CAPZB report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0051016Biological processbarbed-end actin filament capping
GO_0030032Biological processlamellipodium assembly
GO_0022604Biological processregulation of cell morphogenesis
GO_0007010Biological processcytoskeleton organization
GO_0008154Biological processactin polymerization or depolymerization
GO_0051490Biological processnegative regulation of filopodium assembly
GO_0000902Biological processcell morphogenesis
GO_0010591Biological processregulation of lamellipodium assembly
GO_0005903Cellular componentbrush border
GO_0005856Cellular componentcytoskeleton
GO_0098685Cellular componentSchaffer collateral - CA1 synapse
GO_0016020Cellular componentmembrane
GO_0070062Cellular componentextracellular exosome
GO_0098686Cellular componenthippocampal mossy fiber to CA3 synapse
GO_0120212Cellular componentsperm head-tail coupling apparatus
GO_0030863Cellular componentcortical cytoskeleton
GO_0015629Cellular componentactin cytoskeleton
GO_0030017Cellular componentsarcomere
GO_0005829Cellular componentcytosol
GO_0014069Cellular componentpostsynaptic density
GO_0008290Cellular componentF-actin capping protein complex
GO_0071203Cellular componentWASH complex
GO_0030027Cellular componentlamellipodium
GO_0045296Molecular functioncadherin binding
GO_0051015Molecular functionactin filament binding
GO_0005515Molecular functionprotein binding
GO_0003779Molecular functionactin binding

IV. Literature review

[source]
Gene nameCAPZB
Protein nameF-actin-capping protein subunit beta
Capping actin protein of muscle Z-line subunit beta
F-actin-capping protein subunit beta (CapZ beta)
SynonymshCG_41078
DescriptionFUNCTION: 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. Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

AccessionsB1AK87
ENST00000674278.1
P47756
ENST00000674228.1
A0A6I8PIN8
ENST00000375142.6 [P47756-1]
ENST00000433834.5
Q7L4N0
ENST00000264202.8 [P47756-2]
A0A6I8PIH4
ENST00000264203.7
B1AK88
B1AK85
ENST00000674449.1
ENST00000674432.1 [P47756-1]
ENST00000375144.6
A0A6I8PRV6