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Q9HCG7 (GBA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Non-lysosomal glucosylceramidase

Short name=NLGase
EC=3.2.1.45
Alternative name(s):
Beta-glucocerebrosidase 2
Short name=Beta-glucosidase 2
Glucosylceramidase 2
Gene names
Name:GBA2
Synonyms:KIAA1605
ORF Names:AD035
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length927 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide (GlcCer) to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo. Plays a role in central nevous system development. Required for proper formation of motor neuron axons. Ref.10 Ref.11

Catalytic activity

D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine. Ref.1

Enzyme regulation

Enzymatic activity is dependent on membrane association and requires the presence of lipids By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Not localized to lipid rafts. Ref.10

Tissue specificity

Widely expressed. Highly expressed in brain, heart, skeletal muscle, kidney and placenta and expressed at lower level in liver. Ref.1

Involvement in disease

Spastic paraplegia 46, autosomal recessive (SPG46) [MIM:614409]: A neurodegenerative disorder characterized by onset in childhood of slowly progressive spastic paraplegia and cerebellar signs. Some patients have cognitive impairment, cataracts, and cerebral, cerebellar, and corpus callosum atrophy on brain imaging.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12

Sequence similarities

Belongs to the non-lysosomal glucosylceramidase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.7 µM for 3-beta-D-glucosido-lithocholic Ref.9

KM=6.2 µM for 3-beta-D-glucosido-chenodeoxycholic

KM=210 µM for beta-D-glucoside

Sequence caution

The sequence AAG44660.1 differs from that shown. Reason: Frameshift at positions 649 and 691.

The sequence BAB13431.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processLipid metabolism
Sphingolipid metabolism
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Hereditary spastic paraplegia
Neurodegeneration
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid metabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

central nervous system neuron development

Inferred from mutant phenotype Ref.11. Source: UniProtKB

glucosylceramide catabolic process

Inferred from electronic annotation. Source: InterPro

glycoside catabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

glycosphingolipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

smooth endoplasmic reticulum

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionbeta-glucosidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

glucosylceramidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCG7-1)

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: Q9HCG7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     836-927: GLTWEGFQTA...KEAMANLSPE → LLPSGFCLWV...VEVALQRVPS
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9HCG7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-287: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 927927Non-lysosomal glucosylceramidase
PRO_0000283758

Natural variations

Alternative sequence1 – 287287Missing in isoform 3.
VSP_024383
Alternative sequence836 – 92792GLTWE…NLSPE → LLPSGFCLWVIVISSTCWEL LEGKDSTASIYPVEVALQRV PS in isoform 2.
VSP_024384
Natural variant6301R → W in SPG46. Ref.11
VAR_069634
Natural variant8731R → H in SPG46. Ref.12
VAR_069635

Experimental info

Sequence conflict601C → Y in BAB55430. Ref.3
Sequence conflict2221C → R in BAB55430. Ref.3
Sequence conflict4821N → K in BAB55430. Ref.3

Sequences

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

Last modified April 3, 2007. Version 2.
Checksum: 1F6879D6E20A2B1D

FASTA927104,649
        10         20         30         40         50         60 
MGTQDPGNMG TGVPASEQIS CAKEDPQVYC PEETGGTKDV QVTDCKSPED SRPPKETDCC 

        70         80         90        100        110        120 
NPEDSGQLMV SYEGKAMGYQ VPPFGWRICL AHEFTEKRKP FQANNVSLSN MIKHIGMGLR 

       130        140        150        160        170        180 
YLQWWYRKTH VEKKTPFIDM INSVPLRQIY GCPLGGIGGG TITRGWRGQF CRWQLNPGMY 

       190        200        210        220        230        240 
QHRTVIADQF TVCLRREGQT VYQQVLSLER PSVLRSWNWG LCGYFAFYHA LYPRAWTVYQ 

       250        260        270        280        290        300 
LPGQNVTLTC RQITPILPHD YQDSSLPVGV FVWDVENEGD EALDVSIMFS MRNGLGGGDD 

       310        320        330        340        350        360 
APGGLWNEPF CLERSGETVR GLLLHHPTLP NPYTMAVAAR VTAATTVTHI TAFDPDSTGQ 

       370        380        390        400        410        420 
QVWQDLLQDG QLDSPTGQST PTQKGVGIAG AVCVSSKLRP RGQCRLEFSL AWDMPRIMFG 

       430        440        450        460        470        480 
AKGQVHYRRY TRFFGQDGDA APALSHYALC RYAEWEERIS AWQSPVLDDR SLPAWYKSAL 

       490        500        510        520        530        540 
FNELYFLADG GTVWLEVLED SLPEELGRNM CHLRPTLRDY GRFGYLEGQE YRMYNTYDVH 

       550        560        570        580        590        600 
FYASFALIML WPKLELSLQY DMALATLRED LTRRRYLMSG VMAPVKRRNV IPHDIGDPDD 

       610        620        630        640        650        660 
EPWLRVNAYL IHDTADWKDL NLKFVLQVYR DYYLTGDQNF LKDMWPVCLA VMESEMKFDK 

       670        680        690        700        710        720 
DHDGLIENGG YADQTYDGWV TTGPSAYCGG LWLAAVAVMV QMAALCGAQD IQDKFSSILS 

       730        740        750        760        770        780 
RGQEAYERLL WNGRYYNYDS SSRPQSRSVM SDQCAGQWFL KACGLGEGDT EVFPTQHVVR 

       790        800        810        820        830        840 
ALQTIFELNV QAFAGGAMGA VNGMQPHGVP DKSSVQSDEV WVGVVYGLAA TMIQEGLTWE 

       850        860        870        880        890        900 
GFQTAEGCYR TVWERLGLAF QTPEAYCQQR VFRSLAYMRP LSIWAMQLAL QQQQHKKASW 

       910        920 
PKVKQGTGLR TGPMFGPKEA MANLSPE 

« Hide

Isoform 2 [UniParc].

Checksum: 1AF652DAF751EAA5
Show »

FASTA87798,737
Isoform 3 [UniParc].

Checksum: C4DA432626E5B7FD
Show »

FASTA64072,111

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human bile acid beta -glucosidase."
Matern H., Boermans H., Lottspeich F., Matern S.
J. Biol. Chem. 276:37929-37933(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 39-46; 619-636 AND 919-927, ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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] (ISOFORM 1).
Tissue: Kidney and Trachea.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Melanoma.
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Lymph.
[8]Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-780 (ISOFORM 3).
Tissue: Adrenal gland.
[9]"Purification and characterization of a microsomal bile acid beta-glucosidase from human liver."
Matern H., Heinemann H., Legler G., Matern S.
J. Biol. Chem. 272:11261-11267(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[10]"Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2."
Boot R.G., Verhoek M., Donker-Koopman W., Strijland A., van Marle J., Overkleeft H.S., Wennekes T., Aerts J.M.F.G.
J. Biol. Chem. 282:1305-1312(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.
[11]"Loss of function of glucocerebrosidase GBA2 is responsible for motor neuron defects in hereditary spastic paraplegia."
Martin E., Schuele R., Smets K., Rastetter A., Boukhris A., Loureiro J.L., Gonzalez M.A., Mundwiller E., Deconinck T., Wessner M., Jornea L., Oteyza A.C., Durr A., Martin J.J., Schoels L., Mhiri C., Lamari F., Zuechner S. expand/collapse author list , De Jonghe P., Kabashi E., Brice A., Stevanin G.
Am. J. Hum. Genet. 92:238-244(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANT SPG46 TRP-630.
[12]"Mutations in GBA2 cause autosomal-recessive cerebellar ataxia with spasticity."
Hammer M.B., Eleuch-Fayache G., Schottlaender L.V., Nehdi H., Gibbs J.R., Arepalli S.K., Chong S.B., Hernandez D.G., Sailer A., Liu G., Mistry P.K., Cai H., Shrader G., Sassi C., Bouhlal Y., Houlden H., Hentati F., Amouri R., Singleton A.B.
Am. J. Hum. Genet. 92:245-251(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG46 HIS-873.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ309567 mRNA. Translation: CAC83792.1.
AB046825 mRNA. Translation: BAB13431.1. Different initiation.
AK027884 mRNA. Translation: BAB55430.1.
AL834306 mRNA. Translation: CAD38976.1.
AL133410 Genomic DNA. Translation: CAI10981.1.
AL133410 Genomic DNA. Translation: CAI10982.1.
AL133410 Genomic DNA. Translation: CAI10983.1.
CH471071 Genomic DNA. Translation: EAW58348.1.
CH471071 Genomic DNA. Translation: EAW58349.1.
BC011363 mRNA. Translation: AAH11363.1.
AF258662 mRNA. Translation: AAG44660.1. Frameshift.
RefSeqNP_065995.1. NM_020944.2.
UniGeneHs.443134.

3D structure databases

ProteinModelPortalQ9HCG7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121728. 1 interaction.
IntActQ9HCG7. 1 interaction.
MINTMINT-6630061.
STRING9606.ENSP00000367343.

Chemistry

BindingDBQ9HCG7.
ChEMBLCHEMBL3761.

Protein family/group databases

CAZyGH116. Glycoside Hydrolase Family 116.

PTM databases

PhosphoSiteQ9HCG7.

Polymorphism databases

DMDM143018392.

Proteomic databases

PaxDbQ9HCG7.
PRIDEQ9HCG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378094; ENSP00000367334; ENSG00000070610. [Q9HCG7-2]
ENST00000378103; ENSP00000367343; ENSG00000070610. [Q9HCG7-1]
GeneID57704.
KEGGhsa:57704.
UCSCuc003zxw.3. human. [Q9HCG7-1]
uc003zxy.1. human. [Q9HCG7-3]
uc011lpb.1. human. [Q9HCG7-2]

Organism-specific databases

CTD57704.
GeneCardsGC09M035726.
HGNCHGNC:18986. GBA2.
HPAHPA024026.
MIM609471. gene.
614409. phenotype.
neXtProtNX_Q9HCG7.
Orphanet352641. Autosomal recessive cerebellar ataxia with late-onset spasticity.
320391. Autosomal recessive spastic paraplegia type 46.
PharmGKBPA38773.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4354.
HOVERGENHBG105975.
InParanoidQ9HCG7.
KOK17108.
OrthoDBEOG7ZGX2B.
PhylomeDBQ9HCG7.
TreeFamTF313888.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKQ9HCG7.

Gene expression databases

ArrayExpressQ9HCG7.
BgeeQ9HCG7.
CleanExHS_GBA2.
GenevestigatorQ9HCG7.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR014551. Beta_glucosidase_GBA2-type.
IPR024462. GBA2_N.
IPR006775. Glucosylceramidase.
[Graphical view]
PfamPF04685. DUF608. 1 hit.
PF12215. GBA2_N. 1 hit.
[Graphical view]
PIRSFPIRSF028944. Beta_gluc_GBA2. 1 hit.
SUPFAMSSF48208. SSF48208. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGBA2. human.
GeneWikiGBA2.
GenomeRNAi57704.
NextBio64578.
PROQ9HCG7.
SOURCESearch...

Entry information

Entry nameGBA2_HUMAN
AccessionPrimary (citable) accession number: Q9HCG7
Secondary accession number(s): D3DRP2 expand/collapse secondary AC list , Q5TCV6, Q96A51, Q96LY1, Q96SJ2, Q9H2L8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 9

Human chromosome 9: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries