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Q12891

- HYAL2_HUMAN

UniProt

Q12891 - HYAL2_HUMAN

Protein

Hyaluronidase-2

Gene

HYAL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 4 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei135 – 1351Proton donorBy similarity

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. hyaluronic acid binding Source: UniProtKB
    3. hyaluronoglucuronidase activity Source: UniProtKB
    4. hyalurononglucosaminidase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. receptor signaling protein tyrosine kinase inhibitor activity Source: UniProtKB
    7. receptor tyrosine kinase binding Source: UniProtKB
    8. transforming growth factor beta binding Source: BHF-UCL
    9. virus receptor activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cartilage development Source: UniProtKB
    3. cellular response to fibroblast growth factor stimulus Source: UniProtKB
    4. cellular response to interleukin-1 Source: UniProtKB
    5. cellular response to transforming growth factor beta stimulus Source: BHF-UCL
    6. cellular response to tumor necrosis factor Source: UniProtKB
    7. cellular response to UV-B Source: UniProtKB
    8. defense response to virus Source: Ensembl
    9. fusion of virus membrane with host plasma membrane Source: UniProtKB
    10. glycosaminoglycan catabolic process Source: UniProtKB
    11. glycosaminoglycan metabolic process Source: Reactome
    12. hematopoietic progenitor cell differentiation Source: Ensembl
    13. hyaluronan catabolic process Source: UniProtKB
    14. hyaluronan metabolic process Source: Reactome
    15. kidney development Source: UniProtKB
    16. monocyte activation Source: UniProtKB
    17. multicellular organismal aging Source: Ensembl
    18. multicellular organismal iron ion homeostasis Source: Ensembl
    19. negative regulation of cell growth Source: UniProtKB
    20. negative regulation of fibroblast migration Source: UniProtKB
    21. negative regulation of MAP kinase activity Source: UniProtKB
    22. negative regulation of protein kinase B signaling Source: UniProtKB
    23. negative regulation of protein tyrosine kinase activity Source: UniProtKB
    24. positive regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    25. positive regulation of inflammatory response Source: UniProtKB
    26. positive regulation of interleukin-6 secretion Source: UniProtKB
    27. positive regulation of interleukin-8 secretion Source: UniProtKB
    28. positive regulation of protein import into nucleus Source: BHF-UCL
    29. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    30. positive regulation of urine volume Source: UniProtKB
    31. renal water absorption Source: UniProtKB
    32. response to antibiotic Source: UniProtKB
    33. response to reactive oxygen species Source: UniProtKB
    34. response to virus Source: UniProtKB
    35. skeletal system morphogenesis Source: Ensembl
    36. small molecule metabolic process Source: Reactome
    37. transformation of host cell by virus Source: UniProtKB
    38. viral entry into host cell Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Receptor

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00926-MONOMER.
    BRENDAi4.2.2.1. 2681.
    ReactomeiREACT_120996. Hyaluronan uptake and degradation.
    SignaLinkiQ12891.

    Protein family/group databases

    CAZyiGH56. Glycoside Hydrolase Family 56.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hyaluronidase-2 (EC:3.2.1.35)
    Short name:
    Hyal-2
    Alternative name(s):
    Hyaluronoglucosaminidase-2
    Lung carcinoma protein 2
    Short name:
    LuCa-2
    Gene namesi
    Name:HYAL2
    Synonyms:LUCA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:5321. HYAL2.

    Subcellular locationi

    Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: UniProtKB
    2. anchored component of plasma membrane Source: UniProtKB
    3. apical plasma membrane Source: UniProtKB
    4. cell surface Source: UniProtKB
    5. cytoplasm Source: UniProtKB
    6. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    7. cytoplasmic vesicle Source: UniProtKB
    8. cytosol Source: BHF-UCL
    9. endocytic vesicle Source: BHF-UCL
    10. endoplasmic reticulum Source: UniProtKB
    11. Golgi membrane Source: UniProtKB
    12. lysosome Source: UniProtKB
    13. membrane raft Source: UniProtKB
    14. microvillus Source: BHF-UCL
    15. perinuclear region of cytoplasm Source: UniProtKB
    16. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29572.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 448428Hyaluronidase-2PRO_0000012099Add
    BLAST
    Propeptidei449 – 47325Removed in mature formSequence AnalysisPRO_0000012100Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 ↔ 340By similarity
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi211 ↔ 227By similarity
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi365 ↔ 376By similarity
    Disulfide bondi370 ↔ 427By similarity
    Disulfide bondi429 ↔ 438By similarity
    Lipidationi448 – 4481GPI-anchor amidated glycineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiQ12891.
    PaxDbiQ12891.
    PRIDEiQ12891.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ12891.
    BgeeiQ12891.
    CleanExiHS_HYAL2.
    GenevestigatoriQ12891.

    Organism-specific databases

    HPAiHPA036436.

    Interactioni

    Subunit structurei

    Interacts with MST1R.1 Publication

    Protein-protein interaction databases

    BioGridi114239. 1 interaction.
    IntActiQ12891. 4 interactions.
    STRINGi9606.ENSP00000350387.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12891.
    SMRiQ12891. Positions 29-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini361 – 43979EGF-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 56 family.Curated
    Contains 1 EGF-like domain.Curated

    Keywords - Domaini

    EGF-like domain, Signal

    Phylogenomic databases

    eggNOGiNOG77606.
    HOGENOMiHOG000015133.
    HOVERGENiHBG052053.
    InParanoidiQ12891.
    KOiK01197.
    OMAiGWGGEQC.
    PhylomeDBiQ12891.
    TreeFamiTF321598.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR000742. EG-like_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    [Graphical view]
    PANTHERiPTHR11769. PTHR11769. 1 hit.
    PfamiPF01630. Glyco_hydro_56. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
    PRINTSiPR00846. GLHYDRLASE56.
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q12891-1 [UniParc]FASTAAdd to Basket

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    MRAGPGPTVT LALVLAVSWA MELKPTAPPI FTGRPFVVAW DVPTQDCGPR    50
    LKVPLDLNAF DVQASPNEGF VNQNITIFYR DRLGLYPRFD SAGRSVHGGV 100
    PQNVSLWAHR KMLQKRVEHY IRTQESAGLA VIDWEDWRPV WVRNWQDKDV 150
    YRRLSRQLVA SRHPDWPPDR IVKQAQYEFE FAAQQFMLET LRYVKAVRPR 200
    HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW LWAESTALFP 250
    SVYLDETLAS SRHGRNFVSF RVQEALRVAR THHANHALPV YVFTRPTYSR 300
    RLTGLSEMDL ISTIGESAAL GAAGVILWGD AGYTTSTETC QYLKDYLTRL 350
    LVPYVVNVSW ATQYCSRAQC HGHGRCVRRN PSASTFLHLS TNSFRLVPGH 400
    APGEPQLRPV GELSWADIDH LQTHFRCQCY LGWSGEQCQW DHRQAAGGAS 450
    EAWAGSHLTS LLALAALAFT WTL 473
    Length:473
    Mass (Da):53,860
    Last modified:November 2, 2010 - v4
    Checksum:iA8302738478BFE61
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2622SR → AL in CAA03924. (PubMed:9712871)Curated
    Sequence conflicti301 – 3022RL → C in CAA03924. (PubMed:9712871)Curated
    Sequence conflicti375 – 3751Missing in CAA03924. (PubMed:9712871)Curated
    Sequence conflicti378 – 3792RR → PG in CAA03924. (PubMed:9712871)Curated
    Sequence conflicti450 – 4501S → N in CAA03924. (PubMed:9712871)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181S → A.5 Publications
    Corresponds to variant rs709210 [ dbSNP | Ensembl ].
    VAR_028170
    Natural varianti418 – 4181I → L.
    Corresponds to variant rs35455589 [ dbSNP | Ensembl ].
    VAR_061193

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2818.1.
    RefSeqiNP_003764.3. NM_003773.4.
    NP_149348.2. NM_033158.4.
    XP_005265581.1. XM_005265524.1.
    XP_005265582.1. XM_005265525.1.
    UniGeneiHs.76873.

    Genome annotation databases

    EnsembliENST00000357750; ENSP00000350387; ENSG00000068001.
    ENST00000395139; ENSP00000378571; ENSG00000068001.
    ENST00000442581; ENSP00000406657; ENSG00000068001.
    ENST00000447092; ENSP00000401853; ENSG00000068001.
    GeneIDi8692.
    KEGGihsa:8692.
    UCSCiuc003czv.3. human.

    Polymorphism databases

    DMDMi311033483.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS2818.1.
    RefSeqi NP_003764.3. NM_003773.4.
    NP_149348.2. NM_033158.4.
    XP_005265581.1. XM_005265524.1.
    XP_005265582.1. XM_005265525.1.
    UniGenei Hs.76873.

    3D structure databases

    ProteinModelPortali Q12891.
    SMRi Q12891. Positions 29-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114239. 1 interaction.
    IntActi Q12891. 4 interactions.
    STRINGi 9606.ENSP00000350387.

    Chemistry

    DrugBanki DB00070. Hyaluronidase.

    Protein family/group databases

    CAZyi GH56. Glycoside Hydrolase Family 56.

    Polymorphism databases

    DMDMi 311033483.

    Proteomic databases

    MaxQBi Q12891.
    PaxDbi Q12891.
    PRIDEi Q12891.

    Protocols and materials databases

    DNASUi 8692.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357750 ; ENSP00000350387 ; ENSG00000068001 .
    ENST00000395139 ; ENSP00000378571 ; ENSG00000068001 .
    ENST00000442581 ; ENSP00000406657 ; ENSG00000068001 .
    ENST00000447092 ; ENSP00000401853 ; ENSG00000068001 .
    GeneIDi 8692.
    KEGGi hsa:8692.
    UCSCi uc003czv.3. human.

    Organism-specific databases

    CTDi 8692.
    GeneCardsi GC03M050355.
    H-InvDB HIX0003314.
    HGNCi HGNC:5321. HYAL2.
    HPAi HPA036436.
    MIMi 603551. gene.
    neXtProti NX_Q12891.
    PharmGKBi PA29572.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77606.
    HOGENOMi HOG000015133.
    HOVERGENi HBG052053.
    InParanoidi Q12891.
    KOi K01197.
    OMAi GWGGEQC.
    PhylomeDBi Q12891.
    TreeFami TF321598.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00926-MONOMER.
    BRENDAi 4.2.2.1. 2681.
    Reactomei REACT_120996. Hyaluronan uptake and degradation.
    SignaLinki Q12891.

    Miscellaneous databases

    GeneWikii HYAL2.
    GenomeRNAii 8692.
    NextBioi 32597.
    PROi Q12891.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12891.
    Bgeei Q12891.
    CleanExi HS_HYAL2.
    Genevestigatori Q12891.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR000742. EG-like_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    [Graphical view ]
    PANTHERi PTHR11769. PTHR11769. 1 hit.
    Pfami PF01630. Glyco_hydro_56. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038193. Hyaluronidase. 1 hit.
    PRINTSi PR00846. GLHYDRLASE56.
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiHYAL2_HUMAN
    AccessioniPrimary (citable) accession number: Q12891
    Secondary accession number(s): B3KRZ2, O15177, Q9BW29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 138 of the entry and version 4 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

    Caution

    Was originally thought to be lysosomal.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3