Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07686

- HEXB_HUMAN

UniProt

P07686 - HEXB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-hexosaminidase subunit beta

Gene

HEXB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei355 – 3551Proton donorBy similarity
Sitei497 – 4971Not glycosylated (PubMed:11447134)1 Publication

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: ProtInc
  2. protein heterodimerization activity Source: MGI
  3. protein homodimerization activity Source: MGI

GO - Biological processi

  1. astrocyte cell migration Source: Ensembl
  2. carbohydrate metabolic process Source: Reactome
  3. cell death Source: UniProtKB-KW
  4. cellular calcium ion homeostasis Source: Ensembl
  5. cellular protein metabolic process Source: Ensembl
  6. chondroitin sulfate catabolic process Source: Reactome
  7. chondroitin sulfate metabolic process Source: Reactome
  8. ganglioside catabolic process Source: Ensembl
  9. glycosaminoglycan metabolic process Source: Reactome
  10. glycosphingolipid metabolic process Source: Reactome
  11. hyaluronan catabolic process Source: Reactome
  12. hyaluronan metabolic process Source: Reactome
  13. keratan sulfate catabolic process Source: Reactome
  14. keratan sulfate metabolic process Source: Reactome
  15. lipid storage Source: Ensembl
  16. locomotory behavior Source: Ensembl
  17. lysosome organization Source: Ensembl
  18. male courtship behavior Source: Ensembl
  19. myelination Source: Ensembl
  20. neuromuscular process controlling balance Source: Ensembl
  21. oligosaccharide catabolic process Source: Ensembl
  22. oogenesis Source: Ensembl
  23. penetration of zona pellucida Source: Ensembl
  24. phospholipid biosynthetic process Source: Ensembl
  25. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  26. regulation of cell shape Source: Ensembl
  27. sensory perception of sound Source: Ensembl
  28. skeletal system development Source: Ensembl
  29. small molecule metabolic process Source: Reactome
  30. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:HS00629-MONOMER.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_120888. CS/DS degradation.
REACT_120996. Hyaluronan uptake and degradation.
REACT_121313. Keratan sulfate degradation.
SABIO-RKP07686.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:HEXB
ORF Names:HCC7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4879. HEXB.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. lysosomal lumen Source: Reactome
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

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.10 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621S → L in GM2G2. 1 Publication
Corresponds to variant rs820878 [ dbSNP | Ensembl ].
VAR_003247
Natural varianti255 – 2551S → R in GM2G2. 1 Publication
VAR_011704
Natural varianti309 – 3091C → Y in GM2G2; adult type; severe; almost complete absence of activity. 1 Publication
VAR_003250
Natural varianti417 – 4171P → L in GM2G2. 2 Publications
Corresponds to variant rs28942073 [ dbSNP | Ensembl ].
VAR_003251
Natural varianti456 – 4561Y → S in GM2G2. 1 Publication
VAR_003252
Natural varianti504 – 5041P → S in GM2G2. 1 Publication
VAR_011705
Natural varianti505 – 5051R → Q in GM2G2. 2 Publications
VAR_003253
Natural varianti534 – 5341C → Y in GM2G2; infantile type. 1 Publication
VAR_003254
Natural varianti543 – 5431A → T in GM2G2. 1 Publication
VAR_011706

Keywords - Diseasei

Disease mutation, Gangliosidosis, Neurodegeneration

Organism-specific databases

MIMi268800. phenotype.
Orphaneti309169. Sandhoff disease, adult form.
309155. Sandhoff disease, infantile form.
309162. Sandhoff disease, juvenile form.
PharmGKBiPA29257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Sequence AnalysisAdd
BLAST
Propeptidei43 – 121792 PublicationsPRO_0000012002Add
BLAST
Chaini122 – 556435Beta-hexosaminidase subunit betaPRO_0000012003Add
BLAST
Chaini122 – 311190Beta-hexosaminidase subunit beta chain BPRO_0000012004Add
BLAST
Chaini315 – 556242Beta-hexosaminidase subunit beta chain APRO_0000012005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)2 Publications
Disulfide bondi91 ↔ 137
Glycosylationi142 – 1421N-linked (GlcNAc...)1 Publication
Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
Disulfide bondi309 ↔ 360
Glycosylationi323 – 3231N-linked (GlcNAc...)1 Publication
Glycosylationi327 – 3271N-linked (GlcNAc...)3 Publications
Disulfide bondi534 ↔ 551

Post-translational modificationi

N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-GlcNAc2 and Man(5 to 7)-GlcNAc2, respectively.3 Publications
The beta-A and beta-B chains are produced by proteolytic processing of the precursor beta chain.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP07686.
PaxDbiP07686.
PeptideAtlasiP07686.
PRIDEiP07686.

2D gel databases

UCD-2DPAGEP07686.

PTM databases

PhosphoSiteiP07686.

Expressioni

Gene expression databases

BgeeiP07686.
CleanExiHS_HEXB.
ExpressionAtlasiP07686. baseline and differential.
GenevestigatoriP07686.

Organism-specific databases

HPAiHPA055409.
HPA056010.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi109323. 20 interactions.
IntActiP07686. 1 interaction.
MINTiMINT-4528380.
STRINGi9606.ENSP00000261416.

Structurei

Secondary structure

1
556
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 7111
Helixi74 – 763
Beta strandi78 – 814
Beta strandi83 – 864
Helixi92 – 10514
Beta strandi126 – 1316
Beta strandi149 – 1535
Beta strandi155 – 16410
Helixi165 – 17814
Beta strandi187 – 19610
Beta strandi201 – 21212
Helixi216 – 22813
Beta strandi233 – 2375
Helixi253 – 2586
Beta strandi259 – 2613
Beta strandi262 – 2643
Helixi268 – 28013
Beta strandi284 – 29411
Helixi298 – 3014
Beta strandi306 – 3083
Beta strandi318 – 3225
Helixi327 – 34317
Beta strandi346 – 3527
Helixi359 – 3624
Helixi365 – 3739
Helixi380 – 39718
Beta strandi401 – 4055
Helixi406 – 4105
Beta strandi420 – 4234
Helixi429 – 43810
Beta strandi443 – 4453
Helixi447 – 4493
Beta strandi450 – 4534
Beta strandi455 – 4573
Helixi460 – 4656
Helixi475 – 4795
Beta strandi481 – 4888
Helixi490 – 4923
Turni495 – 4973
Helixi498 – 5025
Helixi505 – 51410
Helixi522 – 53817
Beta strandi546 – 5483

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NOUX-ray2.40A/B50-556[»]
1NOWX-ray2.20A/B50-556[»]
1NP0X-ray2.50A/B50-556[»]
1O7AX-ray2.25A/B/C/D/E/F42-556[»]
1QBDmodel-A122-556[»]
2GJXX-ray2.80B/C/F/G54-107[»]
B/C/F/G226-552[»]
2GK1X-ray3.25B/D/F/H50-107[»]
B/C/F/G226-552[»]
3LMYX-ray2.80A/B1-556[»]
ProteinModelPortaliP07686.
SMRiP07686. Positions 54-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07686.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3525.
HOGENOMiHOG000157972.
HOVERGENiHBG005961.
InParanoidiP07686.
KOiK12373.
OrthoDBiEOG7KDFB6.
PhylomeDBiP07686.
TreeFamiTF313036.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07686-1 [UniParc]FASTAAdd to Basket

« Hide

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

CNHENM
Length:556
Mass (Da):63,111
Last modified:February 1, 1991 - v3
Checksum:iB3A0A36594F62536
GO

Sequence cautioni

The sequence AAA51828.1 differs from that shown. Reason: Frameshift at position 21.
The sequence AAA68620.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621S → L in GM2G2. 1 Publication
Corresponds to variant rs820878 [ dbSNP | Ensembl ].
VAR_003247
Natural varianti121 – 1211K → R.
Corresponds to variant rs11556045 [ dbSNP | Ensembl ].
VAR_003248
Natural varianti207 – 2071I → V Probable polymorphism. 2 Publications
Corresponds to variant rs10805890 [ dbSNP | Ensembl ].
VAR_003249
Natural varianti255 – 2551S → R in GM2G2. 1 Publication
VAR_011704
Natural varianti309 – 3091C → Y in GM2G2; adult type; severe; almost complete absence of activity. 1 Publication
VAR_003250
Natural varianti417 – 4171P → L in GM2G2. 2 Publications
Corresponds to variant rs28942073 [ dbSNP | Ensembl ].
VAR_003251
Natural varianti456 – 4561Y → S in GM2G2. 1 Publication
VAR_003252
Natural varianti504 – 5041P → S in GM2G2. 1 Publication
VAR_011705
Natural varianti505 – 5051R → Q in GM2G2. 2 Publications
VAR_003253
Natural varianti534 – 5341C → Y in GM2G2; infantile type. 1 Publication
VAR_003254
Natural varianti543 – 5431A → T in GM2G2. 1 Publication
VAR_011706

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4022.1.
PIRiA31250.
RefSeqiNP_000512.1. NM_000521.3.
NP_001278933.1. NM_001292004.1.
UniGeneiHs.69293.

Genome annotation databases

EnsembliENST00000261416; ENSP00000261416; ENSG00000049860.
GeneIDi3074.
KEGGihsa:3074.
UCSCiuc003kdd.3. human.

Polymorphism databases

DMDMi123081.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

HEXBdb

HEXB mutation database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4022.1.
PIRi A31250.
RefSeqi NP_000512.1. NM_000521.3.
NP_001278933.1. NM_001292004.1.
UniGenei Hs.69293.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 54-107 [» ]
B/C/F/G 226-552 [» ]
2GK1 X-ray 3.25 B/D/F/H 50-107 [» ]
B/C/F/G 226-552 [» ]
3LMY X-ray 2.80 A/B 1-556 [» ]
ProteinModelPortali P07686.
SMRi P07686. Positions 54-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109323. 20 interactions.
IntActi P07686. 1 interaction.
MINTi MINT-4528380.
STRINGi 9606.ENSP00000261416.

Chemistry

BindingDBi P07686.
ChEMBLi CHEMBL3038485.

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

PTM databases

PhosphoSitei P07686.

Polymorphism databases

DMDMi 123081.

2D gel databases

UCD-2DPAGE P07686.

Proteomic databases

MaxQBi P07686.
PaxDbi P07686.
PeptideAtlasi P07686.
PRIDEi P07686.

Protocols and materials databases

DNASUi 3074.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261416 ; ENSP00000261416 ; ENSG00000049860 .
GeneIDi 3074.
KEGGi hsa:3074.
UCSCi uc003kdd.3. human.

Organism-specific databases

CTDi 3074.
GeneCardsi GC05P073935.
HGNCi HGNC:4879. HEXB.
HPAi HPA055409.
HPA056010.
MIMi 268800. phenotype.
606873. gene.
neXtProti NX_P07686.
Orphaneti 309169. Sandhoff disease, adult form.
309155. Sandhoff disease, infantile form.
309162. Sandhoff disease, juvenile form.
PharmGKBi PA29257.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3525.
HOGENOMi HOG000157972.
HOVERGENi HBG005961.
InParanoidi P07686.
KOi K12373.
OrthoDBi EOG7KDFB6.
PhylomeDBi P07686.
TreeFami TF313036.

Enzyme and pathway databases

BioCyci MetaCyc:HS00629-MONOMER.
Reactomei REACT_116105. Glycosphingolipid metabolism.
REACT_120888. CS/DS degradation.
REACT_120996. Hyaluronan uptake and degradation.
REACT_121313. Keratan sulfate degradation.
SABIO-RK P07686.

Miscellaneous databases

ChiTaRSi HEXB. human.
EvolutionaryTracei P07686.
GeneWikii HEXB.
GenomeRNAii 3074.
NextBioi 12159.
PROi P07686.
SOURCEi Search...

Gene expression databases

Bgeei P07686.
CleanExi HS_HEXB.
ExpressionAtlasi P07686. baseline and differential.
Genevestigatori P07686.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProi IPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view ]
Pfami PF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view ]
PIRSFi PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSi PR00738. GLHYDRLASE20.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 122-151 AND 315-340.
  14. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-84; ASN-142; ASN-190 AND ASN-327.
  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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-323 AND ASN-327.
    Tissue: Liver.
  19. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: VARIANT GM2G2 SER-504.

Entry informationi

Entry nameiHEXB_HUMAN
AccessioniPrimary (citable) accession number: P07686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3