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O60656 (UD19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 1-9

Short name=UDPGT 1-9
Short name=UGT1*9
Short name=UGT1-09
Short name=UGT1.9
EC=2.4.1.17
Alternative name(s):
UDP-glucuronosyltransferase 1-I
Short name=UGT-1I
Short name=UGT1I
UDP-glucuronosyltransferase 1A9
lugP4
Gene names
Name:UGT1A9
Synonyms:GNT1, UGT1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols.

Catalytic activity

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

Subcellular location

Microsome. Endoplasmic reticulum membrane; Single-pass membrane protein Potential.

Tissue specificity

Liver.

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Sequence caution

The sequence AAB19791.2 differs from that shown. Reason: Frameshift at positions 59 and 82.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processdrug metabolic process

Inferred from direct assay. Source: BHF-UCL

flavone metabolic process

Inferred from direct assay. Source: BHF-UCL

flavonoid glucuronidation

Inferred from direct assay. Source: BHF-UCL

negative regulation of fatty acid metabolic process

Inferred from direct assay. Source: BHF-UCL

retinoic acid metabolic process

Inferred by curator. Source: BHF-UCL

xenobiotic glucuronidation

Inferred from direct assay. Source: BHF-UCL

   Cellular componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microsome

Non-traceable author statement. Source: UniProtKB

   Molecular functionenzyme binding

Inferred from direct assay. Source: BHF-UCL

enzyme inhibitor activity

Inferred from direct assay. Source: BHF-UCL

glucuronosyltransferase activity

Inferred from direct assay. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction. Source: BHF-UCL

retinoic acid binding

Inferred from direct assay. Source: BHF-UCL

Complete GO annotation...

Alternative products

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

Note: A number of isoforms may be produced. Isoforms have a different N-terminal domain and a common C-terminal domain of 245 residues.
Isoform 1 (identifier: O60656-1)

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 – 2525 Potential
Chain26 – 530505UDP-glucuronosyltransferase 1-9
PRO_0000036008

Regions

Transmembrane488 – 50417Helical; Potential

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Ref.6
Glycosylation2921N-linked (GlcNAc...) Ref.6
Glycosylation3441N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant331M → T. Ref.8
VAR_058587
Natural variant4421S → I in a breast cancer sample; somatic mutation. Ref.7
VAR_036035

Experimental info

Sequence conflict291L → V in AAB19791. Ref.1
Sequence conflict2001A → D in AAB19791. Ref.1
Sequence conflict279 – 2824QGKP → ERKA in AAB19791. Ref.1

Sequences

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

Last modified August 1, 1998. Version 1.
Checksum: C417B9E86B403078

FASTA53059,941
        10         20         30         40         50         60 
MACTGWTSPL PLCVCLLLTC GFAEAGKLLV VPMDGSHWFT MRSVVEKLIL RGHEVVVVMP 

        70         80         90        100        110        120 
EVSWQLGRSL NCTVKTYSTS YTLEDLDREF KAFAHAQWKA QVRSIYSLLM GSYNDIFDLF 

       130        140        150        160        170        180 
FSNCRSLFKD KKLVEYLKES SFDAVFLDPF DNCGLIVAKY FSLPSVVFAR GILCHYLEEG 

       190        200        210        220        230        240 
AQCPAPLSYV PRILLGFSDA MTFKERVRNH IMHLEEHLLC HRFFKNALEI ASEILQTPVT 

       250        260        270        280        290        300 
EYDLYSHTSI WLLRTDFVLD YPKPVMPNMI FIGGINCHQG KPLPMEFEAY INASGEHGIV 

       310        320        330        340        350        360 
VFSLGSMVSE IPEKKAMAIA DALGKIPQTV LWRYTGTRPS NLANNTILVK WLPQNDLLGH 

       370        380        390        400        410        420 
PMTRAFITHA GSHGVYESIC NGVPMVMMPL FGDQMDNAKR METKGAGVTL NVLEMTSEDL 

       430        440        450        460        470        480 
ENALKAVIND KSYKENIMRL SSLHKDRPVE PLDLAVFWVE FVMRHKGAPH LRPAAHDLTW 

       490        500        510        520        530 
YQYHSLDVIG FLLAVVLTVA FITFKCCAYG YRKCLGKKGR VKKAHKSKTH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family."
Wooster R., Sutherland L., Ebner T., Clarke D., da Cruz e Silva O., Burchell B.
Biochem. J. 278:465-469(1991) [PubMed: 1910331] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Human phenol metabolizing UDP-glucuronosyltransferase."
Ciotti M., Potter C., Owens I.S.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Thirteen UDP-glucuronosyltransferase genes are encoded at the human UGT1 gene complex locus."
Gong Q.H., Cho J.W., Huang T., Potter C., Gholami N., Basu N.K., Kubota S., Carvalho S., Pennington M.W., Owens I.S., Popescu N.C.
Pharmacogenetics 11:357-368(2001) [PubMed: 11434514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[5]"Human phenol UDP-glucuronosyltransferase (UGT1A9) gene isozyme exon 1."
Owens I.S., Gong Q., Cho J.W., Potter C., Gholami N.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-285.
[6]"N-Glycosylation plays a role in protein folding of human UGT1A9."
Nakajima M., Koga T., Sakai H., Yamanaka H., Fujiwara R., Yokoi T.
Biochem. Pharmacol. 79:1165-1172(2010) [PubMed: 19951703] [Abstract]
Cited for: GLYCOSYLATION AT ASN-71; ASN-292 AND ASN-344.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-442.
[8]"Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population."
Menard V., Girard H., Harvey M., Perusse L., Guillemette C.
Hum. Mutat. 30:677-687(2009) [PubMed: 19204906] [Abstract]
Cited for: VARIANT THR-33.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S55985 mRNA. Translation: AAB19791.2. Frameshift.
AF056188 mRNA. Translation: AAC31425.1.
AF297093 Genomic DNA. Translation: AAG30418.1.
BC058844 mRNA. Translation: AAH58844.1.
AF297091 Genomic DNA. Translation: AAG29816.1.
IPIIPI00872012.
PIRS17512.
RefSeqNP_066307.1. NM_021027.2.
UniGeneHs.554822.

3D structure databases

ProteinModelPortalO60656.
SMRO60656. Positions 35-62, 278-446.
ModBaseSearch...

Protein-protein interaction databases

STRINGO60656.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

Proteomic databases

PRIDEO60656.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354728; ENSP00000346768; ENSG00000241119.
GeneID54600.
KEGGhsa:54600.
UCSCuc002vus.1. human.

Organism-specific databases

CTD54600.
GeneCardsGC02P234580.
HGNCHGNC:12541. UGT1A9.
MIM191740. gene.
606434. gene.
neXtProtNX_O60656.
PharmGKBPA419.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG004033.
OrthoDBEOG45B1FF.
PhylomeDBO60656.

Enzyme and pathway databases

BRENDA2.4.1.17. 2681.
ReactomeREACT_111217. Metabolism.
REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpressO60656.
GenevestigatorO60656.
GermOnlineENSG00000167165. Homo sapiens.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
KOK00699.
PANTHERPTHR11926. UDP_glucos_trans. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00494. Entacapone.
DB00749. Etodolac.
DB00328. Indomethacin.
DB00762. Irinotecan.
DB01024. Mycophenolic acid.
DB00219. Oxyphenonium.
DB00818. Propofol.
DB00398. Sorafenib.
NextBio57125.
SOURCESearch...

Entry information

Entry nameUD19_HUMAN
AccessionPrimary (citable) accession number: O60656
Secondary accession number(s): P36509, Q9HAX0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families