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Protein

Carbohydrate sulfotransferase 7

Gene

CHST7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi110 – 1167PAPSBy similarity
Nucleotide bindingi278 – 2869PAPSBy similarity

GO - Molecular functioni

  • chondroitin 6-sulfotransferase activity Source: UniProtKB
  • N-acetylglucosamine 6-O-sulfotransferase activity Source: UniProtKB

GO - Biological processi

  • carbohydrate metabolic process Source: Reactome
  • chondroitin sulfate biosynthetic process Source: UniProtKB
  • chondroitin sulfate metabolic process Source: Reactome
  • glycosaminoglycan metabolic process Source: Reactome
  • N-acetylglucosamine metabolic process Source: UniProtKB
  • polysaccharide metabolic process Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • sulfur compound metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS07394-MONOMER.
BRENDAi2.8.2.17. 2681.
ReactomeiREACT_120989. Chondroitin sulfate biosynthesis.
SABIO-RKQ9NS84.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CHST7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:13817. CHST7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini35 – 486452LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26507.

Polymorphism and mutation databases

BioMutaiCHST7.
DMDMi61212141.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Carbohydrate sulfotransferase 7PRO_0000085198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi407 – 4071N-linked (GlcNAc...)1 Publication
Modified residuei462 – 4621Phosphoserine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NS84.
PaxDbiQ9NS84.
PRIDEiQ9NS84.

PTM databases

PhosphoSiteiQ9NS84.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiQ9NS84.
CleanExiHS_CHST7.
GenevisibleiQ9NS84. HS.

Organism-specific databases

HPAiHPA003919.

Interactioni

Protein-protein interaction databases

BioGridi121152. 2 interactions.
STRINGi9606.ENSP00000276055.

Structurei

3D structure databases

ProteinModelPortaliQ9NS84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71363.
GeneTreeiENSGT00530000062902.
HOGENOMiHOG000261614.
HOVERGENiHBG050949.
InParanoidiQ9NS84.
KOiK04743.
OMAiDKGAGHC.
OrthoDBiEOG7RZ5S0.
PhylomeDBiQ9NS84.
TreeFamiTF342871.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.

Sequencei

Sequence statusi: Complete.

Q9NS84-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGRRRRRRE YCKFALLLVL YTLVLLLVPS VLDGGRDGDK GAEHCPGLQR
60 70 80 90 100
SLGVWSLEAA AAGEREQGAE ARAAEEGGAN QSPRFPSNLS GAVGEAVSRE
110 120 130 140 150
KQHIYVHATW RTGSSFLGEL FNQHPDVFYL YEPMWHLWQA LYPGDAESLQ
160 170 180 190 200
GALRDMLRSL FRCDFSVLRL YAPPGDPAAR APDTANLTTA ALFRWRTNKV
210 220 230 240 250
ICSPPLCPGA PRARAEVGLV EDTACERSCP PVAIRALEAE CRKYPVVVIK
260 270 280 290 300
DVRLLDLGVL VPLLRDPGLN LKVVQLFRDP RAVHNSRLKS RQGLLRESIQ
310 320 330 340 350
VLRTRQRGDR FHRVLLAHGV GARPGGQSRA LPAAPRADFF LTGALEVICE
360 370 380 390 400
AWLRDLLFAR GAPAWLRRRY LRLRYEDLVR QPRAQLRRLL RFSGLRALAA
410 420 430 440 450
LDAFALNMTR GAAYGADRPF HLSARDAREA VHAWRERLSR EQVRQVEAAC
460 470 480
APAMRLLAYP RSGEEGDAEQ PREGETPLEM DADGAT
Length:486
Mass (Da):54,266
Last modified:March 15, 2005 - v2
Checksum:i3F1FD1430B3C8E95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti448 – 4481A → V in BAB03217 (PubMed:10781596).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040711 mRNA. Translation: BAB13770.1.
AB037187 mRNA. Translation: BAB03217.1.
AL022165 Genomic DNA. Translation: CAA18154.1.
BC045537 mRNA. Translation: AAH45537.1.
CCDSiCCDS14268.1.
PIRiJC7351.
RefSeqiNP_063939.2. NM_019886.3.
UniGeneiHs.129955.

Genome annotation databases

EnsembliENST00000276055; ENSP00000276055; ENSG00000147119.
GeneIDi56548.
KEGGihsa:56548.
UCSCiuc004dgt.3. human.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040711 mRNA. Translation: BAB13770.1.
AB037187 mRNA. Translation: BAB03217.1.
AL022165 Genomic DNA. Translation: CAA18154.1.
BC045537 mRNA. Translation: AAH45537.1.
CCDSiCCDS14268.1.
PIRiJC7351.
RefSeqiNP_063939.2. NM_019886.3.
UniGeneiHs.129955.

3D structure databases

ProteinModelPortaliQ9NS84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121152. 2 interactions.
STRINGi9606.ENSP00000276055.

PTM databases

PhosphoSiteiQ9NS84.

Polymorphism and mutation databases

BioMutaiCHST7.
DMDMi61212141.

Proteomic databases

MaxQBiQ9NS84.
PaxDbiQ9NS84.
PRIDEiQ9NS84.

Protocols and materials databases

DNASUi56548.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276055; ENSP00000276055; ENSG00000147119.
GeneIDi56548.
KEGGihsa:56548.
UCSCiuc004dgt.3. human.

Organism-specific databases

CTDi56548.
GeneCardsiGC0XP046433.
HGNCiHGNC:13817. CHST7.
HPAiHPA003919.
MIMi300375. gene.
neXtProtiNX_Q9NS84.
PharmGKBiPA26507.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG71363.
GeneTreeiENSGT00530000062902.
HOGENOMiHOG000261614.
HOVERGENiHBG050949.
InParanoidiQ9NS84.
KOiK04743.
OMAiDKGAGHC.
OrthoDBiEOG7RZ5S0.
PhylomeDBiQ9NS84.
TreeFamiTF342871.

Enzyme and pathway databases

BioCyciMetaCyc:HS07394-MONOMER.
BRENDAi2.8.2.17. 2681.
ReactomeiREACT_120989. Chondroitin sulfate biosynthesis.
SABIO-RKQ9NS84.

Miscellaneous databases

GeneWikiiCHST7.
GenomeRNAii56548.
NextBioi62035.
PROiQ9NS84.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NS84.
CleanExiHS_CHST7.
GenevisibleiQ9NS84. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMiSSF52540. SSF52540. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCHST7_HUMAN
AccessioniPrimary (citable) accession number: Q9NS84
Secondary accession number(s): O75667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 22, 2015
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.