LIS1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIS1_RAT
• UniProt AC: P63004
• Protein Name: Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000255|HAMAP-Rule:MF_03141}
• Gene Name: Pafah1b1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 410
• Subcellular Localization: Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Nucleus membrane . Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane
• Protein Description: 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. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). 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. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. 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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Acetylation	EEAYSVFKKEAELDM HHHHHHHHHHHCCCC	47.77	22902405
33	Ubiquitination	EAYSVFKKEAELDMN HHHHHHHHHHCCCCC	51.17	-
46	Acetylation	MNEELDKKYAGLLEK CCHHHHHHHHHHHHH	39.74	22902405
53	Acetylation	KYAGLLEKKWTSVIR HHHHHHHHHHHHHHH	54.29	22902405
54	Acetylation	YAGLLEKKWTSVIRL HHHHHHHHHHHHHHH	46.45	22902405
56	Phosphorylation	GLLEKKWTSVIRLQK HHHHHHHHHHHHHHH	23.23	28432305
57	Phosphorylation	LLEKKWTSVIRLQKK HHHHHHHHHHHHHHH	17.90	28432305
76	Ubiquitination	ESKLNEAKEEFTSGG HHHHHHHHHHHHCCC	52.15	-
88	Ubiquitination	SGGPLGQKRDPKEWI CCCCCCCCCCHHHCC	57.90	-
92	Ubiquitination	LGQKRDPKEWIPRPP CCCCCCHHHCCCCCH	70.71	-
102	Phosphorylation	IPRPPEKYALSGHRS CCCCHHHHCCCCCCC	15.88	28432305
105	Phosphorylation	PPEKYALSGHRSPVT CHHHHCCCCCCCCCE	25.12	28432305
109	Phosphorylation	YALSGHRSPVTRVIF HCCCCCCCCCEEEEE	20.32	28432305
112	Phosphorylation	SGHRSPVTRVIFHPV CCCCCCCEEEEEECC	23.70	28432305

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LIS1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIS1_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LIS1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of LIS1_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.