UniProt ID | AP1M1_MOUSE | |
---|---|---|
UniProt AC | P35585 | |
Protein Name | AP-1 complex subunit mu-1 | |
Gene Name | Ap1m1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 423 | |
Subcellular Localization |
Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. |
|
Protein Description | Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.. | |
Protein Sequence | MSASAVYVLDLKGKVLICRNYRGDVDMSEVEHFMPILMEKEEEGMLSPILAHGGVRFMWIKHNNLYLVATSKKNACVSLVFSFLYKVVQVFSEYFKELEEESIRDNFVIIYELLDELMDFGYPQTTDSKILQEYITQEGHKLETGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIEAVNLLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFDNTGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMVKAKSQFKRRSTANNVEIHIPVPNDADSPKFKTTVGSVKWVPENSEIVWSVKSFPGGKEYLMRAHFGLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRTQ | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MSASAVYVL ------CCCCEEEEE | 30.82 | - | |
12 | Acetylation | AVYVLDLKGKVLICR EEEEEECCCCEEEEC | 57.25 | 23954790 | |
12 | Succinylation | AVYVLDLKGKVLICR EEEEEECCCCEEEEC | 57.25 | 23954790 | |
144 | Phosphorylation | QEGHKLETGAPRPPA HCCCCCCCCCCCCCC | 49.43 | 25619855 | |
152 | Phosphorylation | GAPRPPATVTNAVSW CCCCCCCEEEHHCCC | 33.37 | 25521595 | |
154 | Phosphorylation | PRPPATVTNAVSWRS CCCCCEEEHHCCCCC | 17.07 | 25521595 | |
158 | Phosphorylation | ATVTNAVSWRSEGIK CEEEHHCCCCCCCCC | 17.86 | 25619855 | |
165 | Malonylation | SWRSEGIKYRKNEVF CCCCCCCCCCCCCCH | 50.27 | 26320211 | |
165 | Acetylation | SWRSEGIKYRKNEVF CCCCCCCCCCCCCCH | 50.27 | 15618271 | |
223 | Phosphorylation | DKVLFDNTGRGKSKS CEEEECCCCCCCCCC | 30.05 | 25521595 | |
229 | Malonylation | NTGRGKSKSVELEDV CCCCCCCCCEEHHHC | 63.10 | 26320211 | |
245 | Phosphorylation | FHQCVRLSRFENDRT EEEEEEHHHCCCCCE | 25.10 | 23140645 | |
296 | Phosphoglycerylation | SRIEYMVKAKSQFKR CCHHHHHHCHHHHCC | 33.30 | - | |
322 | Phosphorylation | PVPNDADSPKFKTTV CCCCCCCCCCCCCEE | 31.54 | 30635358 | |
324 | Acetylation | PNDADSPKFKTTVGS CCCCCCCCCCCEECE | 64.54 | 23954790 | |
326 | Ubiquitination | DADSPKFKTTVGSVK CCCCCCCCCEECEEE | 49.79 | - | |
326 | Malonylation | DADSPKFKTTVGSVK CCCCCCCCCEECEEE | 49.79 | 26320211 | |
384 | Phosphorylation | SVKFEIPYFTTSGIQ EEEEEECEEECCCCE | 21.15 | 20531401 | |
386 | Phosphorylation | KFEIPYFTTSGIQVR EEEECEEECCCCEEE | 17.76 | 20531401 | |
388 | Phosphorylation | EIPYFTTSGIQVRYL EECEEECCCCEEEEE | 30.73 | 25367039 | |
396 | Malonylation | GIQVRYLKIIEKSGY CCEEEEEEEHHHHCC | 32.48 | 26320211 | |
400 | Ubiquitination | RYLKIIEKSGYQALP EEEEEHHHHCCCCCC | 38.48 | 22790023 |
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 AP1M1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AP1M1_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 AP1M1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of AP1M1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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