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Q8IZT8

- HS3S5_HUMAN

UniProt

Q8IZT8 - HS3S5_HUMAN

Protein

Heparan sulfate glucosamine 3-O-sulfotransferase 5

Gene

HS3ST5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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. Also generates GlcUA-GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry.1 Publication

    Catalytic activityi

    3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei183 – 1831PAPSBy similarity
    Binding sitei191 – 1911PAPSBy similarity
    Binding sitei293 – 2931PAPSBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi100 – 1045PAPSBy similarity
    Nucleotide bindingi309 – 3135PAPSBy similarity

    GO - Molecular functioni

    1. [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity Source: UniProtKB
    2. 3'-phosphoadenosine 5'-phosphosulfate binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glycosaminoglycan biosynthetic process Source: Reactome
    3. glycosaminoglycan metabolic process Source: Reactome
    4. heparan sulfate proteoglycan biosynthetic process, enzymatic modification Source: UniProtKB
    5. negative regulation of coagulation Source: UniProtKB
    6. protein sulfation Source: UniProtKB
    7. regulation of viral entry into host cell Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_121248. HS-GAG biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heparan sulfate glucosamine 3-O-sulfotransferase 5 (EC:2.8.2.23)
    Alternative name(s):
    Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5
    Short name:
    3-OST-5
    Short name:
    Heparan sulfate 3-O-sulfotransferase 5
    Short name:
    h3-OST-5
    Gene namesi
    Name:HS3ST5
    Synonyms:3OST5, HS3OST5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:19419. HS3ST5.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991R → A: Reduces enzyme activity by over 99%. 1 Publication
    Mutagenesisi104 – 1041R → A: Reduces enzyme activity by 93%,. 1 Publication
    Mutagenesisi155 – 1551K → A: Reduces enzyme activity by over 99%. 1 Publication
    Mutagenesisi195 – 1951Q → A: Reduces enzyme activity by over 99%. 1 Publication
    Mutagenesisi309 – 3091K → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi311 – 3111R → A: Reduces enzyme activity by 98%. 1 Publication

    Organism-specific databases

    PharmGKBiPA164741639.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 346346Heparan sulfate glucosamine 3-O-sulfotransferase 5PRO_0000085222Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi294 ↔ 304By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8IZT8.
    PeptideAtlasiQ8IZT8.
    PRIDEiQ8IZT8.

    PTM databases

    PhosphoSiteiQ8IZT8.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle and fetal brain, and also found in adult brain, spinal cord, cerebellum and colon.2 Publications

    Gene expression databases

    BgeeiQ8IZT8.
    CleanExiHS_HS3ST5.
    GenevestigatoriQ8IZT8.

    Organism-specific databases

    HPAiHPA021823.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000387653.

    Structurei

    Secondary structure

    1
    346
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 976
    Helixi103 – 1108
    Beta strandi116 – 1183
    Helixi129 – 1335
    Helixi136 – 1405
    Beta strandi151 – 1555
    Helixi157 – 1604
    Helixi165 – 1728
    Beta strandi177 – 1826
    Helixi185 – 20218
    Helixi210 – 2145
    Turni217 – 2193
    Helixi227 – 2315
    Helixi234 – 2429
    Helixi247 – 2493
    Beta strandi250 – 2545
    Helixi255 – 2606
    Helixi262 – 27211
    Helixi281 – 2833
    Beta strandi284 – 2874
    Turni288 – 2914
    Beta strandi292 – 2965
    Beta strandi298 – 3003
    Helixi318 – 33922

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BD9X-ray2.30A88-346[»]
    ProteinModelPortaliQ8IZT8.
    SMRiQ8IZT8. Positions 87-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IZT8.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini33 – 346314LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 1287Substrate bindingBy similarity
    Regioni155 – 1584Substrate bindingBy similarity
    Regioni226 – 2272Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG282030.
    HOGENOMiHOG000036663.
    HOVERGENiHBG053377.
    InParanoidiQ8IZT8.
    KOiK08104.
    OMAiGRTFNWP.
    OrthoDBiEOG7PS1GM.
    PhylomeDBiQ8IZT8.
    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.

    Q8IZT8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLFKQQAWLR QKLLVLGSLA VGSLLYLVAR VGSLDRLQPI CPIEGRLGGA    50
    RTQAEFPLRA LQFKRGLLHE FRKGNASKEQ VRLHDLVQQL PKAIIIGVRK 100
    GGTRALLEML NLHPAVVKAS QEIHFFDNDE NYGKGIEWYR KKMPFSYPQQ 150
    ITIEKSPAYF ITEEVPERIY KMNSSIKLLI IVREPTTRAI SDYTQVLEGK 200
    ERKNKTYYKF EKLAIDPNTC EVNTKYKAVR TSIYTKHLER WLKYFPIEQF 250
    HVVDGDRLIT EPLPELQLVE KFLNLPPRIS QYNLYFNATR GFYCLRFNII 300
    FNKCLAGSKG RIHPEVDPSV ITKLRKFFHP FNQKFYQITG RTLNWP 346
    Length:346
    Mass (Da):40,408
    Last modified:March 1, 2003 - v1
    Checksum:iC763F70793FDB156
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti247 – 2471I → N.
    Corresponds to variant rs17793043 [ dbSNP | Ensembl ].
    VAR_052531

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF503292 mRNA. Translation: AAN37737.1.
    AK091074 mRNA. No translation available.
    AK289907 mRNA. Translation: BAF82596.1.
    CH471051 Genomic DNA. Translation: EAW48251.1.
    BC093911 mRNA. Translation: AAH93911.1.
    BC093913 mRNA. Translation: AAH93913.1.
    CCDSiCCDS34517.1.
    RefSeqiNP_705840.2. NM_153612.3.
    XP_006715442.1. XM_006715379.1.
    UniGeneiHs.645477.

    Genome annotation databases

    EnsembliENST00000312719; ENSP00000427888; ENSG00000249853.
    ENST00000411826; ENSP00000440332; ENSG00000249853.
    GeneIDi222537.
    KEGGihsa:222537.
    UCSCiuc003pwg.4. human.

    Polymorphism databases

    DMDMi61214369.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF503292 mRNA. Translation: AAN37737.1 .
    AK091074 mRNA. No translation available.
    AK289907 mRNA. Translation: BAF82596.1 .
    CH471051 Genomic DNA. Translation: EAW48251.1 .
    BC093911 mRNA. Translation: AAH93911.1 .
    BC093913 mRNA. Translation: AAH93913.1 .
    CCDSi CCDS34517.1.
    RefSeqi NP_705840.2. NM_153612.3.
    XP_006715442.1. XM_006715379.1.
    UniGenei Hs.645477.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BD9 X-ray 2.30 A 88-346 [» ]
    ProteinModelPortali Q8IZT8.
    SMRi Q8IZT8. Positions 87-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000387653.

    PTM databases

    PhosphoSitei Q8IZT8.

    Polymorphism databases

    DMDMi 61214369.

    Proteomic databases

    PaxDbi Q8IZT8.
    PeptideAtlasi Q8IZT8.
    PRIDEi Q8IZT8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312719 ; ENSP00000427888 ; ENSG00000249853 .
    ENST00000411826 ; ENSP00000440332 ; ENSG00000249853 .
    GeneIDi 222537.
    KEGGi hsa:222537.
    UCSCi uc003pwg.4. human.

    Organism-specific databases

    CTDi 222537.
    GeneCardsi GC06M114376.
    HGNCi HGNC:19419. HS3ST5.
    HPAi HPA021823.
    MIMi 609407. gene.
    neXtProti NX_Q8IZT8.
    PharmGKBi PA164741639.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282030.
    HOGENOMi HOG000036663.
    HOVERGENi HBG053377.
    InParanoidi Q8IZT8.
    KOi K08104.
    OMAi GRTFNWP.
    OrthoDBi EOG7PS1GM.
    PhylomeDBi Q8IZT8.
    TreeFami TF350755.

    Enzyme and pathway databases

    Reactomei REACT_121248. HS-GAG biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei Q8IZT8.
    GenomeRNAii 222537.
    NextBioi 91615.
    PROi Q8IZT8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8IZT8.
    CleanExi HS_HS3ST5.
    Genevestigatori Q8IZT8.

    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. "Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1."
      Xia G., Chen J., Tiwari V., Ju W., Li J.-P., Malmstroem A., Shukla D., Liu J.
      J. Biol. Chem. 277:37912-37919(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION, FUNCTION IN HSV-1 ENTRY.
      Tissue: Placenta.
    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: Caudate nucleus and Corpus callosum.
    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].
      Tissue: Brain.
    5. "Characterization of a heparan sulfate 3-O-sulfotransferase-5, an enzyme synthesizing a tetrasulfated disaccharide."
      Mochizuki H., Yoshida K., Gotoh M., Sugioka S., Kikuchi N., Kwon Y.-D., Tawada A., Maeyama K., Inaba N., Hiruma T., Kimata K., Narimatsu H.
      J. Biol. Chem. 278:26780-26787(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
    6. "The biosynthesis of anticoagulant heparan sulfate by the heparan sulfate 3-O-sulfotransferase isoform 5."
      Duncan M.B., Chen J., Krise J.P., Liu J.
      Biochim. Biophys. Acta 1671:34-43(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Engineering sulfotransferases to modify heparan sulfate."
      Xu D., Moon A.F., Song D., Pedersen L.C., Liu J.
      Nat. Chem. Biol. 4:200-202(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-346 IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-99; ARG-104; LYS-155; GLN-195; LYS-309 AND ARG-311.

    Entry informationi

    Entry nameiHS3S5_HUMAN
    AccessioniPrimary (citable) accession number: Q8IZT8
    Secondary accession number(s): A8K1J2, Q52LI2, Q8N285
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 106 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 6
      Human chromosome 6: 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