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O43529 (CHSTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbohydrate sulfotransferase 10

EC=2.8.2.-
Alternative name(s):
HNK-1 sulfotransferase
Short name=HNK-1ST
Short name=HNK1ST
Short name=HuHNK-1ST
Gene names
Name:CHST10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

In fetal tissues, it is predominantly expressed in brain, and weakly expressed in lung, kidney and liver. In adult, it is highly expressed in brain, testis, ovary, expressed at intermediate level in heart, pancreas, skeletal muscle, spleen and thymus, and weakly expressed in other tissues. In brain, it is expressed at higher level in the frontal lobe. Ref.1

Sequence similarities

Belongs to the sulfotransferase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Carbohydrate sulfotransferase 10
PRO_0000189657

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain28 – 356329Lumenal Potential
Nucleotide binding127 – 1337PAPS Probable
Nucleotide binding189 – 1979PAPS Probable

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential

Natural variations

Natural variant201V → L.
Corresponds to variant rs35177621 [ dbSNP | Ensembl ].
VAR_033737
Natural variant2581D → N.
Corresponds to variant rs3748932 [ dbSNP | Ensembl ].
VAR_021470

Experimental info

Mutagenesis1281K → A: Loss of function. Ref.7
Mutagenesis1281K → R: Induces a reduction in enzyme activity. Ref.7
Mutagenesis1891R → A or K: Loss of function. Ref.7
Mutagenesis1901D → A: Loss of function. Ref.7
Mutagenesis1901D → E: Induces a mild reduction in enzyme activity. Ref.7
Mutagenesis1911P → A or G: Loss of function. Ref.7
Mutagenesis1971S → A or T: Loss of function. Ref.7

Sequences

Sequence LengthMass (Da)Tools
O43529 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 0AE82883CCD8291A

FASTA35642,207
        10         20         30         40         50         60 
MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDVYSAKQE FLFLTTMPEV RKLPEEKHIP 

        70         80         90        100        110        120 
EELKPTGKEL PDSQLVQPLV YMERLELIRN VCRDDALKNL SHTPVSKFVL DRIFVCDKHK 

       130        140        150        160        170        180 
ILFCQTPKVG NTQWKKVLIV LNGAFSSIEE IPENVVHDHE KNGLPRLSSF SDAEIQKRLK 

       190        200        210        220        230        240 
TYFKFFIVRD PFERLISAFK DKFVHNPRFE PWYRHEIAPG IIRKYRRNRT ETRGIQFEDF 

       250        260        270        280        290        300 
VRYLGDPNHR WLDLQFGDHI IHWVTYVELC APCEIMYSVI GHHETLEDDA PYILKEAGID 

       310        320        330        340        350 
HLVSYPTIPP GITVYNRTKV EHYFLGISKR DIRRLYARFE GDFKLFGYQK PDFLLN 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids."
Ong E., Yeh J.-C., Ding Y., Hindsgaul O., Fukuda M.
J. Biol. Chem. 273:5190-5195(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Brain.
[2]Yu W., Gibbs R.A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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.
[7]"Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis."
Ong E., Yeh J.-C., Ding Y., Hindsgaul O., Pedersen L.C., Negishi M., Fukuda M.
J. Biol. Chem. 274:25608-25612(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-128; ARG-189; ASP-190; PRO-191 AND SER-197.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF033827 mRNA. Translation: AAC04707.1.
AF070594 mRNA. Translation: AAC28651.1.
AK313241 mRNA. Translation: BAG36052.1.
AC012493 Genomic DNA. Translation: AAX93044.1.
CH471127 Genomic DNA. Translation: EAX01841.1.
CH471127 Genomic DNA. Translation: EAX01842.1.
CH471127 Genomic DNA. Translation: EAX01843.1.
CH471127 Genomic DNA. Translation: EAX01844.1.
BC010441 mRNA. Translation: AAH10441.1.
CCDSCCDS2047.1.
RefSeqNP_004845.1. NM_004854.4.
UniGeneHs.516370.
Hs.731724.

3D structure databases

ProteinModelPortalO43529.
SMRO43529. Positions 176-203.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114868. 3 interactions.
IntActO43529. 1 interaction.
STRING9606.ENSP00000264249.

PTM databases

PhosphoSiteO43529.

Proteomic databases

PaxDbO43529.
PRIDEO43529.

Protocols and materials databases

DNASU9486.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264249; ENSP00000264249; ENSG00000115526.
ENST00000409701; ENSP00000387309; ENSG00000115526.
GeneID9486.
KEGGhsa:9486.
UCSCuc002tam.3. human.

Organism-specific databases

CTD9486.
GeneCardsGC02M101008.
HGNCHGNC:19650. CHST10.
HPAHPA012884.
HPA051545.
MIM606376. gene.
neXtProtNX_O43529.
PharmGKBPA134920179.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86863.
HOVERGENHBG050951.
InParanoidO43529.
KOK09674.
PhylomeDBO43529.
TreeFamTF325581.

Gene expression databases

ArrayExpressO43529.
BgeeO43529.
CleanExHS_CHST10.
GenevestigatorO43529.

Family and domain databases

InterProIPR018011. Carb_sulfotransferase-rel.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERPTHR12137. PTHR12137. 1 hit.
PfamPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCHST10.
GenomeRNAi9486.
NextBio35544.
PROO43529.
SOURCESearch...

Entry information

Entry nameCHSTA_HUMAN
AccessionPrimary (citable) accession number: O43529
Secondary accession number(s): Q53T18
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 101 of the entry and version 1 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM