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Protein Page:
PAFAH1B1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: Lipid Metabolism - ether lipid; Cell cycle regulation
Chromosomal Location of Human Ortholog: 17p13.3
Cellular Component: astral microtubule; cell cortex; centrosome; cytosol; kinetochore; leading edge; microtubule associated complex; motile primary cilium; nuclear envelope; perinuclear region of cytoplasm
Molecular Function: dynein binding; heparin binding; microtubule binding; phospholipase A2 activity; phospholipase binding; phosphoprotein binding; protein binding; protein homodimerization activity
Biological Process: acrosome formation; actin cytoskeleton organization and biogenesis; adult locomotory behavior; brain morphogenesis; cerebral cortex development; corpus callosum morphogenesis; establishment of mitotic spindle orientation; G2/M transition of mitotic cell cycle; germ cell development; hippocampus development; layer formation in the cerebral cortex; learning and/or memory; microtubule cytoskeleton organization and biogenesis; microtubule organizing center organization and biogenesis; microtubule-based process; neuroblast proliferation; neuromuscular process controlling balance; neuron migration; nuclear migration; platelet activating factor metabolic process; retrograde axon cargo transport; sister chromatid cohesion; synaptic transmission; transmission of nerve impulse; vesicle transport along microtubule
Disease: Lissencephaly 1
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
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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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 12 Y28‑p SNGYEEAySVFKkEA
0 6 K33‑ub EAySVFKkEAELDVN
0 1 K46 VNEELDKKYAGLLEk
0 1 K46 VNEELDKKYAGLLEk
0 2 K53‑ac KYAGLLEkKWTsVIR
0 1 K54 YAGLLEkKWTsVIRL
0 1 K54 YAGLLEkKWTsVIRL
0 1 T56 GLLEkKWTsVIRLQK
0 4 S57‑p LLEkKWTsVIRLQKk
0 1 K64‑ac sVIRLQKkVMELESk
0 1 K71‑ac kVMELESkLNEAkEE
0 1 K71 kVMELESKLNEAkEE
0 8 K76‑ub ESkLNEAkEEFTsGG
0 1 S81‑p EAkEEFTsGGPLGQk
0 6 K88‑ub sGGPLGQkRDPKEWI
0 2 K92 LGQkRDPKEWIPRPP
0 3 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 S348‑p VRGVLFHsGGKFILS
0 1 K360‑ub ILSCADDkTLRVWDY
0 1 K368‑sc TLRVWDYkNKRCMKT
0 3 Y394‑p DFHKTAPyVVTGSVD
  mouse

 
Y28‑p SNGYEEAySVFKkEA
K33‑ub EAySVFKkEAELDMN
K46 MNEELDKKYAGLLEK
K46‑ub MNEELDKkYAGLLEK
K53 kYAGLLEKkWtsVIR
K54 YAGLLEKKWtsVIRL
K54‑ub YAGLLEKkWtsVIRL
T56‑p GLLEKkWtsVIRLQK
S57‑p LLEKkWtsVIRLQKK
K64 sVIRLQKKVMELESk
K71 KVMELESKLNEAkEE
K71‑ub KVMELESkLNEAkEE
K76‑ub ESkLNEAkEEFTSGG
S81 EAkEEFTSGGPLGQk
K88‑ub SGGPLGQkRDPKEWI
K92 LGQkRDPKEWIPRPP
S109‑p YALSGHRsPVTRVIF
K147 GDFERTLKGHTDSVQ
S251 QDGTLIASCSNDQTV
S253 GTLIASCSNDQTVRV
T257 ASCSNDQTVRVWVVA
T265 VRVWVVATKECKAEL
S304 TGSETKKSGkPGPFL
K306‑ub SETKKSGkPGPFLLS
S313 kPGPFLLSGSRDKTI
S315 GPFLLSGSRDKTIKM
T319 LSGSRDKTIKMWDVS
S348 VRGVLFHSGGKFILS
K360 ILSCADDKTLRVWDY
K368 TLRVWDYKNKRCMKT
Y394‑p DFHKTAPyVVTGSVD
  rat

 
Y28 SNGYEEAYSVFKKEA
K33 EAYSVFKKEAELDMN
K46‑ac MNEELDKkYAGLLEK
K46 MNEELDKKYAGLLEK
K53 kYAGLLEKkWTSVIR
K54‑ac YAGLLEKkWTSVIRL
K54 YAGLLEKKWTSVIRL
T56 GLLEKkWTSVIRLQK
S57 LLEKkWTSVIRLQKK
K64 SVIRLQKKVMELESK
K71 KVMELESKLNEAkEE
K71 KVMELESKLNEAkEE
K76‑ub ESKLNEAkEEFTSGG
S81 EAkEEFTSGGPLGQK
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
S348 VRGVLFHSGGKFILS
K360 ILSCADDKTLRVWDY
K368 TLRVWDYKNKRCMKT
Y394 DFHKTAPYVVTGSVD
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