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Q9H227

- GBA3_HUMAN

UniProt

Q9H227 - GBA3_HUMAN

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Protein

Cytosolic beta-glucosidase

Gene

GBA3

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.3 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Enzyme regulationi

Inhibited by 2,4-dinitrophenyl-2-fluoro-2-deoxy-beta-D-glucopyranoside and sodium taurocholate.2 Publications

Kineticsi

  1. KM=40 µM for 4-methylumbelliferyl-beta-D-glucopyranoside2 Publications
  2. KM=50 µM for 4-methylumbelliferyl-beta-D-galactopyranoside2 Publications
  3. KM=370 µM for 4-nitrophenyl-beta-D-fucopyranoside2 Publications
  4. KM=570 µM for 4-nitrophenyl-alpha-D-arabinopyranoside2 Publications
  5. KM=1.76 mM for 4-nitrophenyl-beta-D-glucopyranoside2 Publications
  6. KM=3.14 mM for 4-nitrophenyl-beta-D-galactopyranoside2 Publications
  7. KM=1.58 mM for 4-nitrophenyl-beta-D-xylopyranoside2 Publications
  8. KM=52.6 mM for 4-nitrophenyl-beta-L-arabinopyranoside2 Publications
  9. KM=35 µM for genistein-7-glucoside2 Publications
  10. KM=118 µM for daidzein-7-glucoside2 Publications
  11. KM=31.8 µM for quercetin-4'-glucoside2 Publications
  12. KM=42.2 µM for quercetin-7-glucoside2 Publications
  13. KM=21.5 µM for apigenin-7-glucoside2 Publications
  14. KM=10 µM for luteolin-4'-glucoside2 Publications
  15. KM=50 µM for luteolin-7-glucoside2 Publications
  16. KM=432 µM for naringenin-7-glucoside2 Publications
  17. KM=253 µM for eriodictyol-7-glucoside2 Publications

Vmax=10 µmol/min/mg enzyme toward 4-nitrophenyl-beta-D-glucopyranoside2 Publications

Vmax=1.73 µmol/min/mg enzyme toward genistein-7-glucoside2 Publications

Vmax=2.75 µmol/min/mg enzyme toward daidzein-7-glucoside2 Publications

Vmax=1.19 µmol/min/mg enzyme toward quercetin-4'-glucoside2 Publications

Vmax=0.77 µmol/min/mg enzyme toward quercetin-7-glucoside2 Publications

Vmax=1.30 µmol/min/mg enzyme toward apigenin-7-glucoside2 Publications

Vmax=1.30 µmol/min/mg enzyme toward luteolin-4'-glucoside2 Publications

Vmax=2.85 µmol/min/mg enzyme toward luteolin-7-glucoside2 Publications

Vmax=0.93 µmol/min/mg enzyme toward naringenin-7-glucoside2 Publications

Vmax=0.90 µmol/min/mg enzyme toward eriodictyol-7-glucoside2 Publications

pH dependencei

Optimum pH is 6.5. Active from pH 5 to 7.5. Activity decreases sharply with increasing acidity and is less than 4% at pH 4.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Stable more than 24 hours at 37 degrees Celsius. Loses activity at 58 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei17 – 171Substrate
Binding sitei120 – 1201Substrate
Binding sitei164 – 1641Substrate
Active sitei165 – 1651Proton donorSequence Analysis
Binding sitei309 – 3091Substrate
Active sitei373 – 3731NucleophileSequence Analysis
Binding sitei417 – 4171Substrate

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB
  2. beta-glucosidase activity Source: UniProtKB
  3. glycosylceramidase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. glycoside catabolic process Source: UniProtKB
  3. glycosphingolipid metabolic process Source: Reactome
  4. glycosylceramide catabolic process Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_116105. Glycosphingolipid metabolism.
SABIO-RKQ9H227.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic beta-glucosidase (EC:3.2.1.21)
Alternative name(s):
Cytosolic beta-glucosidase-like protein 1
Gene namesi
Name:GBA3
Synonyms:CBG, CBGL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:19069. GBA3.

Subcellular locationi

Cytoplasm › cytosol 2 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651E → D: Reduces catalytic activity 2-fold. 2 Publications
Mutagenesisi165 – 1651E → Q: Loss of catalytic activity. 2 Publications
Mutagenesisi168 – 1681V → Y: No change in temperature or pH dependence. Decrease in specific activity. 1 Publication
Mutagenesisi225 – 2251F → S: Decrease in specific activity. 1 Publication
Mutagenesisi308 – 3081Y → F or A: Decrease in specific activity. 1 Publication
Mutagenesisi373 – 3731E → D: Reduces catalytic activity 2-fold. 1 Publication
Mutagenesisi373 – 3731E → Q: Loss of catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA134861643.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Cytosolic beta-glucosidasePRO_0000063908Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiQ9H227.

PTM databases

PhosphoSiteiQ9H227.

Expressioni

Tissue specificityi

Present in small intestine (at protein level). Expressed in liver, small intestine, colon, spleen and kidney. Down-regulated in renal cell carcinomas and hepatocellular carcinomas.2 Publications

Gene expression databases

CleanExiHS_GBA3.
GenevestigatoriQ9H227.

Interactioni

Protein-protein interaction databases

BioGridi121753. 2 interactions.
IntActiQ9H227. 1 interaction.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi15 – 184Combined sources
Helixi24 – 263Combined sources
Helixi31 – 388Combined sources
Beta strandi40 – 434Combined sources
Helixi44 – 463Combined sources
Beta strandi49 – 513Combined sources
Turni55 – 573Combined sources
Helixi59 – 6911Combined sources
Beta strandi72 – 776Combined sources
Helixi80 – 834Combined sources
Helixi94 – 10916Combined sources
Beta strandi113 – 1219Combined sources
Helixi125 – 1295Combined sources
Helixi132 – 1343Combined sources
Helixi138 – 15316Combined sources
Turni154 – 1563Combined sources
Beta strandi159 – 1646Combined sources
Helixi166 – 1749Combined sources
Turni186 – 1883Combined sources
Helixi189 – 21123Combined sources
Helixi213 – 2164Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi223 – 23311Combined sources
Helixi237 – 25014Combined sources
Helixi252 – 2598Combined sources
Helixi266 – 27813Combined sources
Helixi291 – 2977Combined sources
Beta strandi302 – 31615Combined sources
Helixi326 – 3305Combined sources
Beta strandi332 – 3354Combined sources
Helixi351 – 36313Combined sources
Beta strandi369 – 3746Combined sources
Beta strandi378 – 3814Combined sources
Helixi387 – 40519Combined sources
Beta strandi411 – 4177Combined sources
Helixi425 – 4306Combined sources
Beta strandi435 – 4384Combined sources
Beta strandi442 – 4443Combined sources
Beta strandi447 – 4493Combined sources
Helixi451 – 46212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9LX-ray1.60A1-469[»]
2E9MX-ray1.80A1-469[»]
2JFEX-ray2.70X1-469[»]
2ZOXX-ray1.90A1-469[»]
3VKKX-ray2.00A1-469[»]
ProteinModelPortaliQ9H227.
SMRiQ9H227. Positions 1-466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H227.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni424 – 4252Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family. Klotho subfamily.Curated

Phylogenomic databases

HOVERGENiHBG053101.
InParanoidiQ9H227.
KOiK05350.
PhylomeDBiQ9H227.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H227-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAFPAGFGWA AATAAYQVEG GWDADGKGPC VWDTFTHQGG ERVFKNQTGD 
        60         70         80         90        100
VACGSYTLWE EDLKCIKQLG LTHYRFSLSW SRLLPDGTTG FINQKGIDYY 
       110        120        130        140        150
NKIIDDLLKN GVTPIVTLYH FDLPQTLEDQ GGWLSEAIIE SFDKYAQFCF 
       160        170        180        190        200
STFGDRVKQW ITINEANVLS VMSYDLGMFP PGIPHFGTGG YQAAHNLIKA 
       210        220        230        240        250
HARSWHSYDS LFRKKQKGMV SLSLFAVWLE PADPNSVSDQ EAAKRAITFH 
       260        270        280        290        300
LDLFAKPIFI DGDYPEVVKS QIASMSQKQG YPSSRLPEFT EEEKKMIKGT 
       310        320        330        340        350
ADFFAVQYYT TRLIKYQENK KGELGILQDA EIEFFPDPSW KNVDWIYVVP 
       360        370        380        390        400
WGVCKLLKYI KDTYNNPVIY ITENGFPQSD PAPLDDTQRW EYFRQTFQEL 
       410        420        430        440        450
FKAIQLDKVN LQVYCAWSLL DNFEWNQGYS SRFGLFHVDF EDPARPRVPY 
       460 
TSAKEYAKII RNNGLEAHL
Length:469
Mass (Da):53,696
Last modified:October 11, 2005 - v2
Checksum:i9036455485CE2E2F
GO
Isoform 2 (identifier: Q9H227-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-401: Missing.

Show »
Length:162
Mass (Da):18,265
Checksum:iAC2A05DB957E6997
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291P → L in AAH70188. (PubMed:15489334)Curated
Sequence conflicti134 – 1341L → W in AAG39217. (PubMed:11784319)Curated
Sequence conflicti309 – 3091Y → C in BAD96683. 1 PublicationCurated
Sequence conflicti321 – 3211K → R in BAD96683. 1 PublicationCurated
Sequence conflicti326 – 3261I → T in CAC08178. (PubMed:11389701)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061D → N Rare polymorphism. 1 Publication
VAR_023587
Natural varianti172 – 1721M → I.
Corresponds to variant rs36090352 [ dbSNP | Ensembl ].		VAR_049298
Natural varianti213 – 2131R → P.
Corresponds to variant rs17612341 [ dbSNP | Ensembl ].		VAR_023588
Natural varianti354 – 3541C → R.
Corresponds to variant rs16873108 [ dbSNP | Ensembl ].		VAR_023589

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei95 – 401307Missing in isoform 2. 1 PublicationVSP_015835Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017913 mRNA. Translation: BAB18741.1.
AJ278964 mRNA. Translation: CAC08178.1.
AF317840 mRNA. Translation: AAG39217.1.
AF323990 mRNA. Translation: AAL37305.1.
AK222963 mRNA. Translation: BAD96683.1.
BC029362 mRNA. Translation: AAH29362.1.
BC070188 mRNA. Translation: AAH70188.1.
BC101829 mRNA. Translation: AAI01830.1.
BC109377 mRNA. Translation: AAI09378.1.
RefSeqiNP_001121904.1. NM_001128432.2. [Q9H227-2]
NP_001264154.1. NM_001277225.1.
NP_066024.1. NM_020973.4. [Q9H227-1]
UniGeneiHs.653107.

Genome annotation databases

GeneIDi57733.
KEGGihsa:57733.
UCSCiuc031sdv.1. human. [Q9H227-1]
uc031sdw.1. human. [Q9H227-2]

Polymorphism databases

DMDMi77416427.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AB017913 mRNA. Translation: BAB18741.1 .
AJ278964 mRNA. Translation: CAC08178.1 .
AF317840 mRNA. Translation: AAG39217.1 .
AF323990 mRNA. Translation: AAL37305.1 .
AK222963 mRNA. Translation: BAD96683.1 .
BC029362 mRNA. Translation: AAH29362.1 .
BC070188 mRNA. Translation: AAH70188.1 .
BC101829 mRNA. Translation: AAI01830.1 .
BC109377 mRNA. Translation: AAI09378.1 .
RefSeqi NP_001121904.1. NM_001128432.2. [Q9H227-2 ]
NP_001264154.1. NM_001277225.1.
NP_066024.1. NM_020973.4. [Q9H227-1 ]
UniGenei Hs.653107.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E9L X-ray 1.60 A 1-469 [» ]
2E9M X-ray 1.80 A 1-469 [» ]
2JFE X-ray 2.70 X 1-469 [» ]
2ZOX X-ray 1.90 A 1-469 [» ]
3VKK X-ray 2.00 A 1-469 [» ]
ProteinModelPortali Q9H227.
SMRi Q9H227. Positions 1-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121753. 2 interactions.
IntActi Q9H227. 1 interaction.

Chemistry

BindingDBi Q9H227.
ChEMBLi CHEMBL3865.

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

PTM databases

PhosphoSitei Q9H227.

Polymorphism databases

DMDMi 77416427.

Proteomic databases

PRIDEi Q9H227.

Protocols and materials databases

DNASUi 57733.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 57733.
KEGGi hsa:57733.
UCSCi uc031sdv.1. human. [Q9H227-1 ]
uc031sdw.1. human. [Q9H227-2 ]

Organism-specific databases

CTDi 57733.
GeneCardsi GC04P022694.
HGNCi HGNC:19069. GBA3.
MIMi 606619. gene.
neXtProti NX_Q9H227.
PharmGKBi PA134861643.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG053101.
InParanoidi Q9H227.
KOi K05350.
PhylomeDBi Q9H227.

Enzyme and pathway databases

Reactomei REACT_116105. Glycosphingolipid metabolism.
SABIO-RK Q9H227.

Miscellaneous databases

EvolutionaryTracei Q9H227.
GeneWikii GBA3.
GenomeRNAii 57733.
NextBioi 64698.
PROi Q9H227.
SOURCEi Search...

Gene expression databases

CleanExi HS_GBA3.
Genevestigatori Q9H227.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
PRINTSi PR00131. GLHYDRLASE1.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Liver.
  3. "Functional expression of human liver cytosolic beta-glucosidase in Pichia pastoris. Insights into its role in the metabolism of dietary glucosides."
    Berrin J.-G., McLauchlan W.R., Needs P., Williamson G., Puigserver A., Kroon P.A., Juge N.
    Eur. J. Biochem. 269:249-258(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BLOCKAGE OF N-TERMINUS, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Liver.
  4. Hays W.S., VanderJagt D.J., Glew R.H., Johnston D.E.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Small intestine.
  6. "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).
    Tissue: Kidney and Liver.
  7. "Substrate (aglycone) specificity of human cytosolic beta-glucosidase."
    Berrin J.-G., Czjzek M., Kroon P.A., McLauchlan W.R., Puigserver A., Williamson G., Juge N.
    Biochem. J. 373:41-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-168; PHE-225 AND TYR-308.
  8. "Deglycosylation by small intestinal epithelial cell beta-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans."
    Nemeth K., Plumb G.W., Berrin J.-G., Juge N., Jacob R., Naim H.Y., Williamson G., Swallow D.M., Kroon P.A.
    Eur. J. Nutr. 42:29-42(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase."
    Hayashi Y., Okino N., Kakuta Y., Shikanai T., Tani M., Narimatsu H., Ito M.
    J. Biol. Chem. 282:30889-30900(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH GLUCOSE AND GALACTOSE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-165 AND GLU-373.
  10. "The crystal structure of human cytosolic beta-glucosidase unravels the substrate aglycone specificity of a family 1 glycoside hydrolase."
    Tribolo S., Berrin J.G., Kroon P.A., Czjzek M., Juge N.
    J. Mol. Biol. 370:964-975(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  11. "Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase."
    Noguchi J., Hayashi Y., Baba Y., Okino N., Kimura M., Ito M., Kakuta Y.
    Biochem. Biophys. Res. Commun. 374:549-552(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE, MUTAGENESIS OF GLU-165.
  12. "Mutations in the gene encoding cytosolic beta-glucosidase in Gaucher disease."
    Beutler E., Beutler L., West C.
    J. Lab. Clin. Med. 144:65-68(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-106.
+Additional computationally mapped references.

Entry informationi

Entry nameiGBA3_HUMAN
AccessioniPrimary (citable) accession number: Q9H227
Secondary accession number(s): Q32LY7
, Q3MIH4, Q53GG8, Q6NSF4, Q8NHT8, Q9H3T4, Q9H4C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: January 7, 2015
This is version 122 of the entry and version 2 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, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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