Q12794 (HYAL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hyaluronidase-1
Short name=Hyal-1
EC=3.2.1.35

Alternative name(s):
Hyaluronoglucosaminidase-1
Lung carcinoma protein 1
Short name=LuCa-1

Gene names

Name:	HYAL1
Synonyms:	LUCA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth. Ref.4
Catalytic activity	Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.
Subcellular location	Secreted. Lysosome Ref.2.
Tissue specificity	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. Ref.2 Ref.4 Ref.10
Involvement in disease	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. Ref.10
Sequence similarities	Belongs to the glycosyl hydrolase 56 family. Contains 1 EGF-like domain.
Biophysicochemical properties	pH dependence: Optimum pH is about 3.8.
Sequence caution	The sequence AAH25774.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Lysosome Secreted
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Mucopolysaccharidosis
Domain	EGF-like domain Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome cartilage development Inferred from expression pattern PubMed 11944887. Source: UniProtKB cellular response to UV-B Inferred from direct assay PubMed 21699545. Source: UniProtKB cellular response to fibroblast growth factor stimulus Inferred from direct assay PubMed 19577615. Source: UniProtKB cellular response to interleukin-1 Inferred from direct assay PubMed 18390475. Source: UniProtKB cellular response to pH Inferred from direct assay PubMed 19478093. Source: UniProtKB cellular response to platelet-derived growth factor stimulus Inferred from direct assay PubMed 17324121. Source: UniProtKB cellular response to tumor necrosis factor Inferred from expression pattern PubMed 18390475. Source: UniProtKB chondroitin sulfate catabolic process Traceable author statement. Source: Reactome embryonic skeletal joint morphogenesis Inferred from electronic annotation. Source: Compara hyaluronan biosynthetic process Inferred from direct assay PubMed 21829529. Source: UniProtKB hyaluronan catabolic process Inferred from direct assay PubMed 11296287PubMed 17170110PubMed 20473947PubMed 21695196PubMed 21699545PubMed 21829529Ref.4. Source: UniProtKB inflammatory response Inferred from direct assay PubMed 18390475. Source: UniProtKB negative regulation of cell growth Inferred from direct assay PubMed 18725949. Source: UniProtKB positive regulation of S phase of mitotic cell cycle Inferred from direct assay PubMed 21829529. Source: UniProtKB positive regulation of angiogenesis Inferred from direct assay PubMed 21829529. Source: UniProtKB positive regulation of cell adhesion Inferred from mutant phenotype PubMed 20473947. Source: UniProtKB positive regulation of cell growth Inferred from mutant phenotype PubMed 20473947. Source: UniProtKB positive regulation of epithelial cell migration Inferred from direct assay PubMed 21829529. Source: UniProtKB positive regulation of epithelial cell proliferation Inferred from direct assay PubMed 21829529. Source: UniProtKB positive regulation of hyaluranon cable assembly Inferred from direct assay PubMed 16900089. Source: UniProtKB response to antibiotic Inferred from direct assay PubMed 11944887. Source: UniProtKB response to reactive oxygen species Inferred from direct assay PubMed 20554532. Source: UniProtKB response to virus Inferred from direct assay PubMed 11296287. Source: UniProtKB
Cellular_component	cytoplasmic vesicle Inferred from direct assay PubMed 18390475. Source: UniProtKB extracellular space Inferred from direct assay PubMed 17170110PubMed 21695196Ref.2. Source: UniProtKB hyaluranon cable Inferred from direct assay PubMed 16900089. Source: UniProtKB lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	hyaluronan synthase activity Inferred from direct assay PubMed 21829529. Source: UniProtKB hyalurononglucosaminidase activity Inferred from direct assay PubMed 11296287PubMed 11944887PubMed 17170110PubMed 18390475PubMed 19478093PubMed 20473947PubMed 20572808PubMed 21695196PubMed 21699545PubMed 21829529Ref.2Ref.4. Source: UniProtKB transcription factor binding Inferred from direct assay PubMed 18718911. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q12794-1)

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.

Isoform 2 (identifier: Q12794-2)

Also known as: HYAl1v1;

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

Note: Enzymatically inactive.

Isoform 3 (identifier: Q12794-3)

Also known as: HYAl1v2;

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

Note: Enzymatically inactive.

Isoform 4 (identifier: Q12794-4)

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.

Isoform 5 (identifier: Q12794-5)

Also known as: HYAl1v4;

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

Note: Enzymatically inactive.

Isoform 6 (identifier: Q12794-6)

Also known as: HYAl1v5;

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

Note: Enzymatically inactive.

Isoform 7 (identifier: Q12794-7)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 435

414

Hyaluronidase-1

PRO_0000042622

Regions

Domain

354 – 430

77

EGF-like

Sites

Active site

131

1

Proton donor Probable

Amino acid modifications

Glycosylation

99

1

N-linked (GlcNAc...) Ref.9

Glycosylation

216

1

N-linked (GlcNAc...) Ref.9

Glycosylation

350

1

N-linked (GlcNAc...) Ref.9

Disulfide bond

43 ↔ 333

Ref.9

Disulfide bond

207 ↔ 221

Ref.9

Disulfide bond

358 ↔ 369

Ref.9

Disulfide bond

363 ↔ 418

Ref.9

Disulfide bond

420 ↔ 429

Ref.9

Natural variations

Alternative sequence

1 – 339

339

Missing in isoform 6.

VSP_015915

Alternative sequence

1 – 259

259

Missing in isoform 5.

VSP_015916

Alternative sequence

1 – 182

182

Missing in isoform 3.

VSP_015917

Alternative sequence

208 – 209

2

YN → SG in isoform 4.

VSP_015918

Alternative sequence

210 – 435

226

Missing in isoform 4.

VSP_015919

Alternative sequence

301 – 330

30

Missing in isoform 2.

VSP_015920

Alternative sequence

331 – 336

6

ESCQAI → VSLGLA in isoform 7.

VSP_015921

Alternative sequence

337 – 435

99

Missing in isoform 7.

VSP_015922

Natural variant

268

1

E → K in MPS9. Ref.10

VAR_023643

Experimental info

Sequence conflict

3

1

A → G in CAG46731. Ref.6

Sequence conflict

191

1

R → G in AAD53277. Ref.1

Sequence conflict

300

1

L → Q in AAD24460. Ref.3

Secondary structure

1

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435

Helix Strand Turn

Details...

Beta strand

24 – 27

4

Beta strand

30 – 38

9

Helix

40 – 47

8

Beta strand

56 – 59

4

Beta strand

69 – 74

6

Beta strand

78 – 80

3

Helix

97 – 99

3

Helix

102 – 116

15

Beta strand

124 – 128

5

Helix

137 – 139

3

Helix

142 – 144

3

Helix

145 – 158

14

Beta strand

159 – 161

3

Helix

164 – 193

30

Beta strand

197 – 202

6

Helix

223 – 230

8

Helix

233 – 238

6

Beta strand

240 – 243

4

Helix

250 – 252

3

Helix

258 – 275

18

Helix

300 – 304

5

Helix

307 – 312

6

Beta strand

316 – 321

6

Helix

324 – 326

3

Beta strand

327 – 329

3

Helix

330 – 342

13

Helix

344 – 362

19

Beta strand

366 – 371

6

Turn

384 – 386

3

Beta strand

387 – 391

5

Helix

393 – 395

3

Beta strand

398 – 402

5

Helix

406 – 415

10

Beta strand

416 – 420

5

Turn

426 – 429

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 2. Checksum: 9C2B2D8DB361E0BB	FASTA	435	48,368
	10 20 30 40 50 60 MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD VDVSVFDVVA 70 80 90 100 110 120 NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA SLIAHLARTF QDILAAIPAP 130 140 150 160 170 180 DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR SRALVQAQHP DWPAPQVEAV AQDQFQGAAR 190 200 210 220 230 240 AWMAGTLQLG RALRPRGLWG FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR 250 260 270 280 290 300 ALYPSIYMPA VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDTTNHFLPL 310 320 330 340 350 360 DELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQAIKEYM DTTLGPFILN VTSGALLCSQ 370 380 390 400 410 420 ALCSGHGRCV RRTSHPKALL LLNPASFSIQ LTPGGGPLSL RGALSLEDQA QMAVEFKCRC 430 YPGWQAPWCE RKSMW
	Isoform 2 (HYAl1v1) [UniParc]. Checksum: C24DAD360D9CF032	FASTA	405	45,145
	10 20 30 40 50 60 MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD VDVSVFDVVA 70 80 90 100 110 120 NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA SLIAHLARTF QDILAAIPAP 130 140 150 160 170 180 DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR SRALVQAQHP DWPAPQVEAV AQDQFQGAAR 190 200 210 220 230 240 AWMAGTLQLG RALRPRGLWG FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR 250 260 270 280 290 300 ALYPSIYMPA VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDTTNHFLPL 310 320 330 340 350 360 ESCQAIKEYM DTTLGPFILN VTSGALLCSQ ALCSGHGRCV RRTSHPKALL LLNPASFSIQ 370 380 390 400 LTPGGGPLSL RGALSLEDQA QMAVEFKCRC YPGWQAPWCE RKSMW
	Isoform 3 (HYAl1v2) [UniParc]. Checksum: 441C0DB43301E03F	FASTA	253	27,958
	10 20 30 40 50 60 MAGTLQLGRA LRPRGLWGFY GFPDCYNYDF LSPNYTGQCP SGIRAQNDQL GWLWGQSRAL 70 80 90 100 110 120 YPSIYMPAVL EGTGKSQMYV QHRVAEAFRV AVAAGDPNLP VLPYVQIFYD TTNHFLPLDE 130 140 150 160 170 180 LEHSLGESAA QGAAGVVLWV SWENTRTKES CQAIKEYMDT TLGPFILNVT SGALLCSQAL 190 200 210 220 230 240 CSGHGRCVRR TSHPKALLLL NPASFSIQLT PGGGPLSLRG ALSLEDQAQM AVEFKCRCYP 250 GWQAPWCERK SMW
	Isoform 4 (HYAl1v3) [UniParc]. Checksum: 5C1046F8199F3BFF	FASTA	209	23,338
	10 20 30 40 50 60 MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD VDVSVFDVVA 70 80 90 100 110 120 NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA SLIAHLARTF QDILAAIPAP 130 140 150 160 170 180 DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR SRALVQAQHP DWPAPQVEAV AQDQFQGAAR 190 200 AWMAGTLQLG RALRPRGLWG FYGFPDCSG
	Isoform 5 (HYAl1v4) [UniParc]. Checksum: 75F674283B175FDD	FASTA	176	19,367
	10 20 30 40 50 60 MYVQHRVAEA FRVAVAAGDP NLPVLPYVQI FYDTTNHFLP LDELEHSLGE SAAQGAAGVV 70 80 90 100 110 120 LWVSWENTRT KESCQAIKEY MDTTLGPFIL NVTSGALLCS QALCSGHGRC VRRTSHPKAL 130 140 150 160 170 LLLNPASFSI QLTPGGGPLS LRGALSLEDQ AQMAVEFKCR CYPGWQAPWC ERKSMW
	Isoform 6 (HYAl1v5) [UniParc]. Checksum: 70AD570E4305A4E8	FASTA	96	10,435
	10 20 30 40 50 60 MDTTLGPFIL NVTSGALLCS QALCSGHGRC VRRTSHPKAL LLLNPASFSI QLTPGGGPLS 70 80 90 LRGALSLEDQ AQMAVEFKCR CYPGWQAPWC ERKSMW
	Isoform 7 [UniParc]. Checksum: 7D19178001F20E51	FASTA	336	37,439
	10 20 30 40 50 60 MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD VDVSVFDVVA 70 80 90 100 110 120 NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA SLIAHLARTF QDILAAIPAP 130 140 150 160 170 180 DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR SRALVQAQHP DWPAPQVEAV AQDQFQGAAR 190 200 210 220 230 240 AWMAGTLQLG RALRPRGLWG FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR 250 260 270 280 290 300 ALYPSIYMPA VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDTTNHFLPL 310 320 330 DELEHSLGES AAQGAAGVVL WVSWENTRTK VSLGLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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; 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00168847.
IPI00170520.
IPI00170521.
IPI00170522.
IPI00170523.
IPI00178140.
IPI00654773.

PIR

JC5584.

RefSeq

NP_149349.2. NM_033159.3.
NP_695013.1. NM_153281.1.
NP_695014.1. NM_153282.2.
NP_695015.1. NM_153283.2.
NP_695017.1. NM_153285.2.

UniGene

Hs.75619.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PE4	X-ray	2.00	A	22-435	[»]

ProteinModelPortal

Q12794.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12794. 1 interaction.

Protein family/group databases

CAZy

GH56. Glycoside Hydrolase Family 56.

Polymorphism databases

DMDM

74735617.

Proteomic databases

PaxDb

Q12794.

PRIDE

Q12794.

Protocols and materials databases

DNASU

3373.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266031; ENSP00000266031; ENSG00000114378.
ENST00000320295; ENSP00000346068; ENSG00000114378.
ENST00000395143; ENSP00000378575; ENSG00000114378.
ENST00000395144; ENSP00000378576; ENSG00000114378.
ENST00000447605; ENSP00000390149; ENSG00000114378.
ENST00000457214; ENSP00000393358; ENSG00000114378.
ENST00000570958; ENSP00000459254; ENSG00000262208.
ENST00000570967; ENSP00000459311; ENSG00000262208.
ENST00000571551; ENSP00000461900; ENSG00000262208.
ENST00000572970; ENSP00000461261; ENSG00000262208.
ENST00000575445; ENSP00000460624; ENSG00000262208.
ENST00000576782; ENSP00000459906; ENSG00000262208.

GeneID

3373.

KEGG

hsa:3373.

UCSC

uc003czm.3. human.
uc003czn.3. human.
uc003czo.3. human.
uc003czq.3. human.
uc003czt.3. human.

Organism-specific databases

CTD

3373.

GeneCards

GC03M050339.

HGNC

HGNC:5320. HYAL1.

HPA

HPA002112.

MIM

601492. phenotype.
607071. gene.

neXtProt

NX_Q12794.

Orphanet

67041. Hyaluronidase deficiency.

PharmGKB

PA29571.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG77606.

HOVERGEN

HBG052053.

InParanoid

Q12794.

KO

K01197.

OMA

WVSWENT.

OrthoDB

EOG4VDPZD.

PhylomeDB

Q12794.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03763-MONOMER.

BRENDA

3.2.1.35. 2681.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q12794.

Bgee

Q12794.

Genevestigator

Q12794.

GermOnline

ENSG00000114378. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]

PANTHER

PTHR11769. PTHR11769. 1 hit.

Pfam

PF01630. Glyco_hydro_56. 1 hit.
[Graphical view]

PIRSF

PIRSF038193. Hyaluronidase. 1 hit.

PRINTS

PR00846. GLHYDRLASE56.

SMART

SM00181. EGF. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q12794.

ChEMBL

CHEMBL4528.

DrugBank

DB00070. Hyaluronidase.

EvolutionaryTrace

Q12794.

GenomeRNAi

3373.

NextBio

13338.

SOURCE

Search...

Entry information

Entry name

HYAL1_HUMAN

Accession

Primary (citable) accession number: Q12794
Secondary accession number(s): Q6FH23 , Q6PIZ6, Q7KYU2, Q7LE34, Q8NFK5, Q8NFK6, Q8NFK7, Q8NFK8, Q8NFK9, Q93013, Q9UKD5, Q9UNI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.