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Protein

Uronyl 2-sulfotransferase

Gene

Ust

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • establishment of cell polarity Source: MGI
  • regulation of axonogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiR-MMU-2022923. Dermatan sulfate biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Uronyl 2-sulfotransferase (EC:2.8.2.-)
Gene namesi
Name:Ust
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2442406. 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 – 407337LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Uronyl 2-sulfotransferasePRO_0000207682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi85 – 851N-linked (GlcNAc...)Sequence analysis
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence analysis
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence analysis
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence analysis
Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8BUB6.
PaxDbiQ8BUB6.
PRIDEiQ8BUB6.

PTM databases

PhosphoSiteiQ8BUB6.

Expressioni

Gene expression databases

BgeeiQ8BUB6.
CleanExiMM_UST.
GenevisibleiQ8BUB6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052017.

Structurei

3D structure databases

ProteinModelPortaliQ8BUB6.
SMRiQ8BUB6. Positions 106-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 3 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3922. Eukaryota.
ENOG410XTA1. LUCA.
GeneTreeiENSGT00530000063408.
HOGENOMiHOG000059649.
HOVERGENiHBG086208.
InParanoidiQ8BUB6.
KOiK03193.
OMAiRPHFFIP.
OrthoDBiEOG7DZ8JZ.
TreeFamiTF315238.

Family and domain databases

InterProiIPR027417. P-loop_NTPase.
IPR005331. Sulfotransferase.
[Graphical view]
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BUB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKQQQHPG GGTDPWPHGA PVGGAPPCLG SCKRRIPLLP FLRFSLRDYG
60 70 80 90 100
FCMATLLVFC LGSLFYQLSG GPPRFLLDLR QYLGNSTYLD DHGPPPSKVL
110 120 130 140 150
PFPSQVVYNR VGKCGSRTVV LLLRILSEKH GFNLVTSDIH NKTRLTKNEQ
160 170 180 190 200
MELIKNISTA EQPYLFTRHV HFLNFSRFGG DQPVYINIIR DPVSRFLSNY
210 220 230 240 250
FFRRFGDWRG EQNHMIRTPS MRQEERYLDI NECILENYPE CSNPRLFYII
260 270 280 290 300
PYFCGQHPRC REPGEWALER AKLNVNENFL LVGILEELED VLLLLERFLP
310 320 330 340 350
HYFKGVLSIY KDPEHRKLGN MTVTVRKTVP SPEAVQILYQ RMRYEYEFYH
360 370 380 390 400
YVREQFHLLK RKLGLKSRVS GPPVRPQFFI PTPLETEEPI DDEEQDDEKW

LEDIYKR
Length:407
Mass (Da):47,730
Last modified:July 27, 2011 - v3
Checksum:i5DE77416709B9DC6
GO

Sequence cautioni

The sequence BAC39625.1 differs from that shown. Reason: Frameshift at position 318. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571L → V in BAC39625 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK086181 mRNA. Translation: BAC39625.1. Frameshift.
BC138155 mRNA. Translation: AAI38156.1.
CCDSiCCDS35835.1.
RefSeqiNP_796361.2. NM_177387.3.
UniGeneiMm.41163.

Genome annotation databases

EnsembliENSMUST00000061601; ENSMUSP00000052017; ENSMUSG00000047712.
GeneIDi338362.
KEGGimmu:338362.
UCSCiuc007eit.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK086181 mRNA. Translation: BAC39625.1. Frameshift.
BC138155 mRNA. Translation: AAI38156.1.
CCDSiCCDS35835.1.
RefSeqiNP_796361.2. NM_177387.3.
UniGeneiMm.41163.

3D structure databases

ProteinModelPortaliQ8BUB6.
SMRiQ8BUB6. Positions 106-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052017.

PTM databases

PhosphoSiteiQ8BUB6.

Proteomic databases

MaxQBiQ8BUB6.
PaxDbiQ8BUB6.
PRIDEiQ8BUB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061601; ENSMUSP00000052017; ENSMUSG00000047712.
GeneIDi338362.
KEGGimmu:338362.
UCSCiuc007eit.1. mouse.

Organism-specific databases

CTDi10090.
MGIiMGI:2442406. Ust.

Phylogenomic databases

eggNOGiKOG3922. Eukaryota.
ENOG410XTA1. LUCA.
GeneTreeiENSGT00530000063408.
HOGENOMiHOG000059649.
HOVERGENiHBG086208.
InParanoidiQ8BUB6.
KOiK03193.
OMAiRPHFFIP.
OrthoDBiEOG7DZ8JZ.
TreeFamiTF315238.

Enzyme and pathway databases

ReactomeiR-MMU-2022923. Dermatan sulfate biosynthesis.

Miscellaneous databases

ChiTaRSiUst. mouse.
NextBioi400147.
PROiQ8BUB6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BUB6.
CleanExiMM_UST.
GenevisibleiQ8BUB6. MM.

Family and domain databases

InterProiIPR027417. P-loop_NTPase.
IPR005331. Sulfotransferase.
[Graphical view]
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  2. "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.

Entry informationi

Entry nameiUST_MOUSE
AccessioniPrimary (citable) accession number: Q8BUB6
Secondary accession number(s): B2RR02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 27, 2011
Last modified: January 20, 2016
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.