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P43034

- LIS1_HUMAN

UniProt

P43034 - LIS1_HUMAN

Protein

Platelet-activating factor acetylhydrolase IB subunit alpha

Gene

PAFAH1B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    GO - Molecular functioni

    1. dynactin binding Source: BHF-UCL
    2. dynein binding Source: UniProtKB
    3. heparin binding Source: BHF-UCL
    4. microtubule binding Source: BHF-UCL
    5. phospholipase binding Source: BHF-UCL
    6. phosphoprotein binding Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. acrosome assembly Source: BHF-UCL
    2. actin cytoskeleton organization Source: BHF-UCL
    3. adult locomotory behavior Source: BHF-UCL
    4. ameboidal cell migration Source: Ensembl
    5. brain morphogenesis Source: BHF-UCL
    6. cerebral cortex development Source: BHF-UCL
    7. cerebral cortex neuron differentiation Source: Ensembl
    8. corpus callosum morphogenesis Source: BHF-UCL
    9. establishment of centrosome localization Source: Ensembl
    10. establishment of mitotic spindle orientation Source: UniProtKB
    11. G2/M transition of mitotic cell cycle Source: Reactome
    12. hippocampus development Source: BHF-UCL
    13. layer formation in cerebral cortex Source: BHF-UCL
    14. learning or memory Source: BHF-UCL
    15. lipid catabolic process Source: UniProtKB-KW
    16. microtubule-based process Source: UniProtKB
    17. microtubule cytoskeleton organization Source: BHF-UCL
    18. microtubule organizing center organization Source: UniProtKB
    19. mitotic cell cycle Source: Reactome
    20. mitotic nuclear division Source: UniProtKB-KW
    21. negative regulation of JNK cascade Source: Ensembl
    22. negative regulation of neuron projection development Source: Ensembl
    23. neuroblast proliferation Source: BHF-UCL
    24. neuromuscular process controlling balance Source: BHF-UCL
    25. neuron migration Source: UniProtKB
    26. nuclear envelope disassembly Source: Ensembl
    27. nuclear migration Source: Ensembl
    28. osteoclast development Source: Ensembl
    29. platelet activating factor metabolic process Source: BHF-UCL
    30. positive regulation of axon extension Source: Ensembl
    31. positive regulation of cytokine-mediated signaling pathway Source: Ensembl
    32. positive regulation of mitotic cell cycle Source: Ensembl
    33. protein secretion Source: Ensembl
    34. regulation of Rho GTPase activity Source: BHF-UCL
    35. retrograde axon cargo transport Source: BHF-UCL
    36. stem cell division Source: Ensembl
    37. synaptic transmission Source: BHF-UCL
    38. transmission of nerve impulse Source: BHF-UCL
    39. vesicle transport along microtubule Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, Lipid degradation, Lipid metabolism, Mitosis, Neurogenesis, Transport

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiP43034.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-activating factor acetylhydrolase IB subunit alphaUniRule annotation
    Alternative name(s):
    Lissencephaly-1 proteinUniRule annotation
    Short name:
    LIS-1UniRule annotation
    PAF acetylhydrolase 45 kDa subunitUniRule annotation
    Short name:
    PAF-AH 45 kDa subunitUniRule annotation
    PAF-AH alphaUniRule annotation
    Short name:
    PAFAH alphaUniRule annotation
    Gene namesi
    Name:PAFAH1B1UniRule annotation
    Synonyms:LIS1UniRule annotation, MDCR, MDS, PAFAHA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:8574. PAFAH1B1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle UniRule annotation. Nucleus membrane UniRule annotation
    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.By similarity

    GO - Cellular componenti

    1. astral microtubule Source: UniProtKB
    2. cell cortex Source: UniProtKB
    3. cell leading edge Source: Ensembl
    4. centrosome Source: UniProtKB
    5. cytosol Source: BHF-UCL
    6. extracellular vesicular exosome Source: UniProt
    7. growth cone Source: Ensembl
    8. kinesin complex Source: Ensembl
    9. kinetochore Source: UniProtKB
    10. microtubule associated complex Source: UniProtKB
    11. motile primary cilium Source: BHF-UCL
    12. neuronal cell body Source: Ensembl
    13. nuclear envelope Source: UniProtKB
    14. nuclear membrane Source: UniProtKB-SubCell
    15. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311F → S in LIS1. 1 Publication
    VAR_015398
    Natural varianti149 – 1491H → R in LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 1 Publication
    VAR_007724
    Natural varianti162 – 1621G → S in LIS1. 1 Publication
    Corresponds to variant rs28936410 [ dbSNP | Ensembl ].
    VAR_015399
    Natural varianti277 – 2771H → P in LIS1. 1 Publication
    VAR_037301
    Natural varianti317 – 3171D → H in LIS1; reduces neuronal migration in vitro. 1 Publication
    Corresponds to variant rs28936689 [ dbSNP | Ensembl ].
    VAR_015400
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti169 – 1691S → P in SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 1 Publication
    VAR_010203
    Natural varianti241 – 2411R → P in SBH; somatic mosaicism in 18% of lymphocytes and 21% of hair root cells. 1 Publication
    Corresponds to variant rs28936411 [ dbSNP | Ensembl ].
    VAR_037300
    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.

    Keywords - Diseasei

    Disease mutation, Lissencephaly

    Organism-specific databases

    MIMi247200. phenotype.
    607432. phenotype.
    Orphaneti217385. 17p13.3 microduplication syndrome.
    95232. Lissencephaly due to LIS1 mutation.
    531. Miller-Dieker syndrome.
    99796. Subcortical band heterotopia.
    PharmGKBiPA32905.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 410410Platelet-activating factor acetylhydrolase IB subunit alphaPRO_0000051061Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP43034.
    PaxDbiP43034.
    PeptideAtlasiP43034.
    PRIDEiP43034.

    PTM databases

    PhosphoSiteiP43034.

    Expressioni

    Tissue specificityi

    Fairly ubiquitous expression in both the frontal and occipital areas of the brain.

    Gene expression databases

    ArrayExpressiP43034.
    BgeeiP43034.
    CleanExiHS_PAFAH1B1.
    GenevestigatoriP43034.

    Organism-specific databases

    HPAiCAB004489.
    HPA020036.

    Interactioni

    Subunit structurei

    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.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Nde1Q9CZA66EBI-720620,EBI-309934From a different organism.

    Protein-protein interaction databases

    BioGridi111085. 55 interactions.
    DIPiDIP-35691N.
    IntActiP43034. 12 interactions.
    MINTiMINT-5004233.
    STRINGi9606.ENSP00000380378.

    Structurei

    3D structure databases

    ProteinModelPortaliP43034.
    SMRiP43034. Positions 1-79, 92-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 3933LisHUniRule annotationAdd
    BLAST
    Repeati106 – 14742WD 1Add
    BLAST
    Repeati148 – 18740WD 2Add
    BLAST
    Repeati190 – 22940WD 3Add
    BLAST
    Repeati232 – 27140WD 4Add
    BLAST
    Repeati274 – 33360WD 5Add
    BLAST
    Repeati336 – 37742WD 6Add
    BLAST
    Repeati378 – 41033WD 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 102102Interaction with NDEL1UniRule annotationAdd
    BLAST
    Regioni1 – 6666Interaction with NDE1UniRule annotationAdd
    BLAST
    Regioni1 – 3838Required for self-association and interaction with PAFAH1B2 and PAFAH1B3UniRule annotationAdd
    BLAST
    Regioni83 – 410328Interaction with dynein and dynactinAdd
    BLAST
    Regioni367 – 40943Interaction with DCXAdd
    BLAST
    Regioni388 – 41023Interaction with NDEL1UniRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili56 – 8227UniRule annotationAdd
    BLAST

    Domaini

    Dimerization mediated by the LisH domain may be required to activate dynein.UniRule annotation

    Sequence similaritiesi

    Belongs to the WD repeat LIS1/nudF family.UniRule annotation
    Contains 1 LisH domain.UniRule annotation
    Contains 7 WD repeats.UniRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000184015.
    HOVERGENiHBG006271.
    InParanoidiP43034.
    KOiK16794.
    OMAiMKTLYAH.
    PhylomeDBiP43034.
    TreeFamiTF105741.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    HAMAPiMF_03141. lis1.
    InterProiIPR017252. 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]
    PfamiPF08513. LisH. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view]
    PIRSFiPIRSF037647. Dynein_regulator_Lis1. 1 hit.
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00667. LisH. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS50896. LISH. 1 hit.
    PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 7 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P43034-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDVN EELDKKYAGL    50
    LEKKWTSVIR LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE 100
    KYALSGHRSP VTRVIFHPVF SVMVSASEDA TIKVWDYETG DFERTLKGHT 150
    DSVQDISFDH SGKLLASCSA DMTIKLWDFQ GFECIRTMHG HDHNVSSVAI 200
    MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV RPNQDGTLIA 250
    SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE 300
    TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG 350
    KFILSCADDK TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV 400
    DQTVKVWECR 410
    Length:410
    Mass (Da):46,638
    Last modified:January 23, 2007 - v2
    Checksum:i3AB68D2641BA31C9
    GO
    Isoform 2 (identifier: P43034-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:147
    Mass (Da):16,869
    Checksum:iB594509D159C7657
    GO

    Sequence cautioni

    The sequence AAA02882.1 differs from that shown. Reason: Chimeric cDNA.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211S → P in AAL34972. 1 PublicationCurated
    Sequence conflicti21 – 211S → P in AAL34973. 1 PublicationCurated
    Sequence conflicti93 – 931E → G in AAL34973. 1 PublicationCurated
    Sequence conflicti177 – 1771W → R in AAL34973. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311F → S in LIS1. 1 Publication
    VAR_015398
    Natural varianti149 – 1491H → R in LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 1 Publication
    VAR_007724
    Natural varianti162 – 1621G → S in LIS1. 1 Publication
    Corresponds to variant rs28936410 [ dbSNP | Ensembl ].
    VAR_015399
    Natural varianti169 – 1691S → P in SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 1 Publication
    VAR_010203
    Natural varianti241 – 2411R → P in SBH; somatic mosaicism in 18% of lymphocytes and 21% of hair root cells. 1 Publication
    Corresponds to variant rs28936411 [ dbSNP | Ensembl ].
    VAR_037300
    Natural varianti277 – 2771H → P in LIS1. 1 Publication
    VAR_037301
    Natural varianti317 – 3171D → H in LIS1; reduces neuronal migration in vitro. 1 Publication
    Corresponds to variant rs28936689 [ dbSNP | Ensembl ].
    VAR_015400

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei12 – 6453Missing in isoform 2. 1 PublicationVSP_019376Add
    BLAST
    Alternative sequencei134 – 17037Missing in isoform 2. 1 PublicationVSP_019377Add
    BLAST
    Alternative sequencei237 – 2371V → I in isoform 2. 1 PublicationVSP_019378
    Alternative sequencei238 – 410173Missing in isoform 2. 1 PublicationVSP_019379Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS32528.1. [P43034-1]
    PIRiS36113.
    RefSeqiNP_000421.1. NM_000430.3. [P43034-1]
    UniGeneiHs.77318.

    Genome annotation databases

    EnsembliENST00000397195; ENSP00000380378; ENSG00000007168. [P43034-1]
    GeneIDi5048.
    KEGGihsa:5048.
    UCSCiuc002fuw.4. human. [P43034-1]

    Polymorphism databases

    DMDMi1170794.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS32528.1. [P43034-1 ]
    PIRi S36113.
    RefSeqi NP_000421.1. NM_000430.3. [P43034-1 ]
    UniGenei Hs.77318.

    3D structure databases

    ProteinModelPortali P43034.
    SMRi P43034. Positions 1-79, 92-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111085. 55 interactions.
    DIPi DIP-35691N.
    IntActi P43034. 12 interactions.
    MINTi MINT-5004233.
    STRINGi 9606.ENSP00000380378.

    PTM databases

    PhosphoSitei P43034.

    Polymorphism databases

    DMDMi 1170794.

    Proteomic databases

    MaxQBi P43034.
    PaxDbi P43034.
    PeptideAtlasi P43034.
    PRIDEi P43034.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397195 ; ENSP00000380378 ; ENSG00000007168 . [P43034-1 ]
    GeneIDi 5048.
    KEGGi hsa:5048.
    UCSCi uc002fuw.4. human. [P43034-1 ]

    Organism-specific databases

    CTDi 5048.
    GeneCardsi GC17P002496.
    GeneReviewsi PAFAH1B1.
    HGNCi HGNC:8574. PAFAH1B1.
    HPAi CAB004489.
    HPA020036.
    MIMi 247200. phenotype.
    601545. gene.
    607432. phenotype.
    neXtProti NX_P43034.
    Orphaneti 217385. 17p13.3 microduplication syndrome.
    95232. Lissencephaly due to LIS1 mutation.
    531. Miller-Dieker syndrome.
    99796. Subcortical band heterotopia.
    PharmGKBi PA32905.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000184015.
    HOVERGENi HBG006271.
    InParanoidi P43034.
    KOi K16794.
    OMAi MKTLYAH.
    PhylomeDBi P43034.
    TreeFami TF105741.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_682. Mitotic Prometaphase.
    SignaLinki P43034.

    Miscellaneous databases

    ChiTaRSi PAFAH1B1. human.
    GeneWikii PAFAH1B1.
    GenomeRNAii 5048.
    NextBioi 19452.
    PROi P43034.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43034.
    Bgeei P43034.
    CleanExi HS_PAFAH1B1.
    Genevestigatori P43034.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    HAMAPi MF_03141. lis1.
    InterProi IPR017252. 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 ]
    Pfami PF08513. LisH. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view ]
    PIRSFi PIRSF037647. Dynein_regulator_Lis1. 1 hit.
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00667. LisH. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS50896. LISH. 1 hit.
    PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 7 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon.
    7. 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. 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. 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.

    Entry informationi

    Entry nameiLIS1_HUMAN
    AccessioniPrimary (citable) accession number: P43034
    Secondary accession number(s): B2R7Q7, Q8WZ88, Q8WZ89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3