# HAS1

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Protein-coding gene in the species Homo sapiens

HAS1 Identifiers Aliases HAS1, HAS, hyaluronan synthase 1 External IDs OMIM: 601463; MGI: 106590; HomoloGene: 1165; GeneCards: HAS1; OMA:HAS1 - orthologs Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.41 Start 51,713,112 bp[1] End 51,723,991 bp[1] Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 A3.2|17 10.53 cM Start 18,063,585 bp[2] End 18,075,467 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle parietal pleura vena cava germinal epithelium right ovary synovial joint left ovary synovial membrane pericardium middle temporal gyrus Top expressed in ankle joint ankle genital tubercle tail of embryo embryo facial motor nucleus trachea aortic valve submandibular gland ascending aorta More reference expression data BioGPS More reference expression data Gene ontology Molecular function glycosyltransferase activity transferase activity hyaluronan synthase activity protein binding identical protein binding Cellular component cytoplasm integral component of membrane plasma membrane integral component of plasma membrane membrane Biological process cell adhesion negative regulation of fibroblast migration hyaluronan biosynthetic process cellular response to platelet-derived growth factor stimulus extracellular matrix assembly glycosaminoglycan biosynthetic process extracellular polysaccharide biosynthetic process estrous cycle Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 3036 15116 Ensembl ENSG00000105509 ENSMUSG00000003665 UniProt Q92839 Q61647 RefSeq (mRNA) NM_001297436 NM_001523 NM_008215 RefSeq (protein) NP_001284365 NP_001514 NP_032241 Location (UCSC) Chr 19: 51.71 – 51.72 Mb Chr 17: 18.06 – 18.08 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**[Hyaluronan](/source/Hyaluronan) synthase 1** is an [enzyme](/source/Enzyme) that in humans is encoded by the *HAS1* [gene](/source/Gene).[5][6]

## Structure

Hyaluronan or [hyaluronic acid](/source/Hyaluronic_acid) (HA) is a high molecular weight unbranched [polysaccharide](/source/Polysaccharide) synthesized by a wide variety of organisms from bacteria to mammals, and is a constituent of the [extracellular matrix](/source/Extracellular_matrix). It consists of alternating glucuronic acid and N-acetylglucosamine residues that are linked by beta-1-3 and beta-1-4 glycosidic bonds. HA is synthesized by membrane-bound [synthase](/source/Synthase) at the inner surface of the plasma membrane, and the chains are extruded via ABC-transporter into the extracellular space.[7]

## Function

It serves a variety of functions, including space filling, lubrication of [joints](/source/Joints), and provision of a matrix through which cells can migrate. HA is actively produced during [wound healing](/source/Wound_healing) and tissue repair to provide a framework for ingrowth of blood vessels and [fibroblasts](/source/Fibroblasts). Changes in the serum concentration of HA are associated with inflammatory and degenerative [arthropathies](/source/Arthropathies) such as [rheumatoid arthritis](/source/Rheumatoid_arthritis). In addition, the interaction of HA with the leukocyte receptor [CD44](/source/CD44) is important in tissue-specific homing by [leukocytes](/source/Leukocytes), and overexpression of HA receptors has been correlated with tumor [metastasis](/source/Metastasis). HAS1 is a member of the newly identified vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant [homology](/source/Homology_(biology)) to the hasA gene product of [Streptococcus pyogenes](/source/Streptococcus_pyogenes), a [glycosaminoglycan](/source/Glycosaminoglycan) synthetase (DG42) from *[Xenopus laevis](/source/Xenopus_laevis)*, and a recently described murine hyaluronan synthase.[6]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000105509](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000105509) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000003665](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000003665) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=3036). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=15116). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid9169154_5-0)** Spicer AP, Seldin MF, Olsen AS, Brown N, Wells DE, Doggett NA, Itano N, Kimata K, Inazawa J, McDonald JA (Jul 1997). "Chromosomal localization of the human and mouse hyaluronan synthase genes". *Genomics*. **41** (3): 493–7. [doi](/source/Doi_(identifier)):[10.1006/geno.1997.4696](https://doi.org/10.1006%2Fgeno.1997.4696). [PMID](/source/PMID_(identifier)) [9169154](https://pubmed.ncbi.nlm.nih.gov/9169154).

1. ^ [***a***](#cite_ref-entrez_6-0) [***b***](#cite_ref-entrez_6-1) ["Entrez Gene: HAS1 hyaluronan synthase 1"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3036).

1. **[^](#cite_ref-pmid17540771_7-0)** Schulz T, Schumacher U, Prehm P (July 2007). ["Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP"](https://doi.org/10.1074%2Fjbc.M700915200). *J. Biol. Chem*. **282** (29): 20999–1004. [doi](/source/Doi_(identifier)):[10.1074/jbc.M700915200](https://doi.org/10.1074%2Fjbc.M700915200). [PMID](/source/PMID_(identifier)) [17540771](https://pubmed.ncbi.nlm.nih.gov/17540771).

## Further reading

- Spicer AP, Nguyen TK (1999). "Mammalian hyaluronan synthases: investigation of functional relationships in vivo". *Biochem. Soc. Trans*. **27** (2): 109–15. [doi](/source/Doi_(identifier)):[10.1042/bst0270109](https://doi.org/10.1042%2Fbst0270109). [PMID](/source/PMID_(identifier)) [10093717](https://pubmed.ncbi.nlm.nih.gov/10093717).

- Mian N (1987). ["Analysis of cell-growth-phase-related variations in hyaluronate synthase activity of isolated plasma-membrane fractions of cultured human skin fibroblasts"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1146992). *Biochem. J*. **237** (2): 333–42. [doi](/source/Doi_(identifier)):[10.1042/bj2370333](https://doi.org/10.1042%2Fbj2370333). [PMC](/source/PMC_(identifier)) [1146992](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1146992). [PMID](/source/PMID_(identifier)) [3099751](https://pubmed.ncbi.nlm.nih.gov/3099751).

- Itano N, Kimata K (1996). "Molecular cloning of human hyaluronan synthase". *Biochem. Biophys. Res. Commun*. **222** (3): 816–20. [Bibcode](/source/Bibcode_(identifier)):[1996BBRC..222..816I](https://ui.adsabs.harvard.edu/abs/1996BBRC..222..816I). [doi](/source/Doi_(identifier)):[10.1006/bbrc.1996.0827](https://doi.org/10.1006%2Fbbrc.1996.0827). [PMID](/source/PMID_(identifier)) [8651928](https://pubmed.ncbi.nlm.nih.gov/8651928).

- Shyjan AM, Heldin P, Butcher EC, et al. (1996). ["Functional cloning of the cDNA for a human hyaluronan synthase"](https://doi.org/10.1074%2Fjbc.271.38.23395). *J. Biol. Chem*. **271** (38): 23395–9. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.38.23395](https://doi.org/10.1074%2Fjbc.271.38.23395). [PMID](/source/PMID_(identifier)) [8798544](https://pubmed.ncbi.nlm.nih.gov/8798544).

- Simpson MA, Wilson CM, Furcht LT, et al. (2002). ["Manipulation of hyaluronan synthase expression in prostate adenocarcinoma cells alters pericellular matrix retention and adhesion to bone marrow endothelial cells"](https://doi.org/10.1074%2Fjbc.M110069200). *J. Biol. Chem*. **277** (12): 10050–7. [doi](/source/Doi_(identifier)):[10.1074/jbc.M110069200](https://doi.org/10.1074%2Fjbc.M110069200). [PMID](/source/PMID_(identifier)) [11790779](https://pubmed.ncbi.nlm.nih.gov/11790779).

- Calabro A, Oken MM, Hascall VC, Masellis AM (2002). ["Characterization of hyaluronan synthase expression and hyaluronan synthesis in bone marrow mesenchymal progenitor cells: predominant expression of HAS1 mRNA and up-regulated hyaluronan synthesis in bone marrow cells derived from multiple myeloma patients"](https://doi.org/10.1182%2Fblood-2002-01-0030). *Blood*. **100** (7): 2578–85. [doi](/source/Doi_(identifier)):[10.1182/blood-2002-01-0030](https://doi.org/10.1182%2Fblood-2002-01-0030). [PMID](/source/PMID_(identifier)) [12239172](https://pubmed.ncbi.nlm.nih.gov/12239172).

- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). ["Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). *Proc. Natl. Acad. Sci. U.S.A*. **99** (26): 16899–903. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...9916899M](https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M). [doi](/source/Doi_(identifier)):[10.1073/pnas.242603899](https://doi.org/10.1073%2Fpnas.242603899). [PMC](/source/PMC_(identifier)) [139241](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). [PMID](/source/PMID_(identifier)) [12477932](https://pubmed.ncbi.nlm.nih.gov/12477932).

- Adamia S, Crainie M, Kriangkum J, et al. (2003). "Abnormal expression of hyaluronan synthases in patients with Waldenstrom's macroglobulimenia". *Semin. Oncol*. **30** (2): 165–8. [doi](/source/Doi_(identifier)):[10.1053/sonc.2003.50042](https://doi.org/10.1053%2Fsonc.2003.50042). [PMID](/source/PMID_(identifier)) [12720129](https://pubmed.ncbi.nlm.nih.gov/12720129).

- Suzuki K, Yamamoto T, Usui T, et al. (2004). "Expression of hyaluronan synthase in intraocular proliferative diseases: regulation of expression in human vascular endothelial cells by transforming growth factor-beta". *Jpn. J. Ophthalmol*. **47** (6): 557–64. [doi](/source/Doi_(identifier)):[10.1016/j.jjo.2003.09.001](https://doi.org/10.1016%2Fj.jjo.2003.09.001). [PMID](/source/PMID_(identifier)) [14636845](https://pubmed.ncbi.nlm.nih.gov/14636845).

- Adamia S, Reiman T, Crainie M, et al. (2005). ["Intronic splicing of hyaluronan synthase 1 (HAS1): a biologically relevant indicator of poor outcome in multiple myeloma"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1894997). *Blood*. **105** (12): 4836–44. [doi](/source/Doi_(identifier)):[10.1182/blood-2004-10-3825](https://doi.org/10.1182%2Fblood-2004-10-3825). [PMC](/source/PMC_(identifier)) [1894997](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1894997). [PMID](/source/PMID_(identifier)) [15731173](https://pubmed.ncbi.nlm.nih.gov/15731173).

- Yabushita H, Kishida T, Fusano K, et al. (2005). "Role of hyaluronan and hyaluronan synthase in endometrial cancer". *Oncol. Rep*. **13** (6): 1101–5. [doi](/source/Doi_(identifier)):[10.3892/or.13.6.1101](https://doi.org/10.3892%2For.13.6.1101). [PMID](/source/PMID_(identifier)) [15870928](https://pubmed.ncbi.nlm.nih.gov/15870928).

- Stuhlmeier KM, Pollaschek C (2006). ["Adenovirus-mediated gene transfer of mutated IkappaB kinase and IkappaBalpha reveal NF-kappaB-dependent as well as NF-kappaB-independent pathways of HAS1 activation"](https://doi.org/10.1074%2Fjbc.M503374200). *J. Biol. Chem*. **280** (52): 42766–73. [doi](/source/Doi_(identifier)):[10.1074/jbc.M503374200](https://doi.org/10.1074%2Fjbc.M503374200). [PMID](/source/PMID_(identifier)) [16258173](https://pubmed.ncbi.nlm.nih.gov/16258173).

- Grskovic B, Pollaschek C, Mueller MM, Stuhlmeier KM (2006). "Expression of hyaluronan synthase genes in umbilical cord blood stem/progenitor cells". *Biochim. Biophys. Acta*. **1760** (6): 890–5. [doi](/source/Doi_(identifier)):[10.1016/j.bbagen.2006.02.002](https://doi.org/10.1016%2Fj.bbagen.2006.02.002). [PMID](/source/PMID_(identifier)) [16564133](https://pubmed.ncbi.nlm.nih.gov/16564133).

- Kao JJ (2007). "The NF-kappaB inhibitor pyrrolidine dithiocarbamate blocks IL-1beta induced hyaluronan synthase 1 (HAS1) mRNA transcription, pointing at NF-kappaB dependence of the gene HAS1". *Exp. Gerontol*. **41** (6): 641–7. [doi](/source/Doi_(identifier)):[10.1016/j.exger.2006.04.003](https://doi.org/10.1016%2Fj.exger.2006.04.003). [PMID](/source/PMID_(identifier)) [16723203](https://pubmed.ncbi.nlm.nih.gov/16723203). [S2CID](/source/S2CID_(identifier)) [54406345](https://api.semanticscholar.org/CorpusID:54406345).

- Campo GM, Avenoso A, Campo S, et al. (2007). "TNF-alpha, IFN-gamma, and IL-1beta modulate hyaluronan synthase expression in human skin fibroblasts: synergistic effect by concomital treatment with FeSO4 plus ascorbate". *Mol. Cell. Biochem*. **292** (1–2): 169–78. [doi](/source/Doi_(identifier)):[10.1007/s11010-006-9230-7](https://doi.org/10.1007%2Fs11010-006-9230-7). [PMID](/source/PMID_(identifier)) [16786194](https://pubmed.ncbi.nlm.nih.gov/16786194). [S2CID](/source/S2CID_(identifier)) [37598580](https://api.semanticscholar.org/CorpusID:37598580).

- Ewing RM, Chu P, Elisma F, et al. (2007). ["Large-scale mapping of human protein-protein interactions by mass spectrometry"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1847948). *Mol. Syst. Biol*. **3** (1) 89. [doi](/source/Doi_(identifier)):[10.1038/msb4100134](https://doi.org/10.1038%2Fmsb4100134). [PMC](/source/PMC_(identifier)) [1847948](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1847948). [PMID](/source/PMID_(identifier)) [17353931](https://pubmed.ncbi.nlm.nih.gov/17353931).

- Meran S, Thomas D, Stephens P, et al. (2007). ["Involvement of hyaluronan in regulation of fibroblast phenotype"](https://doi.org/10.1074%2Fjbc.M700773200). *J. Biol. Chem*. **282** (35): 25687–97. [doi](/source/Doi_(identifier)):[10.1074/jbc.M700773200](https://doi.org/10.1074%2Fjbc.M700773200). [PMID](/source/PMID_(identifier)) [17611197](https://pubmed.ncbi.nlm.nih.gov/17611197).

- Kyossev Z, Weigel PH (2007). "An enzyme capture assay for analysis of active hyaluronan synthases". *Anal. Biochem*. **371** (1): 62–70. [doi](/source/Doi_(identifier)):[10.1016/j.ab.2007.08.025](https://doi.org/10.1016%2Fj.ab.2007.08.025). [PMID](/source/PMID_(identifier)) [17904513](https://pubmed.ncbi.nlm.nih.gov/17904513).

v t e Transferases: glycosyltransferases (EC 2.4) 2.4.1: Hexosyl- transferases Glucosyl- Phosphorylase Starch Glycogen Cellobiose Myo- Glycogen synthase Debranching enzyme Branching enzyme 1,3-Beta-glucan synthase Ceramide glucosyltransferase N-glycosyltransferase Galactosyl- Lactose synthase B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1) Glucuronosyl- B3GAT1 B3GAT2 B3GAT3 UGT1A1 UGT1A3 UGT1A4 UGT1A5 UGT1A6 UGT1A7 UGT1A8 UGT1A9 UGT1A10 UGT2A1 UGT2A2 UGT2A3 UGT2B4 UGT2B7 UGT2B10 UGT2B11 UGT2B15 UGT2B17 UGT2B28 Hyaluronan synthase: HAS1 HAS2 HAS3 Fucosyl- POFUT1 POFUT2 FUT1 FUT2 FUT3 FUT4 FUT5 FUT6 FUT7 FUT8 FUT9 FUT10 FUT11 Mannosyl- Dolichyl-phosphate-mannose-protein mannosyltransferase POMT1 POMT2 DPM1 DPM3 ALG1 ALG2 ALG3 ALG6 ALG8 ALG9 ALG12 2.4.2: Pentosyl- transferases Ribose ADP-ribosyltransferase NAD+:diphthamide ADP-ribosyltransferase Diphtheria toxin Pseudomonas exotoxin NAD(P)+:arginine ADP-ribosyltransferase Pertussis toxin Cholera toxin Poly ADP ribose polymerase Sirtuin Phosphoribosyltransferase Adenine phosphoribosyltransferase Hypoxanthine-guanine phosphoribosyltransferase Uracil phosphoribosyltransferase Amidophosphoribosyltransferase Other Purine nucleoside phosphorylase: Thymidine phosphorylase TYMP Other Xylosyltransferase XYLT1 XYLT2 Arabinosyltransferase Indolylacetylinositol arabinosyltransferase 2.4.99: Sialyl transferases Beta-galactoside alpha-2,6-sialyltransferase Monosialoganglioside sialyltransferase ST8SIA4

v t e Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics Types EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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Adapted from the Wikipedia article [HAS1](https://en.wikipedia.org/wiki/HAS1) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/HAS1?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.