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Conserved domains on  [gi|148696969|gb|EDL28916|]
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RIKEN cDNA 5430437P03, isoform CRA_b, partial [Mus musculus]

Protein Classification

BRISC and BRCA1-A complex member 1( domain architecture ID 15347962)

BRISC and BRCA1-A complex member 1 (BABAM1) is a component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites

CATH:  3.40.50.410
Gene Ontology:  GO:0007095|GO:0140861|GO:0006302|GO:0051301
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_BABAM1 cd21502
Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and ...
 78-236 1.27e-68

Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and BRCA1 A complex member 1 (BABAM1) is also known as Mediator of RAP80 interactions and targeting subunit of 40 kDa (MERIT40), New component of the BRCA1-A complex (NBA1), HSPC142, or C19orf620. It is a core component of the BRCA1-A and BRISC complexes that function in DNA double-strand break repair and immune signaling, and contain the lysine-63 linkage-specific BRCC36 subunit that is functionalized by scaffold subunits Abraxas and ABRO1, respectively. BABAM1 interacts with Rap80, BRCC36, BRCC45, and Abraxas to form the BRCA1-A complex, a lysine-63-Ub specific deubiquitinating enzyme (DUB) which specifically recognizes lysine-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). BRISC is a DUB complex containing three other subunits, BRCC36, ABRO1 and BRCC45. It specifically hydrolyzes lysine-63 polyubiquitin chains, and is involved in multiple biological processes, including IFN-mediated antiviral immune regulation and inflammatory reaction. BABAM1 likely serves as a scaffold protein by integrating other components to form a functional complex. Furthermore, BABAM1 has been shown to play a critical role in BRISC-mediated regulation of Tankyrase1 (TNKS1) function during spindle assembly; it directly binds to the ankyrin repeat cluster V (ARC-V) domain of TNKS1 via its RXXPEG motif. BABAM1 contains a Von-Willebrand factor A (vWA) domain that is distantly related to classical vWA domains.


:

Pssm-ID: 411071  Cd Length: 216  Bit Score: 211.72  E-value: 1.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148696969  78 CLDLSEEMSVPKLESFNGSRTNALNVSQKMVEMFVRTKHKIDKSHEFALVVVNDDSAWLSGLTSDPRELCSCLYDLETA- 156
Cdd:cd21502    8 CIDLSEEMNTTPFESTNGSKYTRLDMLKRALELFVHTKSRINPRHEFALVVLNESASWLQDFTSDPKDILSALDDLEPSg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148696969 157 SCSTFNLEGLFSLIQQKTELPVTENvQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDIVYIHNGTEEKE 236
Cdd:cd21502   88 SYDSFDLTSLFELIAEKVELPEVED-QNIPPPYVVRVILIYGRSSCIPQLSDEESLKKLLQSPYFFLDVLYLHEPPSEDN 166
 
Name Accession Description Interval E-value
vWA_BABAM1 cd21502
Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and ...
 78-236 1.27e-68

Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and BRCA1 A complex member 1 (BABAM1) is also known as Mediator of RAP80 interactions and targeting subunit of 40 kDa (MERIT40), New component of the BRCA1-A complex (NBA1), HSPC142, or C19orf620. It is a core component of the BRCA1-A and BRISC complexes that function in DNA double-strand break repair and immune signaling, and contain the lysine-63 linkage-specific BRCC36 subunit that is functionalized by scaffold subunits Abraxas and ABRO1, respectively. BABAM1 interacts with Rap80, BRCC36, BRCC45, and Abraxas to form the BRCA1-A complex, a lysine-63-Ub specific deubiquitinating enzyme (DUB) which specifically recognizes lysine-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). BRISC is a DUB complex containing three other subunits, BRCC36, ABRO1 and BRCC45. It specifically hydrolyzes lysine-63 polyubiquitin chains, and is involved in multiple biological processes, including IFN-mediated antiviral immune regulation and inflammatory reaction. BABAM1 likely serves as a scaffold protein by integrating other components to form a functional complex. Furthermore, BABAM1 has been shown to play a critical role in BRISC-mediated regulation of Tankyrase1 (TNKS1) function during spindle assembly; it directly binds to the ankyrin repeat cluster V (ARC-V) domain of TNKS1 via its RXXPEG motif. BABAM1 contains a Von-Willebrand factor A (vWA) domain that is distantly related to classical vWA domains.


Pssm-ID: 411071  Cd Length: 216  Bit Score: 211.72  E-value: 1.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148696969  78 CLDLSEEMSVPKLESFNGSRTNALNVSQKMVEMFVRTKHKIDKSHEFALVVVNDDSAWLSGLTSDPRELCSCLYDLETA- 156
Cdd:cd21502    8 CIDLSEEMNTTPFESTNGSKYTRLDMLKRALELFVHTKSRINPRHEFALVVLNESASWLQDFTSDPKDILSALDDLEPSg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148696969 157 SCSTFNLEGLFSLIQQKTELPVTENvQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDIVYIHNGTEEKE 236
Cdd:cd21502   88 SYDSFDLTSLFELIAEKVELPEVED-QNIPPPYVVRVILIYGRSSCIPQLSDEESLKKLLQSPYFFLDVLYLHEPPSEDN 166
 
Name Accession Description Interval E-value
vWA_BABAM1 cd21502
Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and ...
 78-236 1.27e-68

Von-Willebrand factor A (vWA) domain found in BRISC and BRCA1-A complex member 1; BRISC and BRCA1 A complex member 1 (BABAM1) is also known as Mediator of RAP80 interactions and targeting subunit of 40 kDa (MERIT40), New component of the BRCA1-A complex (NBA1), HSPC142, or C19orf620. It is a core component of the BRCA1-A and BRISC complexes that function in DNA double-strand break repair and immune signaling, and contain the lysine-63 linkage-specific BRCC36 subunit that is functionalized by scaffold subunits Abraxas and ABRO1, respectively. BABAM1 interacts with Rap80, BRCC36, BRCC45, and Abraxas to form the BRCA1-A complex, a lysine-63-Ub specific deubiquitinating enzyme (DUB) which specifically recognizes lysine-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). BRISC is a DUB complex containing three other subunits, BRCC36, ABRO1 and BRCC45. It specifically hydrolyzes lysine-63 polyubiquitin chains, and is involved in multiple biological processes, including IFN-mediated antiviral immune regulation and inflammatory reaction. BABAM1 likely serves as a scaffold protein by integrating other components to form a functional complex. Furthermore, BABAM1 has been shown to play a critical role in BRISC-mediated regulation of Tankyrase1 (TNKS1) function during spindle assembly; it directly binds to the ankyrin repeat cluster V (ARC-V) domain of TNKS1 via its RXXPEG motif. BABAM1 contains a Von-Willebrand factor A (vWA) domain that is distantly related to classical vWA domains.


Pssm-ID: 411071  Cd Length: 216  Bit Score: 211.72  E-value: 1.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148696969  78 CLDLSEEMSVPKLESFNGSRTNALNVSQKMVEMFVRTKHKIDKSHEFALVVVNDDSAWLSGLTSDPRELCSCLYDLETA- 156
Cdd:cd21502    8 CIDLSEEMNTTPFESTNGSKYTRLDMLKRALELFVHTKSRINPRHEFALVVLNESASWLQDFTSDPKDILSALDDLEPSg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148696969 157 SCSTFNLEGLFSLIQQKTELPVTENvQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDIVYIHNGTEEKE 236
Cdd:cd21502   88 SYDSFDLTSLFELIAEKVELPEVED-QNIPPPYVVRVILIYGRSSCIPQLSDEESLKKLLQSPYFFLDVLYLHEPPSEDN 166
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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