======= CAPZB ======= == Gene Information == * **Official Symbol**: CAPZB * **Official Name**: capping actin protein of muscle Z-line subunit beta * **Aliases and Previous Symbols**: N/A * **Entrez ID**: [[https://www.ncbi.nlm.nih.gov/gene/?term=832|832]] * **UniProt**: [[https://www.uniprot.org/uniprot/P47756|P47756]] * **Interactions**: [[https://thebiogrid.org/search.php?search=CAPZB&organism=9606|BioGRID]] * **PubMed articles**: [[https://www.ncbi.nlm.nih.gov/pubmed/?term=gene%20CAPZB|Open PubMed]] * **OMIM**: [[https://omim.org/entry/601572|Open OMIM]] == Function Summary == * **Entrez Summary**: This gene encodes the beta subunit of the barbed-end actin binding protein, which belongs to the F-actin capping protein family. The capping protein is a heterodimeric actin capping protein that blocks actin filament assembly and disassembly at the fast growing (barbed) filament ends and functions in regulating actin filament dynamics as well as in stabilizing actin filament lengths in muscle and nonmuscle cells. A pseudogene of this gene is located on the long arm of chromosome 2. Multiple alternatively spliced transcript variants encoding different isoforms have been found.[provided by RefSeq, Aug 2013]. * **UniProt Summary**: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}. |F actin cap B| |negative regulation of filopodium assembly| |F-actin capping protein complex| |barbed-end actin filament capping| |WASH complex| |negative regulation of plasma membrane bounded cell projection assembly| |regulation of lamellipodium assembly| |actin filament capping| |negative regulation of actin filament depolymerization| |regulation of lamellipodium organization| |regulation of filopodium assembly| |sarcomere| |regulation of actin filament depolymerization| |negative regulation of actin filament polymerization| |negative regulation of protein depolymerization| |negative regulation of protein polymerization| |negative regulation of protein complex disassembly| |regulation of protein depolymerization| |antigen processing and presentation of exogenous peptide antigen via MHC class II| |antigen processing and presentation of peptide antigen via MHC class II| |antigen processing and presentation of peptide or polysaccharide antigen via MHC class II| |regulation of protein complex disassembly| |negative regulation of supramolecular fiber organization| |negative regulation of protein complex assembly| |negative regulation of cytoskeleton organization| |regulation of actin filament polymerization| |antigen processing and presentation of exogenous peptide antigen| |negative regulation of cell projection organization| |regulation of actin polymerization or depolymerization| |regulation of actin filament length| |antigen processing and presentation of exogenous antigen| |antigen processing and presentation of peptide antigen| |regulation of plasma membrane bounded cell projection assembly| |regulation of cell projection assembly| |actin filament binding| |endoplasmic reticulum to Golgi vesicle-mediated transport| |actin cytoskeleton| |antigen processing and presentation| |regulation of protein polymerization| |regulation of actin filament organization| |actin binding| |blood coagulation| |coagulation| |hemostasis| |cadherin binding| |regulation of actin cytoskeleton organization| |regulation of supramolecular fiber organization| |cytoskeleton| |Golgi vesicle transport| |negative regulation of organelle organization| |regulation of cellular component size| |regulation of actin filament-based process| |regulation of protein complex assembly| |wound healing| |regulation of cell morphogenesis| |actin cytoskeleton organization| |regulation of body fluid levels| |regulation of anatomical structure size| |regulation of cytoskeleton organization| |actin filament-based process| |response to wounding| |regulation of plasma membrane bounded cell projection organization| |negative regulation of cellular component organization| |regulation of cell projection organization| |cell morphogenesis| |cellular component morphogenesis| |regulation of cellular component biogenesis| |regulation of anatomical structure morphogenesis| |cytoskeleton organization| |regulation of organelle organization| |intracellular transport| |establishment of localization in cell| |vesicle-mediated transport| \\ === CRISPR Data === ^Screen^Score^ |[[:results:exp21|MLN-4924 0.2μM R00 exp21]]|-2.17| |[[:results:exp209|Deguelin 0.15μM R05 exp209]]|-2.11| |[[:results:exp30|Rapamycin 10μM R00 exp30]]|-1.75| |[[:results:exp25|Oligomycin-A 2μM R00 exp25]]|-1.74| |[[:results:exp500|LY2090314 0.003μM R08 exp500 no dilution day6]]|-1.71| No correlation found to any other genes in chemogenomics. Global Fraction of Cell Lines Where Essential: 653/739 ^Tissue^Fraction Of Cell Lines Where Essential^ |1290807.0|1/1| |909776.0|1/1| |bile duct|25/28| |blood|27/28| |bone|18/26| |breast|31/33| |central nervous system|49/56| |cervix|4/4| |colorectal|16/17| |esophagus|13/13| |fibroblast|0/1| |gastric|15/16| |kidney|20/21| |liver|19/20| |lung|62/75| |lymphocyte|15/16| |ovary|25/26| |pancreas|23/24| |peripheral nervous system|11/16| |plasma cell|12/15| |prostate|0/1| |skin|19/24| |soft tissue|7/9| |thyroid|2/2| |upper aerodigestive|20/22| |urinary tract|27/29| |uterus|5/5| == Essentiality in NALM6 == * **Essentiality Rank**: 1644 * **Expression level (log2 read counts)**: 6.73 {{:chemogenomics:nalm6 dist.png?nolink |}}