UniProt functional annotation for E2AXC7



	UniProt functional annotation for E2AXC7

UniProt code: E2AXC7.

Organism: Camponotus floridanus (Florida carpenter ant).

Taxonomy: Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea; Formicidae; Formicinae; Camponotus.

Function: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity). {ECO:0000250|UniProtKB:Q15018, ECO:0000250|UniProtKB:Q3TCJ1, ECO:0000269|PubMed:26344097}.

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:26344097}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:26344097};

Subunit: Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Within the complex, interacts directly with ABRAXAS2. The heterodimer with ABRAXAS2 assembles into a heterotetramer. The BRISC complex binds polyubiquitin. {ECO:0000269|PubMed:26344097}.

Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P46736}. Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K- fibers. {ECO:0000250|UniProtKB:Q15018}.

Similarity: Belongs to the peptidase M67A family. BRCC36 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Camponotus floridanus (Florida carpenter ant).
Taxonomy:		Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea; Formicidae; Formicinae; Camponotus.



Function:		Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity). {ECO:0000250\|UniProtKB:Q15018, ECO:0000250\|UniProtKB:Q3TCJ1, ECO:0000269\|PubMed:26344097}.


Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269\|PubMed:26344097}; Note=Binds 1 zinc ion per subunit. {ECO:0000269\|PubMed:26344097};
Subunit:		Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Within the complex, interacts directly with ABRAXAS2. The heterodimer with ABRAXAS2 assembles into a heterotetramer. The BRISC complex binds polyubiquitin. {ECO:0000269\|PubMed:26344097}.
Subcellular location:		Cytoplasm {ECO:0000250\|UniProtKB:P46736}. Nucleus {ECO:0000250\|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250\|UniProtKB:Q15018}. Cytoplasm, cytoskeleton {ECO:0000250\|UniProtKB:Q15018}. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K- fibers. {ECO:0000250\|UniProtKB:Q15018}.
Similarity:		Belongs to the peptidase M67A family. BRCC36 subfamily. {ECO:0000305}.