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P70691 (UD12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucuronosyltransferase 1-2

Short name=UDPGT 1-2
Short name=UGT1*2
Short name=UGT1-02
Short name=UGT1.2
EC=2.4.1.17
Alternative name(s):
Bilirubin-specific UDPGT
UDP-glucuronosyltransferase 1A2
Short name=UGT1A2
Gene names
Name:Ugt1a2
Synonyms:Ugt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Microsome By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.

Tissue specificity

Expressed in kidney. Ref.2

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucuronosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

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)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 533506UDP-glucuronosyltransferase 1-2
PRO_0000036012

Regions

Transmembrane491 – 51121Helical; Potential

Amino acid modifications

Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1431S → G in AAP48594. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: FB458439525550FA

FASTA53360,285
        10         20         30         40         50         60 
MDTGLCVPLR GISGLLLLLC ALPWAEGAKV LVLPMEGSQW LSMRDVVREL HARGHQTVVL 

        70         80         90        100        110        120 
ASEVTVHIKG EDFFTLKTYA FPYTKEEYQQ EILSDIEKTF KTQHFVKAFF ETTASIRNFF 

       130        140        150        160        170        180 
DLYSNSCIAL LHNKMLIQQL NSSFFDVILT DPIFPCGAVL AKYLQIPAVF ILRSLSCGIE 

       190        200        210        220        230        240 
YEATQCPNPS SYIPNLLTRL SDHMDFLQRV QNMLYYLVLK YICRLSITPY ESLASELLQR 

       250        260        270        280        290        300 
EVSLVEVLSH ASVWLFRGDF VLDYPRPIMP NMVFIGGINC VTKKPLSQEF EAYVNASGEH 

       310        320        330        340        350        360 
GIVVFSLGSM VSEIPEKKAM EIAEALGRIP QTVLWRYTGT RPSNLAKNTI LVKWLPQNDL 

       370        380        390        400        410        420 
LGHPKTRAFI THSGSHGIYE GICNGVPMVM MPLFGDQMDN AKRMETRGAG VTLNVLEMTA 

       430        440        450        460        470        480 
DDLENALKTV INNKSYKENI MRLSSLHKDR PIEPLDLAVF WVEYVMRHKG APHLRPAAHD 

       490        500        510        520        530 
LTWYQYHSLD VIGFLLAIVL TVVFIVFKCC AYGCRKCFGG KGRVKKSHKS KTH 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15141.1. [P70691-1]
RefSeqNP_038729.1. NM_013701.3. [P70691-1]
UniGeneMm.300095.

3D structure databases

ProteinModelPortalP70691.
SMRP70691. Positions 284-444.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteP70691.

Proteomic databases

MaxQBP70691.
PRIDEP70691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049289; ENSMUSP00000037258; ENSMUSG00000090171. [P70691-1]
GeneID22236.
KEGGmmu:22236.
UCSCuc007byi.1. mouse. [P70691-1]

Organism-specific databases

CTD22236.
MGIMGI:3576049. Ugt1a2.

Phylogenomic databases

GeneTreeENSGT00640000091365.
HOGENOMHOG000220832.
HOVERGENHBG004033.
KOK00699.
OMAFMERIET.
OrthoDBEOG7GBFWS.
PhylomeDBP70691.
TreeFamTF315472.

Gene expression databases

BgeeP70691.
GenevestigatorP70691.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERPTHR11926. PTHR11926. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302289.
PROP70691.
SOURCESearch...

Entry information

Entry nameUD12_MOUSE
AccessionPrimary (citable) accession number: P70691
Secondary accession number(s): Q545X2, Q6XL49
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot