UniProt ID | PEBP1_MOUSE | |
---|---|---|
UniProt AC | P70296 | |
Protein Name | Phosphatidylethanolamine-binding protein 1 | |
Gene Name | Pebp1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 187 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase. Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation (By similarity).; HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity).. | |
Protein Sequence | MAADISQWAGPLCLQEVDEPPQHALRVDYAGVTVDELGKVLTPTQVMNRPSSISWDGLDPGKLYTLVLTDPDAPSRKDPKFREWHHFLVVNMKGNDISSGTVLSDYVGSGPPSGTGLHRYVWLVYEQEQPLSCDEPILSNKSGDNRGKFKVETFRKKYNLGAPVAGTCYQAEWDDYVPKLYEQLSGK | |
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 | Acetylation | ------MAADISQWA ------CCCCHHHHC | 17.53 | - | |
6 | Phosphorylation | --MAADISQWAGPLC --CCCCHHHHCCCCC | 21.88 | 29514104 | |
13 | S-palmitoylation | SQWAGPLCLQEVDEP HHHCCCCCCCCCCCC | 4.08 | 28680068 | |
42 | Phosphorylation | DELGKVLTPTQVMNR HHHCCCCCCHHHHCC | 27.55 | 24925903 | |
44 | Phosphorylation | LGKVLTPTQVMNRPS HCCCCCCHHHHCCCC | 28.67 | 24925903 | |
51 | Phosphorylation | TQVMNRPSSISWDGL HHHHCCCCCCCCCCC | 36.75 | 25521595 | |
52 | Phosphorylation | QVMNRPSSISWDGLD HHHCCCCCCCCCCCC | 24.27 | 25521595 | |
54 | Phosphorylation | MNRPSSISWDGLDPG HCCCCCCCCCCCCCC | 22.51 | 25521595 | |
64 | Phosphorylation | GLDPGKLYTLVLTDP CCCCCCEEEEEEECC | 11.08 | 26160508 | |
65 | Phosphorylation | LDPGKLYTLVLTDPD CCCCCEEEEEEECCC | 22.34 | 21183079 | |
77 | Ubiquitination | DPDAPSRKDPKFREW CCCCCCCCCCCCCCC | 80.75 | 22790023 | |
98 | Phosphorylation | NMKGNDISSGTVLSD ECCCCCCCCCCCCCC | 26.11 | - | |
99 | Phosphorylation | MKGNDISSGTVLSDY CCCCCCCCCCCCCCC | 38.53 | 28464351 | |
106 | Phosphorylation | SGTVLSDYVGSGPPS CCCCCCCCCCCCCCC | 11.88 | 23984901 | |
109 | Phosphorylation | VLSDYVGSGPPSGTG CCCCCCCCCCCCCCC | 37.77 | 19060867 | |
113 | Phosphorylation | YVGSGPPSGTGLHRY CCCCCCCCCCCCHHE | 52.71 | 25521595 | |
115 | Phosphorylation | GSGPPSGTGLHRYVW CCCCCCCCCCHHEEE | 40.69 | 19060867 | |
125 | Phosphorylation | HRYVWLVYEQEQPLS HHEEEEEEECCCCCC | 15.10 | 23140645 | |
132 | Phosphorylation | YEQEQPLSCDEPILS EECCCCCCCCCCCCC | 26.63 | 21082442 | |
133 | S-nitrosylation | EQEQPLSCDEPILSN ECCCCCCCCCCCCCC | 10.14 | 22178444 | |
133 | Glutathionylation | EQEQPLSCDEPILSN ECCCCCCCCCCCCCC | 10.14 | 24333276 | |
133 | S-nitrosocysteine | EQEQPLSCDEPILSN ECCCCCCCCCCCCCC | 10.14 | - | |
139 | Phosphorylation | SCDEPILSNKSGDNR CCCCCCCCCCCCCCC | 42.82 | 25293948 | |
150 | Acetylation | GDNRGKFKVETFRKK CCCCCCEEEEEHHHH | 42.52 | 22826441 | |
153 | Phosphorylation | RGKFKVETFRKKYNL CCCEEEEEHHHHCCC | 31.56 | 21183079 | |
156 | Acetylation | FKVETFRKKYNLGAP EEEEEHHHHCCCCCC | 56.25 | 22826441 | |
157 | Acetylation | KVETFRKKYNLGAPV EEEEHHHHCCCCCCC | 34.81 | 22826441 | |
168 | S-nitrosylation | GAPVAGTCYQAEWDD CCCCCCEEEECCHHH | 2.01 | 21278135 | |
168 | S-palmitoylation | GAPVAGTCYQAEWDD CCCCCCEEEECCHHH | 2.01 | 28526873 | |
168 | S-nitrosocysteine | GAPVAGTCYQAEWDD CCCCCCEEEECCHHH | 2.01 | - | |
176 | Phosphorylation | YQAEWDDYVPKLYEQ EECCHHHHHHHHHHH | 19.04 | 29514104 | |
181 | Phosphorylation | DDYVPKLYEQLSGK- HHHHHHHHHHHCCC- | 14.04 | 22499769 | |
185 | Phosphorylation | PKLYEQLSGK----- HHHHHHHCCC----- | 44.20 | 25521595 | |
187 | Ubiquitination | LYEQLSGK------- HHHHHCCC------- | 54.51 | - | |
187 | Acetylation | LYEQLSGK------- HHHHHCCC------- | 54.51 | 7744109 |
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 PEBP1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PEBP1_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 PEBP1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RAF1_MOUSE | Raf1 | physical | 23055494 | |
MP2K1_MOUSE | Map2k1 | physical | 23055494 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-52 AND SER-54,AND MASS SPECTROMETRY. |