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Protein

Carbohydrate sulfotransferase 11

Gene

CHST11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.

Catalytic activityi

3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate.2 Publications

Kineticsi

  1. KM=0.5 µM for PAPS1 Publication
  2. KM=2.1 mM for chondroitin1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi124 – 1307PAPSBy similarity
    Nucleotide bindingi186 – 1949PAPSBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10284-MONOMER.
    BRENDAi2.8.2.5. 2681.
    ReactomeiREACT_120989. Chondroitin sulfate biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 11 (EC:2.8.2.5)
    Alternative name(s):
    Chondroitin 4-O-sulfotransferase 1
    Chondroitin 4-sulfotransferase 1
    Short name:
    C4S-1
    Short name:
    C4ST-1
    Short name:
    C4ST1
    Gene namesi
    Name:CHST11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17422. CHST11.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei17 – 3721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini38 – 352315LumenalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • Golgi apparatus Source: HPA
    • Golgi membrane Source: Reactome
    • integral component of membrane Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving CHST11 is found in B-cell chronic lymphocytic leukemias. Translocation t(12;14)(q23;q32) with IgH.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251K → Q: Abolishes enzyme activity but does not affect stability of the protein. 1 Publication
    Mutagenesisi205 – 2051N → S: Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-223 and S-321. 1 Publication
    Mutagenesisi223 – 2231N → S: Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-321. 1 Publication
    Mutagenesisi321 – 3211N → S: Induces a strong decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-223.
    Mutagenesisi342 – 3421N → S: Induces a strong decrease in enzyme activity has no effect on stability of the protein. 1 Publication

    Organism-specific databases

    PharmGKBiPA134875681.

    Polymorphism and mutation databases

    BioMutaiCHST11.
    DMDMi61212137.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Carbohydrate sulfotransferase 11PRO_0000189664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi342 – 3421N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    N-glycosylated; required for activity and stability.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9NPF2.
    PaxDbiQ9NPF2.
    PRIDEiQ9NPF2.

    PTM databases

    PhosphoSiteiQ9NPF2.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in spleen, thymus, bone marrow, peripheral blood leukocytes, lymph node, heart, brain, lung and placenta.2 Publications

    Gene expression databases

    BgeeiQ9NPF2.
    CleanExiHS_CHST11.
    ExpressionAtlasiQ9NPF2. baseline and differential.
    GenevisibleiQ9NPF2. HS.

    Organism-specific databases

    HPAiHPA052828.

    Interactioni

    Protein-protein interaction databases

    BioGridi119084. 2 interactions.
    STRINGi9606.ENSP00000305725.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NPF2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfotransferase 2 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG296625.
    GeneTreeiENSGT00760000119214.
    HOGENOMiHOG000231801.
    HOVERGENiHBG050952.
    InParanoidiQ9NPF2.
    KOiK01017.
    OMAiTCRANSV.
    PhylomeDBiQ9NPF2.
    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. AlignAdd to basket

    Isoform 1 (identifier: Q9NPF2-1) [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

            10         20         30         40         50
    MKPALLEVMR MNRICRMVLA TCLGSFILVI FYFQSMLHPV MRRNPFGVDI
    60 70 80 90 100
    CCRKGSRSPL QELYNPIQLE LSNTAVLHQM RRDQVTDTCR ANSATSRKRR
    110 120 130 140 150
    VLTPNDLKHL VVDEDHELIY CYVPKVACTN WKRLMMVLTG RGKYSDPMEI
    160 170 180 190 200
    PANEAHVSAN LKTLNQYSIP EINHRLKSYM KFLFVREPFE RLVSAYRNKF
    210 220 230 240 250
    TQKYNISFHK RYGTKIIKRQ RKNATQEALR KGDDVKFEEF VAYLIDPHTQ
    260 270 280 290 300
    REEPFNEHWQ TVYSLCHPCH IHYDLVGKYE TLEEDSNYVL QLAGVGSYLK
    310 320 330 340 350
    FPTYAKSTRT TDEMTTEFFQ NISSEHQTQL YEVYKLDFLM FNYSVPSYLK

    LE
    Length:352
    Mass (Da):41,555
    Last modified:October 1, 2000 - v1
    Checksum:i55DF1D29D6703307
    GO
    Isoform 2 (identifier: Q9NPF2-2) [UniParc]FASTAAdd to basket

    Also known as: C4S-1A

    The sequence of this isoform differs from the canonical sequence as follows:
         35-40: SMLHPV → I

    Show »
    Length:347
    Mass (Da):41,003
    Checksum:iDEB2646BC0CA5FF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti289 – 2891V → F in CAB87380 (Ref. 3) Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei35 – 406SMLHPV → I in isoform 2. 1 PublicationVSP_012992

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB042326 mRNA. Translation: BAA95485.1.
    AF239820 mRNA. Translation: AAF81691.1.
    AJ269537 mRNA. Translation: CAB87380.1.
    AJ289134 mRNA. Translation: CAB92134.1.
    AK290923 mRNA. Translation: BAF83612.1.
    CH471054 Genomic DNA. Translation: EAW97748.1.
    BC013315 mRNA. Translation: AAH13315.1.
    CCDSiCCDS55878.1. [Q9NPF2-2]
    CCDS9099.1. [Q9NPF2-1]
    PIRiJC7525.
    RefSeqiNP_001167453.1. NM_001173982.1. [Q9NPF2-2]
    NP_060883.1. NM_018413.5. [Q9NPF2-1]
    UniGeneiHs.17569.

    Genome annotation databases

    EnsembliENST00000303694; ENSP00000305725; ENSG00000171310.
    ENST00000549260; ENSP00000450004; ENSG00000171310. [Q9NPF2-2]
    GeneIDi50515.
    KEGGihsa:50515.
    UCSCiuc001tky.3. human. [Q9NPF2-2]
    uc001tkz.3. human. [Q9NPF2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB042326 mRNA. Translation: BAA95485.1.
    AF239820 mRNA. Translation: AAF81691.1.
    AJ269537 mRNA. Translation: CAB87380.1.
    AJ289134 mRNA. Translation: CAB92134.1.
    AK290923 mRNA. Translation: BAF83612.1.
    CH471054 Genomic DNA. Translation: EAW97748.1.
    BC013315 mRNA. Translation: AAH13315.1.
    CCDSiCCDS55878.1. [Q9NPF2-2]
    CCDS9099.1. [Q9NPF2-1]
    PIRiJC7525.
    RefSeqiNP_001167453.1. NM_001173982.1. [Q9NPF2-2]
    NP_060883.1. NM_018413.5. [Q9NPF2-1]
    UniGeneiHs.17569.

    3D structure databases

    ProteinModelPortaliQ9NPF2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119084. 2 interactions.
    STRINGi9606.ENSP00000305725.

    PTM databases

    PhosphoSiteiQ9NPF2.

    Polymorphism and mutation databases

    BioMutaiCHST11.
    DMDMi61212137.

    Proteomic databases

    MaxQBiQ9NPF2.
    PaxDbiQ9NPF2.
    PRIDEiQ9NPF2.

    Protocols and materials databases

    DNASUi50515.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000303694; ENSP00000305725; ENSG00000171310.
    ENST00000549260; ENSP00000450004; ENSG00000171310. [Q9NPF2-2]
    GeneIDi50515.
    KEGGihsa:50515.
    UCSCiuc001tky.3. human. [Q9NPF2-2]
    uc001tkz.3. human. [Q9NPF2-1]

    Organism-specific databases

    CTDi50515.
    GeneCardsiGC12P104849.
    HGNCiHGNC:17422. CHST11.
    HPAiHPA052828.
    MIMi610128. gene.
    neXtProtiNX_Q9NPF2.
    PharmGKBiPA134875681.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG296625.
    GeneTreeiENSGT00760000119214.
    HOGENOMiHOG000231801.
    HOVERGENiHBG050952.
    InParanoidiQ9NPF2.
    KOiK01017.
    OMAiTCRANSV.
    PhylomeDBiQ9NPF2.
    TreeFamiTF325581.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10284-MONOMER.
    BRENDAi2.8.2.5. 2681.
    ReactomeiREACT_120989. Chondroitin sulfate biosynthesis.

    Miscellaneous databases

    ChiTaRSiCHST11. human.
    GeneWikiiCHST11.
    GenomeRNAii50515.
    NextBioi53094.
    PROiQ9NPF2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NPF2.
    CleanExiHS_CHST11.
    ExpressionAtlasiQ9NPF2. baseline and differential.
    GenevisibleiQ9NPF2. HS.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning, expression, and chromosomal mapping of human chondroitin 4-sulfotransferase, whose expression pattern in human tissues is different from that of chondroitin 6-sulfotransferase."
      Okuda T., Mita S., Yamauchi S., Matsubara T., Yagi F., Yamamori D., Fukuta M., Kuroiwa A., Matsuda Y., Habuchi O.
      J. Biochem. 128:763-770(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    2. "Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family."
      Hiraoka N., Nakagawa H., Ong E., Akama O.T., Fukuda N.M., Fukuda M.
      J. Biol. Chem. 275:20188-20196(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
    3. "Cloning and expression of a human chondroitin-4-sulfotransferase similar to members of the HNK-1 sulfotransferase family."
      Xia G., Evers M.R., Schachner M.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    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).
    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.
    7. "Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor. Implication of differential roles in dermatan sulfate biosynthesis."
      Mikami T., Mizumoto S., Kago N., Kitagawa H., Sugahara K.
      J. Biol. Chem. 278:36115-36127(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    8. "Deregulation of the carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11) gene in a B-cell chronic lymphocytic leukemia with a t(12;14)(q23;q32)."
      Schmidt H.H., Dyomin V.G., Palanisamy N., Itoyama T., Nanjangud G., Pirc-Danoewinata H., Haas O.A., Chaganti R.S.K.
      Oncogene 23:6991-6996(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH IGH.
    9. "N-linked oligosaccharides are required to produce and stabilize the active form of chondroitin 4-sulphotransferase-1."
      Yusa A., Kitajima K., Habuchi O.
      Biochem. J. 388:115-121(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, MUTAGENESIS OF LYS-125; ASN-205; ASN-223 AND ASN-342.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCHSTB_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPF2
    Secondary accession number(s): A8K4F8, Q9NXY6, Q9NY36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: October 1, 2000
    Last modified: July 22, 2015
    This is version 115 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 12
      Human chromosome 12: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.