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The annotation and conditions in this rule are derived from the following entries: P43034 (LIS1_HUMAN), Q00664 (LIS1_EMENI)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_03141
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi

  • Recommended name:
    Platelet-activating factor acetylhydrolase IB subunit alpha
    Alternative name(s):
    PAF-AH alpha
    Short name:
    PAFAH alpha
    PAF acetylhydrolase 45 kDa subunit
    Short name:
    PAF-AH 45 kDa subunit
    Lissencephaly-1 protein
    Short name:
    LIS-1
  • Recommended name:
    Nuclear distribution protein nudF
    Alternative name(s):
    Lissencephaly-1 homolog
    Short name:
    LIS-1
  • Recommended name:
    Nuclear distribution protein PAC1
    Alternative name(s):
    Lissencephaly-1 homolog
    Short name:
    LIS-1
    nudF homolog
  • Recommended name:
    Lissencephaly-1 homolog

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi

  • Name:PAFAH1B1, Synonym:LIS1
  • Name:nudF, Synonym:lis1
  • Name:Lis-1
  • Name:lis-1
  • Name:PAC1, Synonym:LIS1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    • Cytoplasm
    • Cytoplasm
    • Cytoplasm
    • Nucleus membrane
    • Note: Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes.
    • Cytoplasm
    • Cytoplasm
    • Note: Localizes to the plus ends of microtubules at the hyphal tip and the mitotic spindle poles.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Can self-associate. Interacts with DCX, dynein, dynactin, IQGAP1, KATNB1, NDE1, NDEL1, NUDC and RSN. Interacts with DISC1, and this interaction is enhanced by NDEL1. Interacts with DAB1 when DAB1 is phosphorylated in response to RELN/reelin signaling. 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.
  • May be a component of a dynein regulatory complex composed of at least lis-1 and nud-2. Interacts with nud-2.
  • Self-associates. Interacts with nudE and dynein.
  • Self-associates. Interacts with NDL1 and dynein.
  • Can self-associate. Interacts with dynein, dynactin, NDE1 and NDEL1.

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This section describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • 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. Also 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. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position.
  • Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. May be required for proliferation of neuronal precursors and neuronal migration.
  • 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.
  • Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck.
  • 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 nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili

  • (to residues corresponding to positions @FROM@i - @TO@i)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei

  • Removed (to residues corresponding to position 1)

<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • Interaction with DCX (to residues corresponding to positions 367 - 409)
  • Interaction with NDEL1 (to residues corresponding to positions @NTER@i - 102)
  • Interaction with dynein and dynactin (to residues corresponding to positions 83 - @CTER@i)
  • Interaction with NDE1 (to residues corresponding to positions @NTER@i - 66)
  • Required for self-association and interaction with PAFAH1B2 and PAFAH1B3 (to residues corresponding to positions @NTER@i - 38)
  • Interaction with NDEL1 (to residues corresponding to positions 388 - @CTER@i)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

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