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Q9EP78

- CHST7_MOUSE

UniProt

Q9EP78 - CHST7_MOUSE

Protein

Carbohydrate sulfotransferase 7

Gene

Chst7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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.1 Publication

    Catalytic activityi

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi108 – 1147PAPSBy similarity
    Nucleotide bindingi276 – 2849PAPSBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. chondroitin sulfate biosynthetic process Source: Ensembl
    3. N-acetylglucosamine metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BRENDAi2.8.2.17. 3474.
    ReactomeiREACT_196514. Chondroitin sulfate biosynthesis.

    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
    Short name:
    mC6ST-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
    Synonyms:Gst5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1891767. Chst7.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484Carbohydrate sulfotransferase 7PRO_0000085199Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ9EP78.

    PTM databases

    PhosphoSiteiQ9EP78.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in kidney. Expressed at lower level in heart, lung and liver.1 Publication

    Gene expression databases

    BgeeiQ9EP78.
    GenevestigatoriQ9EP78.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000043222.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EP78.
    SMRiQ9EP78. Positions 99-137, 365-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini34 – 484451LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71363.
    GeneTreeiENSGT00530000062902.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9EP78.
    KOiK04743.
    OMAiDKGAGHC.
    OrthoDBiEOG7RZ5S0.
    PhylomeDBiQ9EP78.
    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.

    Q9EP78-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGRRRRRRE YCKFTLLLAL YTLLLLLVPS VLDSHSEQDK GRNCPGLQRS    50
    LGVWSLEAAA AGEREQGAEV RSLAEGNPDR SPGSPGNLSA VGEAVTQEKQ 100
    HIYVHATWRT GSSFLGELFN QHPDVFYLYE PMWHLWQALY PGDAESLQGA 150
    LRDMLRSLFR CDFSVLRLYA QPGDPGERAP DSANLTTAML FRWRTNKVIC 200
    SPPLCPAAPR ARADVGLVED KACESTCPPV SLRALEAECR KYPVVVIKDV 250
    RLLDLGVLVP LLRDPGLNLK VVQLFRDPRA VHNSRLKSRQ GLLRESIQVL 300
    RTRQRGDHFH RVLLAHGVDA RPGGQARALP SAPRADFFLT SALEVICEAW 350
    LRDLLFTRGA PAWLRRRYLR LRYEDLVWQP QAQLRRLLRF SGLRTLAALD 400
    AFAFNMTRGS AYGADRPFHL SARDAREAVH AWRERLSQEQ VRQVETACAP 450
    AMRLLAYPRS GDERDRKTVR EGETPLETKA NWAV 484
    Length:484
    Mass (Da):54,767
    Last modified:March 1, 2001 - v1
    Checksum:i9B195537D7AB7193
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101E → K in BAB40372. 1 PublicationCurated
    Sequence conflicti130 – 1301E → D in BAB40372. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040710 mRNA. Translation: BAB13769.1.
    AF280089 Genomic DNA. Translation: AAG48247.1.
    AB046929 mRNA. Translation: BAB40372.1.
    AK011202 mRNA. Translation: BAB27465.1.
    BC019204 mRNA. Translation: AAH19204.1.
    CCDSiCCDS30040.1.
    PIRiJC7350.
    RefSeqiNP_068361.1. NM_021715.1.
    UniGeneiMm.44827.

    Genome annotation databases

    EnsembliENSMUST00000044138; ENSMUSP00000043222; ENSMUSG00000037347.
    GeneIDi60322.
    KEGGimmu:60322.
    UCSCiuc009sss.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040710 mRNA. Translation: BAB13769.1 .
    AF280089 Genomic DNA. Translation: AAG48247.1 .
    AB046929 mRNA. Translation: BAB40372.1 .
    AK011202 mRNA. Translation: BAB27465.1 .
    BC019204 mRNA. Translation: AAH19204.1 .
    CCDSi CCDS30040.1.
    PIRi JC7350.
    RefSeqi NP_068361.1. NM_021715.1.
    UniGenei Mm.44827.

    3D structure databases

    ProteinModelPortali Q9EP78.
    SMRi Q9EP78. Positions 99-137, 365-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000043222.

    PTM databases

    PhosphoSitei Q9EP78.

    Proteomic databases

    PRIDEi Q9EP78.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044138 ; ENSMUSP00000043222 ; ENSMUSG00000037347 .
    GeneIDi 60322.
    KEGGi mmu:60322.
    UCSCi uc009sss.1. mouse.

    Organism-specific databases

    CTDi 56548.
    MGIi MGI:1891767. Chst7.

    Phylogenomic databases

    eggNOGi NOG71363.
    GeneTreei ENSGT00530000062902.
    HOGENOMi HOG000261614.
    HOVERGENi HBG050949.
    InParanoidi Q9EP78.
    KOi K04743.
    OMAi DKGAGHC.
    OrthoDBi EOG7RZ5S0.
    PhylomeDBi Q9EP78.
    TreeFami TF342871.

    Enzyme and pathway databases

    BRENDAi 2.8.2.17. 3474.
    Reactomei REACT_196514. Chondroitin sulfate biosynthesis.

    Miscellaneous databases

    NextBioi 314817.
    PROi Q9EP78.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9EP78.
    Genevestigatori Q9EP78.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6.
    3. "Cloning and expression of mouse chondroitin 6-sulfotransferase-2."
      Kitagawa H., Uyama T., Sugahara K.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary gland.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
    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].
      Strain: FVB/N.
      Tissue: Kidney.

    Entry informationi

    Entry nameiCHST7_MOUSE
    AccessioniPrimary (citable) accession number: Q9EP78
    Secondary accession number(s): Q99NB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3