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Q12891 (HYAL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronidase-2

Short name=Hyal-2
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase-2
Lung carcinoma protein 2
Short name=LuCa-2
Gene names
Name:HYAL2
Synonyms:LUCA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R. Ref.1 Ref.9 Ref.10

Catalytic activity

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

Subunit structure

Interacts with MST1R. Ref.10

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Ref.9.

Tissue specificity

Widely expressed. No expression detected in adult brain. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Caution

Was originally thought to be lysosomal.

Sequence caution

The sequence AAC28656.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Signal
   Molecular functionGlycosidase
Hydrolase
Receptor
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
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 transforming growth factor beta stimulus

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

cellular response to tumor necrosis factor

Inferred from expression pattern PubMed 18390475. Source: UniProtKB

defense response to virus

Inferred from electronic annotation. Source: Ensembl

fusion of virus membrane with host plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

glycosaminoglycan catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

hematopoietic progenitor cell differentiation

Inferred from electronic annotation. Source: Ensembl

hyaluronan catabolic process

Inferred from direct assay PubMed 17170110PubMed 19443707PubMed 20554532PubMed 21699545. Source: UniProtKB

hyaluronan metabolic process

Traceable author statement. Source: Reactome

kidney development

Inferred from sequence or structural similarity. Source: UniProtKB

monocyte activation

Inferred from direct assay PubMed 19443707. Source: UniProtKB

multicellular organismal aging

Inferred from electronic annotation. Source: Ensembl

multicellular organismal iron ion homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAP kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay PubMed 18725949. Source: UniProtKB

negative regulation of fibroblast migration

Inferred from direct assay PubMed 19577615. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of protein tyrosine kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of inflammatory response

Inferred from direct assay PubMed 19443707. Source: UniProtKB

positive regulation of interleukin-6 secretion

Inferred from direct assay PubMed 19443707. Source: UniProtKB

positive regulation of interleukin-8 secretion

Inferred from direct assay PubMed 19443707. Source: UniProtKB

positive regulation of protein import into nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of urine volume

Inferred from sequence or structural similarity. Source: UniProtKB

renal water absorption

Inferred from sequence or structural similarity. Source: UniProtKB

response to antibiotic

Inferred from expression pattern PubMed 11944887. Source: UniProtKB

response to reactive oxygen species

Inferred from direct assay PubMed 20554532. Source: UniProtKB

response to virus

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transformation of host cell by virus

Inferred from direct assay Ref.9. Source: UniProtKB

viral entry into host cell

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from sequence or structural similarity PubMed 21740893. Source: UniProtKB

anchored component of external side of plasma membrane

Inferred from direct assay Ref.9PubMed 16191204PubMed 20554532. Source: UniProtKB

anchored component of plasma membrane

Inferred from direct assay PubMed 18390475PubMed 21740893. Source: UniProtKB

apical plasma membrane

Inferred from direct assay PubMed 20554532. Source: UniProtKB

cell surface

Inferred from direct assay PubMed 17170110. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 17170110. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 16600643. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay PubMed 18390475. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

endocytic vesicle

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

endoplasmic reticulum

Non-traceable author statement PubMed 16191204. Source: UniProtKB

lysosome

Inferred from direct assay PubMed 16600643Ref.1. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 21740893. Source: UniProtKB

microvillus

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16600643. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 19366691. Source: BHF-UCL

hyaluronic acid binding

Inferred from direct assay Ref.10PubMed 19443707. Source: UniProtKB

hyaluronoglucuronidase activity

Inferred from direct assay PubMed 21699545. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from direct assay PubMed 11944887PubMed 16600643PubMed 17170110PubMed 18390475PubMed 19443707PubMed 20554532Ref.1. Source: UniProtKB

receptor signaling protein tyrosine kinase inhibitor activity

Inferred from direct assay Ref.10. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

transforming growth factor beta binding

Inferred from sequence or structural similarity. Source: BHF-UCL

virus receptor activity

Inferred from direct assay Ref.9PubMed 16191204. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 448428Hyaluronidase-2
PRO_0000012099
Propeptide449 – 47325Removed in mature form Potential
PRO_0000012100

Regions

Domain361 – 43979EGF-like

Sites

Active site1351Proton donor By similarity

Amino acid modifications

Lipidation4481GPI-anchor amidated glycine Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 340 By similarity
Disulfide bond211 ↔ 227 By similarity
Disulfide bond365 ↔ 376 By similarity
Disulfide bond370 ↔ 427 By similarity
Disulfide bond429 ↔ 438 By similarity

Natural variations

Natural variant181S → A. Ref.1 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs709210 [ dbSNP | Ensembl ].
VAR_028170
Natural variant4181I → L.
Corresponds to variant rs35455589 [ dbSNP | Ensembl ].
VAR_061193

Experimental info

Sequence conflict261 – 2622SR → AL in CAA03924. Ref.1
Sequence conflict301 – 3022RL → C in CAA03924. Ref.1
Sequence conflict3751Missing in CAA03924. Ref.1
Sequence conflict378 – 3792RR → PG in CAA03924. Ref.1
Sequence conflict4501S → N in CAA03924. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q12891 [UniParc].

Last modified November 2, 2010. Version 4.
Checksum: A8302738478BFE61

FASTA47353,860
        10         20         30         40         50         60 
MRAGPGPTVT LALVLAVSWA MELKPTAPPI FTGRPFVVAW DVPTQDCGPR LKVPLDLNAF 

        70         80         90        100        110        120 
DVQASPNEGF VNQNITIFYR DRLGLYPRFD SAGRSVHGGV PQNVSLWAHR KMLQKRVEHY 

       130        140        150        160        170        180 
IRTQESAGLA VIDWEDWRPV WVRNWQDKDV YRRLSRQLVA SRHPDWPPDR IVKQAQYEFE 

       190        200        210        220        230        240 
FAAQQFMLET LRYVKAVRPR HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW 

       250        260        270        280        290        300 
LWAESTALFP SVYLDETLAS SRHGRNFVSF RVQEALRVAR THHANHALPV YVFTRPTYSR 

       310        320        330        340        350        360 
RLTGLSEMDL ISTIGESAAL GAAGVILWGD AGYTTSTETC QYLKDYLTRL LVPYVVNVSW 

       370        380        390        400        410        420 
ATQYCSRAQC HGHGRCVRRN PSASTFLHLS TNSFRLVPGH APGEPQLRPV GELSWADIDH 

       430        440        450        460        470 
LQTHFRCQCY LGWSGEQCQW DHRQAAGGAS EAWAGSHLTS LLALAALAFT WTL 

« Hide

References

« Hide 'large scale' references
[1]"HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity."
Lepperdinger G., Strobl B., Kreil G.
J. Biol. Chem. 273:22466-22470(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT ALA-18.
[2]"LUCA2 (HYAL2, lysosomal hyaluronidase) a novel human cDNA with homology to human PH-20 gene is homozygously deleted in small cell lung cancer and located in 3p21.3."
Chen J., Bader S., Latif F., Duh F.-M., Lerman M.I., Minna J.D.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[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], VARIANT ALA-18.
Tissue: Placenta and Synovium.
[4]"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].
[5]Mural R.J., Istrail S., Sutton 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], VARIANT ALA-18.
[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], VARIANT ALA-18.
Tissue: Kidney.
[7]Yu W., Gibbs R.A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-473, VARIANT ALA-18.
Tissue: Brain.
[8]"Hyal2 -- less active, but more versatile?"
Lepperdinger G., Mullegger J., Kreil G.
Matrix Biol. 20:509-514(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation."
Rai S.K., Duh F.-M., Vigdorovich V., Danilkovitch-Miagkova A., Lerman M.I., Miller A.D.
Proc. Natl. Acad. Sci. U.S.A. 98:4443-4448(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and mediates transformation of epithelial cells by jaagsiekte sheep retrovirus."
Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D., Liu S.-L., Miller A.D., Lerman M.I.
Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MST1R.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000099 mRNA. Translation: CAA03924.1.
U09577 mRNA. Translation: AAC62823.1.
AK092449 mRNA. Translation: BAG52554.1.
AK127945 mRNA. Translation: BAG54602.1.
AC002455 Genomic DNA. Translation: AAB67045.1.
CH471055 Genomic DNA. Translation: EAW65092.1.
BC000692 mRNA. Translation: AAH00692.1.
AF070608 mRNA. Translation: AAC28656.1. Different initiation.
RefSeqNP_003764.3. NM_003773.4.
NP_149348.2. NM_033158.4.
XP_005265581.1. XM_005265524.1.
XP_005265582.1. XM_005265525.1.
UniGeneHs.76873.

3D structure databases

ProteinModelPortalQ12891.
SMRQ12891. Positions 29-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114239. 1 interaction.
IntActQ12891. 4 interactions.
STRING9606.ENSP00000350387.

Chemistry

DrugBankDB00070. Hyaluronidase.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Polymorphism databases

DMDM311033483.

Proteomic databases

PaxDbQ12891.
PRIDEQ12891.

Protocols and materials databases

DNASU8692.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357750; ENSP00000350387; ENSG00000068001.
ENST00000395139; ENSP00000378571; ENSG00000068001.
ENST00000442581; ENSP00000406657; ENSG00000068001.
ENST00000447092; ENSP00000401853; ENSG00000068001.
ENST00000571614; ENSP00000460851; ENSG00000261921.
ENST00000572136; ENSP00000458862; ENSG00000261921.
ENST00000575564; ENSP00000461372; ENSG00000261921.
ENST00000576042; ENSP00000460938; ENSG00000261921.
GeneID8692.
KEGGhsa:8692.
UCSCuc003czv.3. human.

Organism-specific databases

CTD8692.
GeneCardsGC03M050355.
H-InvDBHIX0003314.
HGNCHGNC:5321. HYAL2.
HPAHPA036436.
MIM603551. gene.
neXtProtNX_Q12891.
PharmGKBPA29572.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77606.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidQ12891.
KOK01197.
OMAGWGGEQC.
PhylomeDBQ12891.
TreeFamTF321598.

Enzyme and pathway databases

BioCycMetaCyc:HS00926-MONOMER.
BRENDA4.2.2.1. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SignaLinkQ12891.

Gene expression databases

ArrayExpressQ12891.
BgeeQ12891.
CleanExHS_HYAL2.
GenevestigatorQ12891.

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.
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHYAL2.
GenomeRNAi8692.
NextBio32597.
PROQ12891.
SOURCESearch...

Entry information

Entry nameHYAL2_HUMAN
AccessionPrimary (citable) accession number: Q12891
Secondary accession number(s): B3KRZ2, O15177, Q9BW29
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 133 of the entry and version 4 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 3

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries