52

Alternative name(s):
Beta-N-acetylhexosaminidase subunit beta
Short name=Hexosaminidase subunit B
Cervical cancer proto-oncogene 7 protein
Short name=HCC-7
N-acetyl-beta-glucosaminidase subunit beta

Cleaved into the following 2 chains:

1. Beta-hexosaminidase subunit beta chain B
2. Beta-hexosaminidase subunit beta chain A

Gene names

Name:	HEXB
ORF Names:	HCC7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	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 an homodimer of two alpha subunits. The two beta chains are derived from the cleavage of the beta subunit.
Subcellular location	Lysosome.
Post-translational modification	N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-GlcNAc2 and Man(5 to 7)-GlcNAc2, respectively. The beta-A and beta-B chains are produced by proteolytic processing of the precursor beta chain.
Involvement in disease	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. Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33
Sequence similarities	Belongs to the glycosyl hydrolase 20 family.
Sequence caution	The sequence AAA51828.1 differs from that shown. Reason: Frameshift at position 21. The sequence AAA68620.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Disease	Disease mutation Gangliosidosis Neurodegeneration
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro protein heterodimerization activity Inferred from direct assay. Source: MGI protein homodimerization activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 42

42

Potential

Propeptide

43 – 121

79

PRO_0000012002

Chain

122 – 556

435

Beta-hexosaminidase subunit beta

PRO_0000012003

Chain

122 – 311

190

Beta-hexosaminidase subunit beta chain B

PRO_0000012004

Chain

315 – 556

242

Beta-hexosaminidase subunit beta chain A

PRO_0000012005

Sites

Active site

355

1

Proton donor By similarity

Amino acid modifications

Glycosylation

84

1

N-linked (GlcNAc...) Ref.18

Glycosylation

142

1

N-linked (GlcNAc...)

Glycosylation

190

1

N-linked (GlcNAc...)

Glycosylation

323

1

N-linked (GlcNAc...) Ref.18

Glycosylation

327

1

N-linked (GlcNAc...) Ref.16 Ref.18

Disulfide bond

91 ↔ 137

Ref.17 Ref.21 Ref.22

Disulfide bond

309 ↔ 360

Ref.17 Ref.21 Ref.22

Disulfide bond

534 ↔ 551

Ref.17 Ref.21 Ref.22

Natural variations

Natural variant

62

1

S → L in GM2G2. Ref.29
Corresponds to variant rs820878 [ dbSNP | Ensembl ].

VAR_003247

Natural variant

121

1

K → R.
Corresponds to variant rs11556045 [ dbSNP | Ensembl ].

VAR_003248

Natural variant

207

1

I → V Probable polymorphism. Ref.24 Ref.30
Corresponds to variant rs10805890 [ dbSNP | Ensembl ].

VAR_003249

Natural variant

255

1

S → R in GM2G2. Ref.32

VAR_011704

Natural variant

309

1

C → Y in GM2G2; adult type; severe; almost complete absence of activity. Ref.28

VAR_003250

Natural variant

417

1

P → L in GM2G2. Ref.25 Ref.28
Corresponds to variant rs28942073 [ dbSNP | Ensembl ].

VAR_003251

Natural variant

456

1

Y → S in GM2G2. Ref.24

VAR_003252

Natural variant

504

1

P → S in GM2G2. Ref.33

VAR_011705

Natural variant

505

1

R → Q in GM2G2. Ref.26 Ref.30

VAR_003253

Natural variant

534

1

C → Y in GM2G2; infantile type. Ref.27

VAR_003254

Natural variant

543

1

A → T in GM2G2. Ref.31

VAR_011706

Secondary structure

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556

Helix Strand Turn

Details...

Beta strand

61 – 71

11

Helix

74 – 76

3

Beta strand

78 – 81

4

Helix

92 – 106

15

Beta strand

126 – 131

6

Beta strand

149 – 153

5

Beta strand

155 – 164

10

Helix

165 – 178

14

Beta strand

187 – 196

10

Beta strand

201 – 212

12

Helix

216 – 228

13

Beta strand

233 – 237

5

Helix

253 – 258

6

Beta strand

259 – 261

3

Helix

268 – 280

13

Beta strand

284 – 294

11

Helix

298 – 301

4

Beta strand

306 – 308

3

Beta strand

318 – 322

5

Helix

327 – 343

17

Beta strand

346 – 352

7

Helix

359 – 363

5

Helix

365 – 373

9

Helix

381 – 397

17

Beta strand

401 – 405

5

Helix

406 – 410

5

Beta strand

420 – 423

4

Helix

429 – 438

10

Beta strand

443 – 445

3

Beta strand

455 – 457

3

Helix

460 – 465

6

Helix

475 – 479

5

Beta strand

481 – 488

8

Turn

495 – 497

3

Helix

498 – 502

5

Helix

505 – 514

10

Helix

522 – 538

17

Beta strand

546 – 548

3

Sequences

	Sequence		Length	Mass (Da)
	P07686 [UniParc]. Last modified February 1, 1991. Version 3. Checksum: B3A0A36594F62536	FASTA	556	63,111
	10 20 30 40 50 60 MELCGLGLPR PPMLLALLLA TLLAAMLALL TQVALVVQVA EAARAPSVSA KPGPALWPLP 70 80 90 100 110 120 LSVKMTPNLL HLAPENFYIS HSPNSTAGPS CTLLEEAFRR YHGYIFGFYK WHHEPAEFQA 130 140 150 160 170 180 KTQVQQLLVS ITLQSECDAF PNISSDESYT LLVKEPVAVL KANRVWGALR GLETFSQLVY 190 200 210 220 230 240 QDSYGTFTIN ESTIIDSPRF SHRGILIDTS RHYLPVKIIL KTLDAMAFNK FNVLHWHIVD 250 260 270 280 290 300 DQSFPYQSIT FPELSNKGSY SLSHVYTPND VRMVIEYARL RGIRVLPEFD TPGHTLSWGK 310 320 330 340 350 360 GQKDLLTPCY SRQNKLDSFG PINPTLNTTY SFLTTFFKEI SEVFPDQFIH LGGDEVEFKC 370 380 390 400 410 420 WESNPKIQDF MRQKGFGTDF KKLESFYIQK VLDIIATINK GSIVWQEVFD DKAKLAPGTI 430 440 450 460 470 480 VEVWKDSAYP EELSRVTASG FPVILSAPWY LDLISYGQDW RKYYKVEPLD FGGTQKQKQL 490 500 510 520 530 540 FIGGEACLWG EYVDATNLTP RLWPRASAVG ERLWSSKDVR DMDDAYDRLT RHRCRMVERG 550 IAAQPLYAGY CNHENM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." 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. J. Biol. Chem. 261:8407-8413(1986) [PubMed: 3013851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of the human HEXB gene encoding lysosomal beta-hexosaminidase." Neote K., Bapat B., Dumbrille-Ross A., Troxel C., Schuster S.M., Mahuran D.J., Gravel R.A. Genomics 3:279-286(1988) [PubMed: 2977375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Gene encoding the human beta-hexosaminidase beta chain: extensive homology of intron placement in the alpha- and beta-chain genes." Proia R.L. Proc. Natl. Acad. Sci. U.S.A. 85:1883-1887(1988) [PubMed: 2964638] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Identification of a new proto-oncogene in human cancers." Kim J.W. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The DNA sequence and comparative analysis of human chromosome 5." 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. Nature 431:268-274(2004) [PubMed: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[8]	"Synthesis and assembly of a catalytically active lysosomal enzyme, beta-hexosaminidase B, in a cell-free system." Sonderfeld-Fresko S., Proia R.L. J. Biol. Chem. 263:13463-13469(1988) [PubMed: 2971039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-67.
[9]	"Translation initiation in the HEXB gene encoding the beta-subunit of human beta-hexosaminidase." Neote K., Brown C.A., Mahuran D.J., Gravel R.A. J. Biol. Chem. 265:20799-20806(1990) [PubMed: 2147427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
[10]	"Localization of the pro-sequence within the total deduced primary structure of human beta-hexosaminidase B." Stirling J., Leung A., Gravel R.A., Mahuran D. FEBS Lett. 231:47-50(1988) [PubMed: 2966076] [Abstract] Cited for: PROTEIN SEQUENCE OF 43-57 AND 122-151.
[11]	"Characterization of human placental beta-hexosaminidase I2. Proteolytic processing intermediates of hexosaminidase A." Mahuran D.J. J. Biol. Chem. 265:6794-6799(1990) [PubMed: 2139028] [Abstract] Cited for: PROTEIN SEQUENCE OF 45-54 AND 315-324.
[12]	"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." Hubbes M., Callahan J., Gravel R., Mahuran D. FEBS Lett. 249:316-320(1989) [PubMed: 2525487] [Abstract] Cited for: PROTEIN SEQUENCE OF 50-59.
[13]	"Proteolytic processing of pro-alpha and pro-beta precursors from human beta-hexosaminidase. Generation of the mature alpha and beta a beta b subunits." Mahuran D.J., Neote K., Klavins M.H., Leung A., Gravel R.A. J. Biol. Chem. 263:4612-4618(1988) [PubMed: 2965147] [Abstract] Cited for: PROTEIN SEQUENCE OF 122-151 AND 315-340.
[14]	"Isolation of cDNA clones coding for the beta subunit of human beta-hexosaminidase." O'Dowd B.F., Quan F., Willard H.F., Lamhonwah A.-M., Korneluk R.G., Lowden J.A., Gravel R.A., Mahuran D.J. Proc. Natl. Acad. Sci. U.S.A. 82:1184-1188(1985) [PubMed: 2579389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-283.
[15]	"Oligosaccharide structure and amino acid sequence of the major glycopeptides of mature human beta-hexosaminidase." O'Dowd B.F., Cumming D.A., Gravel R.A., Mahuran D.J. Biochemistry 27:5216-5226(1988) [PubMed: 2971395] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES.
[16]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-327.
[17]	"Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS." Schuette C.G., Weisgerber J., Sandhoff K. Glycobiology 11:549-556(2001) [PubMed: 11447134] [Abstract] Cited for: DISULFIDE BONDS.
[18]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-323 AND ASN-327, MASS SPECTROMETRY. Tissue: Liver.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease." Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S., Vorgias C.E. Nat. Struct. Biol. 3:638-648(1996) [PubMed: 8673609] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[21]	"Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease." Mark B.L., Mahuran D.J., Cherney M.M., Zhao D., Knapp S., James M.N. J. Mol. Biol. 327:1093-1109(2003) [PubMed: 12662933] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 50-556, DISULFIDE BONDS.
[22]	"The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease." Maier T., Strater N., Schuette C.G., Klingenstein R., Sandhoff K., Saenger W. J. Mol. Biol. 328:669-681(2003) [PubMed: 12706724] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 42-556, DISULFIDE BONDS.
[23]	"The biochemistry of HEXA and HEXB gene mutations causing GM2 gangliosidosis." Mahuran D.J. Biochim. Biophys. Acta 1096:87-94(1991) [PubMed: 1825792] [Abstract] Cited for: REVIEW ON VARIANTS.
[24]	"Molecular basis of an adult form of beta-hexosaminidase B deficiency with motor neuron disease." Banerjee P., Siciliano L., Oliveri D., McCabe N.R., Boyers M.J., Horwitz A.L., Li S.-C., Dawson G. Biochem. Biophys. Res. Commun. 181:108-115(1991) [PubMed: 1720305] [Abstract] Cited for: VARIANT GM2G2 SER-456, VARIANT VAL-207.
[25]	"A novel exon mutation in the human beta-hexosaminidase beta subunit gene affects 3' splice site selection." Wakamatsu N., Kobayashi H., Miyatake T., Tsuji S. J. Biol. Chem. 267:2406-2413(1992) [PubMed: 1531140] [Abstract] Cited for: VARIANT GM2G2 LEU-417.
[26]	"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." Bolhuis P.A., Ponne N.J., Bikker H., Baas F., Vianney de Jong J.M.B. Biochim. Biophys. Acta 1182:142-146(1993) [PubMed: 8357844] [Abstract] Cited for: VARIANT GM2G2 GLN-505.
[27]	"A novel missense mutation (C522Y) is present in the beta-hexosaminidase beta-subunit gene of a Japanese patient with infantile Sandhoff disease." Kuroki Y., Itoh K., Nadaoka Y., Tanaka T., Sakuraba H. Biochem. Biophys. Res. Commun. 212:564-571(1995) [PubMed: 7626071] [Abstract] Cited for: VARIANT GM2G2 TYR-534.
[28]	"A common beta hexosaminidase gene mutation in adult Sandhoff disease patients." Gomez-Lira M., Sangalli A., Mottes M., Perusi C., Pignatti P.F., Rizzuto N., Salviati A. Hum. Genet. 96:417-422(1995) [PubMed: 7557963] [Abstract] Cited for: VARIANTS GM2G2 TYR-309 AND LEU-417.
[29]	"A second, large deletion in the HEXB gene in a patient with infantile Sandhoff disease." Zhang Z.-X., Wakamatsu N., Akerman B.R., Mules E.H., Thomas G.H., Gravel R.A. Hum. Mol. Genet. 4:777-780(1995) [PubMed: 7633435] [Abstract] Cited for: VARIANT GM2G2 LEU-62.
[30]	"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." Redonnet-Vernhet I., Mahuran D.J., Salvayre R., Dubas F., Levade T. Biochim. Biophys. Acta 1317:127-133(1996) [PubMed: 8950198] [Abstract] Cited for: VARIANT GM2G2 GLN-505, VARIANT VAL-207.
[31]	"Molecular basis of heat labile hexosaminidase B among Jews and Arabs." Narkis G., Adam A., Jaber L., Pennybacker M., Proia R.L., Navon R. Hum. Mutat. 10:424-429(1997) [PubMed: 9401004] [Abstract] Cited for: VARIANT GM2G2 THR-543.
[32]	"Two mutations remote from an exon/intron junction in the beta-hexosaminidase beta-subunit gene affect 3'-splice site selection and cause Sandhoff disease." Fujimaru M., Tanaka A., Choeh K., Wakamatsu N., Sakuraba H., Isshiki G. Hum. Genet. 103:462-469(1998) [PubMed: 9856491] [Abstract] Cited for: VARIANT GM2G2 ARG-255.
[33]	"A Pro504 --> Ser substitution in the beta-subunit of beta-hexosaminidase A inhibits alpha-subunit hydrolysis of GM2 ganglioside, resulting in chronic Sandhoff disease." Hou Y., McInnes B., Hinek A., Karpati G., Mahuran D. J. Biol. Chem. 273:21386-21392(1998) [PubMed: 9694901] [Abstract] Cited for: VARIANT GM2G2 SER-504.
+	Additional computationally mapped references.

Web resources

HEXBdb

HEXB mutation database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13519 mRNA. Translation: AAA51828.1. Frameshift.
M23294 , M23282, M23283, M23284, M23285, M23286, M23287, M23288, M23290, M23291, M23292, M23293 Genomic DNA. Translation: AAA52645.1.
M19735 mRNA. Translation: AAA68620.1. Different initiation.
AF378118 mRNA. Translation: AAM46114.1.
BT009919 mRNA. Translation: AAP88921.1.
AC026405 Genomic DNA. No translation available.
AC093214 Genomic DNA. No translation available.
BC017378 mRNA. Translation: AAH17378.1.
M34906 mRNA. Translation: AAA51829.1.

IPI

IPI00012585.

PIR

A31250.

RefSeq

NP_000512.1. NM_000521.3.

UniGene

Hs.69293.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NOU	X-ray	2.40	A/B	50-556	[»]
1NOW	X-ray	2.20	A/B	50-556	[»]
1NP0	X-ray	2.50	A/B	50-556	[»]
1O7A	X-ray	2.25	A/B/C/D/E/F	42-556	[»]
1QBD	model	-	A	122-556	[»]
2GJX	X-ray	2.80	B/C/F/G	50-556	[»]
2GK1	X-ray	3.25	B/D/F/H	50-552	[»]
3LMY	X-ray	2.80	A/B	1-556	[»]

ProteinModelPortal

P07686.

SMR

P07686. Positions 54-553.

ModBase

Search...

Protein-protein interaction databases

STRING

P07686.

Protein family/group databases

CAZy

GH20. Glycoside Hydrolase Family 20.

PTM databases

PhosphoSite

P07686.

Polymorphism databases

DMDM

123081.

2D gel databases

UCD-2DPAGE

P07686.

Proteomic databases

PeptideAtlas

P07686.

PRIDE

P07686.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261416; ENSP00000261416; ENSG00000049860.

GeneID

3074.

KEGG

hsa:3074.

UCSC

uc003kdf.2. human.

Organism-specific databases

CTD

3074.

GeneCards

GC05P074016.

H-InvDB

HIX0004949.

HGNC

HGNC:4879. HEXB.

MIM

268800. phenotype.
606873. gene.

neXtProt

NX_P07686.

Orphanet

796. Sandhoff disease.

PharmGKB

PA29257.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09530.

HOGENOM

HBG591688.

HOVERGEN

HBG005961.

InParanoid

P07686.

OrthoDB

EOG42Z4Q7.

PhylomeDB

P07686.

Enzyme and pathway databases

BioCyc

MetaCyc:HS00629-MONOMER.

Gene expression databases

ArrayExpress

P07686.

Bgee

P07686.

CleanEx

HS_HEXB.

Genevestigator

P07686.

GermOnline

ENSG00000049860. Homo sapiens.

Family and domain databases

InterPro

IPR015882. Acetylhexosaminidase_sua/b.
IPR001540. Glyco_hydro_20.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

KO

K12373.

Pfam

PF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]

PRINTS

PR00738. GLHYDRLASE20.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

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Other

NextBio

12159.

SOURCE

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Entry information

Entry name

HEXB_HUMAN

Accession

Primary (citable) accession number: P07686

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.