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Protein

UDP-glucuronosyltransferase 3A2

Gene

Ugt3a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity).By similarity

Catalytic activityi

UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.

GO - Molecular functioni

  1. glucuronosyltransferase activity Source: GO_Central
  2. UDP-glycosyltransferase activity Source: MGI

GO - Biological processi

  1. cellular response to genistein Source: MGI
  2. cellular response to hormone stimulus Source: GO_Central
  3. flavonoid biosynthetic process Source: GO_Central
  4. flavonoid glucuronidation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucuronosyltransferase 3A2 (EC:2.4.1.17)
Short name:
UDPGT 3A2
Gene namesi
Name:Ugt3a2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2145969. Ugt3a2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 487465ExtracellularSequence AnalysisAdd
BLAST
Transmembranei488 – 50821HelicalSequence AnalysisAdd
BLAST
Topological domaini509 – 52315CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. intracellular membrane-bounded organelle Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 523501UDP-glucuronosyltransferase 3A2PRO_0000299154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8JZZ0.
PaxDbiQ8JZZ0.
PRIDEiQ8JZZ0.

PTM databases

PhosphoSiteiQ8JZZ0.

Expressioni

Tissue specificityi

Highly expressed in kidney, while it is expressed at low levels in liver. Not detected in other tissues examined.1 Publication

Gene expression databases

BgeeiQ8JZZ0.
CleanExiMM_UGT3A2.
GenevestigatoriQ8JZZ0.

Interactioni

Protein-protein interaction databases

IntActiQ8JZZ0. 2 interactions.
MINTiMINT-4116696.

Structurei

3D structure databases

ProteinModelPortaliQ8JZZ0.
SMRiQ8JZZ0. Positions 230-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1819.
GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220831.
HOVERGENiHBG106370.
InParanoidiQ8JZZ0.
OrthoDBiEOG7GBFWS.
PhylomeDBiQ8JZZ0.
TreeFamiTF315472.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8JZZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAHRRWLLM SFLFLEVILL EAAKILTIST LSASHYIVIS RVSQVLHEGG
60 70 80 90 100
HNVTKLLYES ANIPDFRKEK PSYQVINWRP PEDQEKKFAD LRHRLTEEIT
110 120 130 140 150
YGRSKHHTLL KIHQYFGDLC SQLLSRKDIM DFLKNENFDL VLLDSMDLCS
160 170 180 190 200
LLIVEKLGKR FVSFLPFQFS YMDFGLPSAP LSYAPVYGSG LTDQMDFWGR
210 220 230 240 250
VKNFLMFLDF SMKQREILSQ YDSTIQEHFV EGSQPVLSDL LLKAELWFVN
260 270 280 290 300
SDFALDFARP LFPNTVYVGG LLDKPVQPIP QDLENFISQF GDSGFVLVAL
310 320 330 340 350
GSIVSMIQSK EIIKEMNSAF AHLPQGVLWT CKTSHWPKDV SLAPNVKIMD
360 370 380 390 400
WLPQTDLLAH PSIRLFVTHG GMNSVMEAVH HGVPMVGIPF FFDQPENMVR
410 420 430 440 450
VEAKNLGVSI QLQTLKAESF ALTMKKIIED KRYKSAAMAS KIIRHSHPLT
460 470 480 490 500
PAQRLLGWID HILQTGGAAH LKPYAFQQPW HEQYMLDVFL FLLGLMLGTL
510 520
WLSVKVLVAV TRYLSIATKV KEA
Length:523
Mass (Da):59,673
Last modified:August 21, 2007 - v2
Checksum:iBC7BD6ADF197ADD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211S → G in BAE25548 (PubMed:16141072).Curated
Sequence conflicti344 – 3441P → S in AAH34837 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050128 mRNA. Translation: BAC34080.1.
AK143815 mRNA. Translation: BAE25548.1.
BC022134 mRNA. Translation: AAH22134.1.
BC024453 mRNA. Translation: AAH24453.1.
BC034837 mRNA. Translation: AAH34837.1.
CCDSiCCDS27375.1.
RefSeqiNP_659094.1. NM_144845.3.
UniGeneiMm.422853.

Genome annotation databases

EnsembliENSMUST00000072403; ENSMUSP00000072236; ENSMUSG00000049152.
GeneIDi223337.
KEGGimmu:223337.
UCSCiuc007vfl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050128 mRNA. Translation: BAC34080.1.
AK143815 mRNA. Translation: BAE25548.1.
BC022134 mRNA. Translation: AAH22134.1.
BC024453 mRNA. Translation: AAH24453.1.
BC034837 mRNA. Translation: AAH34837.1.
CCDSiCCDS27375.1.
RefSeqiNP_659094.1. NM_144845.3.
UniGeneiMm.422853.

3D structure databases

ProteinModelPortaliQ8JZZ0.
SMRiQ8JZZ0. Positions 230-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8JZZ0. 2 interactions.
MINTiMINT-4116696.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteiQ8JZZ0.

Proteomic databases

MaxQBiQ8JZZ0.
PaxDbiQ8JZZ0.
PRIDEiQ8JZZ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072403; ENSMUSP00000072236; ENSMUSG00000049152.
GeneIDi223337.
KEGGimmu:223337.
UCSCiuc007vfl.1. mouse.

Organism-specific databases

CTDi167127.
MGIiMGI:2145969. Ugt3a2.

Phylogenomic databases

eggNOGiCOG1819.
GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220831.
HOVERGENiHBG106370.
InParanoidiQ8JZZ0.
OrthoDBiEOG7GBFWS.
PhylomeDBiQ8JZZ0.
TreeFamiTF315472.

Miscellaneous databases

NextBioi376697.
PROiQ8JZZ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8JZZ0.
CleanExiMM_UGT3A2.
GenevestigatoriQ8JZZ0.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver and Spleen.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney and Liver.
  3. "Tissue- and gender-specific mRNA expression of UDP-glucuronosyltransferases (UGTs) in mice."
    Buckley D.B., Klaassen C.D.
    Drug Metab. Dispos. 35:121-127(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiUD3A2_MOUSE
AccessioniPrimary (citable) accession number: Q8JZZ0
Secondary accession number(s): A1A4B4, Q3UP49, Q8VC11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: February 4, 2015
This is version 88 of the entry and version 2 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

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.