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Protein Page:
PAFAH1B1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PAFAH1B1 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. 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. Defects in PAFAH1B1 are the cause of lissencephaly type 1 (LIS1); also known as classic lissencephaly. LIS1 is characterized by agyria or pachgyria and disorganization of the clear neuronal lamination of normal six-layered cortex. The cortex is abnormally thick and poorly organized with 4 primitive layers. LIS1 is associated with enlarged and dysmorphic ventricles and often hypoplasia of the corpus callosum. Defects in PAFAH1B1 are the cause of subcortical band heterotopia (SBH). SBH is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric ribbons of gray matter found in the central white matter between the cortex and the ventricular surface. Defects in PAFAH1B1 are a cause of Miller-Dieker lissencephaly syndrome (MDLS). MDLS is a contiguous gene deletion syndrome of chromosome 17p13.3, characterized by classical lissencephaly and distinct facial features. Additional congenital malformations can be part of the condition. Belongs to the WD repeat LIS1/nudF family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cell cycle regulation; Lipid Metabolism - ether lipid
Cellular Component: centrosome; astral microtubule; nuclear membrane; nonmotile primary cilium; leading edge; nuclear envelope; cell cortex; cytosol; kinetochore; kinesin complex; microtubule associated complex; growth cone; cell soma; perinuclear region of cytoplasm; motile primary cilium
Molecular Function: heparin binding; dynein binding; protein binding; protein homodimerization activity; phospholipase binding; microtubule binding; dynein intermediate chain binding; phosphoprotein binding
Biological Process: acrosome formation; negative regulation of JNK cascade; platelet activating factor metabolic process; adult locomotory behavior; positive regulation of axon extension; stem cell division; protein secretion; neuron migration; positive regulation of mitotic cell cycle; retrograde axon cargo transport; cerebral cortex neuron differentiation; microtubule-based process; synaptic transmission; learning and/or memory; establishment of centrosome localization; establishment of mitotic spindle orientation; vesicle transport along microtubule; brain morphogenesis; neuromuscular process controlling balance; G2/M transition of mitotic cell cycle; layer formation in the cerebral cortex; microtubule organizing center organization and biogenesis; mitosis; regulation of Rho GTPase activity; corpus callosum morphogenesis; hippocampus development; transmission of nerve impulse; nuclear envelope disassembly; microtubule cytoskeleton organization and biogenesis; ameboidal cell migration; neuroblast proliferation; mitotic cell cycle; cerebral cortex development; positive regulation of cytokine and chemokine mediated signaling pathway; actin cytoskeleton organization and biogenesis; nuclear migration; lipid catabolic process
Reference #:  P43034 (UniProtKB)
Alt. Names/Synonyms: LIS-1; LIS1; LIS2; lissencephaly 1 protein; Lissencephaly-1 protein; MDCR; MDS; PAF acetylhydrolase 45 kDa subunit; PAF-AH 45 kDa subunit; PAF-AH alpha; PAFAH; PAFAH alpha; PAFAH1B1; PAFAHA; platelet-activating factor acetylhydrolase 1b, regulatory subunit 1 (45kDa); Platelet-activating factor acetylhydrolase IB subunit alpha; platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit (45kD); platelet-activating factor acetylhydrolase, isoform Ib, subunit 1 (45kDa)
Gene Symbols: PAFAH1B1
Molecular weight: 46,638 Da
Basal Isoelectric point: 6.97  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PAFAH1B1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 13 Y28-p SNGYEEAySVFKkEA
0 5 K33-ub EAySVFKkEAELDVN
0 1 K46 VNEELDKKYAGLLEk
0 1 K53-ac KYAGLLEkKWTsVIR
0 1 K54 YAGLLEkKWTsVIRL
0 1 T56 GLLEkKWTsVIRLQK
0 3 S57-p LLEkKWTsVIRLQKk
0 1 K64-ac sVIRLQKkVMELESk
0 1 K71-ac kVMELESkLNEAkEE
0 1 K71 kVMELESKLNEAkEE
0 7 K76-ub ESkLNEAkEEFTSGG
0 5 K88-ub SGGPLGQkRDPKEWI
0 2 K92 LGQkRDPKEWIPRPP
0 2 S109-p YALSGHRsPVTRVIF
0 1 K147-ub GDFERTLkGHTDSVQ
0 1 S251-p QDGTLIAsCsNDQtV
0 1 S253-p GTLIAsCsNDQtVRV
0 1 T257-p AsCsNDQtVRVWVVA
0 1 T265-p VRVWVVAtKECKAEL
0 1 S304-p TGSETKKsGKPGPFL
0 1 K306 SETKKsGKPGPFLLs
0 1 S313-p KPGPFLLsGsRDKtI
0 1 S315-p GPFLLsGsRDKtIKM
0 1 T319-p LsGsRDKtIKMWDVS
0 1 K368-sc TLRVWDYkNKRCMKT
0 3 Y394-p DFHKTAPyVVTGSVD
  mouse

 
Y28-p SNGYEEAySVFKkEA
K33-ub EAySVFKkEAELDMN
K46-ub MNEELDKkYAGLLEK
K53 kYAGLLEKkWtsVIR
K54-ub YAGLLEKkWtsVIRL
T56-p GLLEKkWtsVIRLQK
S57-p LLEKkWtsVIRLQKK
K64 sVIRLQKKVMELESk
K71 KVMELESKLNEAkEE
K71-ub KVMELESkLNEAkEE
K76-ub ESkLNEAkEEFTSGG
K88-ub SGGPLGQkRDPKEWI
K92 LGQkRDPKEWIPRPP
S109 YALSGHRSPVTRVIF
K147 GDFERTLKGHTDSVQ
S251 QDGTLIASCSNDQTV
S253 GTLIASCSNDQTVRV
T257 ASCSNDQTVRVWVVA
T265 VRVWVVATKECKAEL
S304 TGSETKKSGkPGPFL
K306-ub SETKKSGkPGPFLLS
S313 kPGPFLLSGSRDKTI
S315 GPFLLSGSRDKTIKM
T319 LSGSRDKTIKMWDVS
K368 TLRVWDYKNKRCMKT
Y394-p DFHKTAPyVVTGSVD
  rat

 
Y28 SNGYEEAYSVFKKEA
K33 EAYSVFKKEAELDMN
K46 MNEELDKKYAGLLEK
K53 KYAGLLEKKWTSVIR
K54 YAGLLEKKWTSVIRL
T56 GLLEKKWTSVIRLQK
S57 LLEKKWTSVIRLQKK
K64 SVIRLQKKVMELESK
K71 KVMELESKLNEAkEE
K71 KVMELESKLNEAkEE
K76-ub ESKLNEAkEEFTSGG
K88 SGGPLGQKRDPkEWI
K92-ub LGQKRDPkEWIPRPP
S109 YALSGHRSPVTRVIF
K147 GDFERTLKGHTDSVQ
S251 QDGTLIASCSNDQTV
S253 GTLIASCSNDQTVRV
T257 ASCSNDQTVRVWVVA
T265 VRVWVVATKECKAEL
S304 TGSETKKSGKPGPFL
K306 SETKKSGKPGPFLLS
S313 KPGPFLLSGSRDKTI
S315 GPFLLSGSRDKTIKM
T319 LSGSRDKTIKMWDVS
K368 TLRVWDYKNKRCMKT
Y394 DFHKTAPYVVTGSVD
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