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Q9NPF2

- CHSTB_HUMAN

UniProt

Q9NPF2 - CHSTB_HUMAN

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Protein

Carbohydrate sulfotransferase 11

Gene
CHST11
Organism
Homo sapiens (Human)
Status
Reviewed - 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 chondroitin

Regions

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

GO - Molecular functioni

  1. chondroitin 4-sulfotransferase activity Source: UniProtKB
  2. N-acetylgalactosamine 4-O-sulfotransferase activity Source: UniProtKB
  3. N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity Source: Ensembl

GO - Biological processi

  1. carbohydrate biosynthetic process Source: InterPro
  2. carbohydrate metabolic process Source: Reactome
  3. chondrocyte development Source: Ensembl
  4. chondroitin sulfate biosynthetic process Source: UniProtKB
  5. chondroitin sulfate metabolic process Source: Reactome
  6. developmental growth Source: Ensembl
  7. embryonic digit morphogenesis Source: Ensembl
  8. embryonic viscerocranium morphogenesis Source: Ensembl
  9. glycosaminoglycan metabolic process Source: Reactome
  10. negative regulation of apoptotic process Source: Ensembl
  11. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  12. polysaccharide localization Source: Ensembl
  13. post-anal tail morphogenesis Source: Ensembl
  14. post-embryonic development Source: Ensembl
  15. regulation of cell proliferation Source: Ensembl
  16. respiratory gaseous exchange Source: Ensembl
  17. small molecule metabolic process Source: Reactome
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: Chromosome 12

Organism-specific databases

HGNCiHGNC:17422. CHST11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei17 – 3721Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini38 – 352315Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of 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.1 Publication

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.

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...) Reviewed prediction
Glycosylationi223 – 2231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi321 – 3211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi342 – 3421N-linked (GlcNAc...) Inferred

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

ArrayExpressiQ9NPF2.
BgeeiQ9NPF2.
CleanExiHS_CHST11.
GenevestigatoriQ9NPF2.

Organism-specific databases

HPAiHPA052828.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000305725.

Structurei

3D structure databases

ProteinModelPortaliQ9NPF2.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG296625.
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. Align

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

MKPALLEVMR MNRICRMVLA TCLGSFILVI FYFQSMLHPV MRRNPFGVDI    50
CCRKGSRSPL QELYNPIQLE LSNTAVLHQM RRDQVTDTCR ANSATSRKRR 100
VLTPNDLKHL VVDEDHELIY CYVPKVACTN WKRLMMVLTG RGKYSDPMEI 150
PANEAHVSAN LKTLNQYSIP EINHRLKSYM KFLFVREPFE RLVSAYRNKF 200
TQKYNISFHK RYGTKIIKRQ RKNATQEALR KGDDVKFEEF VAYLIDPHTQ 250
REEPFNEHWQ TVYSLCHPCH IHYDLVGKYE TLEEDSNYVL QLAGVGSYLK 300
FPTYAKSTRT TDEMTTEFFQ NISSEHQTQL YEVYKLDFLM FNYSVPSYLK 350
LE 352
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 406SMLHPV → I in isoform 2. VSP_012992

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891V → F in CAB87380. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [Q9NPF2-1]
ENST00000549260; ENSP00000450004; ENSG00000171310. [Q9NPF2-2]
GeneIDi50515.
KEGGihsa:50515.
UCSCiuc001tky.3. human. [Q9NPF2-2]
uc001tkz.3. human. [Q9NPF2-1]

Polymorphism databases

DMDMi61212137.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS55878.1. [Q9NPF2-2 ]
CCDS9099.1. [Q9NPF2-1 ]
PIRi JC7525.
RefSeqi NP_001167453.1. NM_001173982.1. [Q9NPF2-2 ]
NP_060883.1. NM_018413.5. [Q9NPF2-1 ]
UniGenei Hs.17569.

3D structure databases

ProteinModelPortali Q9NPF2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000305725.

PTM databases

PhosphoSitei Q9NPF2.

Polymorphism databases

DMDMi 61212137.

Proteomic databases

MaxQBi Q9NPF2.
PaxDbi Q9NPF2.
PRIDEi Q9NPF2.

Protocols and materials databases

DNASUi 50515.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303694 ; ENSP00000305725 ; ENSG00000171310 . [Q9NPF2-1 ]
ENST00000549260 ; ENSP00000450004 ; ENSG00000171310 . [Q9NPF2-2 ]
GeneIDi 50515.
KEGGi hsa:50515.
UCSCi uc001tky.3. human. [Q9NPF2-2 ]
uc001tkz.3. human. [Q9NPF2-1 ]

Organism-specific databases

CTDi 50515.
GeneCardsi GC12P104849.
HGNCi HGNC:17422. CHST11.
HPAi HPA052828.
MIMi 610128. gene.
neXtProti NX_Q9NPF2.
PharmGKBi PA134875681.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296625.
HOGENOMi HOG000231801.
HOVERGENi HBG050952.
InParanoidi Q9NPF2.
KOi K01017.
OMAi TCRANSV.
PhylomeDBi Q9NPF2.
TreeFami TF325581.

Enzyme and pathway databases

BioCyci MetaCyc:HS10284-MONOMER.
BRENDAi 2.8.2.5. 2681.
Reactomei REACT_120989. Chondroitin sulfate biosynthesis.

Miscellaneous databases

ChiTaRSi CHST11. human.
GeneWikii CHST11.
GenomeRNAii 50515.
NextBioi 53094.
PROi Q9NPF2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NPF2.
Bgeei Q9NPF2.
CleanExi HS_CHST11.
Genevestigatori Q9NPF2.

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

« 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: September 3, 2014
This is version 106 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

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