UD14_HUMAN - dbPTM
UD14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UD14_HUMAN
UniProt AC P22310
Protein Name UDP-glucuronosyltransferase 1-4
Gene Name UGT1A4
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization Microsome. Endoplasmic reticulum membrane
Single-pass membrane protein .
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. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1 (By similarity)..
Protein Sequence MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVVLTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNVSLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDLDFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQREVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
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
14PhosphorylationVPLPRLATGLLLLLS
CCHHHHHHHHHHHHC
32.71-
21PhosphorylationTGLLLLLSVQPWAES
HHHHHHHCCCCCHHC
20.7622210691
28PhosphorylationSVQPWAESGKVLVVP
CCCCCHHCCCEEEEC
35.85-
119N-linked_GlycosylationRSMAIMNNVSLALHR
HHHHHHHHHHHHHHH
13.84UniProtKB CARBOHYD
142N-linked_GlycosylationEALIRHLNATSFDVV
HHHHHHHCCCCCCEE
34.7419159218
296N-linked_GlycosylationQEFEAYINASGEHGI
HHHHHHHHCCCCCEE
18.51UniProtKB CARBOHYD
319UbiquitinationVSEIPEKKAMAIADA
HHCCCHHHHHHHHHH
41.5529901268
333PhosphorylationALGKIPQTVLWRYTG
HHCCCCHHHHHHCCC
16.5323403867
338PhosphorylationPQTVLWRYTGTRPSN
CHHHHHHCCCCCCCH
9.65-
341PhosphorylationVLWRYTGTRPSNLAN
HHHHCCCCCCCHHCC
31.4423403867
344PhosphorylationRYTGTRPSNLANNTI
HCCCCCCCHHCCCEE
40.9823403867
348N-linked_GlycosylationTRPSNLANNTILVKW
CCCCHHCCCEEEEEE
49.7119159218
350PhosphorylationPSNLANNTILVKWLP
CCHHCCCEEEEEECC
18.5923403867
367PhosphorylationDLLGHPMTRAFITHA
CCCCCCCHHHHHHCC
24.2423403867
436PhosphorylationKAVINDKSYKENIMR
HHHHCCHHHHHHHHH
44.2815845768
438UbiquitinationVINDKSYKENIMRLS
HHCCHHHHHHHHHHH
51.9133845483
438AcetylationVINDKSYKENIMRLS
HHCCHHHHHHHHHHH
51.9118530385

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 UD14_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UD14_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 UD14_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UD14_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
143500Gilbert syndrome (GILBS)
218800Crigler-Najjar syndrome 1 (CN1)
606785Crigler-Najjar syndrome 2 (CN2)
Kegg Drug
D00354 Lamotrigine (JAN/USAN/INN); Lamictal (TN)
D06273 Imidafenacin (JAN/INN); Uritos (TN); Staybla (TN)
DrugBank
DB06216Asenapine
DB00363Clozapine
DB04953Ezogabine
DB00555Lamotrigine
DB00683Midazolam
DB00910Paricalcitol
DB00675Tamoxifen
DB00831Trifluoperazine
DB00313Valproic Acid
Regulatory Network of UD14_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-142 AND ASN-348, AND MASSSPECTROMETRY.

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