Q9Y2C2 (UST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uronyl 2-sulfotransferase
EC=2.8.2.-

Gene names

Name:	UST
Synonyms:	DS2ST

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	406 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Widely expressed. Ref.1
Sequence similarities	Belongs to the sulfotransferase 3 family.

Ontologies

Keywords
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 metabolic process Traceable author statement. Source: Reactome chondroitin sulfate metabolic process Traceable author statement. Source: Reactome dermatan sulfate biosynthetic process Traceable author statement. Source: Reactome protein sulfation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	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 – 406	406	Uronyl 2-sulfotransferase		PRO_0000207681
Regions
	Topological domain	1 – 49	49	Cytoplasmic Potential
	Transmembrane	50 – 70	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	71 – 406	336	Lumenal Potential
Amino acid modifications
	Glycosylation	84	1	N-linked (GlcNAc...) Potential
	Glycosylation	140	1	N-linked (GlcNAc...) Potential
	Glycosylation	155	1	N-linked (GlcNAc...) Potential
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	319	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	21	1	M → L. Corresponds to variant rs9498146 [ dbSNP | Ensembl ].		VAR_059819

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2C2 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7F201FEBBFA3B2EA	FASTA	406	47,673
	10 20 30 40 50 60 MKKKQQHPGG GADPWPHGAP MGGAPPGLGS WKRRVPLLPF LRFSLRDYGF CMATLLVFCL 70 80 90 100 110 120 GSLLYQLSGG PPRFLLDLRQ YLGNSTYLDD HGPPPSKVLP FPSQVVYNRV GKCGSRTVVL 130 140 150 160 170 180 LLRILSEKHG FNLVTSDIHN KTRLTKNEQM ELIKNISTAE QPYLFTRHVH FLNFSRFGGD 190 200 210 220 230 240 QPVYINIIRD PVNRFLSNYF FRRFGDWRGE QNHMIRTPSM RQEERYLDIN ECILENYPEC 250 260 270 280 290 300 SNPRLFYIIP YFCGQHPRCR EPGEWALERA KLNVNENFLL VGILEELEDV LLLLERFLPH 310 320 330 340 350 360 YFKGVLSIYK DPEHRKLGNM TVTVKKTVPS PEAVQILYQR MRYEYEFYHY VKEQFHLLKR 370 380 390 400 KFGLKSHVSK PPLRPHFFIP TPLETEEPID DEEQDDEKWL EDIYKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a human uronyl 2-sulfotransferase that sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate." Kobayashi M., Sugumaran G., Liu J., Shworak N.W., Silbert J.E., Rosenberg R.D. J. Biol. Chem. 274:10474-10480(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY. Tissue: Lymphoma.
[2]	"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: Cerebellum.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.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].
[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]. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB020316 mRNA. Translation: BAA77510.1. AK315320 mRNA. Translation: BAG37723.1. AL357992 , AL359252, AL590485, AL807246 Genomic DNA. Translation: CAH70738.1. AL359252 , AL357992, AL590485, AL807246 Genomic DNA. Translation: CAH70147.1. AL590485 , AL357992, AL359252, AL807246 Genomic DNA. Translation: CAI17058.1. AL807246 , AL357992, AL359252, AL590485 Genomic DNA. Translation: CAH74028.1. CH471051 Genomic DNA. Translation: EAW47812.1. BC093668 mRNA. Translation: AAH93668.1. BC093694 mRNA. Translation: AAH93694.1.
IPI	IPI00024704.
RefSeq	NP_005706.1. NM_005715.2.
UniGene	Hs.657370.
3D structure databases
ProteinModelPortal	Q9Y2C2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y2C2. 1 interaction.
STRING	9606.ENSP00000356433.
PTM databases
PhosphoSite	Q9Y2C2.
Polymorphism databases
DMDM	68052988.
Proteomic databases
PaxDb	Q9Y2C2.
PRIDE	Q9Y2C2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367463; ENSP00000356433; ENSG00000111962.
GeneID	10090.
KEGG	hsa:10090.
UCSC	uc003qmg.3. human.
Organism-specific databases
CTD	10090.
GeneCards	GC06P149110.
HGNC	HGNC:17223. UST.
HPA	HPA032022.
MIM	610752. gene.
neXtProt	NX_Q9Y2C2.
PharmGKB	PA38213.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG310311.
HOGENOM	HOG000059649.
HOVERGEN	HBG086208.
InParanoid	Q9Y2C2.
KO	K03193.
OMA	QYLGNST.
OrthoDB	EOG4SJ5F2.
PhylomeDB	Q9Y2C2.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000111962-MONOMER.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
Bgee	Q9Y2C2.
CleanEx	HS_UST.
Genevestigator	Q9Y2C2.
GermOnline	ENSG00000111962. Homo sapiens.
Family and domain databases
InterPro	IPR007734. Heparan_SO4_2-O-STrfase. IPR005331. Sulfotransferase. [Graphical view]
PANTHER	PTHR12129. PTHR12129. 1 hit.
Pfam	PF03567. Sulfotransfer_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	UST. human.
GenomeRNAi	10090.
NextBio	38161.
SOURCE	Search...

Entry information

Entry name

UST_HUMAN

Accession

Primary (citable) accession number: Q9Y2C2
Secondary accession number(s): B2RCX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 87 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.