UD11_HUMAN - dbPTM
UD11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UD11_HUMAN
UniProt AC P22309
Protein Name UDP-glucuronosyltransferase 1-1
Gene Name UGT1A1
Organism Homo sapiens (Human).
Sequence Length 533
Subcellular Localization Isoform 1: Microsome . Endoplasmic reticulum membrane
Single-pass membrane protein .
Isoform 2: Microsome . Endoplasmic reticulum .
Protein Description 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. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1..
Protein Sequence MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVLAPDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDSAMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLEFEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQREVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MAVESQGGRPLV
---CCCCCCCCCCHH		27.76-
102N-linked_GlycosylationLGHNVFENDSFLQRV
CCCCHHCCCHHHHHH		38.4719159218
295N-linked_GlycosylationQEFEAYINASGEHGI
HHHHHHHHCCCCCEE		18.51UniProtKB CARBOHYD
332PhosphorylationALGKIPQTVLWRYTG
HHCCCCHHHHHHCCC		16.5323403867
337PhosphorylationPQTVLWRYTGTRPSN
CHHHHHHCCCCCCCH		9.65-
340PhosphorylationVLWRYTGTRPSNLAN
HHHHCCCCCCCHHCC		31.4423403867
343PhosphorylationRYTGTRPSNLANNTI
HCCCCCCCHHCCCEE		40.9823403867
347N-linked_GlycosylationTRPSNLANNTILVKW
CCCCHHCCCEEEEEE		49.71UniProtKB CARBOHYD
349PhosphorylationPSNLANNTILVKWLP
CCHHCCCEEEEEECC		18.5923403867
366PhosphorylationDLLGHPMTRAFITHA
CCCCCCCHHHHHHCC		24.2423403867
435PhosphorylationKAVINDKSYKENIMR
HHHHCCHHHHHHHHH		44.2815845768
437AcetylationVINDKSYKENIMRLS
HHCCHHHHHHHHHHH		51.9118530377
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of UD11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UD11_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UD11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CP3A4_HUMANCYP3A4physical
15486048
Drug and Disease Associations
Kegg Disease
H00208 Hyperbilirubinemia; Crigler-Najjar syndrome, type I (CN1); Crigler-Najjar syndrome, type II (CN2); G
OMIM Disease
143500Gilbert syndrome (GILBS)
237900Transient familial neonatal hyperbilirubinemia (HBLRTFN)
218800Crigler-Najjar syndrome 1 (CN1)
606785Crigler-Najjar syndrome 2 (CN2)
Kegg Drug
D01061 Irinotecan hydrochloride hydrate (JAN); Irinotecan hydrochloride (USAN); CPT 11; CPT-11; Campto (TN)
D01276 Atazanavir sulfate (JAN/USAN); Reyataz (TN)
D03669 Deferasirox (JAN/USAN/INN); Exjade (TN)
D04023 Erlotinib hydrochloride (JAN/USAN); Tarceva (TN)
D06272 Sorafenib tosilate (JAN); Sorafenib tosylate (USAN); Nexavar (TN)
D06676 Raltegravir (USAN/INN); MK-0518
D07133 Raltegravir potassium (JAN/USAN); Isentress (TN)
D08086 Irinotecan (INN); Biotecan (TN)
D08524 Sorafenib (USAN/INN)
D09318 Indacaterol (USAN/INN)
D09319 Indacaterol maleate (JAN/USAN); Arcapta neohaler (TN)
DrugBank
DB01048Abacavir
DB00316Acetaminophen
DB00173Adenine
DB01076Atorvastatin
DB06626Axitinib
DB00586Diclofenac
DB08930Dolutegravir
DB06210Eltrombopag
DB00530Erlotinib
DB00783Estradiol
DB00773Etoposide
DB00973Ezetimibe
DB04953Ezogabine
DB01544Flunitrazepam
DB00712Flurbiprofen
DB01095Fluvastatin
DB01050Ibuprofen
DB05039Indacaterol
DB00328Indomethacin
DB00762Irinotecan
DB00678Losartan
DB00227Lovastatin
DB00295Morphine
DB00688Mycophenolate mofetil
DB01024Mycophenolic acid
DB00704Naltrexone
DB00788Naproxen
DB04868Nilotinib
DB06589Pazopanib
DB00818Propofol
DB06817Raltegravir
DB08896Regorafenib
DB01045Rifampicin
DB00641Simvastatin
DB00398Sorafenib
DB00870Suprofen
DB01420Testosterone Propionate
Regulatory Network of UD11_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102, AND MASSSPECTROMETRY.

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