UniProt ID | ATG3_MOUSE | |
---|---|---|
UniProt AC | Q9CPX6 | |
Protein Name | Ubiquitin-like-conjugating enzyme ATG3 | |
Gene Name | Atg3 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 314 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.. | |
Protein Sequence | MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTDKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLESKDSIKLQDCSALCDEEDEEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKADAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MQNVINTV -------CCCHHHHH | 6.20 | - | |
11 | Ubiquitination | VINTVKGKALEVAEY HHHHHHHHHHHHHHH | 44.04 | 22790023 | |
18 | Phosphorylation | KALEVAEYLTPVLKE HHHHHHHHHHHHHCH | 13.21 | 25159016 | |
20 | Phosphorylation | LEVAEYLTPVLKESK HHHHHHHHHHHCHHH | 15.50 | 26643407 | |
24 | Ubiquitination | EYLTPVLKESKFKET HHHHHHHCHHHCCCC | 61.24 | 22790023 | |
77 | Acetylation | DKQFLVTKNVPCYKR CCCEEEECCCCHHHH | 48.76 | 22826441 | |
81 | Glutathionylation | LVTKNVPCYKRCKQM EEECCCCHHHHHCCC | 5.64 | 24333276 | |
98 | Ubiquitination | SDELEAIIEEDDGDG CHHHHHHEEECCCCC | 6.46 | 27667366 | |
130 | Phosphorylation | VKEITLESKDSIKLQ HHHCCCCCCCCEEEE | 44.89 | 30352176 | |
131 | Ubiquitination | KEITLESKDSIKLQD HHCCCCCCCCEEEEE | 46.23 | 22790023 | |
133 | Phosphorylation | ITLESKDSIKLQDCS CCCCCCCCEEEEEHH | 25.92 | 27600695 | |
140 | Phosphorylation | SIKLQDCSALCDEED CEEEEEHHHHCCCCC | 32.34 | 29899451 | |
160 | Phosphorylation | EAADMEEYEESGLLE CCCCHHHHHHHCCCC | 16.22 | 24224561 | |
182 | Glutathionylation | TRKIVEACKAKADAG HHHHHHHHHHHCCCC | 2.52 | 24333276 | |
185 | Ubiquitination | IVEACKAKADAGGED HHHHHHHHCCCCCCC | 32.09 | 27667366 | |
203 | Phosphorylation | QTRTYDLYITYDKYY EECEEEEEEEECCCC | 6.58 | - | |
208 | Ubiquitination | DLYITYDKYYQTPRL EEEEEECCCCCCCEE | 35.13 | 22790023 | |
208 | Acetylation | DLYITYDKYYQTPRL EEEEEECCCCCCCEE | 35.13 | 23954790 | |
244 | Phosphorylation | SQDHVKKTVTIENHP CHHHCCCEEEECCCC | 19.71 | - | |
246 | Phosphorylation | DHVKKTVTIENHPHL HHCCCEEEECCCCCC | 28.01 | - | |
259 | S-palmitoylation | HLPPPPMCSVHPCRH CCCCCCCCEECCCCC | 4.79 | 28680068 | |
264 | S-palmitoylation | PMCSVHPCRHAEVMK CCCEECCCCCHHHHH | 2.76 | 28680068 | |
306 | Phosphorylation | AVIPTIEYDYTRHFT HHCCCCCCCCCCCCC | 15.48 | 26643407 | |
308 | Phosphorylation | IPTIEYDYTRHFTM- CCCCCCCCCCCCCC- | 12.55 | 26643407 | |
309 | Phosphorylation | PTIEYDYTRHFTM-- CCCCCCCCCCCCC-- | 18.12 | 26643407 | |
313 | Phosphorylation | YDYTRHFTM------ CCCCCCCCC------ | 18.82 | 26643407 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
203 | Y | Phosphorylation | Kinase | PTK2B | Q14289 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATG3_MOUSE !! |
* 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 ATG3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ATG12_HUMAN | ATG12 | physical | 20723759 | |
ATG7_MOUSE | Atg7 | physical | 22170151 | |
ATG12_MOUSE | Atg12 | physical | 24191030 | |
ATG7_MOUSE | Atg7 | physical | 24191030 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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