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O14792 (HS3S1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 307287Heparan sulfate glucosamine 3-O-sulfotransferase 1
PRO_0000033451

Regions

Nucleotide binding64 – 685PAPS
Nucleotide binding270 – 2745PAPS

Sites

Binding site1471PAPS
Binding site1551PAPS
Binding site2551PAPS

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Disulfide bond256 ↔ 265 Ref.8

Natural variations

Natural variant221P → T. Ref.4
Corresponds to variant rs11559238 [ dbSNP | Ensembl ].
VAR_021515
Natural variant2951K → R.
Corresponds to variant rs34719057 [ dbSNP | Ensembl ].
VAR_052529

Secondary structure

.............................................. 307
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O14792 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: AA1052260633EA1C

FASTA30735,773
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_005105.1. NM_005114.2.
XP_005248278.1. XM_005248221.2.
UniGeneHs.507348.
Hs.605349.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZRHX-ray2.10A36-307[»]
ProteinModelPortalO14792.
SMRO14792. Positions 45-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115282. 2 interactions.
STRING9606.ENSP00000002596.

PTM databases

PhosphoSiteO14792.

Proteomic databases

PaxDbO14792.
PRIDEO14792.

Protocols and materials databases

DNASU9957.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000002596; ENSP00000002596; ENSG00000002587.
GeneID9957.
KEGGhsa:9957.
UCSCuc003gmq.3. human.

Organism-specific databases

CTD9957.
GeneCardsGC04M011394.
H-InvDBHIX0004096.
HGNCHGNC:5194. HS3ST1.
HPAHPA002237.
MIM603244. gene.
neXtProtNX_O14792.
PharmGKBPA29467.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282030.
HOGENOMHOG000036663.
HOVERGENHBG053377.
InParanoidO14792.
KOK01024.
OMAFHEPNKK.
OrthoDBEOG7PS1GM.
PhylomeDBO14792.
TreeFamTF350755.

Enzyme and pathway databases

BioCycMetaCyc:HS00082-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressO14792.
BgeeO14792.
CleanExHS_HS3ST1.
GenevestigatorO14792.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSHS3ST1. human.
EvolutionaryTraceO14792.
GeneWikiHS3ST1.
GenomeRNAi9957.
NextBio37572.
PROO14792.
SOURCESearch...

Entry information

Entry nameHS3S1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM