| UniProt ID | B3GN3_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y2A9 | |
| Protein Name | N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3 | |
| Gene Name | B3GNT3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 372 | |
| Subcellular Localization |
Golgi apparatus membrane Single-pass type II membrane protein . |
|
| Protein Description | Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides. [PubMed: 11042166 Also acts as a core1-1,3-N-acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6-sulfo sialyl Lewis x on extended core1 O-glycans] | |
| Protein Sequence | MKYLRHRRPNATLILAIGAFTLLLFSLLVSPPTCKVQEQPPAIPEALAWPTPPTRPAPAPCHANTSMVTHPDFATQPQHVQNFLLYRHCRHFPLLQDVPPSKCAQPVFLLLVIKSSPSNYVRRELLRRTWGRERKVRGLQLRLLFLVGTASNPHEARKVNRLLELEAQTHGDILQWDFHDSFFNLTLKQVLFLQWQETRCANASFVLNGDDDVFAHTDNMVFYLQDHDPGRHLFVGQLIQNVGPIRAFWSKYYVPEVVTQNERYPPYCGGGGFLLSRFTAAALRRAAHVLDIFPIDDVFLGMCLELEGLKPASHSGIRTSGVRAPSQRLSSFDPCFYRDLLLVHRFLPYEMLLMWDALNQPNLTCGNQTQIY | |
| 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 |
|---|---|---|---|---|---|
| 64 | N-linked_Glycosylation | APAPCHANTSMVTHP CCCCCCCCCCCCCCC | 14.71 | UniProtKB CARBOHYD | |
| 120 | Phosphorylation | IKSSPSNYVRRELLR ECCCCCHHHHHHHHH | 10.32 | - | |
| 184 | N-linked_Glycosylation | DFHDSFFNLTLKQVL CCCHHHHHCHHHHHH | 30.06 | UniProtKB CARBOHYD | |
| 198 | Phosphorylation | LFLQWQETRCANASF HHHHCCCCCCCCEEE | 18.89 | 24043423 | |
| 202 | N-linked_Glycosylation | WQETRCANASFVLNG CCCCCCCCEEEEECC | 39.48 | UniProtKB CARBOHYD | |
| 276 | Phosphorylation | GGGGFLLSRFTAAAL CCCHHHHHHHHHHHH | 27.74 | 17924679 | |
| 362 | N-linked_Glycosylation | WDALNQPNLTCGNQT HHHHCCCCCCCCCCC | 37.91 | UniProtKB CARBOHYD | |
| 367 | N-linked_Glycosylation | QPNLTCGNQTQIY-- CCCCCCCCCCCCC-- | 43.82 | 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 B3GN3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of B3GN3_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 B3GN3_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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| Phosphorylation | |
| Reference | PubMed |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND MASSSPECTROMETRY. | |
