UniProt ID | PHAR1_MOUSE | |
---|---|---|
UniProt AC | Q2M3X8 | |
Protein Name | Phosphatase and actin regulator 1 | |
Gene Name | Phactr1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 580 | |
Subcellular Localization | Cytoplasm. Cell junction, synapse. Nucleus. Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import.. | |
Protein Description | Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival (By similarity). Plays a role in cell motility.. | |
Protein Sequence | MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQARRATLLLPPTLMAASSEDDIDRRPIRRVRSKSDTPYLAEARISFNLGAAEEVERLAAMRSDSLVPGTHTPPIRRRSKFANLGRIFKPWKWRKKKSEKFKHTSAALERKISMRQSREELIKRGVLKEIYDKDGELSISNEDDSLENGQSLSSSQLSLPALSEMEPVPMPRDPCSYEVLQASDIMDGPDPGAPVKLPCLPVKLSPPLPPKKVLICMPVGGPELTLASYAAQKSSQQAVAQHHHTVLPSQMQHQLQYGSHGQHLPSSTGTLPMHPSGCRMIDELNKTLAMTMQRLESSEQRVPCSTSYHSSGLHSSDGITKAGPMGLPEIRQVPTVVIECDDNKENVPHEPDYEDSPCLYGREEEEEEEDEDDDASLYTSSLAMKVCRKDSLAIKLSNRPSKRELEEKNILPRQTDEERLELRQQIGTKLTRRLSQRPTAEELEQRNILKPRNEQEEQEEKREIKRRLTRKLSQRPTVEELRERKILIRFSDYVEVADAQDYDRRADKPWTRLTAADKAAIRKELNEFKSTEMEVHELSRHLTRFHRP | |
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 |
---|---|---|---|---|---|
39 | Phosphorylation | GAQARRATLLLPPTL HHHHHHHHEECCCCH | 19.00 | 19060867 | |
45 | Phosphorylation | ATLLLPPTLMAASSE HHEECCCCHHCCCCC | 27.50 | 20415495 | |
65 | Phosphorylation | RPIRRVRSKSDTPYL CCCHHCCCCCCCCCE | 33.38 | 19060867 | |
67 | Phosphorylation | IRRVRSKSDTPYLAE CHHCCCCCCCCCEEE | 48.22 | 25521595 | |
69 | Phosphorylation | RVRSKSDTPYLAEAR HCCCCCCCCCEEEEH | 22.41 | 19060867 | |
71 | Phosphorylation | RSKSDTPYLAEARIS CCCCCCCCEEEEHHE | 22.19 | 23335269 | |
78 | Phosphorylation | YLAEARISFNLGAAE CEEEEHHEECCCCHH | 11.52 | 19060867 | |
95 | Phosphorylation | ERLAAMRSDSLVPGT HHHHHHCCCCCCCCC | 20.61 | 29899451 | |
97 | Phosphorylation | LAAMRSDSLVPGTHT HHHHCCCCCCCCCCC | 32.29 | 29899451 | |
102 | Phosphorylation | SDSLVPGTHTPPIRR CCCCCCCCCCCCCCC | 19.26 | 19060867 | |
104 | Phosphorylation | SLVPGTHTPPIRRRS CCCCCCCCCCCCCCH | 30.51 | 21082442 | |
145 | Phosphorylation | AALERKISMRQSREE HHHHHHHHHHHCHHH | 15.79 | 23608596 | |
149 | Phosphorylation | RKISMRQSREELIKR HHHHHHHCHHHHHHC | 31.15 | 22324799 | |
170 | Phosphorylation | YDKDGELSISNEDDS HCCCCCEECCCCCCC | 21.48 | 21183079 | |
190 | Phosphorylation | SLSSSQLSLPALSEM CCCHHHCCCCCHHCC | 25.35 | 29899451 | |
215 | Phosphorylation | SYEVLQASDIMDGPD CCEEEHHHHCCCCCC | 18.08 | 29899451 | |
237 | Phosphorylation | PCLPVKLSPPLPPKK CEEECCCCCCCCCCE | 20.82 | 27180971 | |
299 | Phosphorylation | HGQHLPSSTGTLPMH CCCCCCCCCCCCCCC | 28.99 | 22807455 | |
329 | Phosphorylation | MTMQRLESSEQRVPC HHHHHHHCCCCCCCC | 43.71 | - | |
337 | O-linked_Glycosylation | SEQRVPCSTSYHSSG CCCCCCCCCCCCCCC | 17.83 | 22645316 | |
385 | Phosphorylation | NVPHEPDYEDSPCLY CCCCCCCCCCCCCCC | 32.14 | 21183079 | |
423 | Phosphorylation | MKVCRKDSLAIKLSN HHHHCCCCHHHHCCC | 23.80 | 21183079 | |
467 | Phosphorylation | TKLTRRLSQRPTAEE HHHHHHHHCCCCHHH | 23.49 | 27742792 | |
471 | Phosphorylation | RRLSQRPTAEELEQR HHHHCCCCHHHHHHC | 49.22 | 25266776 | |
501 | Phosphorylation | REIKRRLTRKLSQRP HHHHHHHHHHHHCCC | 24.77 | - | |
505 | Phosphorylation | RRLTRKLSQRPTVEE HHHHHHHHCCCCHHH | 27.46 | 27841257 | |
509 | Phosphorylation | RKLSQRPTVEELRER HHHHCCCCHHHHHHC | 42.62 | 29899451 | |
525 | Phosphorylation | ILIRFSDYVEVADAQ EEEECHHCEEECCHH | 9.41 | 29514104 | |
562 | Phosphorylation | KELNEFKSTEMEVHE HHHHHHHCCHHHHHH | 34.61 | 29899451 | |
563 | Phosphorylation | ELNEFKSTEMEVHEL HHHHHHCCHHHHHHH | 39.68 | 29899451 | |
576 | Dimethylation | ELSRHLTRFHRP--- HHHHHHHHHCCC--- | 31.56 | - |
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 PHAR1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PHAR1_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 PHAR1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PHAR1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND MASSSPECTROMETRY. |