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Q12794

- HYAL1_HUMAN

UniProt

Q12794 - HYAL1_HUMAN

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Protein
Hyaluronidase-1
Gene
HYAL1, LUCA1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is about 3.8.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311Proton donor Inferred

GO - Molecular functioni

  1. hyaluronan synthase activity Source: UniProtKB
  2. hyalurononglucosaminidase activity Source: UniProtKB
  3. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cartilage development Source: UniProtKB
  3. cellular response to UV-B Source: UniProtKB
  4. cellular response to fibroblast growth factor stimulus Source: UniProtKB
  5. cellular response to interleukin-1 Source: UniProtKB
  6. cellular response to pH Source: UniProtKB
  7. cellular response to platelet-derived growth factor stimulus Source: UniProtKB
  8. cellular response to tumor necrosis factor Source: UniProtKB
  9. chondroitin sulfate catabolic process Source: Reactome
  10. chondroitin sulfate metabolic process Source: Reactome
  11. embryonic skeletal joint morphogenesis Source: Ensembl
  12. glycosaminoglycan metabolic process Source: Reactome
  13. hyaluronan biosynthetic process Source: UniProtKB
  14. hyaluronan catabolic process Source: UniProtKB
  15. hyaluronan metabolic process Source: UniProtKB
  16. inflammatory response Source: UniProtKB
  17. negative regulation of cell growth Source: UniProtKB
  18. positive regulation of angiogenesis Source: UniProtKB
  19. positive regulation of cell adhesion Source: UniProtKB
  20. positive regulation of cell growth Source: UniProtKB
  21. positive regulation of epithelial cell migration Source: UniProtKB
  22. positive regulation of epithelial cell proliferation Source: UniProtKB
  23. positive regulation of growth Source: UniProtKB
  24. positive regulation of hyaluranon cable assembly Source: UniProtKB
  25. response to antibiotic Source: UniProtKB
  26. response to reactive oxygen species Source: UniProtKB
  27. response to virus Source: UniProtKB
  28. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:HS03763-MONOMER.
BRENDAi3.2.1.35. 2681.
ReactomeiREACT_120888. CS/DS degradation.
REACT_120996. Hyaluronan uptake and degradation.

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase-1 (EC:3.2.1.35)
Short name:
Hyal-1
Alternative name(s):
Hyaluronoglucosaminidase-1
Lung carcinoma protein 1
Short name:
LuCa-1
Gene namesi
Name:HYAL1
Synonyms:LUCA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:5320. HYAL1.

Subcellular locationi

Secreted. Lysosome 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. hyaluranon cable Source: UniProtKB
  6. lysosomal lumen Source: Reactome
  7. lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti268 – 2681E → K in MPS9. 1 Publication
VAR_023643

Keywords - Diseasei

Disease mutation, Mucopolysaccharidosis

Organism-specific databases

MIMi601492. phenotype.
Orphaneti67041. Hyaluronidase deficiency.
PharmGKBiPA29571.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 435414Hyaluronidase-1
PRO_0000042622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 3331 Publication
Glycosylationi99 – 991N-linked (GlcNAc...)1 Publication
Disulfide bondi207 ↔ 2211 Publication
Glycosylationi216 – 2161N-linked (GlcNAc...)1 Publication
Glycosylationi350 – 3501N-linked (GlcNAc...)1 Publication
Disulfide bondi358 ↔ 3691 Publication
Disulfide bondi363 ↔ 4181 Publication
Disulfide bondi420 ↔ 4291 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ12794.
PaxDbiQ12794.
PRIDEiQ12794.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

ArrayExpressiQ12794.
BgeeiQ12794.
GenevestigatoriQ12794.

Organism-specific databases

HPAiHPA002112.

Interactioni

Protein-protein interaction databases

BioGridi109603. 2 interactions.
IntActiQ12794. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 274
Beta strandi30 – 389
Helixi40 – 478
Beta strandi56 – 594
Beta strandi69 – 746
Beta strandi78 – 803
Helixi97 – 993
Helixi102 – 11615
Beta strandi124 – 1285
Helixi137 – 1393
Helixi142 – 1443
Helixi145 – 15814
Beta strandi159 – 1613
Helixi164 – 19330
Beta strandi197 – 2026
Helixi223 – 2308
Helixi233 – 2386
Beta strandi240 – 2434
Helixi250 – 2523
Helixi258 – 27518
Helixi300 – 3045
Helixi307 – 3126
Beta strandi316 – 3216
Helixi324 – 3263
Beta strandi327 – 3293
Helixi330 – 34213
Helixi344 – 36219
Beta strandi366 – 3716
Turni384 – 3863
Beta strandi387 – 3915
Helixi393 – 3953
Beta strandi398 – 4025
Helixi406 – 41510
Beta strandi416 – 4205
Turni426 – 4294

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PE4X-ray2.00A22-435[»]
ProteinModelPortaliQ12794.
SMRiQ12794. Positions 20-435.

Miscellaneous databases

EvolutionaryTraceiQ12794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 43077EGF-like
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Signal

Phylogenomic databases

eggNOGiNOG77606.
HOVERGENiHBG052053.
InParanoidiQ12794.
KOiK01197.
OMAiYPSIYMP.
PhylomeDBiQ12794.
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.
PROSITEiPS01186. EGF_2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q12794-1) [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

MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD    50
VDVSVFDVVA NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA 100
SLIAHLARTF QDILAAIPAP DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR 150
SRALVQAQHP DWPAPQVEAV AQDQFQGAAR AWMAGTLQLG RALRPRGLWG 200
FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR ALYPSIYMPA 250
VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDTTNHFLPL 300
DELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQAIKEYM DTTLGPFILN 350
VTSGALLCSQ ALCSGHGRCV RRTSHPKALL LLNPASFSIQ LTPGGGPLSL 400
RGALSLEDQA QMAVEFKCRC YPGWQAPWCE RKSMW 435
Length:435
Mass (Da):48,368
Last modified:March 1, 2001 - v2
Checksum:i9C2B2D8DB361E0BB
GO
Isoform 2 (identifier: Q12794-2) [UniParc]FASTAAdd to Basket

Also known as: HYAl1v1

The sequence of this isoform differs from the canonical sequence as follows:
     301-330: Missing.

Note: Enzymatically inactive.

Show »
Length:405
Mass (Da):45,145
Checksum:iC24DAD360D9CF032
GO
Isoform 3 (identifier: Q12794-3) [UniParc]FASTAAdd to Basket

Also known as: HYAl1v2

The sequence of this isoform differs from the canonical sequence as follows:
     1-182: Missing.

Note: Enzymatically inactive.

Show »
Length:253
Mass (Da):27,958
Checksum:i441C0DB43301E03F
GO
Isoform 4 (identifier: Q12794-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:209
Mass (Da):23,338
Checksum:i5C1046F8199F3BFF
GO
Isoform 5 (identifier: Q12794-5) [UniParc]FASTAAdd to Basket

Also known as: HYAl1v4

The sequence of this isoform differs from the canonical sequence as follows:
     1-259: Missing.

Note: Enzymatically inactive.

Show »
Length:176
Mass (Da):19,367
Checksum:i75F674283B175FDD
GO
Isoform 6 (identifier: Q12794-6) [UniParc]FASTAAdd to Basket

Also known as: HYAl1v5

The sequence of this isoform differs from the canonical sequence as follows:
     1-339: Missing.

Note: Enzymatically inactive.

Show »
Length:96
Mass (Da):10,435
Checksum:i70AD570E4305A4E8
GO
Isoform 7 (identifier: Q12794-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     331-336: ESCQAI → VSLGLA
     337-435: Missing.

Note: No experimental confirmation available.

Show »
Length:336
Mass (Da):37,439
Checksum:i7D19178001F20E51
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti268 – 2681E → K in MPS9. 1 Publication
VAR_023643

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 339339Missing in isoform 6.
VSP_015915Add
BLAST
Alternative sequencei1 – 259259Missing in isoform 5.
VSP_015916Add
BLAST
Alternative sequencei1 – 182182Missing in isoform 3.
VSP_015917Add
BLAST
Alternative sequencei208 – 2092YN → SG in isoform 4.
VSP_015918
Alternative sequencei210 – 435226Missing in isoform 4.
VSP_015919Add
BLAST
Alternative sequencei301 – 33030Missing in isoform 2.
VSP_015920Add
BLAST
Alternative sequencei331 – 3366ESCQAI → VSLGLA in isoform 7.
VSP_015921
Alternative sequencei337 – 43599Missing in isoform 7.
VSP_015922Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31A → G in CAG46731. 1 Publication
Sequence conflicti191 – 1911R → G in AAD53277. 1 Publication
Sequence conflicti300 – 3001L → Q in AAD24460. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2816.1. [Q12794-1]
CCDS2817.1. [Q12794-2]
CCDS46832.1. [Q12794-3]
CCDS46833.1. [Q12794-5]
PIRiJC5584.
RefSeqiNP_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]
UniGeneiHs.75619.

Genome annotation databases

EnsembliENST00000266031; 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]
GeneIDi3373.
KEGGihsa:3373.
UCSCiuc003czm.4. human. [Q12794-1]
uc003czn.4. human. [Q12794-6]
uc003czo.4. human. [Q12794-5]
uc003czq.4. human. [Q12794-2]
uc003czt.4. human. [Q12794-7]

Polymorphism databases

DMDMi74735617.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2816.1. [Q12794-1 ]
CCDS2817.1. [Q12794-2 ]
CCDS46832.1. [Q12794-3 ]
CCDS46833.1. [Q12794-5 ]
PIRi JC5584.
RefSeqi NP_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 ]
UniGenei Hs.75619.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PE4 X-ray 2.00 A 22-435 [» ]
ProteinModelPortali Q12794.
SMRi Q12794. Positions 20-435.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109603. 2 interactions.
IntActi Q12794. 1 interaction.

Chemistry

BindingDBi Q12794.
ChEMBLi CHEMBL4528.
DrugBanki DB00070. Hyaluronidase.

Protein family/group databases

CAZyi GH56. Glycoside Hydrolase Family 56.

Polymorphism databases

DMDMi 74735617.

Proteomic databases

MaxQBi Q12794.
PaxDbi Q12794.
PRIDEi Q12794.

Protocols and materials databases

DNASUi 3373.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000266031 ; 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 ]
GeneIDi 3373.
KEGGi hsa:3373.
UCSCi uc003czm.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

CTDi 3373.
GeneCardsi GC03M050339.
HGNCi HGNC:5320. HYAL1.
HPAi HPA002112.
MIMi 601492. phenotype.
607071. gene.
neXtProti NX_Q12794.
Orphaneti 67041. Hyaluronidase deficiency.
PharmGKBi PA29571.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG77606.
HOVERGENi HBG052053.
InParanoidi Q12794.
KOi K01197.
OMAi YPSIYMP.
PhylomeDBi Q12794.
TreeFami TF321598.

Enzyme and pathway databases

BioCyci MetaCyc:HS03763-MONOMER.
BRENDAi 3.2.1.35. 2681.
Reactomei REACT_120888. CS/DS degradation.
REACT_120996. Hyaluronan uptake and degradation.

Miscellaneous databases

EvolutionaryTracei Q12794.
GeneWikii HYAL1.
GenomeRNAii 3373.
NextBioi 13338.
PROi Q12794.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12794.
Bgeei Q12794.
Genevestigatori Q12794.

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 PS01186. EGF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHYAL1_HUMAN
AccessioniPrimary (citable) accession number: Q12794
Secondary accession number(s): Q6FH23
, Q6PIZ6, Q7KYU2, Q7LE34, Q8NFK5, Q8NFK6, Q8NFK7, Q8NFK8, Q8NFK9, Q93013, Q9UKD5, Q9UNI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 124 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, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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