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Q9EP78

- CHST7_MOUSE

UniProt

Q9EP78 - CHST7_MOUSE

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Protein

Carbohydrate sulfotransferase 7

Gene
Chst7, Gst5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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.1 Publication

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 1147PAPS By similarity
Nucleotide bindingi276 – 2849PAPS By similarity

GO - Molecular functioni

  1. chondroitin 6-sulfotransferase activity Source: UniProtKB-EC
  2. N-acetylglucosamine 6-O-sulfotransferase activity Source: Ensembl

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. chondroitin sulfate biosynthetic process Source: Ensembl
  3. N-acetylglucosamine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi2.8.2.17. 3474.
ReactomeiREACT_196514. Chondroitin sulfate biosynthesis.

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
Short name:
mC6ST-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
Synonyms:Gst5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1891767. Chst7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei13 – 3321Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini34 – 484451Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Carbohydrate sulfotransferase 7PRO_0000085199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi184 – 1841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi405 – 4051N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9EP78.

PTM databases

PhosphoSiteiQ9EP78.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in kidney. Expressed at lower level in heart, lung and liver.1 Publication

Gene expression databases

BgeeiQ9EP78.
GenevestigatoriQ9EP78.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043222.

Structurei

3D structure databases

ProteinModelPortaliQ9EP78.
SMRiQ9EP78. Positions 99-137, 365-451.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71363.
GeneTreeiENSGT00530000062902.
HOGENOMiHOG000261614.
HOVERGENiHBG050949.
InParanoidiQ9EP78.
KOiK04743.
OMAiDKGAGHC.
OrthoDBiEOG7RZ5S0.
PhylomeDBiQ9EP78.
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.

Q9EP78-1 [UniParc]FASTAAdd to Basket

« Hide

MKGRRRRRRE YCKFTLLLAL YTLLLLLVPS VLDSHSEQDK GRNCPGLQRS    50
LGVWSLEAAA AGEREQGAEV RSLAEGNPDR SPGSPGNLSA VGEAVTQEKQ 100
HIYVHATWRT GSSFLGELFN QHPDVFYLYE PMWHLWQALY PGDAESLQGA 150
LRDMLRSLFR CDFSVLRLYA QPGDPGERAP DSANLTTAML FRWRTNKVIC 200
SPPLCPAAPR ARADVGLVED KACESTCPPV SLRALEAECR KYPVVVIKDV 250
RLLDLGVLVP LLRDPGLNLK VVQLFRDPRA VHNSRLKSRQ GLLRESIQVL 300
RTRQRGDHFH RVLLAHGVDA RPGGQARALP SAPRADFFLT SALEVICEAW 350
LRDLLFTRGA PAWLRRRYLR LRYEDLVWQP QAQLRRLLRF SGLRTLAALD 400
AFAFNMTRGS AYGADRPFHL SARDAREAVH AWRERLSQEQ VRQVETACAP 450
AMRLLAYPRS GDERDRKTVR EGETPLETKA NWAV 484
Length:484
Mass (Da):54,767
Last modified:March 1, 2001 - v1
Checksum:i9B195537D7AB7193
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101E → K in BAB40372. 1 Publication
Sequence conflicti130 – 1301E → D in BAB40372. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB040710 mRNA. Translation: BAB13769.1.
AF280089 Genomic DNA. Translation: AAG48247.1.
AB046929 mRNA. Translation: BAB40372.1.
AK011202 mRNA. Translation: BAB27465.1.
BC019204 mRNA. Translation: AAH19204.1.
CCDSiCCDS30040.1.
PIRiJC7350.
RefSeqiNP_068361.1. NM_021715.1.
UniGeneiMm.44827.

Genome annotation databases

EnsembliENSMUST00000044138; ENSMUSP00000043222; ENSMUSG00000037347.
GeneIDi60322.
KEGGimmu:60322.
UCSCiuc009sss.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB040710 mRNA. Translation: BAB13769.1 .
AF280089 Genomic DNA. Translation: AAG48247.1 .
AB046929 mRNA. Translation: BAB40372.1 .
AK011202 mRNA. Translation: BAB27465.1 .
BC019204 mRNA. Translation: AAH19204.1 .
CCDSi CCDS30040.1.
PIRi JC7350.
RefSeqi NP_068361.1. NM_021715.1.
UniGenei Mm.44827.

3D structure databases

ProteinModelPortali Q9EP78.
SMRi Q9EP78. Positions 99-137, 365-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000043222.

PTM databases

PhosphoSitei Q9EP78.

Proteomic databases

PRIDEi Q9EP78.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000044138 ; ENSMUSP00000043222 ; ENSMUSG00000037347 .
GeneIDi 60322.
KEGGi mmu:60322.
UCSCi uc009sss.1. mouse.

Organism-specific databases

CTDi 56548.
MGIi MGI:1891767. Chst7.

Phylogenomic databases

eggNOGi NOG71363.
GeneTreei ENSGT00530000062902.
HOGENOMi HOG000261614.
HOVERGENi HBG050949.
InParanoidi Q9EP78.
KOi K04743.
OMAi DKGAGHC.
OrthoDBi EOG7RZ5S0.
PhylomeDBi Q9EP78.
TreeFami TF342871.

Enzyme and pathway databases

BRENDAi 2.8.2.17. 3474.
Reactomei REACT_196514. Chondroitin sulfate biosynthesis.

Miscellaneous databases

NextBioi 314817.
PROi Q9EP78.
SOURCEi Search...

Gene expression databases

Bgeei Q9EP78.
Genevestigatori Q9EP78.

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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6.
  3. "Cloning and expression of mouse chondroitin 6-sulfotransferase-2."
    Kitagawa H., Uyama T., Sugahara K.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  5. "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].
    Strain: FVB/N.
    Tissue: Kidney.

Entry informationi

Entry nameiCHST7_MOUSE
AccessioniPrimary (citable) accession number: Q9EP78
Secondary accession number(s): Q99NB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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