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pafah1b1b - platelet-activating factor acetylhydrolase 1b, regulatory subunit 1b (zebrafish)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-18
Description
Predicted to enable dynein complex binding activity; microtubule plus-end binding activity; and protein heterodimerization activity. Acts upstream of or within several processes, including apical protein localization; brain morphogenesis; and photoreceptor cell maintenance. Located in cytoplasm. Is expressed in several structures, including bone tissue; heart; liver; nervous system; and pleuroperitoneal region. Human ortholog(s) of this gene implicated in lissencephaly and lissencephaly 1. Orthologous to human PAFAH1B1 (platelet activating factor acetylhydrolase 1b regulatory subunit 1).

1 Names and Identifiers

1.1 Synonyms

  • Lis1a
  • lissencephaly-1 homolog B

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Wikidata

1.2.4 ZFIN ID

2 Proteins

2.1 Protein Function

Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in the PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (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. May be required for proliferation of neuronal precursors and neuronal migration (By similarity). Involved in the positioning of nuclei in photoreceptor cells.

2.2 Protein 3D Structures

2.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

2.3 Protein Targets

3 Interactions and Pathways

3.1 Chemical-Gene Interactions

3.2 Interactions

3.3 Pathways

4 Expression

5 Literature

5.1 Consolidated References

5.2 Gene-Gene Co-Occurrences in Literature

5.3 Gene-Disease Co-Occurrences in Literature

6 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  4. Comparative Toxicogenomics Database (CTD)
    LICENSE
    It is to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of NC State University.
    http://ctdbase.org/about/legal.jsp
  5. NCBI Gene Expression Omnibus (GEO)
  6. STRING: functional protein association networks
  7. The Zebrafish Information Network (ZFIN)
    LICENSE
    ZFIN data and data annotations are licensed under a Creative Commons Attribution 4.0 International License
    https://zfin.atlassian.net/wiki/spaces/general/pages/1942160112/WARRANTY+AND+LIABILITY+DISCLAIMER+OWNERSHIP+AND+LIMITS+ON+USE
  8. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  9. Wikidata
  10. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
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