HUMAN:UD11

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	UGT1A1 (synonyms: GNT1, UGT1)
Protein Name(s)	UDP-glucuronosyltransferase 1-1 UDPGT 1-1 UGT1*1 UGT1-01 UGT1.1 Bilirubin-specific UDPGT isozyme 1 hUG-BR1 UDP-glucuronosyltransferase 1-A UGT-1A UGT1A UDP-glucuronosyltransferase 1A1
External Links
UniProt	P22309
EMBL	M57899 M84124 M84122 M84123 M84125 DQ364247 AF297093 AC006985 D87674
CCDS	CCDS2510.1
PIR	A39092
RefSeq	NP_000454.1
UniGene	Hs.554822
ProteinModelPortal	P22309
SMR	P22309
BioGrid	120087
IntAct	P22309
STRING	9606.ENSP00000304845
BindingDB	P22309
ChEMBL	CHEMBL1287617
DrugBank	DB01048 DB00316 DB00173 DB01076 DB06626 DB00586 DB08930 DB06210 DB00530 DB00783 DB00773 DB00973 DB04953 DB01544 DB00712 DB01095 DB01050 DB05039 DB00328 DB00762 DB00678 DB00227 DB00295 DB00688 DB01024 DB00704 DB00788 DB04868 DB06589 DB00818 DB06817 DB08896 DB01045 DB00641 DB00398 DB00870 DB01420
CAZy	GT1
PhosphoSite	P22309
DMDM	136729
PaxDb	P22309
PeptideAtlas	P22309
PRIDE	P22309
DNASU	54658
GeneID	54658
KEGG	hsa:54658
UCSC	uc002vvb.3
CTD	54658
GeneCards	GC02P234668
HGNC	HGNC:12530
MIM	143500 191740 218800 237900 601816 606785
neXtProt	NX_P22309
Orphanet	79234 79235 357 240885 240905 240973 241017 2312
PharmGKB	PA420
eggNOG	COG1819
GeneTree	ENSGT00760000118949
HOGENOM	HOG000220832
HOVERGEN	HBG004033
InParanoid	P22309
KO	K00699
OrthoDB	EOG7GBFWS
PhylomeDB	P22309
TreeFam	TF315472
Reactome	REACT_22297 REACT_6784
SABIO-RK	P22309
GenomeRNAi	54658
NextBio	27033972
PRO	PR:P22309
Proteomes	UP000005640
Bgee	P22309
CleanEx	HS_UGT1A1
ExpressionAtlas	P22309
Genevestigator	P22309
GO	GO:0070069 GO:0005783 GO:0005789 GO:0005887 GO:0019899 GO:0004857 GO:0015020 GO:0046982 GO:0042803 GO:0001972 GO:0005496 GO:0006953 GO:0006789 GO:0070980 GO:0052695 GO:0071361 GO:0071385 GO:0007586 GO:0017144 GO:0008210 GO:0051552 GO:0052696 GO:0042167 GO:0046483 GO:0001889 GO:0043086 GO:2001030 GO:0045939 GO:0031100 GO:0006778 GO:0042493 GO:0032496 GO:0007584 GO:0042594 GO:0042573 GO:0044281 GO:0008202 GO:0052697 GO:0006805
InterPro	IPR002213
PANTHER	PTHR11926
Pfam	PF00201
PROSITE	PS00375

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0052695	cellular glucuronidation	PMID:17179145^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0052695	cellular glucuronidation	PMID:22579593^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:17179145^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_in:(GO:0005783) has_direct_input:(UniProtKB:P35503)\|occurs_in(GO:0005783) has_direct_input:(UniProtKB:P22310)\|occurs_in(GO:0005783) has_direct_input:(UniProtKB:P19224)\|occurs_in(GO:0005783) has_direct_input:(UniProtKB:Q9HAW7)\|occurs_in(GO:0005783) has_direct_input:(UniProtKB:Q9HAW9)\|occurs_in(GO:0005783) has_direct_input:(UniProtKB:O60656)\|occurs_in(GO:0005783) has_direct_input:(UniProtKB:Q9HAW8)	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:17179145^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_in:(GO:0005783)	Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:17179145^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:22579593^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(CHEBI:4911)	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:17179145^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:1898728^[3]	ECO:0005801	enzymatic activity assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0052697	xenobiotic glucuronidation	PMID:20056724^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0052696	flavonoid glucuronidation	PMID:20056724^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051552	flavone metabolic process	PMID:18052087^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046483	heterocycle metabolic process	PMID:19996319^[6]	ECO:0000305	curator inference used in manual assertion	GO:0015020	P		Seeded From UniProt	complete
involved_in	GO:0045939	negative regulation of steroid metabolic process	PMID:19996319^[6]	ECO:0000305	curator inference used in manual assertion	GO:0004857	P		Seeded From UniProt	complete
involved_in	GO:0042573	retinoic acid metabolic process	PMID:20308471^[7]	ECO:0000305	curator inference used in manual assertion	GO:0001972	P		Seeded From UniProt	complete
involved_in	GO:0017144	drug metabolic process	PMID:19996319^[6]	ECO:0000305	curator inference used in manual assertion	GO:0015020	P		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:20308471^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(CHEBI:15367)	Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:20056724^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:18052087^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:19996319^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008202	steroid metabolic process	PMID:19996319^[6]	ECO:0000305	curator inference used in manual assertion	GO:0015020	P		Seeded From UniProt	complete
enables	GO:0005496	steroid binding	PMID:19996319^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004857	enzyme inhibitor activity	PMID:19996319^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0001972	retinoic acid binding	PMID:20308471^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0052697	xenobiotic glucuronidation	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000230517 RGD:3935 UniProtKB:O60656 UniProtKB:P22309 UniProtKB:P35503 UniProtKB:Q9HAW7 UniProtKB:Q9HAW9	P		Seeded From UniProt	complete
involved_in	GO:0052696	flavonoid glucuronidation	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000230517 RGD:3935 UniProtKB:O60656 UniProtKB:P22309 UniProtKB:P35503 UniProtKB:Q9HAW7 UniProtKB:Q9HAW9	P		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000230403 RGD:3935 RGD:620895 RGD:620949 RGD:708541	C		Seeded From UniProt	complete
enables	GO:0008194	UDP-glycosyltransferase activity	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2145969 MGI:MGI:2146055 PANTHER:PTN000230403 TAIR:locus:2028190 TAIR:locus:2040570 TAIR:locus:2093089 TAIR:locus:2093104 TAIR:locus:2142654 TAIR:locus:2198791 UniProtKB:Q3SY77 UniProtKB:Q6NUS8 UniProtKB:Q7XT97 UniProtKB:Q9M156	F		Seeded From UniProt	complete
involved_in	GO:0043086	negative regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004857	P		Seeded From UniProt	complete
part_of	GO:0034663	endoplasmic reticulum chaperone complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q63886 ensembl:ENSMUSP00000072803	C		Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q63886 ensembl:ENSMUSP00000072803	C		Seeded From UniProt	complete
involved_in	GO:0071466	cellular response to xenobiotic stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0071392	cellular response to estradiol stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0071385	cellular response to glucocorticoid stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0071361	cellular response to ethanol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0070980	biphenyl catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
part_of	GO:0070069	cytochrome complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	C		Seeded From UniProt	complete
involved_in	GO:0052697	xenobiotic glucuronidation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0052696	flavonoid glucuronidation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0052695	cellular glucuronidation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0051384	response to glucocorticoid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0048545	response to steroid hormone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0045471	response to ethanol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	C		Seeded From UniProt	complete
involved_in	GO:0042594	response to starvation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0032870	cellular response to hormone stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0031100	animal organ regeneration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	F		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	F		Seeded From UniProt	complete
involved_in	GO:0014070	response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0010033	response to organic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0007584	response to nutrient	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
involved_in	GO:0006953	acute-phase response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	C		Seeded From UniProt	complete
involved_in	GO:0001889	liver development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64550 ensembl:ENSRNOP00000025045	P		Seeded From UniProt	complete
enables	GO:0016758	transferase activity, transferring hexosyl groups	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002213	F		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.4.1.17	F		Seeded From UniProt	complete
enables	GO:0015020	glucuronosyltransferase activity	PMID:20610558^[9]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9HAW7-1	F		Seeded From UniProt	complete
involved_in	GO:0052695	cellular glucuronidation	PMID:20610558^[9]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9HAW7-1	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW8-2	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35503-3	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P22310-2	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P22309-2	F		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:20610558^[9]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW9-2	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW7-2	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19224-3	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60656-2	F		Seeded From UniProt	complete
NOT\|involved_in	GO:0017144	drug metabolic process	PMID:20610558^[9]	ECO:0000320	phylogenetic determination of loss of key residues evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904224	negative regulation of glucuronosyltransferase activity	PMID:20610558^[9]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9HAW9-2	P		Seeded From UniProt	complete
involved_in	GO:0045922	negative regulation of fatty acid metabolic process	PMID:20610558^[9]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9HAW9-2	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW8-1	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW7-1	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P22310-1	F		Seeded From UniProt	complete
NOT\|enables	GO:0015020	glucuronosyltransferase activity	PMID:20610558^[9]	ECO:0000320	phylogenetic determination of loss of key residues evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:20610558^[9]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
NOT\|part_of	GO:0005789	endoplasmic reticulum membrane	PMID:20610558^[9]	ECO:0000320	phylogenetic determination of loss of key residues evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW9-1	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW8-1	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW7-1	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35503-1	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P22310-1	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19224-1	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60656-1	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAW9-1	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35503-1	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P22309-1	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19224-1	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:20610558^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60656-1	F		Seeded From UniProt	complete
involved_in	GO:2001030	negative regulation of cellular glucuronidation	PMID:18004212^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008210	estrogen metabolic process	PMID:8780690^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006789	bilirubin conjugation	PMID:1339448^[12] Reactome:R-HSA-159194	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0052695	cellular glucuronidation	Reactome:R-HSA-156588	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042167	heme catabolic process	Reactome:R-HSA-189483	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	Reactome:R-HSA-174931 Reactome:R-HSA-159194 Reactome:R-HSA-159179	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256 UniProtKB-SubCell:SL-0095	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
enables	GO:0016757	transferase activity, transferring glycosyl groups	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0328	F		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0492 UniProtKB-SubCell:SL-0166	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Operaña, TN & Tukey, RH (2007) Oligomerization of the UDP-glucuronosyltransferase 1A proteins: homo- and heterodimerization analysis by fluorescence resonance energy transfer and co-immunoprecipitation. J. Biol. Chem. 282 4821-9 PubMed GONUTS page
↑ ^2.0 ^2.1 Gagez, AL et al. (2012) Simultaneous evaluation of six human glucuronidation activities in liver microsomes using liquid chromatography-tandem mass spectrometry. Anal. Biochem. 427 52-9 PubMed GONUTS page
↑ Ritter, JK et al. (1991) Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells. J. Biol. Chem. 266 1043-7 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Brand, W et al. (2010) Phase II metabolism of hesperetin by individual UDP-glucuronosyltransferases and sulfotransferases and rat and human tissue samples. Drug Metab. Dispos. 38 617-25 PubMed GONUTS page
↑ ^5.0 ^5.1 Joseph, TB et al. () Disposition of flavonoids via enteric recycling: enzyme stability affects characterization of prunetin glucuronidation across species, organs, and UGT isoforms. Mol. Pharm. 4 883-94 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 Bellemare, J et al. (2010) Modulation of the human glucuronosyltransferase UGT1A pathway by splice isoform polypeptides is mediated through protein-protein interactions. J. Biol. Chem. 285 3600-7 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Rowbotham, SE et al. (2010) Role of UDP-glucuronosyltransferase isoforms in 13-cis retinoic acid metabolism in humans. Drug Metab. Dispos. 38 1211-7 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^9.00 ^9.01 ^9.02 ^9.03 ^9.04 ^9.05 ^9.06 ^9.07 ^9.08 ^9.09 ^9.10 ^9.11 ^9.12 ^9.13 ^9.14 ^9.15 ^9.16 ^9.17 ^9.18 ^9.19 ^9.20 ^9.21 ^9.22 ^9.23 ^9.24 ^9.25 ^9.26 ^9.27 ^9.28 ^9.29 ^9.30 ^9.31 Bellemare, J et al. (2010) Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro. Drug Metab. Dispos. 38 1785-9 PubMed GONUTS page
↑ Girard, H et al. (2007) Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity. Pharmacogenet. Genomics 17 1077-89 PubMed GONUTS page
↑ Mojarrabi, B et al. (1996) cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3. Biochem. Biophys. Res. Commun. 225 785-90 PubMed GONUTS page
↑ Ritter, JK et al. (1992) A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J. Biol. Chem. 267 3257-61 PubMed GONUTS page

[PMID:17179145-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Operaña, TN & Tukey, RH (2007) Oligomerization of the UDP-glucuronosyltransferase 1A proteins: homo- and heterodimerization analysis by fluorescence resonance energy transfer and co-immunoprecipitation. J. Biol. Chem. 282 4821-9 PubMed GONUTS page

[PMID:22579593-2] 2.0 ^2.1 Gagez, AL et al. (2012) Simultaneous evaluation of six human glucuronidation activities in liver microsomes using liquid chromatography-tandem mass spectrometry. Anal. Biochem. 427 52-9 PubMed GONUTS page

[PMID:1898728-3] Ritter, JK et al. (1991) Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells. J. Biol. Chem. 266 1043-7 PubMed GONUTS page

[PMID:20056724-4] 4.0 ^4.1 ^4.2 Brand, W et al. (2010) Phase II metabolism of hesperetin by individual UDP-glucuronosyltransferases and sulfotransferases and rat and human tissue samples. Drug Metab. Dispos. 38 617-25 PubMed GONUTS page

[PMID:18052087-5] 5.0 ^5.1 Joseph, TB et al. () Disposition of flavonoids via enteric recycling: enzyme stability affects characterization of prunetin glucuronidation across species, organs, and UGT isoforms. Mol. Pharm. 4 883-94 PubMed GONUTS page

[PMID:19996319-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 Bellemare, J et al. (2010) Modulation of the human glucuronosyltransferase UGT1A pathway by splice isoform polypeptides is mediated through protein-protein interactions. J. Biol. Chem. 285 3600-7 PubMed GONUTS page

[PMID:20308471-7] 7.0 ^7.1 ^7.2 Rowbotham, SE et al. (2010) Role of UDP-glucuronosyltransferase isoforms in 13-cis retinoic acid metabolism in humans. Drug Metab. Dispos. 38 1211-7 PubMed GONUTS page

[PMID:21873635-8] 8.0 ^8.1 ^8.2 ^8.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:20610558-9] 9.00 ^9.01 ^9.02 ^9.03 ^9.04 ^9.05 ^9.06 ^9.07 ^9.08 ^9.09 ^9.10 ^9.11 ^9.12 ^9.13 ^9.14 ^9.15 ^9.16 ^9.17 ^9.18 ^9.19 ^9.20 ^9.21 ^9.22 ^9.23 ^9.24 ^9.25 ^9.26 ^9.27 ^9.28 ^9.29 ^9.30 ^9.31 Bellemare, J et al. (2010) Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro. Drug Metab. Dispos. 38 1785-9 PubMed GONUTS page

[PMID:18004212-10] Girard, H et al. (2007) Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity. Pharmacogenet. Genomics 17 1077-89 PubMed GONUTS page

[PMID:8780690-11] Mojarrabi, B et al. (1996) cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3. Biochem. Biophys. Res. Commun. 225 785-90 PubMed GONUTS page

[PMID:1339448-12] Ritter, JK et al. (1992) A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J. Biol. Chem. 267 3257-61 PubMed GONUTS page

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HUMAN:UD11

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