Mouse Anti-CETN2 Recombinant Antibody (CBYY-C1895) (CBMAB-C3333-YY)

centrin, EF-hand protein, 2

Cystic Fibrosis Transmembrane Conductance Regulator; Channel Conductance-Controlling ATPase; CAMP-Dependent Chloride Channel; EC 3.6.3.49; ABCC7; Cystic Fibrosis Transmembrane Conductance Regulator, ATP-Binding Cassette (Sub-Family C, Member 7); Cystic Fibrosis Transmembrane Conductance Regulator (ATP-Binding Cassette Sub-Family C, Member 7); Cystic Fibrosis Transmembrane Conductance Regulating; ATP-Binding Cassette Sub-Family C, Member 7;

Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.
Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.
The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.
As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores.

Cell division Source: UniProtKB-KW
Centriole replication Source: UniProtKB
Ciliary basal body-plasma membrane docking Source: Reactome
G2/M transition of mitotic cell cycle Source: Reactome
Global genome nucleotide-excision repair Source: Reactome
Mitotic cell cycle Source: GO_Central
mRNA transport Source: UniProtKB-KW
Nucleotide-excision repair Source: UniProtKB
Nucleotide-excision repair, DNA damage recognition Source: Reactome
Nucleotide-excision repair, DNA duplex unwinding Source: Reactome
Nucleotide-excision repair, preincision complex assembly Source: Reactome
Protein transport Source: UniProtKB-KW
Regulation of cytokinesis Source: UniProtKB
Regulation of G2/M transition of mitotic cell cycle Source: Reactome
Spermatogenesis Source: Ensembl

Nucleus envelope; Nuclear pore complex; Nucleus; Centrosome; Centriole