UniProt ID | MLP3B_HUMAN | |
---|---|---|
UniProt AC | Q9GZQ8 | |
Protein Name | Microtubule-associated proteins 1A/1B light chain 3B | |
Gene Name | MAP1LC3B | |
Organism | Homo sapiens (Human). | |
Sequence Length | 125 | |
Subcellular Localization |
Cytoplasm, cytoskeleton. Endomembrane system Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane Lipid-anchor. Cytoplasmic vesicle, autophagosome . LC3-II binds to the autophagic membranes. Localizes also to discrete punctae along the ciliary |
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Protein Description | Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.. | |
Protein Sequence | MPSEKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETFGMKLSV | |
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 |
---|---|---|---|---|---|
5 | Ubiquitination | ---MPSEKTFKQRRT ---CCCHHHHHHHHC | 64.70 | - | |
6 | Phosphorylation | --MPSEKTFKQRRTF --CCCHHHHHHHHCH | 31.82 | 20398630 | |
12 | Phosphorylation | KTFKQRRTFEQRVED HHHHHHHCHHHHHHH | 33.44 | - | |
21 | Methylation | EQRVEDVRLIREQHP HHHHHHHHHHHHHCC | 36.40 | - | |
29 | Phosphorylation | LIREQHPTKIPVIIE HHHHHCCCCCCEEEE | 39.21 | 22817900 | |
30 | Ubiquitination | IREQHPTKIPVIIER HHHHCCCCCCEEEEE | 49.84 | - | |
30 | Acetylation | IREQHPTKIPVIIER HHHHCCCCCCEEEEE | 49.84 | 25953088 | |
30 | Malonylation | IREQHPTKIPVIIER HHHHCCCCCCEEEEE | 49.84 | 26320211 | |
42 | Ubiquitination | IERYKGEKQLPVLDK EEECCCCCCCCCCCC | 66.84 | - | |
42 | 2-Hydroxyisobutyrylation | IERYKGEKQLPVLDK EEECCCCCCCCCCCC | 66.84 | - | |
49 | Ubiquitination | KQLPVLDKTKFLVPD CCCCCCCCCCCCCCC | 49.83 | - | |
50 | Phosphorylation | QLPVLDKTKFLVPDH CCCCCCCCCCCCCCC | 27.05 | - | |
51 | Ubiquitination | LPVLDKTKFLVPDHV CCCCCCCCCCCCCCC | 42.30 | 21890473 | |
51 | 2-Hydroxyisobutyrylation | LPVLDKTKFLVPDHV CCCCCCCCCCCCCCC | 42.30 | - | |
51 | Acetylation | LPVLDKTKFLVPDHV CCCCCCCCCCCCCCC | 42.30 | 25953088 | |
65 | Ubiquitination | VNMSELIKIIRRRLQ CCHHHHHHHHHHHHC | 44.71 | 21890473 | |
120 | Phosphatidylethanolamine amidation | YASQETFGMKLSV-- EECCCCCCCCCCC-- | 21.53 | 15187094 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
6 | T | Phosphorylation | Kinase | PRKACA | P27791 | GPS |
12 | T | Phosphorylation | Kinase | PKA | - | Uniprot |
29 | T | Phosphorylation | Kinase | PRKACA | P27791 | GPS |
50 | T | Phosphorylation | Kinase | PKCZ | Q05513 | PSP |
50 | T | Phosphorylation | Kinase | NEK9 | Q8TD19 | PSP |
50 | T | Phosphorylation | Kinase | MST2 | Q13188 | PSP |
50 | T | Phosphorylation | Kinase | MST1 | Q13043 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | TRAF6 | Q9Y4K3 | PMID:30806153 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
12 | T | Phosphorylation |
| 15187094 |
* 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 MLP3B_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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