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Q9NS84

- CHST7_HUMAN

UniProt

Q9NS84 - CHST7_HUMAN

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Protein
Carbohydrate sulfotransferase 7
Gene
CHST7
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 1167PAPS By similarity
Nucleotide bindingi278 – 2869PAPS By similarity

GO - Molecular functioni

  1. N-acetylglucosamine 6-O-sulfotransferase activity Source: UniProtKB
  2. chondroitin 6-sulfotransferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. N-acetylglucosamine metabolic process Source: UniProtKB
  2. carbohydrate metabolic process Source: Reactome
  3. chondroitin sulfate biosynthetic process Source: UniProtKB
  4. chondroitin sulfate metabolic process Source: Reactome
  5. glycosaminoglycan metabolic process Source: Reactome
  6. polysaccharide metabolic process Source: UniProtKB
  7. small molecule metabolic process Source: Reactome
  8. 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: Chromosome X

Organism-specific databases

HGNCiHGNC:13817. CHST7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini35 – 486452Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26507.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi186 – 1861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi407 – 4071N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

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.
GenevestigatoriQ9NS84.

Organism-specific databases

HPAiHPA003919.

Interactioni

Protein-protein interaction databases

BioGridi121152. 1 interaction.
STRINGi9606.ENSP00000276055.

Structurei

3D structure databases

ProteinModelPortaliQ9NS84.
SMRiQ9NS84. Positions 101-139, 367-458.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71363.
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

MKGRRRRRRE YCKFALLLVL YTLVLLLVPS VLDGGRDGDK GAEHCPGLQR    50
SLGVWSLEAA AAGEREQGAE ARAAEEGGAN QSPRFPSNLS GAVGEAVSRE 100
KQHIYVHATW RTGSSFLGEL FNQHPDVFYL YEPMWHLWQA LYPGDAESLQ 150
GALRDMLRSL FRCDFSVLRL YAPPGDPAAR APDTANLTTA ALFRWRTNKV 200
ICSPPLCPGA PRARAEVGLV EDTACERSCP PVAIRALEAE CRKYPVVVIK 250
DVRLLDLGVL VPLLRDPGLN LKVVQLFRDP RAVHNSRLKS RQGLLRESIQ 300
VLRTRQRGDR FHRVLLAHGV GARPGGQSRA LPAAPRADFF LTGALEVICE 350
AWLRDLLFAR GAPAWLRRRY LRLRYEDLVR QPRAQLRRLL RFSGLRALAA 400
LDAFALNMTR GAAYGADRPF HLSARDAREA VHAWRERLSR EQVRQVEAAC 450
APAMRLLAYP RSGEEGDAEQ PREGETPLEM DADGAT 486
Length:486
Mass (Da):54,266
Last modified:March 15, 2005 - v2
Checksum:i3F1FD1430B3C8E95
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti448 – 4481A → V in BAB03217. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi61212141.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB040711 mRNA. Translation: BAB13770.1 .
AB037187 mRNA. Translation: BAB03217.1 .
AL022165 Genomic DNA. Translation: CAA18154.1 .
BC045537 mRNA. Translation: AAH45537.1 .
CCDSi CCDS14268.1.
PIRi JC7351.
RefSeqi NP_063939.2. NM_019886.3.
UniGenei Hs.129955.

3D structure databases

ProteinModelPortali Q9NS84.
SMRi Q9NS84. Positions 101-139, 367-458.
ModBasei Search...

Protein-protein interaction databases

BioGridi 121152. 1 interaction.
STRINGi 9606.ENSP00000276055.

PTM databases

PhosphoSitei Q9NS84.

Polymorphism databases

DMDMi 61212141.

Proteomic databases

MaxQBi Q9NS84.
PaxDbi Q9NS84.
PRIDEi Q9NS84.

Protocols and materials databases

DNASUi 56548.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276055 ; ENSP00000276055 ; ENSG00000147119 .
GeneIDi 56548.
KEGGi hsa:56548.
UCSCi uc004dgt.3. human.

Organism-specific databases

CTDi 56548.
GeneCardsi GC0XP046433.
HGNCi HGNC:13817. CHST7.
HPAi HPA003919.
MIMi 300375. gene.
neXtProti NX_Q9NS84.
PharmGKBi PA26507.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71363.
HOGENOMi HOG000261614.
HOVERGENi HBG050949.
InParanoidi Q9NS84.
KOi K04743.
OMAi DKGAGHC.
OrthoDBi EOG7RZ5S0.
PhylomeDBi Q9NS84.
TreeFami TF342871.

Enzyme and pathway databases

BioCyci MetaCyc:HS07394-MONOMER.
BRENDAi 2.8.2.17. 2681.
Reactomei REACT_120989. Chondroitin sulfate biosynthesis.
SABIO-RK Q9NS84.

Miscellaneous databases

GeneWikii CHST7.
GenomeRNAii 56548.
NextBioi 62035.
PROi Q9NS84.
SOURCEi Search...

Gene expression databases

Bgeei Q9NS84.
CleanExi HS_CHST7.
Genevestigatori Q9NS84.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view ]
Pfami PF00685. Sulfotransfer_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMi SSF52540. SSF52540. 3 hits.
ProtoNeti Search...

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.

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: September 3, 2014
This is version 106 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