O14792 (HS3S1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heparan sulfate glucosamine 3-O-sulfotransferase 1
EC=2.8.2.23

Alternative name(s):
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1
Short name=3-OST-1
Short name=Heparan sulfate 3-O-sulfotransferase 1
Short name=h3-OST-1

Gene names

Name:	HS3ST1
Synonyms:	3OST, 3OST1

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	307 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	Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Ref.1
Catalytic activity	3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Subcellular location	Golgi apparatus lumen Probable.
Tissue specificity	Highly expressed in the brain and kidney and weakly expressed in the heart, lung and placenta. Ref.7
Sequence similarities	Belongs to the sulfotransferase 1 family.

Ontologies

Keywords
Cellular component	Golgi apparatus
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Transferase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome glycosaminoglycan biosynthetic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome integral to membrane Traceable author statement Ref.7. Source: ProtInc
Molecular_function	[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity Inferred from electronic annotation. Source: EC sulfotransferase activity Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

By similarity

Chain

21 – 307

287

Heparan sulfate glucosamine 3-O-sulfotransferase 1

PRO_0000033451

Regions

Nucleotide binding

64 – 68

5

PAPS

Nucleotide binding

270 – 274

5

PAPS

Sites

Binding site

147

1

PAPS

Binding site

155

1

PAPS

Binding site

255

1

PAPS

Amino acid modifications

Glycosylation

48

1

N-linked (GlcNAc...) Potential

Glycosylation

192

1

N-linked (GlcNAc...) Potential

Glycosylation

242

1

N-linked (GlcNAc...) Potential

Glycosylation

249

1

N-linked (GlcNAc...) Potential

Disulfide bond

256 ↔ 265

Ref.8

Natural variations

Natural variant

22

1

P → T. Ref.4
Corresponds to variant rs11559238 [ dbSNP | Ensembl ].

VAR_021515

Natural variant

295

1

K → R.
Corresponds to variant rs34719057 [ dbSNP | Ensembl ].

VAR_052529

Secondary structure

1

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307

Helix Strand Turn

Details...

Beta strand

56 – 59

4

Helix

67 – 74

8

Beta strand

80 – 82

3

Turn

89 – 91

3

Helix

93 – 96

4

Helix

99 – 105

7

Beta strand

114 – 119

6

Helix

121 – 125

5

Helix

129 – 136

8

Beta strand

141 – 146

6

Helix

149 – 166

18

Helix

174 – 178

5

Helix

189 – 194

6

Helix

196 – 204

9

Helix

209 – 211

3

Beta strand

212 – 216

5

Helix

217 – 222

6

Helix

224 – 234

11

Helix

243 – 245

3

Beta strand

246 – 249

4

Turn

250 – 253

4

Beta strand

254 – 259

6

Beta strand

262 – 264

3

Helix

279 – 288

10

Helix

290 – 300

11

Sequences

	Sequence		Length	Mass (Da)
	O14792 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: AA1052260633EA1C	FASTA	307	35,773
	10 20 30 40 50 60 MAALLLGAVL LVAQPQLVPS RPAELGQQEL LRKAGTLQDD VRDGVAPNGS AQQLPQTIII 70 80 90 100 110 120 GVRKGGTRAL LEMLSLHPDV AAAENEVHFF DWEEHYSHGL GWYLSQMPFS WPHQLTVEKT 130 140 150 160 170 180 PAYFTSPKVP ERVYSMNPSI RLLLILRDPS ERVLSDYTQV FYNHMQKHKP YPSIEEFLVR 190 200 210 220 230 240 DGRLNVDYKA LNRSLYHVHM QNWLRFFPLR HIHIVDGDRL IRDPFPEIQK VERFLKLSPQ 250 260 270 280 290 300 INASNFYFNK TKGFYCLRDS GRDRCLHESK GRAHPQVDPK LLNKLHEYFH EPNKKFFELV GRTFDWH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase." Shworak N.W., Liu J., Fritze L.M.S., Schwartz J.J., Zhang L., Logeart D., Rosenberg R.D. J. Biol. Chem. 272:28008-28019(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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], VARIANT THR-22. Tissue: Brain.
[5]	"Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase." Liu J., Shworak N.W., Fritze L.M., Edelberg J.M., Rosenberg R.D. J. Biol. Chem. 271:27072-27082(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities." Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L., Fritze L.M.S., Rosenberg R.D. J. Biol. Chem. 274:5185-5192(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cDNAs and identification of distinct genomic loci." Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M., Copeland N.G., Jenkins N.A., Rosenberg R.D. J. Biol. Chem. 274:5170-5184(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Crystal structure of human heparan sulfate glucosamine 3-o-sulfotransferase 1 in complex with PAP." Structural genomics consortium (SGC) Submitted (JUN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-307 IN COMPLEX WITH SUBSTRATE ANALOG, DISULFIDE BOND, BINDING SITES.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF019386 mRNA. Translation: AAB84388.1.
AK096823 mRNA. Translation: BAG53368.1.
CH471069 Genomic DNA. Translation: EAW92699.1.
BC057803 mRNA. Translation: AAH57803.1.

IPI

IPI00021377.

RefSeq

NP_005105.1. NM_005114.2.

UniGene

Hs.507348.
Hs.605349.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZRH	X-ray	2.10	A	36-307	[»]

ProteinModelPortal

O14792.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000002596.

PTM databases

PhosphoSite

O14792.

Proteomic databases

PaxDb

O14792.

PRIDE

O14792.

Protocols and materials databases

DNASU

9957.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000002596; ENSP00000002596; ENSG00000002587.

GeneID

9957.

KEGG

hsa:9957.

UCSC

uc003gmq.3. human.

Organism-specific databases

CTD

9957.

GeneCards

GC04M011394.

H-InvDB

HIX0004096.

HGNC

HGNC:5194. HS3ST1.

HPA

HPA002237.

MIM

603244. gene.

neXtProt

NX_O14792.

PharmGKB

PA29467.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282030.

HOGENOM

HOG000036663.

HOVERGEN

HBG053377.

InParanoid

O14792.

KO

K01024.

OMA

GRTFDWH.

OrthoDB

EOG4M65J5.

PhylomeDB

O14792.

Enzyme and pathway databases

BioCyc

MetaCyc:HS00082-MONOMER.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

O14792.

Bgee

O14792.

CleanEx

HS_HS3ST1.

Genevestigator

O14792.

GermOnline

ENSG00000002587. Homo sapiens.

Family and domain databases

InterPro

IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HS3ST1. human.

EvolutionaryTrace

O14792.

GenomeRNAi

9957.

NextBio

37572.

SOURCE

Search...

Entry information

Entry name

HS3S1_HUMAN

Accession

Primary (citable) accession number: O14792
Secondary accession number(s): B3KUA6, Q6PEY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 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.