Q9NS84 (CHST7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbohydrate sulfotransferase 7
EC=2.8.2.-
EC=2.8.2.17

Alternative name(s):
Chondroitin 6-sulfotransferase 2
Short name=C6ST-2
Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5
Short name=GST-5
N-acetylglucosamine 6-O-sulfotransferase 4
Short name=GlcNAc6ST-4
Short name=Gn6st-4

Gene names

Name:

CHST7

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	486 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 non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc. Ref.1 Ref.2 Ref.5
Catalytic activity	3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Widely expressed. Highly expressed in heart, spleen, liver and ovary. Expressed at lower level in brain, placenta, thyroid, spinal cord and peripheral blood leukocytes. Not expressed in adult skin. Ref.1 Ref.2 Ref.5
Sequence similarities	Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
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	N-acetylglucosamine metabolic process Inferred from direct assay Ref.1. Source: UniProtKB chondroitin sulfate biosynthetic process Inferred from direct assay Ref.2. Source: UniProtKB polysaccharide metabolic process Traceable author statement Ref.2. Source: UniProtKB
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	N-acetylglucosamine 6-O-sulfotransferase activity Inferred from direct assay Ref.1. Source: UniProtKB chondroitin 6-sulfotransferase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 486	486	Carbohydrate sulfotransferase 7		PRO_0000085198
Regions
	Topological domain	1 – 13	13	Cytoplasmic Potential
	Transmembrane	14 – 34	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	35 – 486	452	Lumenal Potential
	Nucleotide binding	110 – 116	7	PAPS By similarity
	Nucleotide binding	278 – 286	9	PAPS By similarity
Amino acid modifications
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	186	1	N-linked (GlcNAc...) Potential
	Glycosylation	407	1	N-linked (GlcNAc...) Ref.6
Experimental info
	Sequence conflict	448	1	A → V in BAB03217. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NS84 [UniParc]. Last modified March 15, 2005. Version 2. Checksum: 3F1FD1430B3C8E95	FASTA	486	54,266
	10 20 30 40 50 60 MKGRRRRRRE YCKFALLLVL YTLVLLLVPS VLDGGRDGDK GAEHCPGLQR SLGVWSLEAA 70 80 90 100 110 120 AAGEREQGAE ARAAEEGGAN QSPRFPSNLS GAVGEAVSRE KQHIYVHATW RTGSSFLGEL 130 140 150 160 170 180 FNQHPDVFYL YEPMWHLWQA LYPGDAESLQ GALRDMLRSL FRCDFSVLRL YAPPGDPAAR 190 200 210 220 230 240 APDTANLTTA ALFRWRTNKV ICSPPLCPGA PRARAEVGLV EDTACERSCP PVAIRALEAE 250 260 270 280 290 300 CRKYPVVVIK DVRLLDLGVL VPLLRDPGLN LKVVQLFRDP RAVHNSRLKS RQGLLRESIQ 310 320 330 340 350 360 VLRTRQRGDR FHRVLLAHGV GARPGGQSRA LPAAPRADFF LTGALEVICE AWLRDLLFAR 370 380 390 400 410 420 GAPAWLRRRY LRLRYEDLVR QPRAQLRRLL RFSGLRALAA LDAFALNMTR GAAYGADRPF 430 440 450 460 470 480 HLSARDAREA VHAWRERLSR EQVRQVEAAC APAMRLLAYP RSGEEGDAEQ PREGETPLEM DADGAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities." Uchimura K., Fasakhany F., Kadomatsu K., Matsukawa T., Yamakawa T., Kurosawa N., Muramatsu T. Biochem. Biophys. Res. Commun. 274:291-296(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Brain.
[2]	"Molecular cloning and expression of a novel chondroitin 6-O-sulfotransferase." Kitagawa H., Fujita M., Ito N., Sugahara K. J. Biol. Chem. 275:21075-21080(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Brain.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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.
[5]	"Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5)." Bhakta S., Bartes A., Bowman K.G., Kao W.-M., Polsky I., Lee J.-K., Cook B.N., Bruehl R.E., Rosen S.D., Bertozzi C.R., Hemmerich S. J. Biol. Chem. 275:40226-40234(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-407, MASS SPECTROMETRY. Tissue: Plasma.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB040711 mRNA. Translation: BAB13770.1. AB037187 mRNA. Translation: BAB03217.1. AL022165 Genomic DNA. Translation: CAA18154.1. BC045537 mRNA. Translation: AAH45537.1.
IPI	IPI00008403.
PIR	JC7351.
RefSeq	NP_063939.2. NM_019886.2.
UniGene	Hs.129955.
3D structure databases
ProteinModelPortal	Q9NS84.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000276055.
PTM databases
PhosphoSite	Q9NS84.
Polymorphism databases
DMDM	61212141.
Proteomic databases
PaxDb	Q9NS84.
PRIDE	Q9NS84.
Protocols and materials databases
DNASU	56548.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000276055; ENSP00000276055; ENSG00000147119.
GeneID	56548.
KEGG	hsa:56548.
UCSC	uc004dgt.3. human.
Organism-specific databases
CTD	56548.
GeneCards	GC0XP046433.
HGNC	HGNC:13817. CHST7.
HPA	HPA003919.
MIM	300375. gene.
neXtProt	NX_Q9NS84.
PharmGKB	PA26507.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG71363.
HOGENOM	HOG000261614.
HOVERGEN	HBG050949.
InParanoid	Q9NS84.
KO	K04743.
OMA	GDRFHRV.
OrthoDB	EOG4TQM96.
Enzyme and pathway databases
BioCyc	MetaCyc:HS07394-MONOMER.
BRENDA	2.8.2.17. 2681.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
SABIO-RK	Q9NS84.
Gene expression databases
Bgee	Q9NS84.
CleanEx	HS_CHST7.
Genevestigator	Q9NS84.
GermOnline	ENSG00000147119. 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	56548.
NextBio	62035.
SOURCE	Search...

Entry information

Entry name

CHST7_HUMAN

Accession

Primary (citable) accession number: Q9NS84
Secondary accession number(s): O75667

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 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.