| UniProt ID | MGAT3_HUMAN | |
|---|---|---|
| UniProt AC | Q09327 | |
| Protein Name | Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase | |
| Gene Name | MGAT3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 533 | |
| Subcellular Localization |
Golgi apparatus membrane Single-pass type II membrane protein. |
|
| Protein Description | It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides.. | |
| Protein Sequence | MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLVSSFFWNNAPVTPQASPEPGGPDLLRTPLYSHSPLLQPLPPSKAAEELHRVDLVLPEDTTEYFVRTKAGGVCFKPGTKMLERPPPGRPEEKPEGANGSSARRPPRYLLSARERTGGRGARRKWVECVCLPGWHGPSCGVPTVVQYSNLPTKERLVPREVPRRVINAINVNHEFDLLDVRFHELGDVVDAFVVCESNFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDGVSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLEVVSGCTVDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCSWCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRGLIRTGGWFDGTQQEYPPADPSEHMYAPKYLLKNYDRFHYLLDNPYQEPRSTAAGGWRHRGPEGRPPARGKLDEAEV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 61 | O-linked_Glycosylation | APVTPQASPEPGGPD CCCCCCCCCCCCCCC | 25.25 | OGP | |
| 123 | Acetylation | VCFKPGTKMLERPPP EEECCCCCCCCCCCC | 47.61 | 19826817 | |
| 141 | N-linked_Glycosylation | EEKPEGANGSSARRP CCCCCCCCCCCCCCC | 62.83 | UniProtKB CARBOHYD | |
| 154 | Phosphorylation | RPPRYLLSARERTGG CCCCEEEEHHHHHCC | 23.76 | 24719451 | |
| 241 | N-linked_Glycosylation | AFVVCESNFTAYGEP EEEEECCCCCCCCCC | 18.92 | UniProtKB CARBOHYD | |
| 259 | N-linked_Glycosylation | KFREMLTNGTFEYIR CHHHHHHCCCHHHHH | 43.47 | UniProtKB CARBOHYD | |
| 264 | Phosphorylation | LTNGTFEYIRHKVLY HHCCCHHHHHHHHHE | 10.08 | - | |
| 397 | N-linked_Glycosylation | PNFRQYENRTGHILV CCCCCCCCCCCEEEE | 41.71 | UniProtKB CARBOHYD | |
| 489 | Ubiquitination | YAPKYLLKNYDRFHY CCCHHHHHCCCHHHH | 51.36 | - |
| 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 MGAT3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MGAT3_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 MGAT3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MGAT3_HUMAN !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...