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Q9Y2C2

- UST_HUMAN

UniProt

Q9Y2C2 - UST_HUMAN

Protein

Uronyl 2-sulfotransferase

Gene

UST

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin.

    GO - Molecular functioni

    1. sulfotransferase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. chondroitin sulfate metabolic process Source: Reactome
    3. dermatan sulfate biosynthetic process Source: Reactome
    4. glycosaminoglycan metabolic process Source: Reactome
    5. protein sulfation Source: ProtInc
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000111962-MONOMER.
    ReactomeiREACT_120800. Dermatan sulfate biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Uronyl 2-sulfotransferase (EC:2.8.2.-)
    Gene namesi
    Name:UST
    Synonyms:DS2ST
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17223. UST.

    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

    Organism-specific databases

    PharmGKBiPA38213.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Uronyl 2-sulfotransferasePRO_0000207681Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9Y2C2.
    PaxDbiQ9Y2C2.
    PRIDEiQ9Y2C2.

    PTM databases

    PhosphoSiteiQ9Y2C2.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiQ9Y2C2.
    CleanExiHS_UST.
    GenevestigatoriQ9Y2C2.

    Organism-specific databases

    HPAiHPA032022.

    Interactioni

    Protein-protein interaction databases

    BioGridi115398. 4 interactions.
    IntActiQ9Y2C2. 2 interactions.
    MINTiMINT-7970884.
    STRINGi9606.ENSP00000356433.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2C2.
    SMRiQ9Y2C2. Positions 105-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4949CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini71 – 406336LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei50 – 7021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfotransferase 3 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG310311.
    HOGENOMiHOG000059649.
    HOVERGENiHBG086208.
    InParanoidiQ9Y2C2.
    KOiK03193.
    OMAiQYLGNST.
    OrthoDBiEOG7DZ8JZ.
    PhylomeDBiQ9Y2C2.
    TreeFamiTF315238.

    Family and domain databases

    InterProiIPR007734. Heparan_SO4_2-O-STrfase.
    IPR027417. P-loop_NTPase.
    IPR005331. Sulfotransferase.
    [Graphical view]
    PANTHERiPTHR12129. PTHR12129. 1 hit.
    PfamiPF03567. Sulfotransfer_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9Y2C2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKKQQHPGG GADPWPHGAP MGGAPPGLGS WKRRVPLLPF LRFSLRDYGF    50
    CMATLLVFCL GSLLYQLSGG PPRFLLDLRQ YLGNSTYLDD HGPPPSKVLP 100
    FPSQVVYNRV GKCGSRTVVL LLRILSEKHG FNLVTSDIHN KTRLTKNEQM 150
    ELIKNISTAE QPYLFTRHVH FLNFSRFGGD QPVYINIIRD PVNRFLSNYF 200
    FRRFGDWRGE QNHMIRTPSM RQEERYLDIN ECILENYPEC SNPRLFYIIP 250
    YFCGQHPRCR EPGEWALERA KLNVNENFLL VGILEELEDV LLLLERFLPH 300
    YFKGVLSIYK DPEHRKLGNM TVTVKKTVPS PEAVQILYQR MRYEYEFYHY 350
    VKEQFHLLKR KFGLKSHVSK PPLRPHFFIP TPLETEEPID DEEQDDEKWL 400
    EDIYKR 406
    Length:406
    Mass (Da):47,673
    Last modified:November 1, 1999 - v1
    Checksum:i7F201FEBBFA3B2EA
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211M → L.
    Corresponds to variant rs9498146 [ dbSNP | Ensembl ].
    VAR_059819

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020316 mRNA. Translation: BAA77510.1.
    AK315320 mRNA. Translation: BAG37723.1.
    AL357992
    , AL359252, AL590485, AL807246 Genomic DNA. Translation: CAH70738.1.
    AL359252
    , AL357992, AL590485, AL807246 Genomic DNA. Translation: CAH70147.1.
    AL590485
    , AL357992, AL359252, AL807246 Genomic DNA. Translation: CAI17058.1.
    AL807246
    , AL357992, AL359252, AL590485 Genomic DNA. Translation: CAH74028.1.
    CH471051 Genomic DNA. Translation: EAW47812.1.
    BC093668 mRNA. Translation: AAH93668.1.
    BC093694 mRNA. Translation: AAH93694.1.
    CCDSiCCDS5213.1.
    RefSeqiNP_005706.1. NM_005715.2.
    UniGeneiHs.657370.

    Genome annotation databases

    EnsembliENST00000367463; ENSP00000356433; ENSG00000111962.
    GeneIDi10090.
    KEGGihsa:10090.
    UCSCiuc003qmg.3. human.

    Polymorphism databases

    DMDMi68052988.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020316 mRNA. Translation: BAA77510.1 .
    AK315320 mRNA. Translation: BAG37723.1 .
    AL357992
    , AL359252 , AL590485 , AL807246 Genomic DNA. Translation: CAH70738.1 .
    AL359252
    , AL357992 , AL590485 , AL807246 Genomic DNA. Translation: CAH70147.1 .
    AL590485
    , AL357992 , AL359252 , AL807246 Genomic DNA. Translation: CAI17058.1 .
    AL807246
    , AL357992 , AL359252 , AL590485 Genomic DNA. Translation: CAH74028.1 .
    CH471051 Genomic DNA. Translation: EAW47812.1 .
    BC093668 mRNA. Translation: AAH93668.1 .
    BC093694 mRNA. Translation: AAH93694.1 .
    CCDSi CCDS5213.1.
    RefSeqi NP_005706.1. NM_005715.2.
    UniGenei Hs.657370.

    3D structure databases

    ProteinModelPortali Q9Y2C2.
    SMRi Q9Y2C2. Positions 105-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115398. 4 interactions.
    IntActi Q9Y2C2. 2 interactions.
    MINTi MINT-7970884.
    STRINGi 9606.ENSP00000356433.

    PTM databases

    PhosphoSitei Q9Y2C2.

    Polymorphism databases

    DMDMi 68052988.

    Proteomic databases

    MaxQBi Q9Y2C2.
    PaxDbi Q9Y2C2.
    PRIDEi Q9Y2C2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367463 ; ENSP00000356433 ; ENSG00000111962 .
    GeneIDi 10090.
    KEGGi hsa:10090.
    UCSCi uc003qmg.3. human.

    Organism-specific databases

    CTDi 10090.
    GeneCardsi GC06P149110.
    HGNCi HGNC:17223. UST.
    HPAi HPA032022.
    MIMi 610752. gene.
    neXtProti NX_Q9Y2C2.
    PharmGKBi PA38213.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310311.
    HOGENOMi HOG000059649.
    HOVERGENi HBG086208.
    InParanoidi Q9Y2C2.
    KOi K03193.
    OMAi QYLGNST.
    OrthoDBi EOG7DZ8JZ.
    PhylomeDBi Q9Y2C2.
    TreeFami TF315238.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000111962-MONOMER.
    Reactomei REACT_120800. Dermatan sulfate biosynthesis.

    Miscellaneous databases

    ChiTaRSi UST. human.
    GenomeRNAii 10090.
    NextBioi 38161.
    PROi Q9Y2C2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y2C2.
    CleanExi HS_UST.
    Genevestigatori Q9Y2C2.

    Family and domain databases

    InterProi IPR007734. Heparan_SO4_2-O-STrfase.
    IPR027417. P-loop_NTPase.
    IPR005331. Sulfotransferase.
    [Graphical view ]
    PANTHERi PTHR12129. PTHR12129. 1 hit.
    Pfami PF03567. Sulfotransfer_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a human uronyl 2-sulfotransferase that sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate."
      Kobayashi M., Sugumaran G., Liu J., Shworak N.W., Silbert J.E., Rosenberg R.D.
      J. Biol. Chem. 274:10474-10480(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Lymphoma.
    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: Cerebellum.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 cortex.

    Entry informationi

    Entry nameiUST_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2C2
    Secondary accession number(s): B2RCX6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 98 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3