UniProt ID | MRP_RAT | |
---|---|---|
UniProt AC | Q9EPH2 | |
Protein Name | MARCKS-related protein | |
Gene Name | Marcksl1 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 199 | |
Subcellular Localization |
Cytoplasm. Cell membrane Lipid-anchor . Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca(2+ |
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Protein Description | Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems (By similarity).. | |
Protein Sequence | MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVKSNGDLTPKGEGESPPVNGADEAAGATGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEISACSDEGTAQEGKAAATPESQEPQAKGAEASAVSKGGDAEEEAGPQAAEPSTPSGPESGPASASAENE | |
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 |
---|---|---|---|---|---|
2 | Myristoylation | ------MGSQSSKAP ------CCCCCCCCC | 34.10 | - | |
14 | Phosphorylation | KAPRGDVTAEEAAGA CCCCCCCCHHHHCCC | 32.84 | 23298284 | |
22 | Phosphorylation | AEEAAGASPAKANGQ HHHHCCCCCCHHCCC | 25.19 | 23712012 | |
36 | Phosphorylation | QENGHVKSNGDLTPK CCCCCCCCCCCCCCC | 44.98 | 27097102 | |
41 | Phosphorylation | VKSNGDLTPKGEGES CCCCCCCCCCCCCCC | 27.91 | 23298284 | |
48 | Phosphorylation | TPKGEGESPPVNGAD CCCCCCCCCCCCCCH | 45.41 | 23984901 | |
61 | Phosphorylation | ADEAAGATGDAIEPA CHHHCCCCCCCCCCC | 34.38 | 23984901 | |
71 | Phosphorylation | AIEPAPPSQEAEAKG CCCCCCCCHHHHHCC | 39.32 | 27097102 | |
85 | Phosphorylation | GEVAPKETPKKKKKF CCCCCCCCCCCCCCC | 46.68 | 23712012 | |
91 | Acetylation | ETPKKKKKFSFKKPF CCCCCCCCCCCCCCC | 55.94 | 22902405 | |
93 | Phosphorylation | PKKKKKFSFKKPFKL CCCCCCCCCCCCCCC | 45.06 | 23298284 | |
95 | Acetylation | KKKKFSFKKPFKLSG CCCCCCCCCCCCCCC | 59.34 | 22902405 | |
96 | Acetylation | KKKFSFKKPFKLSGL CCCCCCCCCCCCCCC | 54.39 | 22902405 | |
99 | Acetylation | FSFKKPFKLSGLSFK CCCCCCCCCCCCEEE | 50.71 | 22902405 | |
101 | Phosphorylation | FKKPFKLSGLSFKRN CCCCCCCCCCEEECC | 37.97 | 27097102 | |
104 | Phosphorylation | PFKLSGLSFKRNRKE CCCCCCCEEECCCCC | 32.04 | 23984901 | |
106 | Acetylation | KLSGLSFKRNRKEGG CCCCCEEECCCCCCC | 45.44 | 22902405 | |
116 | Phosphorylation | RKEGGGDSSASSPTE CCCCCCCCCCCCCCH | 30.95 | 30240740 | |
117 | Phosphorylation | KEGGGDSSASSPTEE CCCCCCCCCCCCCHH | 36.59 | 30240740 | |
119 | Phosphorylation | GGGDSSASSPTEEEQ CCCCCCCCCCCHHHH | 38.51 | 30240740 | |
120 | Phosphorylation | GGDSSASSPTEEEQE CCCCCCCCCCHHHHH | 35.24 | 30240740 | |
122 | Phosphorylation | DSSASSPTEEEQEQG CCCCCCCCHHHHHHC | 58.96 | 30240740 | |
132 | Phosphorylation | EQEQGEISACSDEGT HHHHCCCEECCCCCC | 20.94 | 28551015 | |
135 | Phosphorylation | QGEISACSDEGTAQE HCCCEECCCCCCHHC | 38.11 | 30240740 | |
139 | Phosphorylation | SACSDEGTAQEGKAA EECCCCCCHHCCCCC | 24.10 | 28432305 | |
148 | Phosphorylation | QEGKAAATPESQEPQ HCCCCCCCCCCCCCC | 23.90 | 23712012 | |
151 | Phosphorylation | KAAATPESQEPQAKG CCCCCCCCCCCCCCC | 40.84 | 23298284 | |
162 | Phosphorylation | QAKGAEASAVSKGGD CCCCCHHCHHHCCCC | 22.25 | 30240740 | |
165 | Phosphorylation | GAEASAVSKGGDAEE CCHHCHHHCCCCHHH | 25.87 | - | |
182 | Phosphorylation | GPQAAEPSTPSGPES CCCCCCCCCCCCCCC | 44.44 | 27097102 | |
183 | Phosphorylation | PQAAEPSTPSGPESG CCCCCCCCCCCCCCC | 31.99 | 27097102 | |
185 | Phosphorylation | AAEPSTPSGPESGPA CCCCCCCCCCCCCCC | 68.05 | 27097102 | |
189 | Phosphorylation | STPSGPESGPASASA CCCCCCCCCCCCCCC | 53.89 | 27097102 | |
193 | Phosphorylation | GPESGPASASAENE- CCCCCCCCCCCCCC- | 26.37 | 27097102 | |
195 | Phosphorylation | ESGPASASAENE--- CCCCCCCCCCCC--- | 33.35 | 27097102 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
93 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
101 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
104 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
120 | S | Phosphorylation | Kinase | MAPK8 | P49185 | Uniprot |
148 | T | Phosphorylation | Kinase | MAPK8 | P49185 | Uniprot |
183 | T | Phosphorylation | Kinase | MAPK8 | P49185 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
120 | S | Phosphorylation |
| - |
148 | T | Phosphorylation |
| - |
183 | T | Phosphorylation |
| - |
* 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 MRP_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MRP_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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