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Q7L1S5

- CHST9_HUMAN

UniProt

Q7L1S5 - CHST9_HUMAN

Protein

Carbohydrate sulfotransferase 9

Gene

CHST9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carbonic anhydrase VI than toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta. Isoform 2, but not isoform 1, is active toward chondroitin.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi220 – 2267PAPSBy similarity
    Nucleotide bindingi280 – 2889PAPSBy similarity

    GO - Molecular functioni

    1. N-acetylgalactosamine 4-O-sulfotransferase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate biosynthetic process Source: InterPro
    2. carbohydrate metabolic process Source: Reactome
    3. chondroitin sulfate biosynthetic process Source: Reactome
    4. chondroitin sulfate metabolic process Source: Reactome
    5. glycosaminoglycan metabolic process Source: UniProtKB
    6. hormone biosynthetic process Source: UniProtKB
    7. proteoglycan biosynthetic process Source: UniProtKB
    8. small molecule metabolic process Source: Reactome
    9. sulfur compound metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    ReactomeiREACT_120989. Chondroitin sulfate biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 9 (EC:2.8.2.-)
    Alternative name(s):
    GalNAc-4-O-sulfotransferase 2
    Short name:
    GalNAc-4-ST2
    Short name:
    GalNAc4ST-2
    N-acetylgalactosamine-4-O-sulfotransferase 2
    Gene namesi
    Name:CHST9
    ORF Names:UNQ2549/PRO6175
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:19898. CHST9.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. Golgi membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134888782.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Carbohydrate sulfotransferase 9PRO_0000189655Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ7L1S5.
    PRIDEiQ7L1S5.

    PTM databases

    PhosphoSiteiQ7L1S5.

    Expressioni

    Tissue specificityi

    Highly expressed in trachea. Also expressed in fetal lung, adult pancreas, testis and salivary gland. Expressed at low level in pituitary gland, apex of the heart, adult lung, prostate and mammary gland. Weakly or not expressed in heart, liver and spinal cord.2 Publications

    Gene expression databases

    BgeeiQ7L1S5.
    CleanExiHS_CHST9.
    GenevestigatoriQ7L1S5.

    Organism-specific databases

    HPAiHPA011393.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000392091.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7L1S5.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini34 – 443410LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321Helical; 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

    eggNOGiNOG296625.
    HOGENOMiHOG000231801.
    HOVERGENiHBG050950.
    InParanoidiQ7L1S5.
    KOiK09673.
    OMAiNAQVVRQ.
    OrthoDBiEOG7B05D8.
    PhylomeDBiQ7L1S5.
    TreeFamiTF325581.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7L1S5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQPSEMVMNP KQVFLSVLIF GVAGLLLFMY LQVWIEEQHT GRVEKRREQK    50
    VTSGWGPVKY LRPVPRIMST EKIQEHITNQ NPKFHMPEDV REKKENLLLN 100
    SERSTRLLTK TSHSQGGDQA LSKSTGSPTE KLIEKRQGAK TVFNKFSNMN 150
    WPVDIHPLNK SLVKDNKWKK TEETQEKRRS FLQEFCKKYG GVSHHQSHLF 200
    HTVSRIYVED KHKILYCEVP KAGCSNWKRI LMVLNGLASS AYNISHNAVH 250
    YGKHLKKLDS FDLKGIYTRL NTYTKAVFVR DPMERLVSAF RDKFEHPNSY 300
    YHPVFGKAII KKYRPNACEE ALINGSGVKF KEFIHYLLDS HRPVGMDIHW 350
    EKVSKLCYPC LINYDFVGKF ETLEEDANYF LQMIGAPKEL KFPNFKDRHS 400
    SDERTNAQVV RQYLKDLTRT ERQLIYDFYY LDYLMFNYTT PFL 443
    Length:443
    Mass (Da):52,055
    Last modified:May 5, 2009 - v2
    Checksum:i5455E67D20C9F8D6
    GO
    Isoform 2 (identifier: Q7L1S5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-74: MSTEKIQ → KPQVSHA
         75-443: Missing.

    Show »
    Length:74
    Mass (Da):8,591
    Checksum:i1F1A2CBAD277FA16
    GO

    Sequence cautioni

    The sequence AAH25764.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAK01862.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361R → H in AAK01862. (PubMed:11445554)Curated
    Sequence conflicti150 – 1501N → D in AAK01862. (PubMed:11445554)Curated
    Sequence conflicti194 – 1952HH → PP in AAK30370. (PubMed:11139592)Curated
    Sequence conflicti442 – 4421F → L in AAQ88852. (PubMed:12975309)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221S → N.
    Corresponds to variant rs17694469 [ dbSNP | Ensembl ].
    VAR_055150

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 747MSTEKIQ → KPQVSHA in isoform 2. 1 PublicationVSP_043865
    Alternative sequencei75 – 443369Missing in isoform 2. 1 PublicationVSP_043866Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF239821 mRNA. Translation: AAK01862.1. Different initiation.
    AF332472 mRNA. Translation: AAK30369.1.
    AF332473 mRNA. Translation: AAK30370.1. Sequence problems.
    AY358488 mRNA. Translation: AAQ88852.1.
    AK093349 mRNA. Translation: BAC04141.1.
    AC010854 Genomic DNA. No translation available.
    AC023575 Genomic DNA. No translation available.
    AC116017 Genomic DNA. No translation available.
    BC025764 mRNA. Translation: AAH25764.2. Different initiation.
    CCDSiCCDS42422.1. [Q7L1S5-1]
    CCDS58618.1. [Q7L1S5-2]
    RefSeqiNP_001243245.1. NM_001256316.1. [Q7L1S5-2]
    NP_113610.2. NM_031422.5. [Q7L1S5-1]
    UniGeneiHs.44584.
    Hs.706552.

    Genome annotation databases

    EnsembliENST00000284224; ENSP00000284224; ENSG00000154080. [Q7L1S5-1]
    ENST00000580774; ENSP00000464655; ENSG00000154080. [Q7L1S5-2]
    ENST00000581714; ENSP00000462852; ENSG00000154080. [Q7L1S5-1]
    GeneIDi83539.
    KEGGihsa:83539.
    UCSCiuc002kwd.4. human. [Q7L1S5-1]
    uc021uij.2. human. [Q7L1S5-2]

    Polymorphism databases

    DMDMi229462829.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF239821 mRNA. Translation: AAK01862.1 . Different initiation.
    AF332472 mRNA. Translation: AAK30369.1 .
    AF332473 mRNA. Translation: AAK30370.1 . Sequence problems.
    AY358488 mRNA. Translation: AAQ88852.1 .
    AK093349 mRNA. Translation: BAC04141.1 .
    AC010854 Genomic DNA. No translation available.
    AC023575 Genomic DNA. No translation available.
    AC116017 Genomic DNA. No translation available.
    BC025764 mRNA. Translation: AAH25764.2 . Different initiation.
    CCDSi CCDS42422.1. [Q7L1S5-1 ]
    CCDS58618.1. [Q7L1S5-2 ]
    RefSeqi NP_001243245.1. NM_001256316.1. [Q7L1S5-2 ]
    NP_113610.2. NM_031422.5. [Q7L1S5-1 ]
    UniGenei Hs.44584.
    Hs.706552.

    3D structure databases

    ProteinModelPortali Q7L1S5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000392091.

    PTM databases

    PhosphoSitei Q7L1S5.

    Polymorphism databases

    DMDMi 229462829.

    Proteomic databases

    PaxDbi Q7L1S5.
    PRIDEi Q7L1S5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284224 ; ENSP00000284224 ; ENSG00000154080 . [Q7L1S5-1 ]
    ENST00000580774 ; ENSP00000464655 ; ENSG00000154080 . [Q7L1S5-2 ]
    ENST00000581714 ; ENSP00000462852 ; ENSG00000154080 . [Q7L1S5-1 ]
    GeneIDi 83539.
    KEGGi hsa:83539.
    UCSCi uc002kwd.4. human. [Q7L1S5-1 ]
    uc021uij.2. human. [Q7L1S5-2 ]

    Organism-specific databases

    CTDi 83539.
    GeneCardsi GC18M024495.
    HGNCi HGNC:19898. CHST9.
    HPAi HPA011393.
    MIMi 610191. gene.
    neXtProti NX_Q7L1S5.
    PharmGKBi PA134888782.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296625.
    HOGENOMi HOG000231801.
    HOVERGENi HBG050950.
    InParanoidi Q7L1S5.
    KOi K09673.
    OMAi NAQVVRQ.
    OrthoDBi EOG7B05D8.
    PhylomeDBi Q7L1S5.
    TreeFami TF325581.

    Enzyme and pathway databases

    Reactomei REACT_120989. Chondroitin sulfate biosynthesis.

    Miscellaneous databases

    GenomeRNAii 83539.
    NextBioi 72449.
    PROi Q7L1S5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7L1S5.
    CleanExi HS_CHST9.
    Genevestigatori Q7L1S5.

    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. "Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1->4GlcNAc beta 1->R in both N- and O-glycans."
      Hiraoka N., Misra A., Belot F., Hindsgaul O., Fukuda M.
      Glycobiology 11:495-504(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
    2. "Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal beta 1,4-linked N-acetylgalactosamine."
      Kang H.-G., Evers M.R., Xia G., Baenziger J.U., Schachner M.
      J. Biol. Chem. 276:10861-10869(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY, TISSUE SPECIFICITY.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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] (ISOFORM 1).
      Tissue: Testis.
    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] (ISOFORM 1).
      Tissue: Lung.

    Entry informationi

    Entry nameiCHST9_HUMAN
    AccessioniPrimary (citable) accession number: Q7L1S5
    Secondary accession number(s): Q6UX69
    , Q9BXH3, Q9BXH4, Q9BZW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 97 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

    Caution

    It is uncertain whether Met-1 or Met-8 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: 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