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Q12891

- HYAL2_HUMAN

UniProt

Q12891 - HYAL2_HUMAN

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Protein

Hyaluronidase-2

Gene

HYAL2

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

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. receptor signaling protein tyrosine kinase inhibitor activity Source: UniProtKB
  6. receptor tyrosine kinase binding Source: UniProtKB
  7. transforming growth factor beta binding Source: BHF-UCL
  8. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ12891.
CleanExiHS_HYAL2.
ExpressionAtlasiQ12891. baseline and differential.
GenevestigatoriQ12891.

Organism-specific databases

HPAiHPA036436.

Interactioni

Subunit structurei

Interacts with MST1R.1 Publication

Protein-protein interaction databases

BioGridi114239. 4 interactions.
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.
GeneTreeiENSGT00550000074476.
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

« Hide

        10         20         30         40         50
MRAGPGPTVT LALVLAVSWA MELKPTAPPI FTGRPFVVAW DVPTQDCGPR
60 70 80 90 100
LKVPLDLNAF DVQASPNEGF VNQNITIFYR DRLGLYPRFD SAGRSVHGGV
110 120 130 140 150
PQNVSLWAHR KMLQKRVEHY IRTQESAGLA VIDWEDWRPV WVRNWQDKDV
160 170 180 190 200
YRRLSRQLVA SRHPDWPPDR IVKQAQYEFE FAAQQFMLET LRYVKAVRPR
210 220 230 240 250
HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW LWAESTALFP
260 270 280 290 300
SVYLDETLAS SRHGRNFVSF RVQEALRVAR THHANHALPV YVFTRPTYSR
310 320 330 340 350
RLTGLSEMDL ISTIGESAAL GAAGVILWGD AGYTTSTETC QYLKDYLTRL
360 370 380 390 400
LVPYVVNVSW ATQYCSRAQC HGHGRCVRRN PSASTFLHLS TNSFRLVPGH
410 420 430 440 450
APGEPQLRPV GELSWADIDH LQTHFRCQCY LGWSGEQCQW DHRQAAGGAS
460 470
EAWAGSHLTS LLALAALAFT WTL
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 4 interactions.
IntActi Q12891. 4 interactions.
STRINGi 9606.ENSP00000350387.

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.
GeneTreei ENSGT00550000074476.
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

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

Gene expression databases

Bgeei Q12891.
CleanExi HS_HYAL2.
ExpressionAtlasi Q12891. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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