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O14792

- HS3S1_HUMAN

UniProt

O14792 - HS3S1_HUMAN

Protein

Heparan sulfate glucosamine 3-O-sulfotransferase 1

Gene

HS3ST1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Golgi apparatus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29467.

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    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

    1
    307
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14792.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    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

    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: October 1, 2014
    This is version 115 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