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Q9Y663

- HS3SA_HUMAN

UniProt

Q9Y663 - HS3SA_HUMAN

Protein

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1

Gene

HS3ST3A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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 an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in 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. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.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 sitei166 – 1661Substrate
    Binding sitei243 – 2431PAPS
    Binding sitei251 – 2511PAPS

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi162 – 1665PAPS
    Nucleotide bindingi368 – 3725PAPS

    GO - Molecular functioni

    1. [heparan sulfate]-glucosamine 3-sulfotransferase 3 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:HS07937-MONOMER.
    ReactomeiREACT_121248. HS-GAG biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 (EC:2.8.2.30)
    Alternative name(s):
    Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1
    Short name:
    3-OST-3A
    Short name:
    Heparan sulfate 3-O-sulfotransferase 3A1
    Short name:
    h3-OST-3A
    Gene namesi
    Name:HS3ST3A1
    Synonyms:3OST3A1, HS3ST3A
    ORF Names:UNQ2551/PRO6180
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:5196. HS3ST3A1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611K → A: 99.6% loss of enzymatic activity. 1 Publication
    Mutagenesisi162 – 1621K → A: 99.6% loss of enzymatic activity; no HSV1 entry activity. 2 Publications
    Mutagenesisi166 – 1661R → E: 99.8% loss of enzymatic activity. 1 Publication
    Mutagenesisi170 – 1701E → Q: 17% loss of enzymatic activity. 1 Publication
    Mutagenesisi173 – 1731R → S: 44.1% loss of enzymatic activity. 1 Publication
    Mutagenesisi182 – 1821G → A: No effect on enzymatic activity. 1 Publication
    Mutagenesisi184 – 1841E → Q: 99.9% loss of enzymatic activity. 1 Publication
    Mutagenesisi186 – 1861H → F: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi189 – 1891D → N: 99.1% loss of enzymatic activity. 1 Publication
    Mutagenesisi190 – 1901R → E: 32% loss of enzymatic activity. 1 Publication
    Mutagenesisi194 – 1941K → A: 99.5% loss of enzymatic activity. 1 Publication
    Mutagenesisi215 – 2151K → A: 99.9% loss of enzymatic activity. 1 Publication
    Mutagenesisi218 – 2181S → A: 23.3% loss of enzymatic activity. 1 Publication
    Mutagenesisi224 – 2241E → Q: 47.6% loss of enzymatic activity. 1 Publication
    Mutagenesisi255 – 2551Q → A: 99.6% loss of enzymatic activity. 1 Publication
    Mutagenesisi259 – 2591K → A: 48.3% loss of enzymatic activity. 1 Publication
    Mutagenesisi288 – 2881I → A: 65% loss of enzymatic activity. 1 Publication
    Mutagenesisi293 – 2931K → A: 33.6% loss of enzymatic activity. 1 Publication
    Mutagenesisi362 – 3621H → A: No effect on enzymatic activity. 1 Publication
    Mutagenesisi365 – 3651G → A: 43% loss of enzymatic activity. 1 Publication
    Mutagenesisi366 – 3661K → A: 99.8% loss of enzymatic activity. 1 Publication
    Mutagenesisi368 – 3681K → A: 99.9% loss of enzymatic activity. 1 Publication
    Mutagenesisi370 – 3701R → E: 99.2% loss of enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29469.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Heparan sulfate glucosamine 3-O-sulfotransferase 3A1PRO_0000085217Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi351 ↔ 3631 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9Y663.
    PRIDEiQ9Y663.

    PTM databases

    PhosphoSiteiQ9Y663.

    Expressioni

    Tissue specificityi

    Ubiquitous. Most abundant in heart and placenta, followed by liver and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y663.
    BgeeiQ9Y663.
    CleanExiHS_HS3ST3A1.
    GenevestigatoriQ9Y663.

    Interactioni

    Protein-protein interaction databases

    BioGridi115280. 1 interaction.
    STRINGi9606.ENSP00000284110.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi139 – 1479
    Beta strandi154 – 1596
    Helixi165 – 1728
    Beta strandi178 – 1803
    Turni187 – 1904
    Helixi192 – 1943
    Helixi195 – 2028
    Beta strandi211 – 2155
    Helixi217 – 2215
    Helixi225 – 2328
    Beta strandi237 – 2426
    Helixi245 – 25915
    Helixi266 – 2705
    Helixi284 – 2874
    Helixi291 – 2988
    Turni299 – 3013
    Helixi304 – 3063
    Beta strandi307 – 3115
    Helixi312 – 3176
    Helixi319 – 33012
    Helixi338 – 3403
    Beta strandi341 – 3444
    Turni345 – 3484
    Beta strandi349 – 3546
    Helixi377 – 39822

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T8TX-ray1.85A/B139-406[»]
    1T8UX-ray1.95A/B139-406[»]
    ProteinModelPortaliQ9Y663.
    SMRiQ9Y663. Positions 139-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y663.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini44 – 406363LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei25 – 4319Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 1907Substrate binding
    Regioni215 – 2184Substrate binding
    Regioni255 – 2595Substrate binding
    Regioni283 – 2842Substrate binding
    Regioni367 – 3704Substrate binding

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG73846.
    HOGENOMiHOG000036663.
    HOVERGENiHBG053377.
    InParanoidiQ9Y663.
    KOiK07809.
    OMAiSGERLIM.
    OrthoDBiEOG7PS1GM.
    PhylomeDBiQ9Y663.
    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.

    Q9Y663-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPPGPASAL STSAEPLSRS IFRKFLLMLC SLLTSLYVFY CLAERCQTLS    50
    GPVVGLSGGG EEAGAPGGGV LAGGPRELAV WPAAAQRKRL LQLPQWRRRR 100
    PPAPRDDGEE AAWEEESPGL SGGPGGSGAG STVAEAPPGT LALLLDEGSK 150
    QLPQAIIIGV KKGGTRALLE FLRVHPDVRA VGAEPHFFDR SYDKGLAWYR 200
    DLMPRTLDGQ ITMEKTPSYF VTREAPARIS AMSKDTKLIV VVRDPVTRAI 250
    SDYTQTLSKR PDIPTFESLT FKNRTAGLID TSWSAIQIGI YAKHLEHWLR 300
    HFPIRQMLFV SGERLISDPA GELGRVQDFL GLKRIITDKH FYFNKTKGFP 350
    CLKKAEGSSR PHCLGKTKGR THPEIDREVV RRLREFYRPF NLKFYQMTGH 400
    DFGWDG 406
    Length:406
    Mass (Da):44,900
    Last modified:November 1, 1999 - v1
    Checksum:i57B6A0ABC897577A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF105376 mRNA. Translation: AAD30208.1.
    AY358838 mRNA. Translation: AAQ89197.1.
    AK292047 mRNA. Translation: BAF84736.1.
    CH471108 Genomic DNA. Translation: EAW89959.1.
    BC044647 mRNA. Translation: AAH44647.1.
    CCDSiCCDS11165.1.
    RefSeqiNP_006033.1. NM_006042.1.
    UniGeneiHs.462270.

    Genome annotation databases

    EnsembliENST00000284110; ENSP00000284110; ENSG00000153976.
    GeneIDi9955.
    KEGGihsa:9955.
    UCSCiuc002gob.1. human.

    Polymorphism databases

    DMDMi61214551.

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF105376 mRNA. Translation: AAD30208.1 .
    AY358838 mRNA. Translation: AAQ89197.1 .
    AK292047 mRNA. Translation: BAF84736.1 .
    CH471108 Genomic DNA. Translation: EAW89959.1 .
    BC044647 mRNA. Translation: AAH44647.1 .
    CCDSi CCDS11165.1.
    RefSeqi NP_006033.1. NM_006042.1.
    UniGenei Hs.462270.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T8T X-ray 1.85 A/B 139-406 [» ]
    1T8U X-ray 1.95 A/B 139-406 [» ]
    ProteinModelPortali Q9Y663.
    SMRi Q9Y663. Positions 139-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115280. 1 interaction.
    STRINGi 9606.ENSP00000284110.

    PTM databases

    PhosphoSitei Q9Y663.

    Polymorphism databases

    DMDMi 61214551.

    Proteomic databases

    PaxDbi Q9Y663.
    PRIDEi Q9Y663.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284110 ; ENSP00000284110 ; ENSG00000153976 .
    GeneIDi 9955.
    KEGGi hsa:9955.
    UCSCi uc002gob.1. human.

    Organism-specific databases

    CTDi 9955.
    GeneCardsi GC17M013339.
    HGNCi HGNC:5196. HS3ST3A1.
    MIMi 604057. gene.
    neXtProti NX_Q9Y663.
    PharmGKBi PA29469.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73846.
    HOGENOMi HOG000036663.
    HOVERGENi HBG053377.
    InParanoidi Q9Y663.
    KOi K07809.
    OMAi SGERLIM.
    OrthoDBi EOG7PS1GM.
    PhylomeDBi Q9Y663.
    TreeFami TF350755.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07937-MONOMER.
    Reactomei REACT_121248. HS-GAG biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei Q9Y663.
    GeneWikii HS3ST3A1.
    GenomeRNAii 9955.
    NextBioi 37564.
    PROi Q9Y663.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y663.
    Bgeei Q9Y663.
    CleanExi HS_HS3ST3A1.
    Genevestigatori Q9Y663.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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: Spleen.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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.
    6. "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry."
      Shukla D., Liu J., Blaiklock P., Shworak N.W., Bai X., Esko J.D., Cohen G.H., Eisenberg R.J., Rosenberg R.D., Spear P.G.
      Cell 99:13-22(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HSV-1 ENTRY, MUTAGENESIS OF LYS-162.
    7. "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.
    8. "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues."
      Liu J., Shriver Z., Blaiklock P., Yoshida K., Sasisekharan R., Rosenberg R.D.
      J. Biol. Chem. 274:38155-38162(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1."
      Moon A.F., Edavettal S.C., Krahn J.M., Munoz E.M., Negishi M., Linhardt R.J., Liu J., Pedersen L.C.
      J. Biol. Chem. 279:45185-45193(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 139-406 IN A TERNARY COMPLEX WITH PAPS AND A TETRASACCHARIDE, DISULFIDE BOND, BINDING SITES, MUTAGENESIS OF LYS-161; LYS-162; ARG-166; GLU-170; ARG-173; GLY-182; GLU-184; HIS-186; ASP-189; ARG-190; LYS-194; LYS-215; SER-218; GLU-224; GLN-255; LYS-259; ILE-288; LYS-293; HIS-362; GLY-365; LYS-366; LYS-368 AND ARG-370.

    Entry informationi

    Entry nameiHS3SA_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y663
    Secondary accession number(s): A8K7N2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 112 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3