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Protein

Carbohydrate sulfotransferase 10

Gene

CHST10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.1 Publication

Regions

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

GO - Molecular functioni

  1. HNK-1 sulfotransferase activity Source: Ensembl
  2. sulfotransferase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate biosynthetic process Source: InterPro
  2. cell adhesion Source: ProtInc
  3. learning Source: Ensembl
  4. long-term memory Source: Ensembl
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
Short name:
HuHNK-1ST
Gene namesi
Name:CHST10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:19650. 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

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 1281K → A: Loss of function. 1 Publication
Mutagenesisi128 – 1281K → R: Induces a reduction in enzyme activity. 1 Publication
Mutagenesisi189 – 1891R → A or K: Loss of function. 1 Publication
Mutagenesisi190 – 1901D → A: Loss of function. 1 Publication
Mutagenesisi190 – 1901D → E: Induces a mild reduction in enzyme activity. 1 Publication
Mutagenesisi191 – 1911P → A or G: Loss of function. 1 Publication
Mutagenesisi197 – 1971S → A or T: Loss of function. 1 Publication

Organism-specific databases

PharmGKBiPA134920179.

Polymorphism and mutation databases

BioMutaiCHST10.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Carbohydrate sulfotransferase 10PRO_0000189657Add
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

PaxDbiO43529.
PRIDEiO43529.

PTM databases

PhosphoSiteiO43529.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO43529.
CleanExiHS_CHST10.
ExpressionAtlasiO43529. baseline and differential.
GenevestigatoriO43529.

Organism-specific databases

HPAiHPA012884.
HPA051545.

Interactioni

Protein-protein interaction databases

BioGridi114868. 16 interactions.
IntActiO43529. 1 interaction.
STRINGi9606.ENSP00000264249.

Structurei

3D structure databases

ProteinModelPortaliO43529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 2 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG86863.
GeneTreeiENSGT00760000119214.
HOVERGENiHBG050951.
InParanoidiO43529.
KOiK09674.
PhylomeDBiO43529.
TreeFamiTF325581.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O43529-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDVYSAKQE FLFLTTMPEV
60 70 80 90 100
RKLPEEKHIP EELKPTGKEL PDSQLVQPLV YMERLELIRN VCRDDALKNL
110 120 130 140 150
SHTPVSKFVL DRIFVCDKHK ILFCQTPKVG NTQWKKVLIV LNGAFSSIEE
160 170 180 190 200
IPENVVHDHE KNGLPRLSSF SDAEIQKRLK TYFKFFIVRD PFERLISAFK
210 220 230 240 250
DKFVHNPRFE PWYRHEIAPG IIRKYRRNRT ETRGIQFEDF VRYLGDPNHR
260 270 280 290 300
WLDLQFGDHI IHWVTYVELC APCEIMYSVI GHHETLEDDA PYILKEAGID
310 320 330 340 350
HLVSYPTIPP GITVYNRTKV EHYFLGISKR DIRRLYARFE GDFKLFGYQK

PDFLLN
Length:356
Mass (Da):42,207
Last modified:June 1, 1998 - v1
Checksum:i0AE82883CCD8291A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201V → L.
Corresponds to variant rs35177621 [ dbSNP | Ensembl ].
VAR_033737
Natural varianti258 – 2581D → N.
Corresponds to variant rs3748932 [ dbSNP | Ensembl ].
VAR_021470

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2047.1.
RefSeqiNP_004845.1. NM_004854.4.
UniGeneiHs.516370.
Hs.731724.

Genome annotation databases

EnsembliENST00000264249; ENSP00000264249; ENSG00000115526.
ENST00000409701; ENSP00000387309; ENSG00000115526.
GeneIDi9486.
KEGGihsa:9486.
UCSCiuc002tam.3. human.

Polymorphism and mutation databases

BioMutaiCHST10.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2047.1.
RefSeqiNP_004845.1. NM_004854.4.
UniGeneiHs.516370.
Hs.731724.

3D structure databases

ProteinModelPortaliO43529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114868. 16 interactions.
IntActiO43529. 1 interaction.
STRINGi9606.ENSP00000264249.

PTM databases

PhosphoSiteiO43529.

Polymorphism and mutation databases

BioMutaiCHST10.

Proteomic databases

PaxDbiO43529.
PRIDEiO43529.

Protocols and materials databases

DNASUi9486.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264249; ENSP00000264249; ENSG00000115526.
ENST00000409701; ENSP00000387309; ENSG00000115526.
GeneIDi9486.
KEGGihsa:9486.
UCSCiuc002tam.3. human.

Organism-specific databases

CTDi9486.
GeneCardsiGC02M101008.
HGNCiHGNC:19650. CHST10.
HPAiHPA012884.
HPA051545.
MIMi606376. gene.
neXtProtiNX_O43529.
PharmGKBiPA134920179.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG86863.
GeneTreeiENSGT00760000119214.
HOVERGENiHBG050951.
InParanoidiO43529.
KOiK09674.
PhylomeDBiO43529.
TreeFamiTF325581.

Miscellaneous databases

ChiTaRSiCHST10. human.
GeneWikiiCHST10.
GenomeRNAii9486.
NextBioi35544.
PROiO43529.
SOURCEiSearch...

Gene expression databases

BgeeiO43529.
CleanExiHS_CHST10.
ExpressionAtlasiO43529. baseline and differential.
GenevestigatoriO43529.

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. "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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiCHSTA_HUMAN
AccessioniPrimary (citable) accession number: O43529
Secondary accession number(s): Q53T18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 1998
Last modified: April 29, 2015
This is version 107 of the entry and version 1 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.