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Protein

Uronyl 2-sulfotransferase

Gene

UST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.

GO - Molecular functioni

  • sulfotransferase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000111962-MONOMER.
ReactomeiREACT_120800. Dermatan sulfate biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Uronyl 2-sulfotransferase (EC:2.8.2.-)
Gene namesi
Name:UST
Synonyms:DS2ST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17223. UST.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei50 – 7021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini71 – 406336LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: Reactome
  • integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38213.

Polymorphism and mutation databases

BioMutaiUST.
DMDMi68052988.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Uronyl 2-sulfotransferasePRO_0000207681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9Y2C2.
PaxDbiQ9Y2C2.
PRIDEiQ9Y2C2.

PTM databases

PhosphoSiteiQ9Y2C2.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9Y2C2.
CleanExiHS_UST.
GenevisibleiQ9Y2C2. HS.

Organism-specific databases

HPAiHPA032022.

Interactioni

Protein-protein interaction databases

BioGridi115398. 5 interactions.
IntActiQ9Y2C2. 2 interactions.
MINTiMINT-7970884.
STRINGi9606.ENSP00000356433.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2C2.
SMRiQ9Y2C2. Positions 105-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 3 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG310311.
GeneTreeiENSGT00530000063408.
HOGENOMiHOG000059649.
HOVERGENiHBG086208.
InParanoidiQ9Y2C2.
KOiK03193.
OMAiQYLGNST.
OrthoDBiEOG7DZ8JZ.
PhylomeDBiQ9Y2C2.
TreeFamiTF315238.

Family and domain databases

InterProiIPR007734. Heparan_SO4_2-O-STrfase.
IPR027417. P-loop_NTPase.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12129. PTHR12129. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y2C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKQQHPGG GADPWPHGAP MGGAPPGLGS WKRRVPLLPF LRFSLRDYGF
60 70 80 90 100
CMATLLVFCL GSLLYQLSGG PPRFLLDLRQ YLGNSTYLDD HGPPPSKVLP
110 120 130 140 150
FPSQVVYNRV GKCGSRTVVL LLRILSEKHG FNLVTSDIHN KTRLTKNEQM
160 170 180 190 200
ELIKNISTAE QPYLFTRHVH FLNFSRFGGD QPVYINIIRD PVNRFLSNYF
210 220 230 240 250
FRRFGDWRGE QNHMIRTPSM RQEERYLDIN ECILENYPEC SNPRLFYIIP
260 270 280 290 300
YFCGQHPRCR EPGEWALERA KLNVNENFLL VGILEELEDV LLLLERFLPH
310 320 330 340 350
YFKGVLSIYK DPEHRKLGNM TVTVKKTVPS PEAVQILYQR MRYEYEFYHY
360 370 380 390 400
VKEQFHLLKR KFGLKSHVSK PPLRPHFFIP TPLETEEPID DEEQDDEKWL

EDIYKR
Length:406
Mass (Da):47,673
Last modified:November 1, 1999 - v1
Checksum:i7F201FEBBFA3B2EA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211M → L.
Corresponds to variant rs9498146 [ dbSNP | Ensembl ].
VAR_059819

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5213.1.
RefSeqiNP_005706.1. NM_005715.2.
UniGeneiHs.657370.

Genome annotation databases

EnsembliENST00000367463; ENSP00000356433; ENSG00000111962.
GeneIDi10090.
KEGGihsa:10090.
UCSCiuc003qmg.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5213.1.
RefSeqiNP_005706.1. NM_005715.2.
UniGeneiHs.657370.

3D structure databases

ProteinModelPortaliQ9Y2C2.
SMRiQ9Y2C2. Positions 105-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115398. 5 interactions.
IntActiQ9Y2C2. 2 interactions.
MINTiMINT-7970884.
STRINGi9606.ENSP00000356433.

PTM databases

PhosphoSiteiQ9Y2C2.

Polymorphism and mutation databases

BioMutaiUST.
DMDMi68052988.

Proteomic databases

MaxQBiQ9Y2C2.
PaxDbiQ9Y2C2.
PRIDEiQ9Y2C2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367463; ENSP00000356433; ENSG00000111962.
GeneIDi10090.
KEGGihsa:10090.
UCSCiuc003qmg.3. human.

Organism-specific databases

CTDi10090.
GeneCardsiGC06P149110.
HGNCiHGNC:17223. UST.
HPAiHPA032022.
MIMi610752. gene.
neXtProtiNX_Q9Y2C2.
PharmGKBiPA38213.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310311.
GeneTreeiENSGT00530000063408.
HOGENOMiHOG000059649.
HOVERGENiHBG086208.
InParanoidiQ9Y2C2.
KOiK03193.
OMAiQYLGNST.
OrthoDBiEOG7DZ8JZ.
PhylomeDBiQ9Y2C2.
TreeFamiTF315238.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000111962-MONOMER.
ReactomeiREACT_120800. Dermatan sulfate biosynthesis.

Miscellaneous databases

ChiTaRSiUST. human.
GenomeRNAii10090.
NextBioi38161.
PROiQ9Y2C2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2C2.
CleanExiHS_UST.
GenevisibleiQ9Y2C2. HS.

Family and domain databases

InterProiIPR007734. Heparan_SO4_2-O-STrfase.
IPR027417. P-loop_NTPase.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12129. PTHR12129. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiUST_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2C2
Secondary accession number(s): B2RCX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 104 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 6
    Human chromosome 6: 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.