| UniProt ID | MLEC_HUMAN | |
|---|---|---|
| UniProt AC | Q14165 | |
| Protein Name | Malectin | |
| Gene Name | MLEC | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 292 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type I membrane protein. |
|
| Protein Description | Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation (By similarity).. | |
| Protein Sequence | MLGAWAVEGTAVALLRLLLLLLPPAIRGPGLGVAGVAGAAGAGLPESVIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRASDYGMKLPILRSNPEDQILYQTERYNEETFGYEVPIKEEGDYVLVLKFAEVYFAQSQQKVFDVRLNGHVVVKDLDIFDRVGHSTAHDEIIPMSIRKGKLSVQGEVSTFTGKLYIEFVKGYYDNPKVCALYIMAGTVDDVPKLQPHPGLEKKEEEEEEEEYDEGSNLKKQTNKNRVQSGPRTPNPYASDNSSLMFPILVAFGVFIPTLFCLCRL | |
| 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 |
|---|---|---|---|---|---|
| 85 | 2-Hydroxyisobutyrylation | RASDYGMKLPILRSN CHHHCCCCCCEECCC | 46.91 | - | |
| 99 | Phosphorylation | NPEDQILYQTERYNE CHHHCEEEEEECCCC | 18.28 | 28152594 | |
| 101 | O-linked_Glycosylation | EDQILYQTERYNEET HHCEEEEEECCCCCC | 14.63 | OGP | |
| 101 | Phosphorylation | EDQILYQTERYNEET HHCEEEEEECCCCCC | 14.63 | 28152594 | |
| 104 | Phosphorylation | ILYQTERYNEETFGY EEEEEECCCCCCCCE | 22.24 | 21406692 | |
| 108 | Phosphorylation | TERYNEETFGYEVPI EECCCCCCCCEEEEC | 19.04 | 21406692 | |
| 111 | Phosphorylation | YNEETFGYEVPIKEE CCCCCCCEEEECCCC | 15.01 | 21406692 | |
| 121 | Phosphorylation | PIKEEGDYVLVLKFA ECCCCCCEEEEEEEE | 13.41 | - | |
| 131 | Phosphorylation | VLKFAEVYFAQSQQK EEEEEEEEEECCCCE | 5.68 | - | |
| 151 | Acetylation | LNGHVVVKDLDIFDR ECCEEEECCCCCCCC | 40.75 | 26051181 | |
| 179 | Phosphorylation | SIRKGKLSVQGEVST EEECCCEEEEEEEEE | 18.84 | 20068231 | |
| 185 | Phosphorylation | LSVQGEVSTFTGKLY EEEEEEEEECCEEEE | 17.32 | 25954137 | |
| 186 | Phosphorylation | SVQGEVSTFTGKLYI EEEEEEEECCEEEEE | 30.32 | 20068231 | |
| 188 | Phosphorylation | QGEVSTFTGKLYIEF EEEEEECCEEEEEEE | 33.23 | 20068231 | |
| 192 | Phosphorylation | STFTGKLYIEFVKGY EECCEEEEEEEHHCC | 11.24 | 25954137 | |
| 199 | Phosphorylation | YIEFVKGYYDNPKVC EEEEHHCCCCCHHEE | 11.26 | - | |
| 200 | Phosphorylation | IEFVKGYYDNPKVCA EEEHHCCCCCHHEEE | 20.22 | - | |
| 230 | Acetylation | PHPGLEKKEEEEEEE CCCCCCHHHHHHHHH | 62.07 | 26051181 | |
| 239 | Phosphorylation | EEEEEEEYDEGSNLK HHHHHHHCCCCCCHH | 23.68 | 25159151 | |
| 246 | Ubiquitination | YDEGSNLKKQTNKNR CCCCCCHHHHCCCCC | 47.27 | 21906983 | |
| 246 | Acetylation | YDEGSNLKKQTNKNR CCCCCCHHHHCCCCC | 47.27 | 26051181 | |
| 268 | N-linked_Glycosylation | PNPYASDNSSLMFPI CCCCCCCCCCCHHHH | 30.88 | 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 MLEC_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MLEC_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 MLEC_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RS16_HUMAN | RPS16 | physical | 22939629 | |
| CATD_HUMAN | CTSD | physical | 26344197 | |
| RBM8A_HUMAN | RBM8A | physical | 26344197 | |
| STT3B_HUMAN | STT3B | physical | 27173435 |
| 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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