P43034 (LIS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet-activating factor acetylhydrolase IB subunit alpha

Alternative name(s):
Lissencephaly-1 protein
Short name=LIS-1
PAF acetylhydrolase 45 kDa subunit
Short name=PAF-AH 45 kDa subunit
PAF-AH alpha
Short name=PAFAH alpha

Gene names

Name:	PAFAH1B1
Synonyms:	LIS1, MDCR, MDS, PAFAHA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.15
Subunit structure	Component of cytosolic PAF-AH IB, which is composed of PAFAH1B1 (alpha), PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Trimer formation is not essential for the catalytic activity of the enzyme which is contributed solely by the PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Interacts with IQGAP1, KATNB1 and NUDC. Interacts with DAB1 when DAB1 is phosphorylated in response to RELN/reelin signaling By similarity. Can self-associate. Interacts with DCX, dynein, dynactin, NDE1, NDEL1 and RSN. Interacts with DISC1, and this interaction is enhanced by NDEL1. Interacts with ASUN. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.19
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle By similarity. Nucleus membrane Potential. Note: Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes By similarity. Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Ref.11 Ref.12 Ref.15
Tissue specificity	Fairly ubiquitous expression in both the frontal and occipital areas of the brain.
Domain	Dimerization mediated by the LisH domain may be required to activate dynein By similarity. HAMAP-Rule MF_03141
Involvement in disease	Lissencephaly 1 (LIS1) [MIM:607432]: A classical lissencephaly. It is characterized by agyria or pachygyria and disorganization of the clear neuronal lamination of normal six-layered cortex. The cortex is abnormally thick and poorly organized with 4 primitive layers. Associated with enlarged and dysmorphic ventricles and often hypoplasia of the corpus callosum. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.10 Ref.15 Ref.21 Ref.23 Subcortical band heterotopia (SBH) [MIM:607432]: SBH is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.15 Ref.20 Ref.22 Miller-Dieker lissencephaly syndrome (MDLS) [MIM:247200]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the WD repeat LIS1/nudF family. Contains 1 LisH domain. Contains 7 WD repeats.
Sequence caution	The sequence AAA02882.1 differs from that shown. Reason: Chimeric cDNA.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Lipid degradation Lipid metabolism Mitosis Neurogenesis Transport
Cellular component	Cytoplasm Cytoskeleton Membrane Microtubule Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Lissencephaly
Domain	Coiled coil Repeat WD repeat
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome acrosome assembly Inferred from sequence or structural similarity. Source: BHF-UCL actin cytoskeleton organization Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL adult locomotory behavior Inferred from mutant phenotype Ref.2. Source: BHF-UCL ameboidal cell migration Inferred from electronic annotation. Source: Compara brain morphogenesis Inferred from mutant phenotype Ref.2. Source: BHF-UCL cerebral cortex neuron differentiation Inferred from electronic annotation. Source: Compara corpus callosum morphogenesis Inferred from mutant phenotype Ref.2. Source: BHF-UCL establishment of centrosome localization Inferred from electronic annotation. Source: Compara establishment of mitotic spindle orientation Inferred from mutant phenotype PubMed 11056532. Source: UniProtKB hippocampus development Inferred from sequence or structural similarity. Source: BHF-UCL layer formation in cerebral cortex Inferred from sequence or structural similarity. Source: BHF-UCL learning or memory Inferred from sequence or structural similarity. Source: BHF-UCL lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center organization Inferred from mutant phenotype Ref.10. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome negative regulation of JNK cascade Inferred from electronic annotation. Source: Compara negative regulation of neuron projection development Inferred from electronic annotation. Source: Compara neuroblast proliferation Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL neuromuscular process controlling balance Inferred from mutant phenotype Ref.2. Source: BHF-UCL neuron migration Inferred from mutant phenotype Ref.10. Source: UniProtKB nuclear envelope disassembly Inferred from electronic annotation. Source: Compara nuclear migration Inferred from electronic annotation. Source: Compara osteoclast development Inferred from electronic annotation. Source: Compara platelet activating factor metabolic process Inferred from sequence or structural similarity PubMed 8028668. Source: BHF-UCL positive regulation of axon extension Inferred from electronic annotation. Source: Compara positive regulation of cytokine-mediated signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara protein secretion Inferred from electronic annotation. Source: Compara regulation of Rho GTPase activity Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL retrograde axon cargo transport Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL stem cell division Inferred from electronic annotation. Source: Compara synaptic transmission Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL vesicle transport along microtubule Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL
Cellular_component	astral microtubule Inferred from direct assay Ref.12. Source: UniProtKB axon part Inferred from electronic annotation. Source: Compara cell cortex Inferred from direct assay Ref.12. Source: UniProtKB cell leading edge Inferred from electronic annotation. Source: Compara centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytosol Inferred from sequence or structural similarity PubMed 8028668. Source: BHF-UCL growth cone Inferred from electronic annotation. Source: Compara kinesin complex Inferred from electronic annotation. Source: Compara kinetochore Inferred from direct assay PubMed 11056532Ref.11Ref.12. Source: UniProtKB microtubule associated complex Inferred from direct assay Ref.11. Source: UniProtKB motile primary cilium Inferred from sequence or structural similarity. Source: BHF-UCL neuronal cell body Inferred from electronic annotation. Source: Compara nuclear envelope Inferred from direct assay Ref.12. Source: UniProtKB nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	dynactin binding Inferred from sequence or structural similarity PubMed 11056532. Source: BHF-UCL dynein binding Inferred from direct assay Ref.11. Source: UniProtKB heparin binding Inferred from sequence or structural similarity PubMed 8028668. Source: BHF-UCL microtubule binding Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL phospholipase binding Inferred from sequence or structural similarity PubMed 8028668. Source: BHF-UCL phosphoprotein binding Inferred from sequence or structural similarity. Source: BHF-UCL protein homodimerization activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Nde1	Q9CZA6	6	EBI-720620,EBI-309934	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P43034-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P43034-2)

The sequence of this isoform differs from the canonical sequence as follows:
     12-64: Missing.
     134-170: Missing.
     237-237: V → I
     238-410: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 410	410	Platelet-activating factor acetylhydrolase IB subunit alpha HAMAP-Rule MF_03141		PRO_0000051061
Regions
	Domain	7 – 39	33	LisH
	Repeat	106 – 147	42	WD 1 HAMAP-Rule MF_03141
	Repeat	148 – 187	40	WD 2 HAMAP-Rule MF_03141
	Repeat	190 – 229	40	WD 3 HAMAP-Rule MF_03141
	Repeat	232 – 271	40	WD 4 HAMAP-Rule MF_03141
	Repeat	274 – 333	60	WD 5 HAMAP-Rule MF_03141
	Repeat	336 – 377	42	WD 6 HAMAP-Rule MF_03141
	Repeat	378 – 410	33	WD 7 HAMAP-Rule MF_03141
	Region	1 – 102	102	Interaction with NDEL1 By similarity
	Region	1 – 66	66	Interaction with NDE1 By similarity
	Region	1 – 38	38	Required for self-association and interaction with PAFAH1B2 and PAFAH1B3 By similarity
	Region	83 – 410	328	Interaction with dynein and dynactin HAMAP-Rule MF_03141
	Region	367 – 409	43	Interaction with DCX HAMAP-Rule MF_03141
	Region	388 – 410	23	Interaction with NDEL1 By similarity
	Coiled coil	56 – 82	27	Potential
Amino acid modifications
	Modified residue	28	1	Phosphotyrosine By similarity
	Modified residue	53	1	N6-acetyllysine Ref.17
Natural variations
	Alternative sequence	12 – 64	53	Missing in isoform 2.		VSP_019376
	Alternative sequence	134 – 170	37	Missing in isoform 2.		VSP_019377
	Alternative sequence	237	1	V → I in isoform 2.		VSP_019378
	Alternative sequence	238 – 410	173	Missing in isoform 2.		VSP_019379
	Natural variant	31	1	F → S in LIS1. Ref.21		VAR_015398
	Natural variant	149	1	H → R in LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro. Ref.2 Ref.10 Ref.15		VAR_007724
	Natural variant	162	1	G → S in LIS1. Ref.21 Corresponds to variant rs28936410 [ dbSNP | Ensembl ].		VAR_015399
	Natural variant	169	1	S → P in SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro. Ref.10 Ref.15 Ref.20		VAR_010203
	Natural variant	241	1	R → P in SBH; somatic mosaicism in 18% of lymphocytes and 21% of hair root cells. Ref.22 Corresponds to variant rs28936411 [ dbSNP | Ensembl ].		VAR_037300
	Natural variant	277	1	H → P in LIS1. Ref.23		VAR_037301
	Natural variant	317	1	D → H in LIS1; reduces neuronal migration in vitro. Ref.15 Ref.21 Corresponds to variant rs28936689 [ dbSNP | Ensembl ].		VAR_015400
Experimental info
	Sequence conflict	21	1	S → P in AAL34972. Ref.3
	Sequence conflict	21	1	S → P in AAL34973. Ref.3
	Sequence conflict	93	1	E → G in AAL34973. Ref.3
	Sequence conflict	177	1	W → R in AAL34973. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3AB68D2641BA31C9	FASTA	410	46,638
	10 20 30 40 50 60 MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDVN EELDKKYAGL LEKKWTSVIR 70 80 90 100 110 120 LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF 130 140 150 160 170 180 SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ 190 200 210 220 230 240 GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV 250 260 270 280 290 300 RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE 310 320 330 340 350 360 TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK 370 380 390 400 410 TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR
	Isoform 2 [UniParc]. Checksum: B594509D159C7657	FASTA	147	16,869
	10 20 30 40 50 60 MVLSQRQRDE LVMELESKLN EAKEEFTSGG PLGQKRDPKE WIPRPPEKYA LSGHRSPVTR 70 80 90 100 110 120 VIFHPVFSVM VSASEDATIK DMTIKLWDFQ GFECIRTMHG HDHNVSSVAI MPNGDHIVSA 130 140 SRDKTIKMWE VQTGYCVKTF TGHREWI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a Miller-Dieker lissencephaly gene containing G protein beta-subunit-like repeats." Reiner O., Carrozzo R., Shen Y., Wehnert M., Faustinella F., Dobyns W.B., Caskey C.T., Ledbetter D.H. Nature 364:717-721(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain and Kidney.
[2]	"Point mutations and an intragenic deletion in LIS1, the lissencephaly causative gene in isolated lissencephaly sequence and Miller-Dieker syndrome." Lo Nigro C., Chong S.S., Smith A.C.M., Dobyns W.B., Carrozzo R., Ledbetter D.H. Hum. Mol. Genet. 6:157-164(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LIS1 ARG-149.
[3]	"High expression of the lissencephaly gene in hepatocarcinoma patients." Zhao M.J., Xia S.L., Li T.P. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[4]	Feng Z., Zhang B., Peng X., Yuan J., Qiang B. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hippocampus.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Colon.
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[9]	"Interaction between LIS1 and doublecortin, two lissencephaly gene products." Caspi M., Atlas R., Kantor A., Sapir T., Reiner O. Hum. Mol. Genet. 9:2205-2213(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCX.
[10]	"LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome." Feng Y., Olson E.C., Stukenberg P.T., Flanagan L.A., Kirschner M.W., Walsh C.A. Neuron 28:665-679(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDE1, CHARACTERIZATION OF VARIANTS LIS1 ARG-149 AND SBH PRO-169.
[11]	"Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function." Tai C.-Y., Dujardin D.L., Faulkner N.E., Vallee R.B. J. Cell Biol. 156:959-968(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SELF-ASSOCIATION, INTERACTION WITH RSN; DYNEIN AND DYNACTIN, SUBCELLULAR LOCATION.
[12]	"LIS1, CLIP-170's key to the dynein/dynactin pathway." Coquelle F.M., Caspi M., Cordelieres F.P., Dompierre J.P., Dujardin D.L., Koifman C., Martin P., Hoogenraad C.C., Akhmanova A., Galjart N., De Mey J.R., Reiner O. Mol. Cell. Biol. 22:3089-3102(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"Human Nudel and NudE as regulators of cytoplasmic dynein in poleward protein transport along the mitotic spindle." Yan X., Li F., Liang Y., Shen Y., Zhao X., Huang Q., Zhu X. Mol. Cell. Biol. 23:1239-1250(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDEL1.
[14]	"Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein." Liang Y., Yu W., Li Y., Yang Z., Yan X., Huang Q., Zhu X. J. Cell Biol. 164:557-566(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDEL1.
[15]	"Lis1 and doublecortin function with dynein to mediate coupling of the nucleus to the centrosome in neuronal migration." Tanaka T., Serneo F.F., Higgins C., Gambello M.J., Wynshaw-Boris A., Gleeson J.G. J. Cell Biol. 165:709-721(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS LIS1 ARG-149; SBH PRO-169 AND LIS1 HIS-317.
[16]	"Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders." Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M., Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S., Whiting P.J. Mol. Cell. Neurosci. 25:42-55(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DISC1.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, MASS SPECTROMETRY.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Human Asunder promotes dynein recruitment and centrosomal tethering to the nucleus at mitotic entry." Jodoin J.N., Shboul M., Sitaram P., Zein-Sabatto H., Reversade B., Lee E., Lee L.A. Mol. Biol. Cell 23:4713-4724(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASUN.
[20]	"Subcortical band heterotopia in rare affected males can be caused by missense mutations in DCX (XLIS) or LIS1." Pilz D.T., Kuc J., Matsumoto N., Bodurtha J., Bernadi B., Tassinari C.A., Dobyns W.B., Ledbetter D.H. Hum. Mol. Genet. 8:1757-1760(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SBH PRO-169.
[21]	"LIS1 missense mutations cause milder lissencephaly phenotypes including a child with normal IQ." Leventer R.J., Cardoso C., Ledbetter D.H., Dobyns W.B. Neurology 57:416-422(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LIS1 SER-31; SER-162 AND HIS-317.
[22]	"Mosaic mutations of the LIS1 gene cause subcortical band heterotopia." Sicca F., Kelemen A., Genton P., Das S., Mei D., Moro F., Dobyns W.B., Guerrini R. Neurology 61:1042-1046(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SBH PRO-241.
[23]	"Mutation screening in a cohort of patients with lissencephaly and subcortical band heterotopia." Torres F.R., Montenegro M.A., Marques-de-Faria A.P., Guerreiro M.M., Cendes F., Lopes-Cendes I. Neurology 62:799-802(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LIS1 PRO-277.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	L13385 mRNA. Translation: AAA02880.1. L13386 mRNA. Translation: AAA02881.1. L13387 mRNA. Translation: AAA02882.1. Sequence problems. U72342 , U72334, U72335, U72336, U72337, U72338, U72339, U72340, U72341 Genomic DNA. Translation: AAC51111.1. AF208837 mRNA. Translation: AAL34972.1. AF208838 mRNA. Translation: AAL34973.1. AF400434 mRNA. Translation: AAK92483.1. AK313078 mRNA. Translation: BAG35904.1. BX538346 mRNA. Translation: CAD98141.1. CH471108 Genomic DNA. Translation: EAW90536.1. BC064638 mRNA. Translation: AAH64638.1.
IPI	IPI00218728. IPI00760905.
PIR	S36113.
RefSeq	NP_000421.1. NM_000430.3.
UniGene	Hs.77318.
3D structure databases
ProteinModelPortal	P43034.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35691N.
IntAct	P43034. 11 interactions.
MINT	MINT-5004233.
STRING	9606.ENSP00000380378.
PTM databases
PhosphoSite	P43034.
Polymorphism databases
DMDM	1170794.
Proteomic databases
PaxDb	P43034.
PeptideAtlas	P43034.
PRIDE	P43034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000397195; ENSP00000380378; ENSG00000007168.
GeneID	5048.
KEGG	hsa:5048.
UCSC	uc002fuw.4. human.
Organism-specific databases
CTD	5048.
GeneCards	GC17P002496.
HGNC	HGNC:8574. PAFAH1B1.
HPA	CAB004489. HPA020036.
MIM	247200. phenotype. 601545. gene. 607432. phenotype.
neXtProt	NX_P43034.
Orphanet	217385. 17p13.3 microduplication syndrome. 95232. Lissencephaly due to LIS1 mutation. 531. Miller-Dieker syndrome.
PharmGKB	PA32905.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOGENOM	HOG000184015.
HOVERGEN	HBG006271.
InParanoid	P43034.
KO	K16794.
OMA	WVRGLAF.
OrthoDB	EOG4P5K93.
PhylomeDB	P43034.
Enzyme and pathway databases
Pathway_Interaction_DB	lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development. reelinpathway. Reelin signaling pathway.
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	P43034.
Bgee	P43034.
CleanEx	HS_PAFAH1B1.
Genevestigator	P43034.
GermOnline	ENSG00000007168. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.10. 1 hit.
HAMAP	MF_03141. lis1.
InterPro	IPR017252. Dynein_regulator. IPR020472. G-protein_beta_WD-40_rep. IPR006594. LisH_dimerisation. IPR013720. LisH_dimerisation_subgr. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
PANTHER	PTHR22847:SF51. PTHR22847:SF51. 1 hit.
Pfam	PF08513. LisH. 1 hit. PF00400. WD40. 7 hits. [Graphical view]
PIRSF	PIRSF037647. Dynein_regulator_Lis1. 1 hit.
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00667. LisH. 1 hit. SM00320. WD40. 7 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS50896. LISH. 1 hit. PS00678. WD_REPEATS_1. 4 hits. PS50082. WD_REPEATS_2. 7 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PAFAH1B1. human.
GenomeRNAi	5048.
NextBio	19452.
SOURCE	Search...

Entry information

Entry name

LIS1_HUMAN

Accession

Primary (citable) accession number: P43034
Secondary accession number(s): B2R7Q7, Q8WZ88, Q8WZ89

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.