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Q8WVB3 (HEXDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexosaminidase D

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase
Beta-hexosaminidase D
Hexosaminidase domain-containing protein
N-acetyl-beta-galactosaminidase
Gene names
Name:HEXDC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has hexosaminidase activity. Ref.1

Catalytic activity

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

Enzyme regulation

Inhibited by O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate (PUGNAc) By similarity.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Cytoplasm. Nucleus By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Sequence caution

The sequence AAH18205.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAH35561.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB85072.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WVB3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WVB3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     355-486: EGAGSFPGSN...SPGRDVAQDP → QAPCSPPCPL...EGSSTGRPAL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Hexosaminidase D
PRO_0000316790

Sites

Active site1491Proton donor By similarity

Natural variations

Alternative sequence355 – 486132EGAGS…VAQDP → QAPCSPPCPLLPLPFPRPWR QLFSAGLSAGRGPAPSLAAT SLPLSHKSASICAALWMRCW RATGMSLAGSAPTTASGSSS TRSWFSTSSPQRSASWHSGA PSCRSWRLPCSWLSTRMPWR SGWRKTCTPACSGCKLCCRT SARCLPPRCHPPALAGTLLR TPEGRAHARGLLLEAGGALH CQMAWAIRAHVGVVPSGPAV SCPHSVPEGPGQPLGERLEN TEGSSTGRPAL in isoform 2.
VSP_030777
Natural variant1451I → V.
Corresponds to variant rs4789773 [ dbSNP | Ensembl ].
VAR_038395
Natural variant2321H → Y. Ref.4
Corresponds to variant rs17853433 [ dbSNP | Ensembl ].
VAR_060726

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: 8634D2CC438EA5DA

FASTA48653,790
        10         20         30         40         50         60 
MSGSTPFQMR LVHLDLKGAP PKVSYLSEIF PLFRALGANG LLIEYEDMFP YEGPLRLLRA 

        70         80         90        100        110        120 
KYAYSPSEIK EILHLAGLNE LEVIPLVQTF GHMEFVLKHT AFAHLREVGS FPCTLNPHEA 

       130        140        150        160        170        180 
ESLALVGAMI DQVLELHPGA QRLHIGCDEV YYLGEGEASR RWLQQEQNST GKLCLSHMRA 

       190        200        210        220        230        240 
VASGVKARRP SVTPLVWDDM LRDLPEDQLA ASGVPQLVEP VLWDYTADLD VHGKVLLMQK 

       250        260        270        280        290        300 
YRRCGFPQLW AASAFKGATG PSQAVPPVEH HLRNHVQWLQ VAGSGPTDSL QGIILTGWQR 

       310        320        330        340        350        360 
YDHYSVLCEL LPAGVPSLAA CLQLLLRGGF DEDVKAKVEN LLGISSLEKT DPVREGAGSF 

       370        380        390        400        410        420 
PGSNILALVT QVSLHLRSSV DALLEGNRYV TGWFSPYHRQ RKLIHPVMVQ HIQPAALSLL 

       430        440        450        460        470        480 
AQWSTLVQEL EAALQLAFYP DAVEEWLEEN VHPSLQRLQA LLQDLSEVSA PPLPPTSPGR 


DVAQDP 

« Hide

Isoform 2 [UniParc].

Checksum: 71AB241D7DFCDDEB
Show »

FASTA58563,502

References

« Hide 'large scale' references
[1]"Mammalian cells contain a second nucleocytoplasmic hexosaminidase."
Gutternigg M., Rendic D., Voglauer R., Iskratsch T., Wilson I.B.
Biochem. J. 419:83-90(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 2), VARIANT TYR-232.
Tissue: Blood and Cervix.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-486 (ISOFORM 1).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204887 mRNA. Translation: CAR57925.1.
AC132938 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89773.1.
BC018205 mRNA. Translation: AAH18205.2. Different initiation.
BC035561 mRNA. Translation: AAH35561.1. Different initiation.
AK074405 mRNA. Translation: BAB85072.1. Different initiation.
RefSeqNP_775891.2. NM_173620.2.
XP_005256404.1. XM_005256347.1.
UniGeneHs.744207.

3D structure databases

ProteinModelPortalQ8WVB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129726. 8 interactions.
IntActQ8WVB3. 9 interactions.
MINTMINT-1383902.
STRING9606.ENSP00000337854.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Polymorphism databases

DMDM167008870.

Proteomic databases

PaxDbQ8WVB3.
PRIDEQ8WVB3.

Protocols and materials databases

DNASU284004.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327949; ENSP00000332634; ENSG00000169660. [Q8WVB3-1]
ENST00000337014; ENSP00000337854; ENSG00000169660. [Q8WVB3-2]
GeneID284004.
KEGGhsa:284004.
UCSCuc002kev.4. human. [Q8WVB3-2]
uc002kew.3. human. [Q8WVB3-1]

Organism-specific databases

CTD284004.
GeneCardsGC17P080382.
HGNCHGNC:26307. HEXDC.
HPAHPA022834.
HPA023379.
HPA027844.
neXtProtNX_Q8WVB3.
PharmGKBPA142671693.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72156.
HOGENOMHOG000047740.
HOVERGENHBG061201.
KOK14459.
OMASWRLPCS.
OrthoDBEOG7N63M4.
TreeFamTF314313.

Gene expression databases

ArrayExpressQ8WVB3.
BgeeQ8WVB3.
CleanExHS_HEXDC.
GenevestigatorQ8WVB3.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi284004.
NextBio94440.
PROQ8WVB3.

Entry information

Entry nameHEXDC_HUMAN
AccessionPrimary (citable) accession number: Q8WVB3
Secondary accession number(s): B7UUP6, Q8IYN4, Q8TE81
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: March 19, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries