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Q9NS84 (CHST7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Carbohydrate sulfotransferase 7
PRO_0000085198

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain35 – 486452Lumenal Potential
Nucleotide binding110 – 1167PAPS By similarity
Nucleotide binding278 – 2869PAPS By similarity

Amino acid modifications

Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Ref.6

Experimental info

Sequence conflict4481A → V in BAB03217. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9NS84 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: 3F1FD1430B3C8E95

FASTA48654,266
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
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.
PIRJC7351.
RefSeqNP_063939.2. NM_019886.3.
UniGeneHs.129955.

3D structure databases

ProteinModelPortalQ9NS84.
SMRQ9NS84. Positions 101-139, 367-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121152. 1 interaction.
STRING9606.ENSP00000276055.

PTM databases

PhosphoSiteQ9NS84.

Polymorphism databases

DMDM61212141.

Proteomic databases

PaxDbQ9NS84.
PRIDEQ9NS84.

Protocols and materials databases

DNASU56548.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276055; ENSP00000276055; ENSG00000147119.
GeneID56548.
KEGGhsa:56548.
UCSCuc004dgt.3. human.

Organism-specific databases

CTD56548.
GeneCardsGC0XP046433.
HGNCHGNC:13817. CHST7.
HPAHPA003919.
MIM300375. gene.
neXtProtNX_Q9NS84.
PharmGKBPA26507.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71363.
HOGENOMHOG000261614.
HOVERGENHBG050949.
InParanoidQ9NS84.
KOK04743.
OMADKGAGHC.
OrthoDBEOG7RZ5S0.
PhylomeDBQ9NS84.
TreeFamTF342871.

Enzyme and pathway databases

BioCycMetaCyc:HS07394-MONOMER.
BRENDA2.8.2.17. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ9NS84.

Gene expression databases

BgeeQ9NS84.
CleanExHS_CHST7.
GenevestigatorQ9NS84.

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. 3 hits.
ProtoNetSearch...

Other

GeneWikiCHST7.
GenomeRNAi56548.
NextBio62035.
PROQ9NS84.
SOURCESearch...

Entry information

Entry nameCHST7_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 103 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

MIM cross-references

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

Human chromosome X

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