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O43529

- CHSTA_HUMAN

UniProt

O43529 - CHSTA_HUMAN

Protein

Carbohydrate sulfotransferase 10

Gene

CHST10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi127 – 1337PAPSCurated
    Nucleotide bindingi189 – 1979PAPSCurated

    GO - Molecular functioni

    1. HNK-1 sulfotransferase activity Source: Ensembl
    2. sulfotransferase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate biosynthetic process Source: InterPro
    2. cell adhesion Source: ProtInc
    3. learning Source: Ensembl
    4. long-term memory Source: Ensembl

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 10 (EC:2.8.2.-)
    Alternative name(s):
    HNK-1 sulfotransferase
    Short name:
    HNK-1ST
    Short name:
    HNK1ST
    Short name:
    HuHNK-1ST
    Gene namesi
    Name:CHST10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:19650. CHST10.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: ProtInc
    2. Golgi membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: ProtInc

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi128 – 1281K → A: Loss of function. 1 Publication
    Mutagenesisi128 – 1281K → R: Induces a reduction in enzyme activity. 1 Publication
    Mutagenesisi189 – 1891R → A or K: Loss of function. 1 Publication
    Mutagenesisi190 – 1901D → A: Loss of function. 1 Publication
    Mutagenesisi190 – 1901D → E: Induces a mild reduction in enzyme activity. 1 Publication
    Mutagenesisi191 – 1911P → A or G: Loss of function. 1 Publication
    Mutagenesisi197 – 1971S → A or T: Loss of function. 1 Publication

    Organism-specific databases

    PharmGKBiPA134920179.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356Carbohydrate sulfotransferase 10PRO_0000189657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiO43529.
    PRIDEiO43529.

    PTM databases

    PhosphoSiteiO43529.

    Expressioni

    Tissue specificityi

    In fetal tissues, it is predominantly expressed in brain, and weakly expressed in lung, kidney and liver. In adult, it is highly expressed in brain, testis, ovary, expressed at intermediate level in heart, pancreas, skeletal muscle, spleen and thymus, and weakly expressed in other tissues. In brain, it is expressed at higher level in the frontal lobe.1 Publication

    Gene expression databases

    ArrayExpressiO43529.
    BgeeiO43529.
    CleanExiHS_CHST10.
    GenevestigatoriO43529.

    Organism-specific databases

    HPAiHPA012884.
    HPA051545.

    Interactioni

    Protein-protein interaction databases

    BioGridi114868. 3 interactions.
    IntActiO43529. 1 interaction.
    STRINGi9606.ENSP00000264249.

    Structurei

    3D structure databases

    ProteinModelPortaliO43529.
    SMRiO43529. Positions 176-203.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini28 – 356329LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfotransferase 2 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG86863.
    HOVERGENiHBG050951.
    InParanoidiO43529.
    KOiK09674.
    PhylomeDBiO43529.
    TreeFamiTF325581.

    Family and domain databases

    InterProiIPR018011. Carb_sulfotransferase-rel.
    IPR005331. Sulfotransferase.
    [Graphical view]
    PANTHERiPTHR12137. PTHR12137. 1 hit.
    PfamiPF03567. Sulfotransfer_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O43529-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDVYSAKQE FLFLTTMPEV    50
    RKLPEEKHIP EELKPTGKEL PDSQLVQPLV YMERLELIRN VCRDDALKNL 100
    SHTPVSKFVL DRIFVCDKHK ILFCQTPKVG NTQWKKVLIV LNGAFSSIEE 150
    IPENVVHDHE KNGLPRLSSF SDAEIQKRLK TYFKFFIVRD PFERLISAFK 200
    DKFVHNPRFE PWYRHEIAPG IIRKYRRNRT ETRGIQFEDF VRYLGDPNHR 250
    WLDLQFGDHI IHWVTYVELC APCEIMYSVI GHHETLEDDA PYILKEAGID 300
    HLVSYPTIPP GITVYNRTKV EHYFLGISKR DIRRLYARFE GDFKLFGYQK 350
    PDFLLN 356
    Length:356
    Mass (Da):42,207
    Last modified:June 1, 1998 - v1
    Checksum:i0AE82883CCD8291A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201V → L.
    Corresponds to variant rs35177621 [ dbSNP | Ensembl ].
    VAR_033737
    Natural varianti258 – 2581D → N.
    Corresponds to variant rs3748932 [ dbSNP | Ensembl ].
    VAR_021470

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF033827 mRNA. Translation: AAC04707.1.
    AF070594 mRNA. Translation: AAC28651.1.
    AK313241 mRNA. Translation: BAG36052.1.
    AC012493 Genomic DNA. Translation: AAX93044.1.
    CH471127 Genomic DNA. Translation: EAX01841.1.
    CH471127 Genomic DNA. Translation: EAX01842.1.
    CH471127 Genomic DNA. Translation: EAX01843.1.
    CH471127 Genomic DNA. Translation: EAX01844.1.
    BC010441 mRNA. Translation: AAH10441.1.
    CCDSiCCDS2047.1.
    RefSeqiNP_004845.1. NM_004854.4.
    UniGeneiHs.516370.
    Hs.731724.

    Genome annotation databases

    EnsembliENST00000264249; ENSP00000264249; ENSG00000115526.
    ENST00000409701; ENSP00000387309; ENSG00000115526.
    GeneIDi9486.
    KEGGihsa:9486.
    UCSCiuc002tam.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF033827 mRNA. Translation: AAC04707.1 .
    AF070594 mRNA. Translation: AAC28651.1 .
    AK313241 mRNA. Translation: BAG36052.1 .
    AC012493 Genomic DNA. Translation: AAX93044.1 .
    CH471127 Genomic DNA. Translation: EAX01841.1 .
    CH471127 Genomic DNA. Translation: EAX01842.1 .
    CH471127 Genomic DNA. Translation: EAX01843.1 .
    CH471127 Genomic DNA. Translation: EAX01844.1 .
    BC010441 mRNA. Translation: AAH10441.1 .
    CCDSi CCDS2047.1.
    RefSeqi NP_004845.1. NM_004854.4.
    UniGenei Hs.516370.
    Hs.731724.

    3D structure databases

    ProteinModelPortali O43529.
    SMRi O43529. Positions 176-203.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114868. 3 interactions.
    IntActi O43529. 1 interaction.
    STRINGi 9606.ENSP00000264249.

    PTM databases

    PhosphoSitei O43529.

    Proteomic databases

    PaxDbi O43529.
    PRIDEi O43529.

    Protocols and materials databases

    DNASUi 9486.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264249 ; ENSP00000264249 ; ENSG00000115526 .
    ENST00000409701 ; ENSP00000387309 ; ENSG00000115526 .
    GeneIDi 9486.
    KEGGi hsa:9486.
    UCSCi uc002tam.3. human.

    Organism-specific databases

    CTDi 9486.
    GeneCardsi GC02M101008.
    HGNCi HGNC:19650. CHST10.
    HPAi HPA012884.
    HPA051545.
    MIMi 606376. gene.
    neXtProti NX_O43529.
    PharmGKBi PA134920179.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86863.
    HOVERGENi HBG050951.
    InParanoidi O43529.
    KOi K09674.
    PhylomeDBi O43529.
    TreeFami TF325581.

    Miscellaneous databases

    GeneWikii CHST10.
    GenomeRNAii 9486.
    NextBioi 35544.
    PROi O43529.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43529.
    Bgeei O43529.
    CleanExi HS_CHST10.
    Genevestigatori O43529.

    Family and domain databases

    InterProi IPR018011. Carb_sulfotransferase-rel.
    IPR005331. Sulfotransferase.
    [Graphical view ]
    PANTHERi PTHR12137. PTHR12137. 1 hit.
    Pfami PF03567. Sulfotransfer_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids."
      Ong E., Yeh J.-C., Ding Y., Hindsgaul O., Fukuda M.
      J. Biol. Chem. 273:5190-5195(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Yu W., Gibbs R.A.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    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: Brain.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
    7. "Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis."
      Ong E., Yeh J.-C., Ding Y., Hindsgaul O., Pedersen L.C., Negishi M., Fukuda M.
      J. Biol. Chem. 274:25608-25612(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-128; ARG-189; ASP-190; PRO-191 AND SER-197.

    Entry informationi

    Entry nameiCHSTA_HUMAN
    AccessioniPrimary (citable) accession number: O43529
    Secondary accession number(s): Q53T18
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 102 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 2
      Human chromosome 2: 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