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BABAM1

Gene
babam1
Protein
BRISC and BRCA1-A complex member 1
Organism
Danio rerio
Length
370 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of babam2 and help the 'Lys-63'-linked deubiquitinase activity mediated by brcc3/brcc36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
40.901 kDa
Sequence
METTEPGQADGEERMMDLRPRTRSNPEGAEDRRSSTGSLNSSLPSAPQPAVGSRVEGEGEAASSDSPPVSATAIAATASVPVAAVGNTTTTNTASLPAMSPAVKERPKPSQPTMPTQIPPSAELHLRAPRVNCPEKVIICLDLSEEMSLQKLESINGSKTNALNISQKMIEMFVRTKHKIDKRHEFALVVVNDDAMWLSGFTSDPRELCSCLYDLETNVCESFNLEDLFNVILQKIELPQMENIQTIPPPFVVRTLLVFSRHAGMLQFNPSDAVKKMLQSPYFFFDVVFLHNGTEEQTEDTSWKDVYASFCELDTKGMCYRFEVSLCGPAIELHNCMAKLLCHPLQRPFQSHASYSLLEDEDTLENEATV

Gene
Babam1
Protein
BRISC and BRCA1-A complex member 1
Organism
Rattus norvegicus
Length
334 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
36.878 kDa
Sequence
MEVAEANSPTEEEEEEEEEEGEEPISEPRPHTRSNPEGAEDRAIGAQANVGSRSEGEGEAATADDGAASVPGAVPKPWQVPAPASEVQIRTPRVNCPEKVIICLDLSEEMSVPKLESFNGSRTNALNVSQKMVEMFVRTKHKIDKSHEFALVVVNDDSAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDIIYIHSGPEEKEDDMSWKDMFAFMGSLDTKGTSYKYAVALAGPALELHNCVAKLLAHPLQRPCQSHASYSLLEEDEEAGEGEATV

Gene
Babam1
Protein
BRISC and BRCA1-A complex member 1
Organism
Mus musculus
Length
333 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
36.793 kDa
Sequence
MEVAEANSPTEEEEEEEEEGEETISEPRPHTRSNPEGAEDRALGAQASVGSRSEGEGEAATADGGAASVPGAGPKPWQVPASASEVQIRTPRVNCPEKVIICLDLSEEMSVPKLESFNGSRTNALNVSQKMVEMFVRTKHKIDKSHEFALVVVNDDSAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDIVYIHNGTEEKEEDMSWKDMFAFMGSLDTKGASYKYEVALAGPALELHNCMAKLLAHPLQRPCQTHASYSLLEEDEEAGEEEATV

Gene
BABAM1
Protein
BRISC and BRCA1-A complex member 1
Organism
Bos taurus
Length
332 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
36.886 kDa
Sequence
MEVAEPSCPTEEEEEEEEEEEQSAEPRPRTRSNPEGAEDRALGAQTSVGSRSEGEGEAASADDGTANPPGAGPKPWQVPPPAPEVQVRTPRVNCPEKVIICLDLSEEMALPKLESFNGSKTNALNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDVVYIHNGADEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLEEDDEATEVEATV

Gene
BABAM1
Protein
BRISC and BRCA1-A complex member 1
Organism
Callithrix jacchus
Length
329 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
36.541 kDa
Sequence
MEVAEPSSPTEEEEEEEEHSAEPRPHTRSNPEGAEDRAVAAQASVGSHSEGEGEAASADDGSPSTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNALNISQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTEFPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDLVYIHNGAEEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALAGPALELHNCMVKLLAHPLQRPCQSHASYSLLEEEDEATEVEATV

Gene
BABAM1
Protein
BRISC and BRCA1-A complex member 1
Organism
Homo sapiens
Length
329 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is 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 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985).
Similarity
Belongs to the BABAM1 family.
Mass
36.56 kDa
Sequence
MEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGAQASVGSRSEGEGEAASADDGSLNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNALNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLEEEDEAIEVEATV

Gene
BABAM1
Protein
BRISC and BRCA1-A complex member 1
Organism
Pongo abelii
Length
329 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
36.558 kDa
Sequence
MEVPEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGAQASVGSRSEGEGEAASADDGSPNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNALNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLEEEDEATEVEATV

Gene
babam1
Protein
BRISC and BRCA1-A complex member 1
Organism
Xenopus laevis
Length
328 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of babam2 and help the 'Lys-63'-linked deubiquitinase activity mediated by brcc3/brcc36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
36.953 kDa
Sequence
MDNSTEETFSMDTSEPLEEGEQTHEQRPHTRSNPEGAEDRGVVHQAGVGSRSEGEGEAAQVEDPLPTTTTVPTNSTPPPTLEFQLKTPRVNCPEKVIICLDLSEEMSTQKLESFNGSKANALNSSQKMIEMFVRTKHKIDKRHEFALVVANNEAMWLSGFTSDPREVCSCLYDLETNVCESFNLEGLFNLIQQRTEFPVTDNVQTIPPPYVVRIILIYSRPASQPALALTDNMKKMLQCPYFFFDVIYIHNGSEEEELCWKDIFGFFSSLDSKGTSYKYEVSITGPALELHNCMARLLAHPLQRPFQSHAAYSLLEEEEESPESEVTV

Gene
babam1
Protein
BRISC and BRCA1-A complex member 1
Organism
Xenopus tropicalis
Length
318 amino acids
Function
Component of the BRCA1-A complex, a complex that specifically recognizes '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. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by brcc3/brcc36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination.
Similarity
Belongs to the BABAM1 family.
Mass
35.897 kDa
Sequence
MDTSEPLEEGDRTHEQRPHTRSNPEGAEDREGLPQAGVGSRSEGEGEAAQVDDPLPTTTAVPTNCTPPPTLEFQLKTPRVNCPEKVIICLDLSEEMSTQKLESFNGSKANALNSSQKMIEMFVRTKHKIDKRHEFALVVANNEAMWLSGFTSDPREVCSCLYDLETNVCESFNLEGLFNLIQQRTEFPVTDNVQTIPPPYVVRIILIYSRPASQPALNLTDNMKKMLQCPYFFFDVIYIHNGSEEEELRWKDIFSFFSGLDSKGTSYKYEVSITGPALELHNCMARLLAHPLQRPFQSHAAYSLLEEEEESPESEVTV