Aliases for CETN2 Gene
External Ids for CETN2 Gene
Previous HGNC Symbols for CETN2 Gene
Previous GeneCards Identifiers for CETN2 Gene
Caltractin belongs to a family of calcium-binding proteins and is a structural component of the centrosome. The high level of conservation from algae to humans and its association with the centrosome suggested that caltractin plays a fundamental role in the structure and function of the microtubule-organizing center, possibly required for the proper duplication and segregation of the centrosome. [provided by RefSeq, Jul 2008]
GeneCards Summary for CETN2 Gene
CETN2 (Centrin 2) is a Protein Coding gene. Diseases associated with CETN2 include Xeroderma Pigmentosum, Complementation Group C and Xeroderma Pigmentosum, Variant Type. Among its related pathways are Cell Cycle, Mitotic and Transcription-Coupled Nucleotide Excision Repair (TC-NER). Gene Ontology (GO) annotations related to this gene include nucleic acid binding and microtubule binding. An important paralog of this gene is CETN1.
UniProtKB/Swiss-Prot Summary for CETN2 Gene
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.