HS3ST3A1

Protein-coding gene in the species Homo sapiens

HS3ST3A1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1T8T, 1T8U

Identifiers

Aliases

HS3ST3A1, 30ST3A1, 3OST3A1, 3-OST-3A, heparan sulfate-glucosamine 3-sulfotransferase 3A1

External IDs

OMIM: 604057; MGI: 1333861; HomoloGene: 88735; GeneCards: HS3ST3A1; OMA:HS3ST3A1 - orthologs

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17p12	Start	13,494,032 bp^[1]
Band	17p12	End	13,601,929 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11 B3\|11 40.24 cM	Start	64,326,158 bp^[2]
Band	11 B3\|11 40.24 cM	End	64,413,667 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

cartilage tissue

testicle

tibia

gingival epithelium

oral cavity

glomerulus

metanephric glomerulus

seminal vesicula

stromal cell of endometrium

germinal epithelium

Top expressed in

metatarsal bones

condyle

second metatarsal bone

fifth metatarsal bone

iris

footplate

Gonadal ridge

third metatarsal bone

ciliary body

renal corpuscle

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity sulfotransferase activity [heparan sulfate-glucosamine 3-sulfotransferase 3 activity] [heparan sulfate-glucosamine 3-sulfotransferase 1 activity] heparan sulfate sulfotransferase activity
Cellular component	integral component of membrane Golgi membrane Golgi apparatus membrane
Biological process	glycosaminoglycan biosynthetic process heparan sulfate proteoglycan biosynthetic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


9955


15478

Ensembl


ENSG00000153976


ENSMUSG00000047759

UniProt


Q9Y663


Q8BKN6

RefSeq (mRNA)


NM_006042


NM_178870

RefSeq (protein)


NP_006033


NP_849201

Location (UCSC)

Chr 17: 13.49 – 13.6 Mb

Chr 11: 64.33 – 64.41 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene.^[5]^[6]

Heparan sulfate biosynthetic enzymes are key components in generating myriad distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family.

It is a type II integral membrane protein and possesses heparan sulfate glucosaminyl 3-O-sulfotransferase activity. The sulfotransferase domain of this enzyme is highly similar to the same domain of heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1, and these two enzymes sulfate an identical disaccharide. This gene is widely expressed, with the most abundant expression in the liver and placenta.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000153976 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000047759 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD (Mar 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". J Biol Chem. 274 (8): 5170–84. doi:10.1074/jbc.274.8.5170. PMID 9988767.
^ ^a ^b "Entrez Gene: HS3ST3A1 heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1".

Razi N, Lindahl U (1995). "Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides". J. Biol. Chem. 270 (19): 11267–75. doi:10.1074/jbc.270.19.11267. PMID 7744762.
Liu J, Shworak NW, Sinaÿ P, et al. (1999). "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities". J. Biol. Chem. 274 (8): 5185–92. doi:10.1074/jbc.274.8.5185. PMID 9988768.
Shukla D, Liu J, Blaiklock P, et al. (1999). "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry". Cell. 99 (1): 13–22. doi:10.1016/S0092-8674(00)80058-6. PMID 10520990. S2CID 14139940.
Liu J, Shriver Z, Blaiklock P, et al. (2000). "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues". J. Biol. Chem. 274 (53): 38155–62. doi:10.1074/jbc.274.53.38155. PMID 10608887.
Salehi LB, Mangino M, De Serio S, et al. (2002). "Assignment of a locus for autosomal dominant idiopathic scoliosis (IS) to human chromosome 17p11". Hum. Genet. 111 (4–5): 401–4. doi:10.1007/s00439-002-0785-4. PMID 12384783. S2CID 29912776.
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". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
Moon AF, Edavettal SC, Krahn JM, et al. (2004). "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1". J. Biol. Chem. 279 (43): 45185–93. doi:10.1074/jbc.M405013200. PMC 4114238. PMID 15304505.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

PDB gallery

1t8t: Crystal Structure of human 3-O-Sulfotransferase-3 with bound PAP
1t8u: Crystal Structure of human 3-O-Sulfotransferase-3 with bound PAP and tetrasaccharide substrate