| UniProt ID | UDB10_HUMAN | |
|---|---|---|
| UniProt AC | P36537 | |
| Protein Name | UDP-glucuronosyltransferase 2B10 | |
| Gene Name | UGT2B10 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 528 | |
| Subcellular Localization |
Microsome membrane Single-pass membrane protein . 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.. | |
| Protein Sequence | MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSASILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAINDIIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFERHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLGRPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMSSTDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 66 | N-linked_Glycosylation | ASILFDPNDSSTLKL EEEEECCCCCCCEEE | 64.74 | UniProtKB CARBOHYD | |
| 131 | Phosphorylation | NFCKDVVSNKKLMKK HHHHHHHCCHHHHHH | 42.66 | 26657352 | |
| 134 | Succinylation | KDVVSNKKLMKKLQE HHHHCCHHHHHHHHH | 59.05 | - | |
| 235 | Phosphorylation | MKKWDQFYSEVLGRP CHHHHHHHHHHHCCC | 9.78 | - | |
| 314 | N-linked_Glycosylation | SLGSMVSNMTEERAN ECCHHHCCCCHHHHH | 29.95 | 16335952 | |
| 325 | Phosphorylation | ERANVIATALAKIPQ HHHHHHHHHHHHCCH | 15.87 | - | |
| 445 | Phosphorylation | KENIMKLSRIQHDQP HHHHHHHHHCCCCCC | 23.09 | - | |
| 481 | N-linked_Glycosylation | HLRVAAHNLTWFQYH CHHHEEECCCHHHHC | 34.14 | UniProtKB CARBOHYD |
| 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 UDB10_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UDB10_HUMAN !! | ||||||
* 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 UDB10_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of UDB10_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "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-314, AND MASSSPECTROMETRY. | |
| "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-314, AND MASSSPECTROMETRY. | |
