UIMC1

This gene encodes a nuclear protein that interacts with Brca1 (breast cancer 1) in a complex to recognize and repair DNA lesions. This protein binds ubiquitinated lysine 63 of histone H2A and H2AX. This protein may also function as a repressor of transcription. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2015]

Ubiquitin Interaction Motif Containing 1

Ubiquitin-binding protein (PubMed:24627472).
Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19328070, Ref.38). Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1.

Biological Process chromatin organization Source:UniProtKB-KW
Biological Process double-strand break repair Source:UniProtKB5 Publications
Biological Process histone H2A K63-linked deubiquitination Source:UniProtKB1 Publication
Biological Process mitotic G2 DNA damage checkpoint signaling Source:UniProtKB5 Publications
Biological Process mitotic G2/M transition checkpoint Source:ComplexPortal1 Publication
Biological Process negative regulation of DNA-templated transcription Source:HGNC-UCL1 Publication
Biological Process positive regulation of DNA repair Source:UniProtKB5 Publications
Biological Process regulation of DNA repair Source:ComplexPortal1 Publication
Biological Process response to ionizing radiation Source:UniProtKB5 Publications

Nucleus
Localizes at sites of DNA damage at double-strand breaks (DSBs).

Sumoylated.
Phosphorylated upon DNA damage by ATM or ATR.