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Protein

Hyaluronidase-1

Gene

HYAL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 donorCurated

GO - Molecular functioni

  • hyaluronan synthase activity Source: UniProtKB
  • hyalurononglucosaminidase activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • carbohydrate metabolic process Source: Reactome
  • cartilage development Source: UniProtKB
  • cellular response to fibroblast growth factor stimulus Source: UniProtKB
  • cellular response to interleukin-1 Source: UniProtKB
  • cellular response to pH Source: UniProtKB
  • cellular response to platelet-derived growth factor stimulus Source: UniProtKB
  • cellular response to tumor necrosis factor Source: UniProtKB
  • cellular response to UV-B Source: UniProtKB
  • chondroitin sulfate catabolic process Source: Reactome
  • chondroitin sulfate metabolic process Source: Reactome
  • embryonic skeletal joint morphogenesis Source: Ensembl
  • glycosaminoglycan metabolic process Source: Reactome
  • hyaluronan biosynthetic process Source: UniProtKB
  • hyaluronan catabolic process Source: UniProtKB
  • hyaluronan metabolic process Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: UniProtKB
  • positive regulation of growth Source: UniProtKB
  • positive regulation of hyaluranon cable assembly Source: UniProtKB
  • response to antibiotic Source: UniProtKB
  • response to reactive oxygen species Source: UniProtKB
  • response to virus Source: UniProtKB
  • 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.
4.2.2.1. 2681.
ReactomeiREACT_120888. CS/DS degradation.
REACT_120996. Hyaluronan uptake and degradation.
REACT_147739. MPS IX - Natowicz syndrome.

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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:5320. HYAL1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • hyaluranon cable Source: UniProtKB
  • lysosomal lumen Source: Reactome
  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 9 (MPS9)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:601492
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.

Polymorphism and mutation databases

BioMutaiHYAL1.
DMDMi74735617.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 435414Hyaluronidase-1PRO_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

BgeeiQ12794.
ExpressionAtlasiQ12794. baseline and differential.
GenevisibleiQ12794. HS.

Organism-specific databases

HPAiHPA002112.

Interactioni

Protein-protein interaction databases

BioGridi109603. 8 interactions.
IntActiQ12794. 1 interaction.

Structurei

Secondary structure

1
435
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 274Combined sources
Beta strandi30 – 389Combined sources
Helixi40 – 478Combined sources
Beta strandi56 – 594Combined sources
Beta strandi69 – 746Combined sources
Beta strandi78 – 803Combined sources
Helixi97 – 993Combined sources
Helixi102 – 11615Combined sources
Beta strandi124 – 1285Combined sources
Helixi137 – 1393Combined sources
Helixi142 – 1443Combined sources
Helixi145 – 15814Combined sources
Beta strandi159 – 1613Combined sources
Helixi164 – 19330Combined sources
Beta strandi197 – 2026Combined sources
Helixi223 – 2308Combined sources
Helixi233 – 2386Combined sources
Beta strandi240 – 2434Combined sources
Helixi250 – 2523Combined sources
Helixi258 – 27518Combined sources
Helixi300 – 3045Combined sources
Helixi307 – 3126Combined sources
Beta strandi316 – 3216Combined sources
Helixi324 – 3263Combined sources
Beta strandi327 – 3293Combined sources
Helixi330 – 34213Combined sources
Helixi344 – 36219Combined sources
Beta strandi366 – 3716Combined sources
Turni384 – 3863Combined sources
Beta strandi387 – 3915Combined sources
Helixi393 – 3953Combined sources
Beta strandi398 – 4025Combined sources
Helixi406 – 41510Combined sources
Beta strandi416 – 4205Combined sources
Turni426 – 4294Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PE4X-ray2.00A22-435[»]
ProteinModelPortaliQ12794.
SMRiQ12794. Positions 20-435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 43077EGF-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.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD
60 70 80 90 100
VDVSVFDVVA NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA
110 120 130 140 150
SLIAHLARTF QDILAAIPAP DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR
160 170 180 190 200
SRALVQAQHP DWPAPQVEAV AQDQFQGAAR AWMAGTLQLG RALRPRGLWG
210 220 230 240 250
FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR ALYPSIYMPA
260 270 280 290 300
VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDTTNHFLPL
310 320 330 340 350
DELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQAIKEYM DTTLGPFILN
360 370 380 390 400
VTSGALLCSQ ALCSGHGRCV RRTSHPKALL LLNPASFSIQ LTPGGGPLSL
410 420 430
RGALSLEDQA QMAVEFKCRC YPGWQAPWCE RKSMW
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31A → G in CAG46731 (Ref. 6) Curated
Sequence conflicti191 – 1911R → G in AAD53277 (PubMed:8603390).Curated
Sequence conflicti300 – 3001L → Q in AAD24460 (PubMed:10702795).Curated

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. 1 PublicationVSP_015915Add
BLAST
Alternative sequencei1 – 259259Missing in isoform 5. 1 PublicationVSP_015916Add
BLAST
Alternative sequencei1 – 182182Missing in isoform 3. 1 PublicationVSP_015917Add
BLAST
Alternative sequencei208 – 2092YN → SG in isoform 4. 1 PublicationVSP_015918
Alternative sequencei210 – 435226Missing in isoform 4. 1 PublicationVSP_015919Add
BLAST
Alternative sequencei301 – 33030Missing in isoform 2. 2 PublicationsVSP_015920Add
BLAST
Alternative sequencei331 – 3366ESCQAI → VSLGLA in isoform 7. 1 PublicationVSP_015921
Alternative sequencei337 – 43599Missing in isoform 7. 1 PublicationVSP_015922Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
ENST00000618175; ENSP00000477903; ENSG00000114378. [Q12794-1]
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]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PE4X-ray2.00A22-435[»]
ProteinModelPortaliQ12794.
SMRiQ12794. Positions 20-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109603. 8 interactions.
IntActiQ12794. 1 interaction.

Chemistry

BindingDBiQ12794.
ChEMBLiCHEMBL4528.

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Polymorphism and mutation databases

BioMutaiHYAL1.
DMDMi74735617.

Proteomic databases

MaxQBiQ12794.
PaxDbiQ12794.
PRIDEiQ12794.

Protocols and materials databases

DNASUi3373.
Structural Biology KnowledgebaseSearch...

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]
ENST00000618175; ENSP00000477903; ENSG00000114378. [Q12794-1]
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]

Organism-specific databases

CTDi3373.
GeneCardsiGC03M050339.
HGNCiHGNC:5320. HYAL1.
HPAiHPA002112.
MIMi601492. phenotype.
607071. gene.
neXtProtiNX_Q12794.
Orphaneti67041. Hyaluronidase deficiency.
PharmGKBiPA29571.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG77606.
GeneTreeiENSGT00550000074476.
HOVERGENiHBG052053.
InParanoidiQ12794.
KOiK01197.
OMAiYPSIYMP.
PhylomeDBiQ12794.
TreeFamiTF321598.

Enzyme and pathway databases

BioCyciMetaCyc:HS03763-MONOMER.
BRENDAi3.2.1.35. 2681.
4.2.2.1. 2681.
ReactomeiREACT_120888. CS/DS degradation.
REACT_120996. Hyaluronan uptake and degradation.
REACT_147739. MPS IX - Natowicz syndrome.

Miscellaneous databases

EvolutionaryTraceiQ12794.
GeneWikiiHYAL1.
GenomeRNAii3373.
NextBioi13338.
PROiQ12794.
SOURCEiSearch...

Gene expression databases

BgeeiQ12794.
ExpressionAtlasiQ12794. baseline and differential.
GenevisibleiQ12794. HS.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 133 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.