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O14792

- HS3S1_HUMAN

UniProt

O14792 - HS3S1_HUMAN

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Protein
Heparan sulfate glucosamine 3-O-sulfotransferase 1
Gene
HS3ST1, 3OST, 3OST1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471PAPS
Binding sitei155 – 1551PAPS
Binding sitei255 – 2551PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 685PAPS
Nucleotide bindingi270 – 2745PAPS

GO - Molecular functioni

  1. [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity Source: UniProtKB-EC
  2. sulfotransferase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glycosaminoglycan biosynthetic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS00082-MONOMER.
ReactomeiREACT_121248. HS-GAG biosynthesis.

Names & Taxonomyi

Protein namesi
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 namesi
Name:HS3ST1
Synonyms:3OST, 3OST1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:5194. HS3ST1.

Subcellular locationi

GO - Cellular componenti

  1. Golgi lumen Source: Reactome
  2. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29467.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 By similarity
Add
BLAST
Chaini21 – 307287Heparan sulfate glucosamine 3-O-sulfotransferase 1
PRO_0000033451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi192 – 1921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi242 – 2421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi249 – 2491N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi256 ↔ 2651 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO14792.
PRIDEiO14792.

PTM databases

PhosphoSiteiO14792.

Expressioni

Tissue specificityi

Highly expressed in the brain and kidney and weakly expressed in the heart, lung and placenta.1 Publication

Gene expression databases

ArrayExpressiO14792.
BgeeiO14792.
CleanExiHS_HS3ST1.
GenevestigatoriO14792.

Organism-specific databases

HPAiHPA002237.

Interactioni

Protein-protein interaction databases

BioGridi115282. 3 interactions.
STRINGi9606.ENSP00000002596.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 594
Helixi67 – 748
Beta strandi80 – 823
Turni89 – 913
Helixi93 – 964
Helixi99 – 1057
Beta strandi114 – 1196
Helixi121 – 1255
Helixi129 – 1368
Beta strandi141 – 1466
Helixi149 – 16618
Helixi174 – 1785
Helixi189 – 1946
Helixi196 – 2049
Helixi209 – 2113
Beta strandi212 – 2165
Helixi217 – 2226
Helixi224 – 23411
Helixi243 – 2453
Beta strandi246 – 2494
Turni250 – 2534
Beta strandi254 – 2596
Beta strandi262 – 2643
Helixi279 – 28810
Helixi290 – 30011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZRHX-ray2.10A36-307[»]
ProteinModelPortaliO14792.
SMRiO14792. Positions 45-307.

Miscellaneous databases

EvolutionaryTraceiO14792.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG282030.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiO14792.
KOiK01024.
OMAiWEEHYSQ.
OrthoDBiEOG7PS1GM.
PhylomeDBiO14792.
TreeFamiTF350755.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O14792-1 [UniParc]FASTAAdd to Basket

« Hide

MAALLLGAVL LVAQPQLVPS RPAELGQQEL LRKAGTLQDD VRDGVAPNGS    50
AQQLPQTIII GVRKGGTRAL LEMLSLHPDV AAAENEVHFF DWEEHYSHGL 100
GWYLSQMPFS WPHQLTVEKT PAYFTSPKVP ERVYSMNPSI RLLLILRDPS 150
ERVLSDYTQV FYNHMQKHKP YPSIEEFLVR DGRLNVDYKA LNRSLYHVHM 200
QNWLRFFPLR HIHIVDGDRL IRDPFPEIQK VERFLKLSPQ INASNFYFNK 250
TKGFYCLRDS GRDRCLHESK GRAHPQVDPK LLNKLHEYFH EPNKKFFELV 300
GRTFDWH 307
Length:307
Mass (Da):35,773
Last modified:January 1, 1998 - v1
Checksum:iAA1052260633EA1C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221P → T.1 Publication
Corresponds to variant rs11559238 [ dbSNP | Ensembl ].
VAR_021515
Natural varianti295 – 2951K → R.
Corresponds to variant rs34719057 [ dbSNP | Ensembl ].
VAR_052529

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF019386 mRNA. Translation: AAB84388.1.
AK096823 mRNA. Translation: BAG53368.1.
CH471069 Genomic DNA. Translation: EAW92699.1.
BC057803 mRNA. Translation: AAH57803.1.
CCDSiCCDS3408.1.
RefSeqiNP_005105.1. NM_005114.2.
XP_005248278.1. XM_005248221.2.
UniGeneiHs.507348.
Hs.605349.

Genome annotation databases

EnsembliENST00000002596; ENSP00000002596; ENSG00000002587.
GeneIDi9957.
KEGGihsa:9957.
UCSCiuc003gmq.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF019386 mRNA. Translation: AAB84388.1 .
AK096823 mRNA. Translation: BAG53368.1 .
CH471069 Genomic DNA. Translation: EAW92699.1 .
BC057803 mRNA. Translation: AAH57803.1 .
CCDSi CCDS3408.1.
RefSeqi NP_005105.1. NM_005114.2.
XP_005248278.1. XM_005248221.2.
UniGenei Hs.507348.
Hs.605349.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZRH X-ray 2.10 A 36-307 [» ]
ProteinModelPortali O14792.
SMRi O14792. Positions 45-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115282. 3 interactions.
STRINGi 9606.ENSP00000002596.

PTM databases

PhosphoSitei O14792.

Proteomic databases

PaxDbi O14792.
PRIDEi O14792.

Protocols and materials databases

DNASUi 9957.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000002596 ; ENSP00000002596 ; ENSG00000002587 .
GeneIDi 9957.
KEGGi hsa:9957.
UCSCi uc003gmq.3. human.

Organism-specific databases

CTDi 9957.
GeneCardsi GC04M011394.
H-InvDB HIX0004096.
HGNCi HGNC:5194. HS3ST1.
HPAi HPA002237.
MIMi 603244. gene.
neXtProti NX_O14792.
PharmGKBi PA29467.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282030.
HOGENOMi HOG000036663.
HOVERGENi HBG053377.
InParanoidi O14792.
KOi K01024.
OMAi WEEHYSQ.
OrthoDBi EOG7PS1GM.
PhylomeDBi O14792.
TreeFami TF350755.

Enzyme and pathway databases

BioCyci MetaCyc:HS00082-MONOMER.
Reactomei REACT_121248. HS-GAG biosynthesis.

Miscellaneous databases

ChiTaRSi HS3ST1. human.
EvolutionaryTracei O14792.
GeneWikii HS3ST1.
GenomeRNAii 9957.
NextBioi 37572.
PROi O14792.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14792.
Bgeei O14792.
CleanExi HS_HS3ST1.
Genevestigatori O14792.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view ]
Pfami PF00685. Sulfotransfer_1. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiHS3S1_HUMAN
AccessioniPrimary (citable) accession number: O14792
Secondary accession number(s): B3KUA6, Q6PEY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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