O43916 (CHST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbohydrate sulfotransferase 1
EC=2.8.2.21

Alternative name(s):
Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1
Short name=GST-1
Keratan sulfate Gal-6 sulfotransferase
Short name=KS6ST
Short name=KSGal6ST
Short name=KSST

Gene names

Name:

CHST1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence 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 galactose (Gal) residues of keratan. Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal Gal residues are sulfated. May function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. Participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Ref.7 Ref.8
Catalytic activity	3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate. Ref.1
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Widely expressed at low level. Expressed in brain and skeletal muscle. Expressed by high endothelial cells (HEVs) and leukocytes. Ref.1 Ref.9
Sequence similarities	Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily.
Caution	Was originally (Ref.2) thought to be the ortholog of chicken CHST3 and therefore named C6ST. However, it has no strong chondroitin 6-sulfotransferase activity.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Inflammatory response
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	galactose metabolic process Inferred from direct assay Ref.8. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW keratan sulfate biosynthetic process Traceable author statement. Source: Reactome polysaccharide metabolic process Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	keratan sulfotransferase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 411	411	Carbohydrate sulfotransferase 1		PRO_0000085182
Regions
	Topological domain	1 – 2	2	Cytoplasmic Potential
	Transmembrane	3 – 23	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	24 – 411	388	Lumenal Potential
	Nucleotide binding	69 – 75	7	PAPS By similarity
	Nucleotide binding	234 – 242	9	PAPS By similarity
	Motif	337 – 339	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	56	1	N-linked (GlcNAc...) Potential
	Glycosylation	145	1	N-linked (GlcNAc...) Potential
	Glycosylation	189	1	N-linked (GlcNAc...) Potential
	Glycosylation	334	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O43916 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: F07D0A23B6338A09	FASTA	411	46,715
	10 20 30 40 50 60 MQCSWKAVLL LALASIAIQY TAIRTFTAKS FHTCPGLAEA GLAERLCEES PTFAYNLSRK 70 80 90 100 110 120 THILILATTR SGSSFVGQLF NQHLDVFYLF EPLYHVQNTL IPRFTQGKSP ADRRVMLGAS 130 140 150 160 170 180 RDLLRSLYDC DLYFLENYIK PPPVNHTTDR IFRRGASRVL CSRPVCDPPG PADLVLEEGD 190 200 210 220 230 240 CVRKCGLLNL TVAAEACRER SHVAIKTVRV PEVNDLRALV EDPRLNLKVI QLVRDPRGIL 250 260 270 280 290 300 ASRSETFRDT YRLWRLWYGT GRKPYNLDVT QLTTVCEDFS NSVSTGLMRP PWLKGKYMLV 310 320 330 340 350 360 RYEDLARNPM KKTEEIYGFL GIPLDSHVAR WIQNNTRGDP TLGKHKYGTV RNSAATAEKW 370 380 390 400 410 RFRLSYDIVA FAQNACQQVL AQLGYKIAAS EEELKNPSVS LVEERDFRPF S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of human keratan sulfate Gal-6-sulfotransferase." Fukuta M., Inazawa J., Torii T., Tsuzuki K., Shimada E., Habuchi O. J. Biol. Chem. 272:32321-32328(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Fetal brain.
[2]	"Human chondroitin 6-sulfotransferase: cloning, gene structure, and chromosomal localization." Mazany K.D., Peng T., Watson C.E., Tabas I., Williams K.J. Biochim. Biophys. Acta 1407:92-97(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"CHST1 and CHST2 sulfotransferases expressed by human vascular endothelial cells: cDNA cloning, expression, and chromosomal localization." Li X., Tedder T.F. Genomics 55:345-347(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Umbilical vein endothelial cell.
[4]	NIEHS SNPs program Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. , 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 (SEP-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]. Tissue: Brain.
[7]	"Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase." Torii T., Fukuta M., Habuchi O. Glycobiology 10:203-211(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE SPECIFICITY, FUNCTION.
[8]	"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: FUNCTION.
[9]	"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.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB003791 mRNA. Translation: BAA24840.1. U65637 mRNA. Translation: AAC28776.1. AF090137 mRNA. Translation: AAD19878.1. AY339617 Genomic DNA. Translation: AAP88041.1. CH471064 Genomic DNA. Translation: EAW68035.1. CH471064 Genomic DNA. Translation: EAW68038.1. BC022567 mRNA. Translation: AAH22567.1. BC028235 mRNA. Translation: AAH28235.1.
IPI	IPI00021119.
RefSeq	NP_003645.1. NM_003654.5.
UniGene	Hs.104576.
3D structure databases
ProteinModelPortal	O43916.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43916. 2 interactions.
MINT	MINT-1440600.
STRING	9606.ENSP00000309270.
PTM databases
PhosphoSite	O43916.
Proteomic databases
PaxDb	O43916.
PRIDE	O43916.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308064; ENSP00000309270; ENSG00000175264.
GeneID	8534.
KEGG	hsa:8534.
UCSC	uc001mys.2. human.
Organism-specific databases
CTD	8534.
GeneCards	GC11M045670.
HGNC	HGNC:1969. CHST1.
MIM	603797. gene.
neXtProt	NX_O43916.
PharmGKB	PA26501.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG80862.
HOGENOM	HOG000261614.
HOVERGEN	HBG106811.
InParanoid	O43916.
KO	K01022.
OMA	LWRIWDG.
OrthoDB	EOG418BNF.
Enzyme and pathway databases
BRENDA	2.8.2.21. 2681.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
SABIO-RK	O43916.
Gene expression databases
Bgee	O43916.
CleanEx	HS_CHST1.
Genevestigator	O43916.
GermOnline	ENSG00000175264. Homo sapiens.
Family and domain databases
InterPro	IPR016469. Carbohydrate_sulfotransferase. IPR000863. Sulfotransferase_dom. [Graphical view]
Pfam	PF00685. Sulfotransfer_1. 1 hit. [Graphical view]
PIRSF	PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	8534.
NextBio	31964.
SOURCE	Search...

Entry information

Entry name

CHST1_HUMAN

Accession

Primary (citable) accession number: O43916
Secondary accession number(s): D3DQP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.