BRISC and BRCA1-A complex member 2 isoform X2 [Rattus norvegicus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| BRE | cd23664 | BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as ... |
19-328 | 0e+00 | |||||
BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis. : Pssm-ID: 467821 Cd Length: 364 Bit Score: 526.76 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| BRE | cd23664 | BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as ... |
19-328 | 0e+00 | |||||
BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis. Pssm-ID: 467821 Cd Length: 364 Bit Score: 526.76 E-value: 0e+00
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| BRE | pfam06113 | Brain and reproductive organ-expressed protein (BRE); This family consists of several ... |
15-283 | 4.39e-146 | |||||
Brain and reproductive organ-expressed protein (BRE); This family consists of several eukaryotic brain and reproductive organ-expressed (BRE) proteins. BRE is a putative stress-modulating gene, found able to down-regulate TNF-alpha-induced-NF-kappaB activation upon over expression. A total of six isoforms are produced by alternative splicing predominantly at either end of the gene.Compared to normal cells, immortalized human cell lines uniformly express higher levels of BRE. Peripheral blood monocytes respond to LPS by down-regulating the expression of all the BRE isoforms.It is thought that the function of BRE and its isoforms is to regulate peroxisomal activities. Pssm-ID: 461832 Cd Length: 320 Bit Score: 414.53 E-value: 4.39e-146
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| Name | Accession | Description | Interval | E-value | ||||||
| BRE | cd23664 | BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as ... |
19-328 | 0e+00 | ||||||
BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis. Pssm-ID: 467821 Cd Length: 364 Bit Score: 526.76 E-value: 0e+00
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| BRE | pfam06113 | Brain and reproductive organ-expressed protein (BRE); This family consists of several ... |
15-283 | 4.39e-146 | ||||||
Brain and reproductive organ-expressed protein (BRE); This family consists of several eukaryotic brain and reproductive organ-expressed (BRE) proteins. BRE is a putative stress-modulating gene, found able to down-regulate TNF-alpha-induced-NF-kappaB activation upon over expression. A total of six isoforms are produced by alternative splicing predominantly at either end of the gene.Compared to normal cells, immortalized human cell lines uniformly express higher levels of BRE. Peripheral blood monocytes respond to LPS by down-regulating the expression of all the BRE isoforms.It is thought that the function of BRE and its isoforms is to regulate peroxisomal activities. Pssm-ID: 461832 Cd Length: 320 Bit Score: 414.53 E-value: 4.39e-146
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| BRE-like | cd23520 | BRCA1-A and BRISC complex subunit BRE and related proteins; BRCA1-A and BRISC complex subunit ... |
19-327 | 6.91e-140 | ||||||
BRCA1-A and BRISC complex subunit BRE and related proteins; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (consisting of BRE/BRCC45, BRCC36, MERIT40 and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis. Pssm-ID: 467820 Cd Length: 352 Bit Score: 399.90 E-value: 6.91e-140
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| BRE-like_insects | cd23665 | BRCA1-A and BRISC complex subunit BRE-like protein found in insects; BRCA1-A and BRISC complex ... |
19-325 | 3.17e-97 | ||||||
BRCA1-A and BRISC complex subunit BRE-like protein found in insects; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding; in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. This model contains the BRE domain of BRISC complexes found in insects. Pssm-ID: 467822 Cd Length: 364 Bit Score: 291.80 E-value: 3.17e-97
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| BRE-like_plant | cd23666 | BRCA1-A and BRISC complex subunit BRE-like protein found in plants; BRCA1-A and BRISC complex ... |
19-319 | 4.14e-43 | ||||||
BRCA1-A and BRISC complex subunit BRE-like protein found in plants; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40, and RAP80 and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers composed of BRCC36, ABRAXAS, BRE, and MERIT40 form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40, and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A, however the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1 it is involved in RAP80 integration, BRCA1 sequestration, and ubiquitin binding; in BRISC it is involved in dimerization, SHMT2 recruitment, DUB inhibition, and ubiquitin binding. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair, and BRCC36-Abraxas 2 complexes have been found in Arabidopsis. This model contains the BRE domain of BRISC complexes found in plants. Pssm-ID: 467823 Cd Length: 370 Bit Score: 152.52 E-value: 4.14e-43
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