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Q8NCG5 (CHST4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbohydrate sulfotransferase 4

EC=2.8.2.-
Alternative name(s):
Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3
Short name=GST-3
High endothelial cells N-acetylglucosamine 6-O-sulfotransferase
Short name=HEC-GlcNAc6ST
L-selectin ligand sulfotransferase
Short name=LSST
N-acetylglucosamine 6-O-sulfotransferase 2
Short name=GlcNAc6ST-2
Short name=Gn6st-2
Gene names
Name:CHST4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 within mucin-associated glycans that ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X on receptors SPN/CD43, GLYCAM1 and MADCAM1. Also involved in biosynthesis of SELL ligand recognized by MECA-79 antibody. Plays a central role in lymphocyte trafficking during chronic inflammation. Has a catalytic preference for core 2-branched mucin-type O-glycans. Can use GlcNAcbeta1-6[Galbeta1-3]GalNAc-pNP (core 2), GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharide structures as acceptors. Has also activity toward core 3 of GlcNAcbeta1-3GalNAc-pNP. Its substrate specificity may be influenced by its subcellular location. Ref.1

Subunit structure

Monomer. Ref.10

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.9.

Tissue specificity

Specifically expressed in HEV. Weakly expressed in spleen. Not expressed in other tissues. Expressed in colonic mucinous adenocarcinoma. Ref.1 Ref.6 Ref.7

Induction

Upon cytokine activation, it is expressed at low level. Ref.6

Miscellaneous

May serve as a antiinflammatory target.

Sequence similarities

Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily.

Sequence caution

The sequence AAH35282.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Inflammatory response
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylglucosamine metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

carbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

cellular component movement

Traceable author statement Ref.1. Source: ProtInc

immune response

Traceable author statement Ref.1. Source: ProtInc

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte tethering or rolling

Inferred from electronic annotation. Source: Ensembl

protein sulfation

Traceable author statement Ref.1. Source: ProtInc

sulfur compound metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of Golgi membrane

Non-traceable author statement Ref.9. Source: UniProtKB

trans-Golgi network

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionN-acetylglucosamine 6-O-sulfotransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

sulfotransferase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Carbohydrate sulfotransferase 4
PRO_0000085193

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 386358Lumenal Potential
Nucleotide binding51 – 577PAPS By similarity
Nucleotide binding205 – 2139PAPS By similarity

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential

Natural variations

Natural variant3611H → Q.
Corresponds to variant rs3813744 [ dbSNP | Ensembl ].
VAR_052528

Experimental info

Sequence conflict2251S → N in BAC11177. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8NCG5 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: 0C3BB4022417143A

FASTA38645,134
        10         20         30         40         50         60 
MLLPKKMKLL LFLVSQMAIL ALFFHMYSHN ISSLSMKAQP ERMHVLVLSS WRSGSSFVGQ 

        70         80         90        100        110        120 
LFGQHPDVFY LMEPAWHVWM TFKQSTAWML HMAVRDLIRA VFLCDMSVFD AYMEPGPRRQ 

       130        140        150        160        170        180 
SSLFQWENSR ALCSAPACDI IPQDEIIPRA HCRLLCSQQP FEVVEKACRS YSHVVLKEVR 

       190        200        210        220        230        240 
FFNLQSLYPL LKDPSLNLHI VHLVRDPRAV FRSRERTKGD LMIDSRIVMG QHEQKLKKED 

       250        260        270        280        290        300 
QPYYVMQVIC QSQLEIYKTI QSLPKALQER YLLVRYEDLA RAPVAQTSRM YEFVGLEFLP 

       310        320        330        340        350        360 
HLQTWVHNIT RGKGMGDHAF HTNARDALNV SQAWRWSLPY EKVSRLQKAC GDAMNLLGYR 

       370        380 
HVRSEQEQRN LLLDLLSTWT VPEQIH 

« Hide

References

« Hide 'large scale' references
[1]"Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin."
Bistrup A., Bhakta S., Lee J.K., Belov Y.Y., Gunn M.D., Zuo F.-R., Huang C.-C., Kannagi R., Rosen S.D., Hemmerich S.
J. Cell Biol. 145:899-910(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Tonsil.
[2]"Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase."
Yeh J.-C., Hiraoka N., Petryniak B., Nakayama J., Ellies L.G., Rabuka D., Hindsgaul O., Marth J.D., Lowe J.B., Fakuda M.
Cell 105:957-969(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Chromosomal localization and genomic organization for the galactose/ N-acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene family."
Hemmerich S., Lee J.K., Bhakta S., Bistrup A., Ruddle N.R., Rosen S.D.
Glycobiology 11:75-87(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Tonsil.
[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].
Tissue: Teratocarcinoma.
[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].
Tissue: Brain.
[6]"CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells regulates shear-resistant leukocyte rolling via L-selectin."
Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.
J. Leukoc. Biol. 69:565-574(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[7]"Ectopic expression of a GlcNAc 6-O-sulfotransferase, GlcNAc6ST-2, in colonic mucinous adenocarcinoma."
Seko A., Nagata K., Yonezawa S., Yamashita K.
Glycobiology 12:379-388(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to L-selectin ligand synthesis and tumor-associated enzyme expression."
Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E., Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.
J. Biol. Chem. 277:3979-3984(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY.
[9]"Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis."
de Graffenried C.L., Bertozzi C.R.
J. Biol. Chem. 278:40282-40295(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of substrate specificity."
de Graffenried C.L., Bertozzi C.R.
J. Biol. Chem. 279:40035-40043(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF131235 mRNA. Translation: AAD33015.1.
AF149783 mRNA. Translation: AAK48417.1.
AF280088 mRNA. Translation: AAG48246.1.
AK074746 mRNA. Translation: BAC11177.1.
BC035282 mRNA. Translation: AAH35282.1. Different initiation.
CCDSCCDS10902.1.
RefSeqNP_001159867.1. NM_001166395.1.
NP_005760.1. NM_005769.2.
UniGeneHs.251383.

3D structure databases

ProteinModelPortalQ8NCG5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115466. 1 interaction.
IntActQ8NCG5. 1 interaction.
STRING9606.ENSP00000341206.

Chemistry

ChEMBLCHEMBL2239.

PTM databases

PhosphoSiteQ8NCG5.

Polymorphism databases

DMDM61211834.

Proteomic databases

PaxDbQ8NCG5.
PRIDEQ8NCG5.

Protocols and materials databases

DNASU10164.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338482; ENSP00000341206; ENSG00000140835.
ENST00000539698; ENSP00000441204; ENSG00000140835.
ENST00000572450; ENSP00000461839; ENSG00000140835.
GeneID10164.
KEGGhsa:10164.
UCSCuc002fan.3. human.

Organism-specific databases

CTD10164.
GeneCardsGC16P071560.
HGNCHGNC:1972. CHST4.
HPAHPA021955.
neXtProtNX_Q8NCG5.
PharmGKBPA26504.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80862.
HOGENOMHOG000261614.
HOVERGENHBG050949.
InParanoidQ8NCG5.
KOK04746.
OMAFHTNARN.
OrthoDBEOG7RZ5S0.
PhylomeDBQ8NCG5.
TreeFamTF342871.

Enzyme and pathway databases

SABIO-RKQ8NCG5.

Gene expression databases

BgeeQ8NCG5.
CleanExHS_CHST4.
GenevestigatorQ8NCG5.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

GeneWikiCHST4.
GenomeRNAi10164.
NextBio38482.
PROQ8NCG5.

Entry information

Entry nameCHST4_HUMAN
AccessionPrimary (citable) accession number: Q8NCG5
Secondary accession number(s): Q8IV46, Q9Y5R3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 96 of the entry and version 2 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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM