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Q9NS84

- CHST7_HUMAN

UniProt

Q9NS84 - CHST7_HUMAN

Protein

Carbohydrate sulfotransferase 7

Gene

CHST7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (15 Mar 2005)
      Previous versions | rss
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    Functioni

    Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc.3 Publications

    Catalytic activityi

    3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi110 – 1167PAPSBy similarity
    Nucleotide bindingi278 – 2869PAPSBy similarity

    GO - Molecular functioni

    1. chondroitin 6-sulfotransferase activity Source: UniProtKB
    2. N-acetylglucosamine 6-O-sulfotransferase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. chondroitin sulfate biosynthetic process Source: UniProtKB
    3. chondroitin sulfate metabolic process Source: Reactome
    4. glycosaminoglycan metabolic process Source: Reactome
    5. N-acetylglucosamine metabolic process Source: UniProtKB
    6. polysaccharide metabolic process Source: UniProtKB
    7. small molecule metabolic process Source: Reactome
    8. sulfur compound metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07394-MONOMER.
    BRENDAi2.8.2.17. 2681.
    ReactomeiREACT_120989. Chondroitin sulfate biosynthesis.
    SABIO-RKQ9NS84.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 7 (EC:2.8.2.-, EC:2.8.2.17)
    Alternative name(s):
    Chondroitin 6-sulfotransferase 2
    Short name:
    C6ST-2
    Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5
    Short name:
    GST-5
    N-acetylglucosamine 6-O-sulfotransferase 4
    Short name:
    GlcNAc6ST-4
    Short name:
    Gn6st-4
    Gene namesi
    Name:CHST7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13817. CHST7.

    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

    Organism-specific databases

    PharmGKBiPA26507.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Carbohydrate sulfotransferase 7PRO_0000085198Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi407 – 4071N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9NS84.
    PaxDbiQ9NS84.
    PRIDEiQ9NS84.

    PTM databases

    PhosphoSiteiQ9NS84.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in heart, spleen, liver and ovary. Expressed at lower level in brain, placenta, thyroid, spinal cord and peripheral blood leukocytes. Not expressed in adult skin.3 Publications

    Gene expression databases

    BgeeiQ9NS84.
    CleanExiHS_CHST7.
    GenevestigatoriQ9NS84.

    Organism-specific databases

    HPAiHPA003919.

    Interactioni

    Protein-protein interaction databases

    BioGridi121152. 1 interaction.
    STRINGi9606.ENSP00000276055.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NS84.
    SMRiQ9NS84. Positions 101-139, 367-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini35 – 486452LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71363.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9NS84.
    KOiK04743.
    OMAiDKGAGHC.
    OrthoDBiEOG7RZ5S0.
    PhylomeDBiQ9NS84.
    TreeFamiTF342871.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9NS84-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGRRRRRRE YCKFALLLVL YTLVLLLVPS VLDGGRDGDK GAEHCPGLQR    50
    SLGVWSLEAA AAGEREQGAE ARAAEEGGAN QSPRFPSNLS GAVGEAVSRE 100
    KQHIYVHATW RTGSSFLGEL FNQHPDVFYL YEPMWHLWQA LYPGDAESLQ 150
    GALRDMLRSL FRCDFSVLRL YAPPGDPAAR APDTANLTTA ALFRWRTNKV 200
    ICSPPLCPGA PRARAEVGLV EDTACERSCP PVAIRALEAE CRKYPVVVIK 250
    DVRLLDLGVL VPLLRDPGLN LKVVQLFRDP RAVHNSRLKS RQGLLRESIQ 300
    VLRTRQRGDR FHRVLLAHGV GARPGGQSRA LPAAPRADFF LTGALEVICE 350
    AWLRDLLFAR GAPAWLRRRY LRLRYEDLVR QPRAQLRRLL RFSGLRALAA 400
    LDAFALNMTR GAAYGADRPF HLSARDAREA VHAWRERLSR EQVRQVEAAC 450
    APAMRLLAYP RSGEEGDAEQ PREGETPLEM DADGAT 486
    Length:486
    Mass (Da):54,266
    Last modified:March 15, 2005 - v2
    Checksum:i3F1FD1430B3C8E95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti448 – 4481A → V in BAB03217. (PubMed:10781596)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040711 mRNA. Translation: BAB13770.1.
    AB037187 mRNA. Translation: BAB03217.1.
    AL022165 Genomic DNA. Translation: CAA18154.1.
    BC045537 mRNA. Translation: AAH45537.1.
    CCDSiCCDS14268.1.
    PIRiJC7351.
    RefSeqiNP_063939.2. NM_019886.3.
    UniGeneiHs.129955.

    Genome annotation databases

    EnsembliENST00000276055; ENSP00000276055; ENSG00000147119.
    GeneIDi56548.
    KEGGihsa:56548.
    UCSCiuc004dgt.3. human.

    Polymorphism databases

    DMDMi61212141.

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040711 mRNA. Translation: BAB13770.1 .
    AB037187 mRNA. Translation: BAB03217.1 .
    AL022165 Genomic DNA. Translation: CAA18154.1 .
    BC045537 mRNA. Translation: AAH45537.1 .
    CCDSi CCDS14268.1.
    PIRi JC7351.
    RefSeqi NP_063939.2. NM_019886.3.
    UniGenei Hs.129955.

    3D structure databases

    ProteinModelPortali Q9NS84.
    SMRi Q9NS84. Positions 101-139, 367-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121152. 1 interaction.
    STRINGi 9606.ENSP00000276055.

    PTM databases

    PhosphoSitei Q9NS84.

    Polymorphism databases

    DMDMi 61212141.

    Proteomic databases

    MaxQBi Q9NS84.
    PaxDbi Q9NS84.
    PRIDEi Q9NS84.

    Protocols and materials databases

    DNASUi 56548.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000276055 ; ENSP00000276055 ; ENSG00000147119 .
    GeneIDi 56548.
    KEGGi hsa:56548.
    UCSCi uc004dgt.3. human.

    Organism-specific databases

    CTDi 56548.
    GeneCardsi GC0XP046433.
    HGNCi HGNC:13817. CHST7.
    HPAi HPA003919.
    MIMi 300375. gene.
    neXtProti NX_Q9NS84.
    PharmGKBi PA26507.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71363.
    HOGENOMi HOG000261614.
    HOVERGENi HBG050949.
    InParanoidi Q9NS84.
    KOi K04743.
    OMAi DKGAGHC.
    OrthoDBi EOG7RZ5S0.
    PhylomeDBi Q9NS84.
    TreeFami TF342871.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07394-MONOMER.
    BRENDAi 2.8.2.17. 2681.
    Reactomei REACT_120989. Chondroitin sulfate biosynthesis.
    SABIO-RK Q9NS84.

    Miscellaneous databases

    GeneWikii CHST7.
    GenomeRNAii 56548.
    NextBioi 62035.
    PROi Q9NS84.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NS84.
    CleanExi HS_CHST7.
    Genevestigatori Q9NS84.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view ]
    Pfami PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMi SSF52540. SSF52540. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities."
      Uchimura K., Fasakhany F., Kadomatsu K., Matsukawa T., Yamakawa T., Kurosawa N., Muramatsu T.
      Biochem. Biophys. Res. Commun. 274:291-296(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Molecular cloning and expression of a novel chondroitin 6-O-sulfotransferase."
      Kitagawa H., Fujita M., Ito N., Sugahara K.
      J. Biol. Chem. 275:21075-21080(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      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. Cited for: FUNCTION, TISSUE SPECIFICITY.
    6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-407.
      Tissue: Plasma.

    Entry informationi

    Entry nameiCHST7_HUMAN
    AccessioniPrimary (citable) accession number: Q9NS84
    Secondary accession number(s): O75667
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 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 X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3