UST_HUMAN
ID UST_HUMAN Reviewed; 406 AA.
AC Q9Y2C2; B2RCX6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Uronyl 2-sulfotransferase;
DE EC=2.8.2.-;
GN Name=UST; Synonyms=DS2ST;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Lymphoma;
RX PubMed=10187838; DOI=10.1074/jbc.274.15.10474;
RA Kobayashi M., Sugumaran G., Liu J., Shworak N.W., Silbert J.E.,
RA Rosenberg R.D.;
RT "Molecular cloning and characterization of a human uronyl 2-
RT sulfotransferase that sulfates iduronyl and glucuronyl residues in
RT dermatan/chondroitin sulfate.";
RL J. Biol. Chem. 274:10474-10480(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sulfotransferase that catalyzes the transfer of sulfate to
CC the position 2 of uronyl residues. Has mainly activity toward iduronyl
CC residues in dermatan sulfate, and weaker activity toward glucuronyl
CC residues of chondroitin sulfate. Has no activity toward desulfated N-
CC resulfated heparin.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10187838}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
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DR EMBL; AB020316; BAA77510.1; -; mRNA.
DR EMBL; AK315320; BAG37723.1; -; mRNA.
DR EMBL; AL357992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47812.1; -; Genomic_DNA.
DR EMBL; BC093668; AAH93668.1; -; mRNA.
DR EMBL; BC093694; AAH93694.1; -; mRNA.
DR CCDS; CCDS5213.1; -.
DR RefSeq; NP_005706.1; NM_005715.2.
DR AlphaFoldDB; Q9Y2C2; -.
DR SMR; Q9Y2C2; -.
DR BioGRID; 115398; 34.
DR IntAct; Q9Y2C2; 22.
DR MINT; Q9Y2C2; -.
DR STRING; 9606.ENSP00000356433; -.
DR GlyConnect; 1887; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Y2C2; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9Y2C2; -.
DR PhosphoSitePlus; Q9Y2C2; -.
DR BioMuta; UST; -.
DR DMDM; 68052988; -.
DR EPD; Q9Y2C2; -.
DR jPOST; Q9Y2C2; -.
DR MassIVE; Q9Y2C2; -.
DR MaxQB; Q9Y2C2; -.
DR PaxDb; Q9Y2C2; -.
DR PeptideAtlas; Q9Y2C2; -.
DR PRIDE; Q9Y2C2; -.
DR ProteomicsDB; 85723; -.
DR Antibodypedia; 33260; 170 antibodies from 19 providers.
DR DNASU; 10090; -.
DR Ensembl; ENST00000367463.5; ENSP00000356433.4; ENSG00000111962.8.
DR GeneID; 10090; -.
DR KEGG; hsa:10090; -.
DR MANE-Select; ENST00000367463.5; ENSP00000356433.4; NM_005715.3; NP_005706.1.
DR UCSC; uc003qmg.4; human.
DR CTD; 10090; -.
DR DisGeNET; 10090; -.
DR GeneCards; UST; -.
DR HGNC; HGNC:17223; UST.
DR HPA; ENSG00000111962; Low tissue specificity.
DR MIM; 610752; gene.
DR neXtProt; NX_Q9Y2C2; -.
DR OpenTargets; ENSG00000111962; -.
DR PharmGKB; PA38213; -.
DR VEuPathDB; HostDB:ENSG00000111962; -.
DR eggNOG; KOG3922; Eukaryota.
DR GeneTree; ENSGT00530000063408; -.
DR HOGENOM; CLU_056190_0_0_1; -.
DR InParanoid; Q9Y2C2; -.
DR OMA; YHYVREQ; -.
DR OrthoDB; 877221at2759; -.
DR PhylomeDB; Q9Y2C2; -.
DR TreeFam; TF315238; -.
DR BioCyc; MetaCyc:ENSG00000111962-MON; -.
DR PathwayCommons; Q9Y2C2; -.
DR Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR SignaLink; Q9Y2C2; -.
DR BioGRID-ORCS; 10090; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; UST; human.
DR GenomeRNAi; 10090; -.
DR Pharos; Q9Y2C2; Tbio.
DR PRO; PR:Q9Y2C2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y2C2; protein.
DR Bgee; ENSG00000111962; Expressed in pons and 182 other tissues.
DR Genevisible; Q9Y2C2; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0030208; P:dermatan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0006477; P:protein sulfation; TAS:ProtInc.
DR GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007734; Heparan_SO4_2-O-STrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12129; PTHR12129; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..406
FT /note="Uronyl 2-sulfotransferase"
FT /id="PRO_0000207681"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..406
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 387..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 21
FT /note="M -> L (in dbSNP:rs9498146)"
FT /id="VAR_059819"
SQ SEQUENCE 406 AA; 47673 MW; 7F201FEBBFA3B2EA CRC64;
MKKKQQHPGG GADPWPHGAP MGGAPPGLGS WKRRVPLLPF LRFSLRDYGF CMATLLVFCL
GSLLYQLSGG PPRFLLDLRQ YLGNSTYLDD HGPPPSKVLP FPSQVVYNRV GKCGSRTVVL
LLRILSEKHG FNLVTSDIHN KTRLTKNEQM ELIKNISTAE QPYLFTRHVH FLNFSRFGGD
QPVYINIIRD PVNRFLSNYF FRRFGDWRGE QNHMIRTPSM RQEERYLDIN ECILENYPEC
SNPRLFYIIP YFCGQHPRCR EPGEWALERA KLNVNENFLL VGILEELEDV LLLLERFLPH
YFKGVLSIYK DPEHRKLGNM TVTVKKTVPS PEAVQILYQR MRYEYEFYHY VKEQFHLLKR
KFGLKSHVSK PPLRPHFFIP TPLETEEPID DEEQDDEKWL EDIYKR
