O43529 (CHSTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CHST10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate biosynthetic process Inferred from electronic annotation. Source: InterPro cell adhesion Traceable author statement Ref.1. Source: ProtInc learning Inferred from electronic annotation. Source: Compara long-term memory Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Traceable author statement Ref.1. Source: ProtInc Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	HNK-1 sulfotransferase activity Inferred from electronic annotation. Source: Compara sulfotransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Carbohydrate sulfotransferase 10		PRO_0000189657
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	28 – 356	329	Lumenal Potential
	Nucleotide binding	127 – 133	7	PAPS Probable
	Nucleotide binding	189 – 197	9	PAPS Probable
Amino acid modifications
	Glycosylation	99	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	20	1	V → L. Corresponds to variant rs35177621 [ dbSNP | Ensembl ].		VAR_033737
	Natural variant	258	1	D → N. Corresponds to variant rs3748932 [ dbSNP | Ensembl ].		VAR_021470
Experimental info
	Mutagenesis	128	1	K → A: Loss of function. Ref.7
	Mutagenesis	128	1	K → R: Induces a reduction in enzyme activity. Ref.7
	Mutagenesis	189	1	R → A or K: Loss of function. Ref.7
	Mutagenesis	190	1	D → A: Loss of function. Ref.7
	Mutagenesis	190	1	D → E: Induces a mild reduction in enzyme activity. Ref.7
	Mutagenesis	191	1	P → A or G: Loss of function. Ref.7
	Mutagenesis	197	1	S → A or T: Loss of function. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	O43529 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 0AE82883CCD8291A	FASTA	356	42,207
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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.
IPI	IPI01014699.
RefSeq	NP_004845.1. NM_004854.4.
UniGene	Hs.516370. Hs.731724.
3D structure databases
ProteinModelPortal	O43529.
SMR	O43529. Positions 117-143.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43529. 1 interaction.
STRING	9606.ENSP00000264249.
PTM databases
PhosphoSite	O43529.
Proteomic databases
PaxDb	O43529.
PRIDE	O43529.
Protocols and materials databases
DNASU	9486.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264249; ENSP00000264249; ENSG00000115526. ENST00000409701; ENSP00000387309; ENSG00000115526.
GeneID	9486.
KEGG	hsa:9486.
UCSC	uc002tam.3. human.
Organism-specific databases
CTD	9486.
GeneCards	GC02M101008.
HGNC	HGNC:19650. CHST10.
HPA	HPA012884.
MIM	606376. gene.
neXtProt	NX_O43529.
PharmGKB	PA134920179.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG86863.
HOVERGEN	HBG050951.
InParanoid	O43529.
KO	K09674.
OrthoDB	EOG40ZQZ3.
PhylomeDB	O43529.
Gene expression databases
ArrayExpress	O43529.
Bgee	O43529.
CleanEx	HS_CHST10.
Genevestigator	O43529.
GermOnline	ENSG00000115526. Homo sapiens.
Family and domain databases
InterPro	IPR018011. Carb_sulfotransferase-rel. IPR005331. Sulfotransferase. [Graphical view]
PANTHER	PTHR12137. PTHR12137. 1 hit.
Pfam	PF03567. Sulfotransfer_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9486.
NextBio	35544.
SOURCE	Search...

Entry information

Entry name

CHSTA_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.