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Protein

Carbohydrate sulfotransferase 10

Gene

Chst10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi127 – 1337PAPSBy similarity
Nucleotide bindingi189 – 1979PAPSBy similarity

GO - Molecular functioni

  • sulfotransferase activity Source: MGI

GO - Biological processi

  • carbohydrate biosynthetic process Source: InterPro
  • learning Source: MGI
  • long-term memory Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Carbohydrate sulfotransferase 10 (EC:2.8.2.-)
Alternative name(s):
HNK-1 sulfotransferase
Short name:
HNK-1ST
Short name:
HNK1ST
Gene namesi
Name:Chst10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2138283. Chst10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 356329LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable, fertile and show normal cerebellar granule neuron migration. The anatomy of all major brain areas are histologically normal. However, basal synaptic transmission in pyramidal cells in the CA1 region of the hippocampus are increased and long-term potentiation evoked by theta-burst stimulation are reduced. Mice show an impaired long-term memory and a poorer spatial learning when a short inter-trial interval is used.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Carbohydrate sulfotransferase 10PRO_0000189658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ6PGK7.
PaxDbiQ6PGK7.
PRIDEiQ6PGK7.

PTM databases

PhosphoSiteiQ6PGK7.

Expressioni

Gene expression databases

BgeeiQ6PGK7.
CleanExiMM_CHST10.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027249.

Structurei

3D structure databases

ProteinModelPortaliQ6PGK7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 2 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4651. Eukaryota.
ENOG4111GJR. LUCA.
HOGENOMiHOG000200781.
HOVERGENiHBG050951.
InParanoidiQ6PGK7.
KOiK09674.

Family and domain databases

InterProiIPR018011. Carb_sulfotransferase-rel.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12137. PTHR12137. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PGK7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDGYSAKQE FVFLTTMPEA
60 70 80 90 100
EKLRGEKHFP EVPKPTGKML SDSRPDQPPV YLERLELIRN TCKEEALRNL
110 120 130 140 150
SHTEVSKFVL DRIFVCDKHK ILFCQTPKVG NTQWKKVLIV LNGAFSSIEE
160 170 180 190 200
IPENVVHDHE KNGLPRLSSF SKIGIQKRLK TYFKFFIVRD PFERLISAFK
210 220 230 240 250
DKFVHNPRFE PWYRHEIAPG IIRKYRKNRT ETRGIQFEDF VRYLGDPNRR
260 270 280 290 300
WLDLQFGDHI IHWVTYVELC APCEIKYSVV GHHETLEADA PYILKEAGID
310 320 330 340 350
HLVSYPTIPP GITMYNRTKV EQYFLGISKR DIRRLYARFE GDFKLFGYQK

PDFLLN
Length:356
Mass (Da):42,055
Last modified:March 15, 2005 - v2
Checksum:i72A4D0BA9A93F879
GO
Isoform 2 (identifier: Q6PGK7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MHHQWLLLAACFWVIFMFMVASKFITLTFKDPD → MAKTLRDIK
     144-188: AFSSIEEIPE...LKTYFKFFIV → MCGVGGGGTS...GSLCCFPHSS
     189-356: Missing.

Note: No experimental confirmation available.
Show »
Length:164
Mass (Da):18,221
Checksum:iBF3C7CE7A7EA6B3E
GO

Sequence cautioni

The sequence BAC34375.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BC056956 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381E → A in BAC34375 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MHHQW…FKDPD → MAKTLRDIK in isoform 2. 1 PublicationVSP_012989Add
BLAST
Alternative sequencei144 – 18845AFSSI…KFFIV → MCGVGGGGTSVMGEGLRLAL KDGVASSEKTHNLSEGSLCC FPHSS in isoform 2. 1 PublicationVSP_012990Add
BLAST
Alternative sequencei189 – 356168Missing in isoform 2. 1 PublicationVSP_012991Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF360543 mRNA. Translation: AAK52908.1.
AK046415 mRNA. Translation: BAC32718.1.
AK047378 mRNA. Translation: BAC33040.1.
AK050676 mRNA. Translation: BAC34375.1. Different initiation.
BC026960 mRNA. Translation: AAH26960.1.
BC056956 mRNA. No translation available.
RefSeqiNP_660124.2. NM_145142.2.
XP_006496428.1. XM_006496365.2. [Q6PGK7-1]
UniGeneiMm.260054.

Genome annotation databases

GeneIDi98388.
KEGGimmu:98388.
UCSCiuc007ata.1. mouse. [Q6PGK7-2]
uc011wjt.1. mouse. [Q6PGK7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF360543 mRNA. Translation: AAK52908.1.
AK046415 mRNA. Translation: BAC32718.1.
AK047378 mRNA. Translation: BAC33040.1.
AK050676 mRNA. Translation: BAC34375.1. Different initiation.
BC026960 mRNA. Translation: AAH26960.1.
BC056956 mRNA. No translation available.
RefSeqiNP_660124.2. NM_145142.2.
XP_006496428.1. XM_006496365.2. [Q6PGK7-1]
UniGeneiMm.260054.

3D structure databases

ProteinModelPortaliQ6PGK7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027249.

PTM databases

PhosphoSiteiQ6PGK7.

Proteomic databases

MaxQBiQ6PGK7.
PaxDbiQ6PGK7.
PRIDEiQ6PGK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi98388.
KEGGimmu:98388.
UCSCiuc007ata.1. mouse. [Q6PGK7-2]
uc011wjt.1. mouse. [Q6PGK7-1]

Organism-specific databases

CTDi9486.
MGIiMGI:2138283. Chst10.

Phylogenomic databases

eggNOGiKOG4651. Eukaryota.
ENOG4111GJR. LUCA.
HOGENOMiHOG000200781.
HOVERGENiHBG050951.
InParanoidiQ6PGK7.
KOiK09674.

Miscellaneous databases

NextBioi353444.
PROiQ6PGK7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PGK7.
CleanExiMM_CHST10.

Family and domain databases

InterProiIPR018011. Carb_sulfotransferase-rel.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12137. PTHR12137. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence of murine HNK-1 sulfotransferase."
    Spanjaard R.A., Zhao X.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Melanoma.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Corpora quadrigemina.
  3. "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] (ISOFORM 1).
    Strain: C57BL/6J and Czech II.
    Tissue: Brain and Mammary tumor.
  4. "HNK-1 sulfotransferase null mice express glucuronyl glycoconjugates and show normal cerebellar granule neuron migration in vivo and in vitro."
    Chou D.K.H., Schachner M., Jungalwala F.B.
    J. Neurochem. 82:1239-1251(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  5. "Mice deficient for the HNK-1 sulfotransferase show alterations in synaptic efficacy and spatial learning and memory."
    Senn C., Kutsche M., Saghatelyan A., Boesl M.R., Loehler J., Bartsch U., Morellini F., Schachner M.
    Mol. Cell. Neurosci. 20:712-729(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.

Entry informationi

Entry nameiCHSTA_MOUSE
AccessioniPrimary (citable) accession number: Q6PGK7
Secondary accession number(s): Q8BKU3
, Q8BL08, Q8R2Y5, Q91Y40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 11, 2015
This is version 95 of the entry and version 2 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

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 one 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.