UniProt functional annotation for Q5U5Q9



	UniProt functional annotation for Q5U5Q9

UniProt code: Q5U5Q9.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Ubiquitin-binding protein. Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19536136). 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 (By similarity). {ECO:0000250|UniProtKB:Q96RL1, ECO:0000269|PubMed:19536136}.

Subunit: Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (By similarity). Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (By similarity). In the BRCA1-A complex, interacts directly with ABRAXAS1 (By similarity). Interacts with ESR1 (By similarity). Interacts with UBE2I (By similarity). Interacts with NR6A1 (PubMed:7760852). Interacts with TSP57 (PubMed:12954732). Interacts with TRAIP (By similarity). {ECO:0000250|UniProtKB:Q96RL1, ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:7760852}.

Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96RL1}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q96RL1}.

Domain: The tandem UIM domains form a continuous 60 Angstrom-long alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and UIM2 bind to the proximal and distal ubiquitin moieties and recognize an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM domains determines the selectivity for 'Lys-63'-linkage, and its length is very important for specificity. {ECO:0000269|PubMed:19536136}.

Domain: The Abraxas-interacting region (AIR) mediates the interaction with ABRAXAS1. {ECO:0000250|UniProtKB:Q96RL1}.

Ptm: Sumoylated. {ECO:0000250|UniProtKB:Q96RL1}.

Ptm: Phosphorylated upon DNA damage by ATM or ATR. {ECO:0000250|UniProtKB:Q96RL1}.

Similarity: Belongs to the RAP80 family. {ECO:0000305}.

Sequence caution: Sequence=AAH37092.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Ubiquitin-binding protein. Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19536136). 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 (By similarity). {ECO:0000250\|UniProtKB:Q96RL1, ECO:0000269\|PubMed:19536136}.


Subunit:		Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (By similarity). Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (By similarity). In the BRCA1-A complex, interacts directly with ABRAXAS1 (By similarity). Interacts with ESR1 (By similarity). Interacts with UBE2I (By similarity). Interacts with NR6A1 (PubMed:7760852). Interacts with TSP57 (PubMed:12954732). Interacts with TRAIP (By similarity). {ECO:0000250\|UniProtKB:Q96RL1, ECO:0000269\|PubMed:12954732, ECO:0000269\|PubMed:7760852}.
Subcellular location:		Nucleus {ECO:0000250\|UniProtKB:Q96RL1}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250\|UniProtKB:Q96RL1}.
Domain:		The tandem UIM domains form a continuous 60 Angstrom-long alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and UIM2 bind to the proximal and distal ubiquitin moieties and recognize an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM domains determines the selectivity for 'Lys-63'-linkage, and its length is very important for specificity. {ECO:0000269\|PubMed:19536136}.
Domain:		The Abraxas-interacting region (AIR) mediates the interaction with ABRAXAS1. {ECO:0000250\|UniProtKB:Q96RL1}.
Ptm:		Sumoylated. {ECO:0000250\|UniProtKB:Q96RL1}.
Ptm:		Phosphorylated upon DNA damage by ATM or ATR. {ECO:0000250\|UniProtKB:Q96RL1}.
Similarity:		Belongs to the RAP80 family. {ECO:0000305}.
Sequence caution:		Sequence=AAH37092.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};