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Protein

UDP-glucuronosyltransferase 1-2

Gene

Ugt1a2

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

Functioni

UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_290010. Glucuronidation.
REACT_341594. Heme degradation.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucuronosyltransferase 1-2 (EC:2.4.1.17)
Short name:
UDPGT 1-2
Short name:
UGT1*2
Short name:
UGT1-02
Short name:
UGT1.2
Alternative name(s):
Bilirubin-specific UDPGT
UDP-glucuronosyltransferase 1A2
Short name:
UGT1A2
Gene namesi
Name:Ugt1a2
Synonyms:Ugt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:3576049. Ugt1a2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei491 – 51121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 533506UDP-glucuronosyltransferase 1-2PRO_0000036012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP70691.
PRIDEiP70691.

PTM databases

PhosphoSiteiP70691.

Expressioni

Tissue specificityi

Expressed in kidney.1 Publication

Gene expression databases

BgeeiP70691.
GenevisibleiP70691. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000037258.

Structurei

3D structure databases

ProteinModelPortaliP70691.
SMRiP70691. Positions 284-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220832.
HOVERGENiHBG004033.
InParanoidiP70691.
KOiK00699.
OMAiIFPCGAV.
OrthoDBiEOG7GBFWS.
PhylomeDBiP70691.
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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. The different isozymes have a different N-terminal domain and a common C-terminal domain of 245 residues.

Isoform 1 (identifier: P70691-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDTGLCVPLR GISGLLLLLC ALPWAEGAKV LVLPMEGSQW LSMRDVVREL
60 70 80 90 100
HARGHQTVVL ASEVTVHIKG EDFFTLKTYA FPYTKEEYQQ EILSDIEKTF
110 120 130 140 150
KTQHFVKAFF ETTASIRNFF DLYSNSCIAL LHNKMLIQQL NSSFFDVILT
160 170 180 190 200
DPIFPCGAVL AKYLQIPAVF ILRSLSCGIE YEATQCPNPS SYIPNLLTRL
210 220 230 240 250
SDHMDFLQRV QNMLYYLVLK YICRLSITPY ESLASELLQR EVSLVEVLSH
260 270 280 290 300
ASVWLFRGDF VLDYPRPIMP NMVFIGGINC VTKKPLSQEF EAYVNASGEH
310 320 330 340 350
GIVVFSLGSM VSEIPEKKAM EIAEALGRIP QTVLWRYTGT RPSNLAKNTI
360 370 380 390 400
LVKWLPQNDL LGHPKTRAFI THSGSHGIYE GICNGVPMVM MPLFGDQMDN
410 420 430 440 450
AKRMETRGAG VTLNVLEMTA DDLENALKTV INNKSYKENI MRLSSLHKDR
460 470 480 490 500
PIEPLDLAVF WVEYVMRHKG APHLRPAAHD LTWYQYHSLD VIGFLLAIVL
510 520 530
TVVFIVFKCC AYGCRKCFGG KGRVKKSHKS KTH
Length:533
Mass (Da):60,285
Last modified:February 1, 1997 - v1
Checksum:iFB458439525550FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431S → G in AAP48594 (PubMed:14672974).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87866 mRNA. Translation: BAA13482.1.
AY227195 mRNA. Translation: AAP48594.1.
AK002629 mRNA. Translation: BAB22243.1.
CH466520 Genomic DNA. Translation: EDL40122.1.
BC138676 mRNA. Translation: AAI38677.1.
BC145969 mRNA. Translation: AAI45970.1.
CCDSiCCDS15141.1. [P70691-1]
RefSeqiNP_038729.1. NM_013701.3. [P70691-1]
UniGeneiMm.300095.

Genome annotation databases

EnsembliENSMUST00000049289; ENSMUSP00000037258; ENSMUSG00000090171. [P70691-1]
GeneIDi22236.
KEGGimmu:22236.
UCSCiuc007byi.1. mouse. [P70691-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87866 mRNA. Translation: BAA13482.1.
AY227195 mRNA. Translation: AAP48594.1.
AK002629 mRNA. Translation: BAB22243.1.
CH466520 Genomic DNA. Translation: EDL40122.1.
BC138676 mRNA. Translation: AAI38677.1.
BC145969 mRNA. Translation: AAI45970.1.
CCDSiCCDS15141.1. [P70691-1]
RefSeqiNP_038729.1. NM_013701.3. [P70691-1]
UniGeneiMm.300095.

3D structure databases

ProteinModelPortaliP70691.
SMRiP70691. Positions 284-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000037258.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteiP70691.

Proteomic databases

MaxQBiP70691.
PRIDEiP70691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049289; ENSMUSP00000037258; ENSMUSG00000090171. [P70691-1]
GeneIDi22236.
KEGGimmu:22236.
UCSCiuc007byi.1. mouse. [P70691-1]

Organism-specific databases

CTDi22236.
MGIiMGI:3576049. Ugt1a2.

Phylogenomic databases

GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220832.
HOVERGENiHBG004033.
InParanoidiP70691.
KOiK00699.
OMAiIFPCGAV.
OrthoDBiEOG7GBFWS.
PhylomeDBiP70691.
TreeFamiTF315472.

Enzyme and pathway databases

ReactomeiREACT_290010. Glucuronidation.
REACT_341594. Heme degradation.

Miscellaneous databases

ChiTaRSiUggt1. mouse.
NextBioi302289.
PROiP70691.
SOURCEiSearch...

Gene expression databases

BgeeiP70691.
GenevisibleiP70691. MM.

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. "Isolation of cDNAs for mouse phenol and bilirubin UDP-glucuronosyltransferases and mapping of the mouse gene for phenol UDP-glucuronosyltransferase (Ugtla1) to chromosome 1 by restriction fragment length variations."
    Koiwai O., Hasada K., Yasui Y., Sakai Y., Sato H., Watanabe T.
    Biochem. Genet. 33:111-122(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  2. "Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation."
    Zhang T., Haws P., Wu Q.
    Genome Res. 14:79-89(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  3. "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: Kidney.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., 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].

Entry informationi

Entry nameiUD12_MOUSE
AccessioniPrimary (citable) accession number: P70691
Secondary accession number(s): Q545X2, Q6XL49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 115 of the entry and version 1 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.