ABRAXAS2
entrez
23172
canonical
uniprot
Q15018
canonical
ensembl
ENSG00000165660
resolver
ensp
ENSP00000298492
resolver
enst
ENST00000298492
resolver
genesymbol
ABRAXAS2
resolver
genesymbol_syn
ABRO1
resolver
genesymbol_syn
FAM175B
resolver
genesymbol_syn
KIAA0157
resolver
hgnc
HGNC:28975
resolver
uniprot
B4DKR2
resolver
uniprot
Q96H11
resolver
uniprot_entry
ABRX2_HUMAN
resolver
uniprot_sec
B4DKR2
resolver
uniprot_sec
Q96H11
resolver
amino_acid_sequence
MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQPCSKLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVLHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAEVNKLRRQITQRKNEKEQERRLQQAVLSRQMPSESLDPAFSPRMPSSGFAAEGRSTLGDAEASDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSNYASTSAGLKYPGSGADLPPPQRAAGDSGEDSDDSDYENLIDPTEPSNSEYSHSKDSRPMAHPDEDPRNTQTSQI
uniprot
proteins
function
FUNCTION: Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates (PubMed:19214193, PubMed:20032457, PubMed:20656690, PubMed:24075985). May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (PubMed:20656690). 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 NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression (PubMed:24075985, PubMed:26344097). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). Required for normal induction of p53/TP53 in response to DNA damage (PubMed:25283148). Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (PubMed:25283148). {ECO:0000250|UniProtKB:Q3TCJ1, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:20032457, ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}.
uniprot
proteins
mass_dalton
46901
uniprot
proteins
mutagenesis
MUTAGEN 11..12; /note="SA->RR: Slightly reduces interaction with BBRC36. Abolishes interaction with SHMT2. Strongly reduces interactions with BABAM2 and BABAM1."; /evidence="ECO:0000269|PubMed:26344097"; MUTAGEN 215..222; /note="Missing: Reduces interaction with SHMT2, but has no effect on interaction with BRCC3."; /evidence="ECO:0000269|PubMed:24075985"; MUTAGEN 220; /note="V->R: Strongly reduces interaction with BBRC3; SHMT2; BABAM2 and BABAM1; when associated with Y-231. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with Y-231 and Y-241."; /evidence="ECO:0000269|PubMed:26344097"; MUTAGEN 231; /note="E->Y: Strongly reduces interaction with BBRC3; SHMT2; BABAM2 and BABAM1; when associated with R-220. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with R-220 and Y-241."; /evidence="ECO:0000269|PubMed:26344097"; MUTAGEN 241; /note="V->R: Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with R-220 and Y-231."; /evidence="ECO:0000269|PubMed:26344097
uniprot
proteins
protein_family
Abro1 subfamily
uniprot
proteins
protein_family
FAM175 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525340
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19214193
uniprot
proteins
pubmed
19261749
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20032457
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20656690
uniprot
proteins
pubmed
21195082
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21282113
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22974638
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24075985
uniprot
proteins
pubmed
25283148
uniprot
proteins
pubmed
26195665
uniprot
proteins
pubmed
26344097
uniprot
proteins
pubmed
8590280
uniprot
proteins
sequence_length
415
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:21195082, ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}. Nucleus {ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26195665}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26195665}. Note=A minor proportion is detected in the nucleus (PubMed:21282113, PubMed:22974638). Translocates into the nucleus in response to DNA damage (PubMed:25283148). Directly binds to microtubules and is detected at the minus end of K-fibers (PubMed:26195665). Co-localizes with NUMA1 at mitotic spindle poles (PubMed:26195665). {ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:25283148, ECO:0000269|PubMed:26195665}.
uniprot
proteins