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Q9NPF2 (CHSTB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CHST11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate. Ref.1 Ref.2

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Widely expressed. Highly expressed in spleen, thymus, bone marrow, peripheral blood leukocytes, lymph node, heart, brain, lung and placenta. Ref.1 Ref.2

Post-translational modification

N-glycosylated; required for activity and stability. Ref.9

Involvement in disease

A chromosomal aberration involving CHST11 is found in B-cell chronic lymphocytic leukemias. Translocation t(12;14)(q23;q32) with IgH. Ref.8

Sequence similarities

Belongs to the sulfotransferase 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.5 µM for PAPS Ref.9

KM=2.1 mM for chondroitin

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate biosynthetic process

Inferred from electronic annotation. Source: InterPro

carbohydrate metabolic process

Traceable author statement. Source: Reactome

chondrocyte development

Inferred from electronic annotation. Source: Ensembl

chondroitin sulfate biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

developmental growth

Inferred from electronic annotation. Source: Ensembl

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic viscerocranium morphogenesis

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

polysaccharide localization

Inferred from electronic annotation. Source: Ensembl

post-anal tail morphogenesis

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionN-acetylgalactosamine 4-O-sulfotransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity

Inferred from electronic annotation. Source: Ensembl

chondroitin 4-sulfotransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NPF2-1)

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.
Isoform 2 (identifier: Q9NPF2-2)

Also known as: C4S-1A;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Carbohydrate sulfotransferase 11
PRO_0000189664

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain38 – 352315Lumenal Potential
Nucleotide binding124 – 1307PAPS By similarity
Nucleotide binding186 – 1949PAPS By similarity

Amino acid modifications

Glycosylation2051N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Probable

Natural variations

Alternative sequence35 – 406SMLHPV → I in isoform 2.
VSP_012992

Experimental info

Mutagenesis1251K → Q: Abolishes enzyme activity but does not affect stability of the protein. Ref.9
Mutagenesis2051N → 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. Ref.9
Mutagenesis2231N → 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. Ref.9
Mutagenesis3211N → 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.
Mutagenesis3421N → S: Induces a strong decrease in enzyme activity has no effect on stability of the protein. Ref.9
Sequence conflict2891V → F in CAB87380. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 55DF1D29D6703307

FASTA35241,555
        10         20         30         40         50         60 
MKPALLEVMR MNRICRMVLA TCLGSFILVI FYFQSMLHPV MRRNPFGVDI CCRKGSRSPL 

        70         80         90        100        110        120 
QELYNPIQLE LSNTAVLHQM RRDQVTDTCR ANSATSRKRR VLTPNDLKHL VVDEDHELIY 

       130        140        150        160        170        180 
CYVPKVACTN WKRLMMVLTG RGKYSDPMEI PANEAHVSAN LKTLNQYSIP EINHRLKSYM 

       190        200        210        220        230        240 
KFLFVREPFE RLVSAYRNKF TQKYNISFHK RYGTKIIKRQ RKNATQEALR KGDDVKFEEF 

       250        260        270        280        290        300 
VAYLIDPHTQ REEPFNEHWQ TVYSLCHPCH IHYDLVGKYE TLEEDSNYVL QLAGVGSYLK 

       310        320        330        340        350 
FPTYAKSTRT TDEMTTEFFQ NISSEHQTQL YEVYKLDFLM FNYSVPSYLK LE 

« Hide

Isoform 2 (C4S-1A) [UniParc].

Checksum: DEB2646BC0CA5FF8
Show »

FASTA34741,003

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS55878.1. [Q9NPF2-2]
CCDS9099.1. [Q9NPF2-1]
PIRJC7525.
RefSeqNP_001167453.1. NM_001173982.1. [Q9NPF2-2]
NP_060883.1. NM_018413.5. [Q9NPF2-1]
UniGeneHs.17569.

3D structure databases

ProteinModelPortalQ9NPF2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000305725.

PTM databases

PhosphoSiteQ9NPF2.

Polymorphism databases

DMDM61212137.

Proteomic databases

MaxQBQ9NPF2.
PaxDbQ9NPF2.
PRIDEQ9NPF2.

Protocols and materials databases

DNASU50515.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303694; ENSP00000305725; ENSG00000171310. [Q9NPF2-1]
ENST00000549260; ENSP00000450004; ENSG00000171310. [Q9NPF2-2]
GeneID50515.
KEGGhsa:50515.
UCSCuc001tky.3. human. [Q9NPF2-2]
uc001tkz.3. human. [Q9NPF2-1]

Organism-specific databases

CTD50515.
GeneCardsGC12P104849.
HGNCHGNC:17422. CHST11.
HPAHPA052828.
MIM610128. gene.
neXtProtNX_Q9NPF2.
PharmGKBPA134875681.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296625.
HOGENOMHOG000231801.
HOVERGENHBG050952.
InParanoidQ9NPF2.
KOK01017.
OMATCRANSV.
PhylomeDBQ9NPF2.
TreeFamTF325581.

Enzyme and pathway databases

BioCycMetaCyc:HS10284-MONOMER.
BRENDA2.8.2.5. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ9NPF2.
BgeeQ9NPF2.
CleanExHS_CHST11.
GenevestigatorQ9NPF2.

Family and domain databases

InterProIPR018011. Carb_sulfotransferase-rel.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERPTHR12137. PTHR12137. 1 hit.
PfamPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHST11. human.
GeneWikiCHST11.
GenomeRNAi50515.
NextBio53094.
PROQ9NPF2.
SOURCESearch...

Entry information

Entry nameCHSTB_HUMAN
AccessionPrimary (citable) accession number: Q9NPF2
Secondary accession number(s): A8K4F8, Q9NXY6, Q9NY36
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM