| UniProt ID | AG10A_HUMAN | |
|---|---|---|
| UniProt AC | Q5BKT4 | |
| Protein Name | Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase | |
| Gene Name | ALG10 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 473 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein. |
|
| Protein Description | Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.. | |
| Protein Sequence | MAQLEGYYFSAALSCTFLVSCLLFSAFSRALREPYMDEIFHLPQAQRYCEGHFSLSQWDPMITTLPGLYLVSIGVIKPAIWIFGWSEHVVCSIGMLRFVNLLFSVGNFYLLYLLFCKVQPRNKAASSIQRVLSTLTLAVFPTLYFFNFLYYTEAGSMFFTLFAYLMCLYGNHKTSAFLGFCGFMFRQTNIIWAVFCAGNVIAQKLTEAWKTELQKKEDRLPPIKGPFAEFRKILQFLLAYSMSFKNLSMLLLLTWPYILLGFLFCAFVVVNGGIVIGDRSSHEACLHFPQLFYFFSFTLFFSFPHLLSPSKIKTFLSLVWKRRILFFVVTLVSVFLVWKFTYAHKYLLADNRHYTFYVWKRVFQRYETVKYLLVPAYIFAGWSIADSLKSKSIFWNLMFFICLFTVIVPQKLLEFRYFILPYVIYRLNIPLPPTSRLICELSCYAVVNFITFFIFLNKTFQWPNSQDIQRFMW | |
| 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 |
|---|---|---|---|---|---|
| 123 | Ubiquitination | CKVQPRNKAASSIQR CCCCCCCHHHHHHHH | 46.76 | 27667366 | |
| 210 | Acetylation | QKLTEAWKTELQKKE HHHHHHHHHHHHHHH | 38.89 | 26822725 | |
| 210 | Ubiquitination | QKLTEAWKTELQKKE HHHHHHHHHHHHHHH | 38.89 | 32142685 | |
| 224 | Ubiquitination | EDRLPPIKGPFAEFR HCCCCCCCCCHHHHH | 67.32 | 21906983 | |
| 308 | Phosphorylation | FSFPHLLSPSKIKTF HCCHHHCCHHHHHHH | 33.22 | 24719451 | |
| 314 | O-linked_Glycosylation | LSPSKIKTFLSLVWK CCHHHHHHHHHHHHH | 33.03 | 30620550 | |
| 330 | Phosphorylation | RILFFVVTLVSVFLV HHHHHHHHHHHHHHH | 19.01 | 50564629 | |
| 366 | Phosphorylation | WKRVFQRYETVKYLL HHHHHHHHHHHHHHH | 12.74 | 22817900 | |
| 368 | Phosphorylation | RVFQRYETVKYLLVP HHHHHHHHHHHHHHC | 17.23 | 68720815 | |
| 387 | Phosphorylation | AGWSIADSLKSKSIF HCCHHHHHHHCCHHH | 28.77 | 22817900 |
| 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 AG10A_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AG10A_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 AG10A_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of AG10A_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 |
| "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-366 AND SER-387, ANDMASS SPECTROMETRY. | |
