UDP-glucuronosyltransferase 1-9 precursor

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O60656 (UD19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	drug 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 component	endoplasmic 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 function	enzyme 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

Potential

Chain

26 – 530

505

UDP-glucuronosyltransferase 1-9

PRO_0000036008

Regions

Transmembrane

488 – 504

Helical; Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Ref.6

Glycosylation

292

N-linked (GlcNAc...) Ref.6

Glycosylation

344

N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant

M → T. Ref.8

VAR_058587

Natural variant

442

S → I in a breast cancer sample; somatic mutation. Ref.7

VAR_036035

Experimental info

Sequence conflict

L → V in AAB19791. Ref.1

Sequence conflict

200

A → D in AAB19791. Ref.1

Sequence conflict

279 – 282

QGKP → ERKA in AAB19791. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

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

FASTA

530

59,941

        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' referencesShow '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. 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.
IPI	IPI00872012.
PIR	S17512.
RefSeq	NP_066307.1. NM_021027.2.
UniGene	Hs.554822.
3D structure databases
ProteinModelPortal	O60656.
SMR	O60656. Positions 35-62, 278-446.
ModBase	Search...
Protein-protein interaction databases
STRING	O60656.
Protein family/group databases
CAZy	GT1. Glycosyltransferase Family 1.
Proteomic databases
PRIDE	O60656.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354728; ENSP00000346768; ENSG00000241119.
GeneID	54600.
KEGG	hsa:54600.
UCSC	uc002vus.1. human.
Organism-specific databases
CTD	54600.
GeneCards	GC02P234580.
HGNC	HGNC:12541. UGT1A9.
MIM	191740. gene. 606434. gene.
neXtProt	NX_O60656.
PharmGKB	PA419.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG004033.
OrthoDB	EOG45B1FF.
PhylomeDB	O60656.
Enzyme and pathway databases
BRENDA	2.4.1.17. 2681.
Reactome	REACT_111217. Metabolism. REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	O60656.
Genevestigator	O60656.
GermOnline	ENSG00000167165. Homo sapiens.
Family and domain databases
InterPro	IPR002213. UDP_glucos_trans. [Graphical view]
KO	K00699.
PANTHER	PTHR11926. UDP_glucos_trans. 1 hit.
Pfam	PF00201. UDPGT. 1 hit. [Graphical view]
PROSITE	PS00375. UDPGT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00494. Entacapone. DB00749. Etodolac. DB00328. Indomethacin. DB00762. Irinotecan. DB01024. Mycophenolic acid. DB00219. Oxyphenonium. DB00818. Propofol. DB00398. Sorafenib.
NextBio	57125.
SOURCE	Search...

Entry information

Entry name

UD19_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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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

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents