Q9HAW9 (UD18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-glucuronosyltransferase 1-8
Short name=UDPGT 1-8
Short name=UGT1*8
Short name=UGT1-08
Short name=UGT1.8
EC=2.4.1.17

Alternative name(s):
UDP-glucuronosyltransferase 1-H
Short name=UGT-1H
Short name=UGT1H
UDP-glucuronosyltransferase 1A8

Gene names

Name:	UGT1A8
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.
Catalytic activity	UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.
Subcellular location	Microsome. Endoplasmic reticulum membrane; Single-pass membrane protein Potential.
Tissue specificity	Colon specific. Ref.1
Sequence similarities	Belongs to the UDP-glycosyltransferase family.

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	coumarin metabolic process Inferred by curator. Source: BHF-UCL drug metabolic process Inferred from direct assay. Source: BHF-UCL fatty acid 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 by curator. Source: BHF-UCL negative regulation of steroid metabolic process Inferred by curator. Source: BHF-UCL retinoic acid metabolic process Inferred by curator. Source: BHF-UCL steroid metabolic process Inferred by curator. Source: BHF-UCL xenobiotic glucuronidation Inferred from direct assay. Source: BHF-UCL
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from direct assay. Source: BHF-UCL
Molecular function	drug binding Inferred by curator. Source: BHF-UCL enzyme binding Inferred by curator. Source: BHF-UCL enzyme inhibitor activity Inferred from direct assay. Source: BHF-UCL fatty acid binding 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 by curator. Source: BHF-UCL steroid 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: Q9HAW9-1)

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	25	Potential
	Chain	26 – 530	505	UDP-glucuronosyltransferase 1-8		PRO_0000036007
Regions
	Transmembrane	488 – 504	17	Helical; Potential
Amino acid modifications
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
	Glycosylation	292	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	344	1	N-linked (GlcNAc...) Ref.6
Natural variations
	Natural variant	53	1	H → N. Corresponds to variant rs45504099 [ dbSNP | Ensembl ].		VAR_052463
	Natural variant	132	1	K → R. Ref.1 Ref.5		VAR_015543
	Natural variant	144	1	A → V. Ref.7 Corresponds to variant rs17862841 [ dbSNP | Ensembl ].		VAR_058585
	Natural variant	154	1	G → A. Ref.1 Ref.5		VAR_015544
	Natural variant	173	1	A → G in allele UGT1A8*2. Ref.1 Ref.3 Ref.4 Ref.5 Ref.7 Corresponds to variant rs1042597 [ dbSNP | Ensembl ].		VAR_015545
	Natural variant	173	1	A → V. Corresponds to variant rs1042597 [ dbSNP | Ensembl ].		VAR_061871
	Natural variant	202	1	T → A. Ref.1 Ref.5		VAR_015546
	Natural variant	212	1	M → L. Ref.1 Ref.5		VAR_015547
	Natural variant	231	1	A → T. Ref.7		VAR_058586
	Natural variant	277	1	C → Y in allele UGT1A8*3; dramatic reduction in catalytic activity. Ref.3 Ref.7 Corresponds to variant rs17863762 [ dbSNP | Ensembl ].		VAR_015549

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: AD838436940F4190	FASTA	530	59,742
	10 20 30 40 50 60 MARTGWTSPI PLCVSLLLTC GFAEAGKLLV VPMDGSHWFT MQSVVEKLIL RGHEVVVVMP 70 80 90 100 110 120 EVSWQLGKSL NCTVKTYSTS YTLEDLDREF MDFADAQWKA QVRSLFSLFL SSSNGFFNLF 130 140 150 160 170 180 FSHCRSLFND RKLVEYLKES SFDAVFLDPF DACGLIVAKY FSLPSVVFAR GIACHYLEEG 190 200 210 220 230 240 AQCPAPLSYV PRILLGFSDA MTFKERVRNH IMHLEEHLFC QYFSKNALEI ASEILQTPVT 250 260 270 280 290 300 AYDLYSHTSI 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8." Strassburg C.P., Manns M.P., Tukey R.H. J. Biol. Chem. 273:8719-8726(1998) [PubMed: 9535849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-132; ALA-154; GLY-173; ALA-202 AND LEU-212.
[2]	"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].
[3]	"Identification and functional characterization of UDP-glucuronosyltransferases UGT1A8*1, UGT1A8*2 and UGT1A8*3." Huang Y.-H., Galijatovic A., Nguyen N., Geske D., Beaton D., Green J., Green M., Peters W.H., Tukey R.H. Pharmacogenetics 12:287-297(2002) [PubMed: 12042666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-173 AND TYR-277. Tissue: Colon.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-173. Tissue: Tongue.
[5]	"Identification of genetic polymorphisms within the human extrahepatic UGT1A8 gene." Strassburg C.P., Vogel A., Manns M.P. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-285, VARIANTS ARG-132; ALA-154; GLY-173; ALA-202 AND LEU-212.
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-292 AND ASN-344, MASS SPECTROMETRY. Tissue: Liver.
[7]	"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: VARIANTS VAL-144; GLY-173; THR-231 AND TYR-277.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF030310 mRNA. Translation: AAB84259.1. AF297093 Genomic DNA. Translation: AAG30416.1. AF462267 mRNA. Translation: AAL75963.1. AF462268 mRNA. Translation: AAL75964.1. AK313488 mRNA. Translation: BAG36270.1. AF465198 Genomic DNA. Translation: AAL73506.1. AF465199 Genomic DNA. Translation: AAL73507.1. AF465200 Genomic DNA. Translation: AAL73508.1.
IPI	IPI00039666.
RefSeq	NP_061949.3. NM_019076.4.
UniGene	Hs.554822.
3D structure databases
ProteinModelPortal	Q9HAW9.
SMR	Q9HAW9. Positions 35-62, 278-446.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9HAW9.
Protein family/group databases
CAZy	GT1. Glycosyltransferase Family 1.
PTM databases
PhosphoSite	Q9HAW9.
Polymorphism databases
DMDM	29839637.
Proteomic databases
PRIDE	Q9HAW9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000373450; ENSP00000362549; ENSG00000242366.
GeneID	54576.
KEGG	hsa:54576.
UCSC	uc002vup.1. human.
Organism-specific databases
CTD	54576.
GeneCards	GC02P234526.
H-InvDB	HIX0002936.
HGNC	HGNC:12540. UGT1A8.
MIM	191740. gene. 606433. gene.
neXtProt	NX_Q9HAW9.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00560000076681.
HOVERGEN	HBG004033.
OMA	MARTGWT.
OrthoDB	EOG45B1FF.
PhylomeDB	Q9HAW9.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14916.
BRENDA	2.4.1.17. 2681.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9HAW9.
Genevestigator	Q9HAW9.
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
NextBio	57078.
SOURCE	Search...

Entry information

Entry name

UD18_HUMAN

Accession

Primary (citable) accession number: Q9HAW9
Secondary accession number(s): B2R8S3 , O14928, Q8TEX4, Q8WTQ9, Q8WX85

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 90 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.