LIS1_HUMAN - dbPTM
LIS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIS1_HUMAN
UniProt AC P43034
Protein Name Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000255|HAMAP-Rule:MF_03141}
Gene Name PAFAH1B1 {ECO:0000255|HAMAP-Rule:MF_03141}
Organism Homo sapiens (Human).
Sequence Length 410
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle . Nucleus membrane . Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette
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. [PubMed: 22956769]
Protein Sequence MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
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 Orthologous
Protein Cluster
4Phosphorylation----MVLSQRQRDEL
----CCCCHHHHHHH		16.3525599653
21PhosphorylationAIADYLRSNGYEEAY
HHHHHHHHCCCHHHH		31.8224719451
23 (in isoform 2)Ubiquitination-32.2621906983
24PhosphorylationDYLRSNGYEEAYSVF
HHHHHCCCHHHHHHH		18.1728152594
28PhosphorylationSNGYEEAYSVFKKEA
HCCCHHHHHHHHHHC		14.5128152594
29PhosphorylationNGYEEAYSVFKKEAE
CCCHHHHHHHHHHCC		28.2928152594
32AcetylationEEAYSVFKKEAELDV
HHHHHHHHHHCCCCC		47.7725038526
33UbiquitinationEAYSVFKKEAELDVN
HHHHHHHHHCCCCCC		51.1721906983
33 (in isoform 1)Ubiquitination-51.1721906983
332-HydroxyisobutyrylationEAYSVFKKEAELDVN
HHHHHHHHHCCCCCC		51.17-
35 (in isoform 2)Ubiquitination-31.3721906983
45AcetylationDVNEELDKKYAGLLE
CCCHHHHHHHHHHHH		61.3825953088
46AcetylationVNEELDKKYAGLLEK
CCHHHHHHHHHHHHH		39.7425953088
46MalonylationVNEELDKKYAGLLEK
CCHHHHHHHHHHHHH		39.7426320211
46UbiquitinationVNEELDKKYAGLLEK
CCHHHHHHHHHHHHH		39.74-
47PhosphorylationNEELDKKYAGLLEKK
CHHHHHHHHHHHHHH		16.1929496907
53AcetylationKYAGLLEKKWTSVIR
HHHHHHHHHHHHHHH		54.2919608861
532-HydroxyisobutyrylationKYAGLLEKKWTSVIR
HHHHHHHHHHHHHHH		54.29-
53UbiquitinationKYAGLLEKKWTSVIR
HHHHHHHHHHHHHHH		54.2919608861
54AcetylationYAGLLEKKWTSVIRL
HHHHHHHHHHHHHHH		46.4525953088
54UbiquitinationYAGLLEKKWTSVIRL
HHHHHHHHHHHHHHH		46.45-
54MalonylationYAGLLEKKWTSVIRL
HHHHHHHHHHHHHHH		46.4526320211
56PhosphorylationGLLEKKWTSVIRLQK
HHHHHHHHHHHHHHH		23.2329514088
57PhosphorylationLLEKKWTSVIRLQKK
HHHHHHHHHHHHHHH		17.9029514088
64AcetylationSVIRLQKKVMELESK
HHHHHHHHHHHHHHH		33.587823027
64MalonylationSVIRLQKKVMELESK
HHHHHHHHHHHHHHH		33.5826320211
66SulfoxidationIRLQKKVMELESKLN
HHHHHHHHHHHHHHH		7.1730846556
71AcetylationKVMELESKLNEAKEE
HHHHHHHHHHHHHHH		46.0523236377
71UbiquitinationKVMELESKLNEAKEE
HHHHHHHHHHHHHHH		46.05-
76UbiquitinationESKLNEAKEEFTSGG
HHHHHHHHHHHHCCC		52.1521906983
76 (in isoform 1)Ubiquitination-52.1521906983
80PhosphorylationNEAKEEFTSGGPLGQ
HHHHHHHHCCCCCCC		29.7327050516
81PhosphorylationEAKEEFTSGGPLGQK
HHHHHHHCCCCCCCC		47.2621815630
88UbiquitinationSGGPLGQKRDPKEWI
CCCCCCCCCCHHHCC		57.9021906983
882-HydroxyisobutyrylationSGGPLGQKRDPKEWI
CCCCCCCCCCHHHCC		57.90-
88 (in isoform 1)Ubiquitination-57.9021906983
92UbiquitinationLGQKRDPKEWIPRPP
CCCCCCHHHCCCCCH		70.71-
102PhosphorylationIPRPPEKYALSGHRS
CCCCHHHHCCCCCCC		15.8827251275
105PhosphorylationPPEKYALSGHRSPVT
CHHHHCCCCCCCCCE		25.1229214152
109PhosphorylationYALSGHRSPVTRVIF
HCCCCCCCCCEEEEE		20.3215173193
112PhosphorylationSGHRSPVTRVIFHPV
CCCCCCCEEEEEECC		23.7027251275
147 (in isoform 1)Ubiquitination-48.2921906983
147UbiquitinationGDFERTLKGHTDSVQ
CCHHHHHCCCCCCCE		48.292190698
150PhosphorylationERTLKGHTDSVQDIS
HHHHCCCCCCCEEEC		38.3420873877
152PhosphorylationTLKGHTDSVQDISFD
HHCCCCCCCEEECCC		23.8820873877
157PhosphorylationTDSVQDISFDHSGKL
CCCCEEECCCCCCCE		32.6726437602
163UbiquitinationISFDHSGKLLASCSA
ECCCCCCCEEEECCC		43.26-
172SulfoxidationLASCSADMTIKLWDF
EEECCCCEEEEEEEE		4.1121406390
223PhosphorylationIKMWEVQTGYCVKTF
EEEEEEECCEEEEEE		34.9825002506
225PhosphorylationMWEVQTGYCVKTFTG
EEEEECCEEEEEECC		9.4725002506
229PhosphorylationQTGYCVKTFTGHREW
ECCEEEEEECCCCCE		13.1629083192
231PhosphorylationGYCVKTFTGHREWVR
CEEEEEECCCCCEEE		36.9929083192
234MethylationVKTFTGHREWVRMVR
EEEECCCCCEEEEEC		40.60115486327
251PhosphorylationQDGTLIASCSNDQTV
CCCCEEEECCCCCEE		15.87-
253PhosphorylationGTLIASCSNDQTVRV
CCEEEECCCCCEEEE		40.73-
257PhosphorylationASCSNDQTVRVWVVA
EECCCCCEEEEEEEE		17.09-
265PhosphorylationVRVWVVATKECKAEL
EEEEEEEEHHHHHHH		18.77-
266AcetylationRVWVVATKECKAELR
EEEEEEEHHHHHHHH		51.9125953088
269UbiquitinationVVATKECKAELREHE
EEEEHHHHHHHHHCC		46.09-
302UbiquitinationEATGSETKKSGKPGP
HHHCCCCCCCCCCCC		40.67-
303UbiquitinationATGSETKKSGKPGPF
HHCCCCCCCCCCCCE		72.38-
304PhosphorylationTGSETKKSGKPGPFL
HCCCCCCCCCCCCEE		54.31-
306UbiquitinationSETKKSGKPGPFLLS
CCCCCCCCCCCEEEE		54.62-
313PhosphorylationKPGPFLLSGSRDKTI
CCCCEEEECCCCCCE		36.55-
315PhosphorylationGPFLLSGSRDKTIKM
CCEEEECCCCCCEEE		33.65-
319PhosphorylationLSGSRDKTIKMWDVS
EECCCCCCEEEEECC		30.07-
348PhosphorylationVRGVLFHSGGKFILS
EEEEEEECCCEEEEE		41.7423911959
360UbiquitinationILSCADDKTLRVWDY
EEEECCCCCEEEEEC		50.43-
3602-HydroxyisobutyrylationILSCADDKTLRVWDY
EEEECCCCCEEEEEC		50.43-
360AcetylationILSCADDKTLRVWDY
EEEECCCCCEEEEEC		50.4325953088
361PhosphorylationLSCADDKTLRVWDYK
EEECCCCCEEEEECC		27.1328857561
363MethylationCADDKTLRVWDYKNK
ECCCCCEEEEECCCC		32.48115486335
367PhosphorylationKTLRVWDYKNKRCMK
CCEEEEECCCCCHHH		10.7630576142
368UbiquitinationTLRVWDYKNKRCMKT
CEEEEECCCCCHHHH		54.22-
368AcetylationTLRVWDYKNKRCMKT
CEEEEECCCCCHHHH		54.2227452117
368SuccinylationTLRVWDYKNKRCMKT
CEEEEECCCCCHHHH		54.2223954790
370UbiquitinationRVWDYKNKRCMKTLN
EEEECCCCCHHHHCC		42.70-
390UbiquitinationVTSLDFHKTAPYVVT
EEECCCCCCCCEEEE		46.50-
391PhosphorylationTSLDFHKTAPYVVTG
EECCCCCCCCEEEEC		25.0528152594
394PhosphorylationDFHKTAPYVVTGSVD
CCCCCCCEEEECCCC		12.7028152594
397PhosphorylationKTAPYVVTGSVDQTV
CCCCEEEECCCCCEE		17.4428152594
399PhosphorylationAPYVVTGSVDQTVKV
CCEEEECCCCCEEEE		17.1028152594
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIS1_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUDC_HUMANNUDCphysical
9601647
NDEL1_HUMANNDEL1physical
11163260
TBA1A_HUMANTUBA1Aphysical
9384577
LIS1_HUMANPAFAH1B1physical
11889140
DCTN2_HUMANDCTN2physical
11889140
DYHC1_HUMANDYNC1H1physical
11889140
DCX_HUMANDCXphysical
11001923
CLIP1_HUMANCLIP1physical
11940666
PA1B2_HUMANPAFAH1B2physical
10727864
PA1B3_HUMANPAFAH1B3physical
10727864
WDR5_HUMANWDR5physical
17041588
DYL1_HUMANDYNLL1physical
11056532
DCTN1_HUMANDCTN1physical
11056532
HS90A_HUMANHSP90AA1physical
20675372
NUDC_HUMANNUDCphysical
20675372
TAT_HV1H2tatphysical
15698475
PA1B3_HUMANPAFAH1B3physical
19622634
PA1B2_HUMANPAFAH1B2physical
19622634
DYHC1_HUMANDYNC1H1physical
19622634
KTNA1_HUMANKATNA1physical
16203747
KTNB1_HUMANKATNB1physical
16203747
NUDC_HUMANNUDCphysical
12885786
NDE1_HUMANNDE1physical
12885786
NDEL1_HUMANNDEL1physical
12885786
LIS1_HUMANPAFAH1B1physical
12885786
PA1B2_HUMANPAFAH1B2physical
12885786
DCX_HUMANDCXphysical
12885786
CLIP1_HUMANCLIP1physical
12885786
DYHC1_HUMANDYNC1H1physical
12885786
LIS1_HUMANPAFAH1B1physical
16258276
HS90A_HUMANHSP90AA1physical
20133715
PDE4B_HUMANPDE4Bphysical
21652625
PDE4D_HUMANPDE4Dphysical
21652625
DC1I1_HUMANDYNC1I1physical
21652625
NDE1_HUMANNDE1physical
10931877
ASNS_HUMANASNSphysical
22863883
HMGB3_HUMANHMGB3physical
22863883
PAK2_HUMANPAK2physical
22863883
RUXF_HUMANSNRPFphysical
22863883
AP1G1_HUMANAP1G1physical
26344197
ASNS_HUMANASNSphysical
26344197
CHID1_HUMANCHID1physical
26344197
CHM2B_HUMANCHMP2Bphysical
26344197
CSTF1_HUMANCSTF1physical
26344197
DYHC1_HUMANDYNC1H1physical
26344197
SBDS_HUMANSBDSphysical
26344197
SCLY_HUMANSCLYphysical
26344197
DC1I1_HUMANDYNC1I1physical
19622634
DYHC1_HUMANDYNC1H1physical
27173435
PA1B2_HUMANPAFAH1B2physical
27173435
NDEL1_HUMANNDEL1physical
27173435
MARE1_HUMANMAPRE1physical
27173435
TC1D2_HUMANTCTEX1D2physical
27173435
MARE2_HUMANMAPRE2physical
27173435
DLRB2_HUMANDYNLRB2physical
27173435
AHI1_HUMANAHI1physical
27173435
DCTN1_HUMANDCTN1physical
27173435
Drug and Disease Associations
Kegg Disease
H00268 Lissencephaly (LIS); Miller-Dieker syndrome (MDLS)
OMIM Disease
607432Lissencephaly 1 (LIS1)
607432Subcortical band heterotopia (SBH)
247200Miller-Dieker lissencephaly syndrome (MDLS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIS1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-225, AND MASSSPECTROMETRY.

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