| UniProt ID | LIS1_MOUSE | |
|---|---|---|
| UniProt AC | P63005 | |
| Protein Name | Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000255|HAMAP-Rule:MF_03141} | |
| Gene Name | Pafah1b1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 410 | |
| Subcellular Localization | Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Nucleus membrane . May localize to the nuclear membrane (By similarity). Localizes to the plus end of microtubules and to t | |
| Protein Description | Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity).. | |
| Protein Sequence | MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR | |
| 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 |
|---|---|---|---|---|---|
| 28 | Phosphorylation | SNGYEEAYSVFKKEA HCCCHHHHHHHHHHH | 14.51 | 22817900 | |
| 29 | Phosphorylation | NGYEEAYSVFKKEAE CCCHHHHHHHHHHHC | 28.29 | 25367039 | |
| 33 | Ubiquitination | EAYSVFKKEAELDMN HHHHHHHHHHCCCCC | 51.17 | 22790023 | |
| 46 | Malonylation | MNEELDKKYAGLLEK CCHHHHHHHHHHHHH | 39.74 | 26320211 | |
| 46 | Ubiquitination | MNEELDKKYAGLLEK CCHHHHHHHHHHHHH | 39.74 | - | |
| 47 | Phosphorylation | NEELDKKYAGLLEKK CHHHHHHHHHHHHHH | 16.19 | 29514104 | |
| 53 | Acetylation | KYAGLLEKKWTSVIR HHHHHHHHHHHHHHH | 54.29 | - | |
| 54 | Ubiquitination | YAGLLEKKWTSVIRL HHHHHHHHHHHHHHH | 46.45 | - | |
| 54 | Malonylation | YAGLLEKKWTSVIRL HHHHHHHHHHHHHHH | 46.45 | 26320211 | |
| 56 | Phosphorylation | GLLEKKWTSVIRLQK HHHHHHHHHHHHHHH | 23.23 | 20139300 | |
| 57 | Phosphorylation | LLEKKWTSVIRLQKK HHHHHHHHHHHHHHH | 17.90 | 20139300 | |
| 71 | Ubiquitination | KVMELESKLNEAKEE HHHHHHHHHHHHHHH | 46.05 | 22790023 | |
| 76 | Ubiquitination | ESKLNEAKEEFTSGG HHHHHHHHHHHHCCC | 52.15 | 22790023 | |
| 81 | Phosphorylation | EAKEEFTSGGPLGQK HHHHHHHCCCCCCCC | 47.26 | 27841257 | |
| 88 | Ubiquitination | SGGPLGQKRDPKEWI CCCCCCCCCCHHHCC | 57.90 | 22790023 | |
| 105 | Phosphorylation | PPEKYALSGHRSPVT CHHHHCCCCCCCCCE | 25.12 | 26824392 | |
| 109 | Phosphorylation | YALSGHRSPVTRVIF HCCCCCCCCCEEEEE | 20.32 | 28507225 | |
| 112 | Phosphorylation | SGHRSPVTRVIFHPV CCCCCCCEEEEEECC | 23.70 | 28066266 | |
| 225 | Phosphorylation | MWEVQTGYCVKTFTG EEEEECCEEEEEECC | 9.47 | 17693683 | |
| 252 | S-nitrosylation | DGTLIASCSNDQTVR CCCEEEECCCCCEEE | 3.05 | 21278135 | |
| 252 | Glutathionylation | DGTLIASCSNDQTVR CCCEEEECCCCCEEE | 3.05 | 24333276 | |
| 252 | S-nitrosocysteine | DGTLIASCSNDQTVR CCCEEEECCCCCEEE | 3.05 | - | |
| 306 | Ubiquitination | SETKKSGKPGPFLLS CCCCCCCCCCCEEEE | 54.62 | 22790023 | |
| 360 | Acetylation | ILSCADDKTLRVWDY EEEECCCCCEEEEEC | 50.43 | 22826441 | |
| 394 | Phosphorylation | DFHKTAPYVVTGSVD CCCCCCCEEEECCCC | 12.70 | - |
| 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 LIS1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LIS1_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 LIS1_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28, AND MASSSPECTROMETRY. | |
