CAPZA2 [The Human Chemical-Genetic Interaction Map Project]

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======= CAPZA2 =======


== Gene Information ==
  * **<color #00a2e8>Official Symbol</color>**: CAPZA2
  * **<color #00a2e8>Official Name</color>**: capping actin protein of muscle Z-line subunit alpha 2
  * **<color #00a2e8>Aliases and Previous Symbols</color>**: N/A
  * **<color #00a2e8>Entrez ID</color>**: [[https://www.ncbi.nlm.nih.gov/gene/?term=830|830]]
  * **<color #00a2e8>UniProt</color>**: [[https://www.uniprot.org/uniprot/P47755|P47755]]
  * **<color #00a2e8>Interactions</color>**: [[https://thebiogrid.org/search.php?search=CAPZA2&organism=9606|BioGRID]]
  * **<color #00a2e8>PubMed articles</color>**: [[https://www.ncbi.nlm.nih.gov/pubmed/?term=gene%20CAPZA2|Open PubMed]]
  * **<color #00a2e8>OMIM</color>**: [[https://omim.org/entry/601571|Open OMIM]]

== Function Summary ==
  * **<color #00a2e8>Entrez Summary</color>**: N/A
  * **<color #00a2e8>UniProt Summary</color>**:  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.

<button type='primary' size='sm' modal='Pfam_Domains'>Pfam Domains</button>
<button type='primary' size='sm' modal='GO_terms'>GO Terms</button>


<modal id='Pfam_Domains' size='lg' title='Pfam Domains'>
|F-actin cap A|
</modal>

<modal id='GO_terms' size='lg' title='GO Terms'>
|F-actin capping protein complex|
|barbed-end actin filament capping|
|actin cortical patch|
|actin filament capping|
|negative regulation of actin filament depolymerization|
|regulation of actin filament depolymerization|
|brush border|
|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 or polysaccharide antigen via MHC class II|
|antigen processing and presentation of peptide 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|
|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|
|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|
|blood coagulation|
|coagulation|
|hemostasis|
|regulation of actin cytoskeleton organization|
|regulation of supramolecular fiber organization|
|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|
|actin cytoskeleton organization|
|regulation of body fluid levels|
|regulation of anatomical structure size|
|regulation of cytoskeleton organization|
|actin filament-based process|
|response to wounding|
|negative regulation of cellular component organization|
|innate immune response|
|defense response to other organism|
|regulation of cellular component biogenesis|
|cytoskeleton organization|
|regulation of organelle organization|
|response to other organism|
|response to external biotic stimulus|
|response to biotic stimulus|
|defense response|
|intracellular transport|
|protein-containing complex assembly|
|establishment of localization in cell|
|protein-containing complex subunit organization|
|immune response|
|extracellular region|
|vesicle-mediated transport|
|membrane|
</modal>
\\

 === CRISPR Data ===
<button type='primary' size='small' modal='Compound_Hit'>Compound Hit</button>
<button type='primary' size='small' modal='Most_Correlated_Genes'>Most Correlated Genes in Chemogenomics</button>
<button type='primary' size='small' modal='Essential_Avana'>Tissues where Essential in the Avana Dataset (DepMap 20Q1)</button>

<modal id='Compound_Hit' size='lg' title='Compound Hit'>
^Screen^Score^
|[[:results:exp372|Ibrutinib 1μM R07 exp372]]|-2.14|
|[[:results:exp1|5-Fluorouracil 2μM R00 exp1]]|-1.8|
|[[:results:exp214|2-Deoxy-D-glucose 800μM R05 exp214]]|1.73|
|[[:results:exp152|SGC2043 10μM R03 exp152]]|2.54|
</modal>

<modal id='Most_Correlated_Genes' size='lg' title='Most Correlated Genes in Chemogenomics'>
^Gene^Correlation^
|[[:human genes:r:rrm1|RRM1]]|0.547|
</modal>

<modal id='Essential_Avana' size='lg' title='Tissues where Essential in the Avana Dataset (DepMap 20Q1)'>
Global Fraction of Cell Lines Where Essential: 0/739
^Tissue^Fraction Of Cell Lines Where Essential^
|1290807.0|0/1|
|909776.0|0/1|
|bile duct|0/28|
|blood|0/28|
|bone|0/26|
|breast|0/33|
|central nervous system|0/56|
|cervix|0/4|
|colorectal|0/17|
|esophagus|0/13|
|fibroblast|0/1|
|gastric|0/16|
|kidney|0/21|
|liver|0/20|
|lung|0/75|
|lymphocyte|0/16|
|ovary|0/26|
|pancreas|0/24|
|peripheral nervous system|0/16|
|plasma cell|0/15|
|prostate|0/1|
|skin|0/24|
|soft tissue|0/9|
|thyroid|0/2|
|upper aerodigestive|0/22|
|urinary tract|0/29|
|uterus|0/5|
</modal>

== Essentiality in NALM6  ==
    * **<color #00a2e8>Essentiality Rank</color>**: 4733
    * **<color #00a2e8>Expression level (log2 read counts)</color>**: 5.42 
<button type='primary' size='small' modal='Dist_expr'>Expression Distribution</button>
<modal id='Dist_expr' size='lg' title='CAPZA2 Expression in NALM6 Cells: 5.42'>
{{:chemogenomics:nalm6 dist.png?nolink |}}
</modal>