Mouse Anti-WRAP53 Recombinant Antibody (CBT1300) (V2LY-0625-LY2882)

WD Repeat Containing Antisense To TP53

RNA chaperone that plays a key role in telomere maintenance and RNA localization to Cajal bodies (PubMed:29804836, PubMed:29695869).
Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC) (PubMed:19285445, PubMed:20351177, PubMed:29804836, PubMed:29695869).
Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes (PubMed:19179534, PubMed:20351177, PubMed:26170453, PubMed:29695869).
In the telomerase holoenzyme complex, required to stimulate the catalytic activity of the complex (PubMed:27525486, PubMed:29804836).
Acts by specifically binding the CAB box of the TERC RNA and controlling the folding of the CR4/CR5 region of the TERC RNA, a critical step for telomerase activity (PubMed:29804836).
In addition, also controls telomerase holoenzyme complex localization to Cajal body (PubMed:22547674).
During S phase, required for delivery of TERC to telomeres during S phase and for telomerase activity (PubMed:29804836).
In addition to its role in telomere maintenance, also required for Cajal body formation, probably by mediating localization of scaRNAs to Cajal bodies (PubMed:19285445, PubMed:21072240).
Also plays a role in DNA repair: phosphorylated by ATM in response to DNA damage and relocalizes to sites of DNA double-strand breaks to promote the repair of DNA double-strand breaks (PubMed:25512560, PubMed:27715493).
Acts by recruiting the ubiquitin ligase RNF8 to DNA breaks and promote both homologous recombination (HR) and non-homologous end joining (NHEJ) (PubMed:25512560, PubMed:27715493).

Biological Process Cajal body organization Source:UniProtKB1 Publication
Biological Process DNA repair Source:UniProtKB-KW
Biological Process positive regulation of DNA repair Source:UniProtKB1 Publication
Biological Process positive regulation of double-strand break repair Source:UniProtKB1 Publication
Biological Process positive regulation of double-strand break repair via homologous recombination Source:UniProtKB1 Publication
Biological Process positive regulation of double-strand break repair via nonhomologous end joining Source:UniProtKB1 Publication
Biological Process positive regulation of establishment of protein localization to telomere Source:BHF-UCL1 Publication
Biological Process positive regulation of telomerase activity Source:UniProtKB2 Publications
Biological Process protein localization to Cajal body Source:UniProtKB1 Publication
Biological Process RNA folding Source:UniProtKB1 Publication
Biological Process scaRNA localization to Cajal body Source:UniProtKB1 Publication
Biological Process telomerase RNA localization to Cajal body Source:BHF-UCL1 Publication
Biological Process telomere formation via telomerase Source:UniProtKB1 Publication
Biological Process telomere maintenance via telomerase Source:UniProtKB2 Publications

Nucleus, Cajal body
Chromosome, telomere
Chromosome
Released from telomerase RNA template component (TERC) in mitotic cells coincident with delocalization from Cajal bodies (PubMed:26170453).
In response to DNA damage, localizes to sites of DNA double-strand breaks following phosphorylation by ATM (PubMed:26734725, PubMed:27715493).

Dyskeratosis congenita, autosomal recessive, 3 (DKCB3):
A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.

Phosphorylated at Ser-64 by ATM in response to DNA damage, promoting its interaction with histone H2AX and localization to sites of DNA double-strand breaks.