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Q12794 (HYAL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronidase-1

Short name=Hyal-1
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase-1
Lung carcinoma protein 1
Short name=LuCa-1
Gene names
Name:HYAL1
Synonyms:LUCA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth. Ref.4

Catalytic activity

Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

Subcellular location

Secreted. Lysosome Ref.2.

Tissue specificity

Highly expressed in the liver, kidney and heart. Weakly expressed in lung, placenta and skeletal muscle. No expression detected in adult brain. Isoform 1 is expressed only in bladder and prostate cancer cells, G2/G3 bladder tumor tissues and lymph node specimens showing tumor invasive tumors cells. Isoform 3, isoform 4, isoform 5 and isoform 6 are expressed in normal bladder and bladder tumor tissues. Ref.2 Ref.4 Ref.10

Involvement in disease

Mucopolysaccharidosis 9 (MPS9) [MIM:601492]: A lysosomal storage disease characterized by high hyaluronan concentration in the serum. The clinical features are periarticular soft tissue masses, mild short stature and acetabular erosions, and absence of neurological or visceral involvement.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Biophysicochemical properties

pH dependence:

Optimum pH is about 3.8.

Sequence caution

The sequence AAH25774.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentLysosome
Secreted
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Mucopolysaccharidosis
   DomainEGF-like domain
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cartilage development

Inferred from expression pattern PubMed 11944887. Source: UniProtKB

cellular response to UV-B

Inferred from direct assay PubMed 21699545. Source: UniProtKB

cellular response to fibroblast growth factor stimulus

Inferred from direct assay PubMed 19577615. Source: UniProtKB

cellular response to interleukin-1

Inferred from direct assay PubMed 18390475. Source: UniProtKB

cellular response to pH

Inferred from direct assay PubMed 19478093. Source: UniProtKB

cellular response to platelet-derived growth factor stimulus

Inferred from direct assay PubMed 17324121. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from expression pattern PubMed 18390475. Source: UniProtKB

chondroitin sulfate catabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

embryonic skeletal joint morphogenesis

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

hyaluronan biosynthetic process

Inferred from direct assay PubMed 21829529. Source: UniProtKB

hyaluronan catabolic process

Inferred from direct assay PubMed 11296287PubMed 17170110PubMed 20473947PubMed 21695196PubMed 21699545PubMed 21829529Ref.4. Source: UniProtKB

hyaluronan metabolic process

Inferred from direct assay PubMed 19478093. Source: UniProtKB

inflammatory response

Inferred from direct assay PubMed 18390475. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay PubMed 18725949. Source: UniProtKB

positive regulation of angiogenesis

Inferred from direct assay PubMed 21829529. Source: UniProtKB

positive regulation of cell adhesion

Inferred from mutant phenotype PubMed 20473947. Source: UniProtKB

positive regulation of cell growth

Inferred from mutant phenotype PubMed 20473947. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from direct assay PubMed 21829529. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from direct assay PubMed 21829529. Source: UniProtKB

positive regulation of growth

Inferred from direct assay PubMed 21829529. Source: UniProtKB

positive regulation of hyaluranon cable assembly

Inferred from direct assay PubMed 16900089. Source: UniProtKB

response to antibiotic

Inferred from direct assay PubMed 11944887. Source: UniProtKB

response to reactive oxygen species

Inferred from direct assay PubMed 20554532. Source: UniProtKB

response to virus

Inferred from direct assay PubMed 11296287. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 21829529. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay PubMed 18390475. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 17170110PubMed 21695196Ref.2. Source: UniProtKB

hyaluranon cable

Inferred from direct assay PubMed 16900089. Source: UniProtKB

lysosomal lumen

Traceable author statement. Source: Reactome

lysosome

Inferred from direct assay PubMed 16600643PubMed 20572808. Source: UniProtKB

   Molecular_functionhyaluronan synthase activity

Inferred from direct assay PubMed 21829529. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from direct assay PubMed 11296287PubMed 11944887PubMed 17170110PubMed 18390475PubMed 19478093PubMed 20473947PubMed 20572808PubMed 21695196PubMed 21699545PubMed 21829529Ref.2Ref.4. Source: UniProtKB

transcription factor binding

Inferred from direct assay PubMed 18718911. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12794-1)

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: Q12794-2)

Also known as: HYAl1v1;

The sequence of this isoform differs from the canonical sequence as follows:
     301-330: Missing.
Note: Enzymatically inactive.
Isoform 3 (identifier: Q12794-3)

Also known as: HYAl1v2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-182: Missing.
Note: Enzymatically inactive.
Isoform 4 (identifier: Q12794-4)

Also known as: HYAl1v3;

The sequence of this isoform differs from the canonical sequence as follows:
     208-209: YN → SG
     210-435: Missing.
Note: Enzymatically inactive.
Isoform 5 (identifier: Q12794-5)

Also known as: HYAl1v4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-259: Missing.
Note: Enzymatically inactive.
Isoform 6 (identifier: Q12794-6)

Also known as: HYAl1v5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-339: Missing.
Note: Enzymatically inactive.
Isoform 7 (identifier: Q12794-7)

The sequence of this isoform differs from the canonical sequence as follows:
     331-336: ESCQAI → VSLGLA
     337-435: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 435414Hyaluronidase-1
PRO_0000042622

Regions

Domain354 – 43077EGF-like

Sites

Active site1311Proton donor Probable

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Ref.9
Glycosylation2161N-linked (GlcNAc...) Ref.9
Glycosylation3501N-linked (GlcNAc...) Ref.9
Disulfide bond43 ↔ 333 Ref.9
Disulfide bond207 ↔ 221 Ref.9
Disulfide bond358 ↔ 369 Ref.9
Disulfide bond363 ↔ 418 Ref.9
Disulfide bond420 ↔ 429 Ref.9

Natural variations

Alternative sequence1 – 339339Missing in isoform 6.
VSP_015915
Alternative sequence1 – 259259Missing in isoform 5.
VSP_015916
Alternative sequence1 – 182182Missing in isoform 3.
VSP_015917
Alternative sequence208 – 2092YN → SG in isoform 4.
VSP_015918
Alternative sequence210 – 435226Missing in isoform 4.
VSP_015919
Alternative sequence301 – 33030Missing in isoform 2.
VSP_015920
Alternative sequence331 – 3366ESCQAI → VSLGLA in isoform 7.
VSP_015921
Alternative sequence337 – 43599Missing in isoform 7.
VSP_015922
Natural variant2681E → K in MPS9. Ref.10
VAR_023643

Experimental info

Sequence conflict31A → G in CAG46731. Ref.6
Sequence conflict1911R → G in AAD53277. Ref.1
Sequence conflict3001L → Q in AAD24460. Ref.3

Secondary structure

................................................................. 435
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 2.
Checksum: 9C2B2D8DB361E0BB

FASTA43548,368
        10         20         30         40         50         60 
MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD VDVSVFDVVA 

        70         80         90        100        110        120 
NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA SLIAHLARTF QDILAAIPAP 

       130        140        150        160        170        180 
DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR SRALVQAQHP DWPAPQVEAV AQDQFQGAAR 

       190        200        210        220        230        240 
AWMAGTLQLG RALRPRGLWG FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR 

       250        260        270        280        290        300 
ALYPSIYMPA VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDTTNHFLPL 

       310        320        330        340        350        360 
DELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQAIKEYM DTTLGPFILN VTSGALLCSQ 

       370        380        390        400        410        420 
ALCSGHGRCV RRTSHPKALL LLNPASFSIQ LTPGGGPLSL RGALSLEDQA QMAVEFKCRC 

       430 
YPGWQAPWCE RKSMW 

« Hide

Isoform 2 (HYAl1v1) [UniParc].

Checksum: C24DAD360D9CF032
Show »

FASTA40545,145
Isoform 3 (HYAl1v2) [UniParc].

Checksum: 441C0DB43301E03F
Show »

FASTA25327,958
Isoform 4 (HYAl1v3) [UniParc].

Checksum: 5C1046F8199F3BFF
Show »

FASTA20923,338
Isoform 5 (HYAl1v4) [UniParc].

Checksum: 75F674283B175FDD
Show »

FASTA17619,367
Isoform 6 (HYAl1v5) [UniParc].

Checksum: 70AD570E4305A4E8
Show »

FASTA9610,435
Isoform 7 [UniParc].

Checksum: 7D19178001F20E51
Show »

FASTA33637,439

References

« Hide 'large scale' references
[1]"Construction of a 600-kilobase cosmid clone contig and generation of a transcriptional map surrounding the lung cancer tumor suppressor gene (TSG) locus on human chromosome 3p21.3: progress toward the isolation of a lung cancer TSG."
Wei M.H., Latif F., Bader S., Kashuba V., Chen J.Y., Duh F.-M., Sekido Y., Lee C.C., Geil L., Kuzmin I., Zabarovsky E., Klein G., Zbar B., Minna J.D., Lerman M.I.
Cancer Res. 56:1487-1492(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart and Lung cancer.
[2]"Purification, cloning, and expression of human plasma hyaluronidase."
Frost G.I., Csoka A.B., Wong T., Stern R.
Biochem. Biophys. Res. Commun. 236:10-15(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 22-37; 72-84; 248-259 AND 261-273, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Plasma.
[3]"HYAL1(LUCA-1), a candidate tumor suppressor gene on chromosome 3p21.3, is inactivated in head and neck squamous cell carcinomas by aberrant splicing of pre-mRNA."
Frost G.I., Mohapatra G., Wong T.M., Csoka A.B., Gray J.W., Stern R.
Oncogene 19:870-877(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Regulation of hyaluronidase activity by alternative mRNA splicing."
Lokeshwar V.B., Schroeder G.L., Carey R.I., Soloway M.S., Iida N.
J. Biol. Chem. 277:33654-33663(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), FUNCTION, TISSUE SPECIFICITY.
[5]Forgacs E., Sekido Y., Bader S., Cundiff S., Compton L., Latif F., Lerman M.I., Minna J.D.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 7).
Tissue: Colon and Pancreas.
[9]"Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis."
Chao K.L., Muthukumar L., Herzberg O.
Biochemistry 46:6911-6920(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-435; IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-99; ASN-216 AND ASN-350, DISULFIDE BONDS.
[10]"Mutations in HYAL1, a member of a tandemly distributed multigene family encoding disparate hyaluronidase activities, cause a newly described lysosomal disorder, mucopolysaccharidosis IX."
Triggs-Raine B., Salo T.J., Zhang H., Wicklow B.A., Natowicz M.R.
Proc. Natl. Acad. Sci. U.S.A. 96:6296-6300(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS9 LYS-268, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03056 mRNA. Translation: AAD09137.2.
U96078 mRNA. Translation: AAD04190.1.
AF118821 mRNA. Translation: AAD24460.1.
AF502904 mRNA. Translation: AAM60770.1.
AF502905 mRNA. Translation: AAM60771.1.
AF502906 mRNA. Translation: AAM60772.1.
AF502907 mRNA. Translation: AAM60773.1.
AF502908 mRNA. Translation: AAM60774.1.
AF173154 mRNA. Translation: AAD53277.1.
CR541933 mRNA. Translation: CAG46731.1.
AC002455 Genomic DNA. Translation: AAB67046.1.
U73167 Genomic DNA. Translation: AAC02730.1.
BC025774 mRNA. Translation: AAH25774.1. Different initiation.
BC035695 mRNA. Translation: AAH35695.1.
CCDSCCDS2816.1. [Q12794-1]
CCDS2817.1. [Q12794-2]
CCDS46832.1. [Q12794-3]
CCDS46833.1. [Q12794-5]
PIRJC5584.
RefSeqNP_149349.2. NM_033159.3. [Q12794-1]
NP_695013.1. NM_153281.1. [Q12794-1]
NP_695014.1. NM_153282.2. [Q12794-2]
NP_695015.1. NM_153283.2. [Q12794-3]
NP_695017.1. NM_153285.2. [Q12794-5]
UniGeneHs.75619.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PE4X-ray2.00A22-435[»]
ProteinModelPortalQ12794.
SMRQ12794. Positions 20-435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109603. 2 interactions.
IntActQ12794. 1 interaction.

Chemistry

BindingDBQ12794.
ChEMBLCHEMBL4528.
DrugBankDB00070. Hyaluronidase.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Polymorphism databases

DMDM74735617.

Proteomic databases

MaxQBQ12794.
PaxDbQ12794.
PRIDEQ12794.

Protocols and materials databases

DNASU3373.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266031; ENSP00000266031; ENSG00000114378. [Q12794-1]
ENST00000320295; ENSP00000346068; ENSG00000114378. [Q12794-1]
ENST00000395143; ENSP00000378575; ENSG00000114378. [Q12794-2]
ENST00000395144; ENSP00000378576; ENSG00000114378. [Q12794-1]
ENST00000447605; ENSP00000390149; ENSG00000114378. [Q12794-5]
ENST00000457214; ENSP00000393358; ENSG00000114378. [Q12794-3]
ENST00000570958; ENSP00000459254; ENSG00000262208. [Q12794-1]
ENST00000570967; ENSP00000459311; ENSG00000262208. [Q12794-3]
ENST00000571551; ENSP00000461900; ENSG00000262208. [Q12794-5]
ENST00000572970; ENSP00000461261; ENSG00000262208. [Q12794-1]
ENST00000575445; ENSP00000460624; ENSG00000262208. [Q12794-1]
ENST00000576782; ENSP00000459906; ENSG00000262208. [Q12794-2]
GeneID3373.
KEGGhsa:3373.
UCSCuc003czm.4. human. [Q12794-1]
uc003czn.4. human. [Q12794-6]
uc003czo.4. human. [Q12794-5]
uc003czq.4. human. [Q12794-2]
uc003czt.4. human. [Q12794-7]

Organism-specific databases

CTD3373.
GeneCardsGC03M050339.
HGNCHGNC:5320. HYAL1.
HPAHPA002112.
MIM601492. phenotype.
607071. gene.
neXtProtNX_Q12794.
Orphanet67041. Hyaluronidase deficiency.
PharmGKBPA29571.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77606.
HOVERGENHBG052053.
InParanoidQ12794.
KOK01197.
OMAYPSIYMP.
PhylomeDBQ12794.
TreeFamTF321598.

Enzyme and pathway databases

BioCycMetaCyc:HS03763-MONOMER.
BRENDA3.2.1.35. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ12794.
BgeeQ12794.
GenevestigatorQ12794.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS01186. EGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12794.
GeneWikiHYAL1.
GenomeRNAi3373.
NextBio13338.
PROQ12794.
SOURCESearch...

Entry information

Entry nameHYAL1_HUMAN
AccessionPrimary (citable) accession number: Q12794
Secondary accession number(s): Q6FH23 expand/collapse secondary AC list , Q6PIZ6, Q7KYU2, Q7LE34, Q8NFK5, Q8NFK6, Q8NFK7, Q8NFK8, Q8NFK9, Q93013, Q9UKD5, Q9UNI8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 123 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 3

Human chromosome 3: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries