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P43034 (LIS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle 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 processCell cycle
Cell division
Differentiation
Lipid degradation
Lipid metabolism
Mitosis
Neurogenesis
Transport
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Lissencephaly
   DomainCoiled coil
Repeat
WD repeat
   Molecular functionDevelopmental protein
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/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: Ensembl

brain morphogenesis

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

cerebral cortex development

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

cerebral cortex neuron differentiation

Inferred from electronic annotation. Source: Ensembl

corpus callosum morphogenesis

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

establishment of centrosome localization

Inferred from electronic annotation. Source: Ensembl

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 cytoskeleton organization

Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL

microtubule organizing center organization

Inferred from mutant phenotype Ref.10. Source: UniProtKB

microtubule-based process

Inferred from direct assay Ref.12. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

nuclear migration

Inferred from electronic annotation. Source: Ensembl

osteoclast development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of cytokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

protein secretion

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

synaptic transmission

Inferred from sequence or structural similarity PubMed 10729324. Source: BHF-UCL

transmission of nerve impulse

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_componentastral microtubule

Inferred from direct assay Ref.12. Source: UniProtKB

cell cortex

Inferred from direct assay Ref.12. Source: UniProtKB

cell leading edge

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity PubMed 8028668. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

growth cone

Inferred from electronic annotation. Source: Ensembl

kinesin complex

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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

   Molecular_functiondynactin 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

Nde1Q9CZA66EBI-720620,EBI-309934From 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Platelet-activating factor acetylhydrolase IB subunit alpha HAMAP-Rule MF_03141
PRO_0000051061

Regions

Domain7 – 3933LisH
Repeat106 – 14742WD 1 HAMAP-Rule MF_03141
Repeat148 – 18740WD 2 HAMAP-Rule MF_03141
Repeat190 – 22940WD 3 HAMAP-Rule MF_03141
Repeat232 – 27140WD 4 HAMAP-Rule MF_03141
Repeat274 – 33360WD 5 HAMAP-Rule MF_03141
Repeat336 – 37742WD 6 HAMAP-Rule MF_03141
Repeat378 – 41033WD 7 HAMAP-Rule MF_03141
Region1 – 102102Interaction with NDEL1 By similarity
Region1 – 6666Interaction with NDE1 By similarity
Region1 – 3838Required for self-association and interaction with PAFAH1B2 and PAFAH1B3 By similarity
Region83 – 410328Interaction with dynein and dynactin HAMAP-Rule MF_03141
Region367 – 40943Interaction with DCX HAMAP-Rule MF_03141
Region388 – 41023Interaction with NDEL1 By similarity
Coiled coil56 – 8227 Potential

Amino acid modifications

Modified residue531N6-acetyllysine Ref.17

Natural variations

Alternative sequence12 – 6453Missing in isoform 2.
VSP_019376
Alternative sequence134 – 17037Missing in isoform 2.
VSP_019377
Alternative sequence2371V → I in isoform 2.
VSP_019378
Alternative sequence238 – 410173Missing in isoform 2.
VSP_019379
Natural variant311F → S in LIS1. Ref.21
VAR_015398
Natural variant1491H → R in LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro. Ref.2 Ref.10 Ref.15
VAR_007724
Natural variant1621G → S in LIS1. Ref.21
Corresponds to variant rs28936410 [ dbSNP | Ensembl ].
VAR_015399
Natural variant1691S → P in SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro. Ref.10 Ref.15 Ref.20
VAR_010203
Natural variant2411R → 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 variant2771H → P in LIS1. Ref.23
VAR_037301
Natural variant3171D → H in LIS1; reduces neuronal migration in vitro. Ref.15 Ref.21
Corresponds to variant rs28936689 [ dbSNP | Ensembl ].
VAR_015400

Experimental info

Sequence conflict211S → P in AAL34972. Ref.3
Sequence conflict211S → P in AAL34973. Ref.3
Sequence conflict931E → G in AAL34973. Ref.3
Sequence conflict1771W → R in AAL34973. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3AB68D2641BA31C9

FASTA41046,638
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B594509D159C7657
Show »

FASTA14716,869

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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

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 expand/collapse EMBL AC list , 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.
PIRS36113.
RefSeqNP_000421.1. NM_000430.3.
UniGeneHs.77318.

3D structure databases

ProteinModelPortalP43034.
SMRP43034. Positions 1-79, 92-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111085. 54 interactions.
DIPDIP-35691N.
IntActP43034. 12 interactions.
MINTMINT-5004233.
STRING9606.ENSP00000380378.

PTM databases

PhosphoSiteP43034.

Polymorphism databases

DMDM1170794.

Proteomic databases

PaxDbP43034.
PeptideAtlasP43034.
PRIDEP43034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397195; ENSP00000380378; ENSG00000007168. [P43034-1]
GeneID5048.
KEGGhsa:5048.
UCSCuc002fuw.4. human. [P43034-1]

Organism-specific databases

CTD5048.
GeneCardsGC17P002496.
HGNCHGNC:8574. PAFAH1B1.
HPACAB004489.
HPA020036.
MIM247200. phenotype.
601545. gene.
607432. phenotype.
neXtProtNX_P43034.
Orphanet217385. 17p13.3 microduplication syndrome.
95232. Lissencephaly due to LIS1 mutation.
531. Miller-Dieker syndrome.
99796. Subcortical band heterotopia.
PharmGKBPA32905.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000184015.
HOVERGENHBG006271.
InParanoidP43034.
KOK16794.
OMAWVRGLAF.
PhylomeDBP43034.
TreeFamTF105741.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkP43034.

Gene expression databases

ArrayExpressP43034.
BgeeP43034.
CleanExHS_PAFAH1B1.
GenevestigatorP43034.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
HAMAPMF_03141. lis1.
InterProIPR017252. Dynein_regulator_LIS1.
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]
PfamPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PIRSFPIRSF037647. Dynein_regulator_Lis1. 1 hit.
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00667. LisH. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAFAH1B1. human.
GeneWikiPAFAH1B1.
GenomeRNAi5048.
NextBio19452.
PROP43034.
SOURCESearch...

Entry information

Entry nameLIS1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM