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Protein Page:
UGT1A1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
UGT1A1 UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Is also able to catalyze the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4- methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone. Part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Expressed in liver. Not expressed in skin or kidney. Belongs to the UDP-glycosyltransferase family. 1 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Xenobiotic Metabolism - drug metabolism - cytochrome P450; Lipid Metabolism - androgen and estrogen; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Carbohydrate Metabolism - ascorbate and aldarate; Transferase; Cofactor and Vitamin Metabolism - retinol; Carbohydrate Metabolism - pentose and glucuronate interconversions; Xenobiotic Metabolism - metabolism by cytochrome P450; EC 2.4.1.17; Xenobiotic Metabolism - drug metabolism - other enzymes; Membrane protein, integral; Carbohydrate Metabolism - starch and sucrose
Cellular Component: endoplasmic reticulum membrane; integral to plasma membrane
Molecular Function: enzyme inhibitor activity; enzyme binding; protein homodimerization activity; retinoic acid binding; protein heterodimerization activity; glucuronosyltransferase activity; steroid binding
Biological Process: steroid metabolic process; response to drug; estrogen metabolic process; negative regulation of steroid metabolic process; organ regeneration; response to lipopolysaccharide; liver development; response to starvation; bilirubin conjugation; heme catabolic process; xenobiotic metabolic process; negative regulation of catalytic activity; porphyrin metabolic process; digestion; acute-phase response; flavone metabolic process; retinoic acid metabolic process; heterocycle metabolic process; drug metabolic process; response to nutrient
Reference #:  P22309 (UniProtKB)
Alt. Names/Synonyms: bilirubin UDP-glucuronosyltransferase 1-1; bilirubin UDP-glucuronosyltransferase isozyme 1; Bilirubin-specific UDPGT isozyme 1; GNT1; hUG-BR1; UD11; UDP glucuronosyltransferase 1 family, polypeptide A1; UDP glucuronosyltransferase 1A1; UDP glycosyltransferase 1 family, polypeptide A1; UDP-glucuronosyltransferase 1-1; UDP-glucuronosyltransferase 1-A; UDP-glucuronosyltransferase 1A1; UDPGT; UDPGT 1-1; UGT-1A; UGT1; UGT1*1; UGT1-01; UGT1.1; UGT1A; UGT1A1
Gene Symbols: UGT1A1
Molecular weight: 59,591 Da
Basal Isoelectric point: 8.19  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

UGT1A1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T78 GAFYTLKTYPVPFQR
0 1 R85 TYPVPFQREDVKESF
0 4 K353 ANNTILVKWLPQNDL
  mouse

 
K80-u GSFYTLRkFPVPFQk
K87-u kFPVPFQkENVTATL
K355-a AKNTILVkWLPQNDL
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