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BAH and coiled-coil domain-containing protein 1 isoform X1 [Mus musculus]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
BAH_BAHCC1 | cd04714 | BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ... |
2517-2680 | 2.06e-58 | ||||
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions. : Pssm-ID: 240065 Cd Length: 121 Bit Score: 197.62 E-value: 2.06e-58
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Tudor_BAHCC1 | cd20470 | Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ... |
1975-2042 | 1.17e-39 | ||||
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. : Pssm-ID: 410541 Cd Length: 70 Bit Score: 141.87 E-value: 1.17e-39
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Name | Accession | Description | Interval | E-value | ||||
BAH_BAHCC1 | cd04714 | BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ... |
2517-2680 | 2.06e-58 | ||||
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions. Pssm-ID: 240065 Cd Length: 121 Bit Score: 197.62 E-value: 2.06e-58
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Tudor_BAHCC1 | cd20470 | Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ... |
1975-2042 | 1.17e-39 | ||||
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410541 Cd Length: 70 Bit Score: 141.87 E-value: 1.17e-39
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BAH | smart00439 | Bromo adjacent homology domain; |
2519-2679 | 7.03e-13 | ||||
Bromo adjacent homology domain; Pssm-ID: 214664 [Multi-domain] Cd Length: 121 Bit Score: 67.32 E-value: 7.03e-13
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BAH | pfam01426 | BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ... |
2518-2679 | 4.82e-10 | ||||
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction. Pssm-ID: 460207 Cd Length: 120 Bit Score: 59.24 E-value: 4.82e-10
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Tudor_3 | pfam18115 | DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ... |
1985-2037 | 5.94e-05 | ||||
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2. Pssm-ID: 436284 Cd Length: 50 Bit Score: 42.55 E-value: 5.94e-05
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Name | Accession | Description | Interval | E-value | ||||
BAH_BAHCC1 | cd04714 | BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ... |
2517-2680 | 2.06e-58 | ||||
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions. Pssm-ID: 240065 Cd Length: 121 Bit Score: 197.62 E-value: 2.06e-58
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Tudor_BAHCC1 | cd20470 | Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ... |
1975-2042 | 1.17e-39 | ||||
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410541 Cd Length: 70 Bit Score: 141.87 E-value: 1.17e-39
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Tudor_BAHCC1-like | cd20397 | Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ... |
1977-2042 | 1.16e-32 | ||||
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The family of BAHCC1 includes BAHCC1 and trinucleotide repeat-containing gene 18 protein (TNRC18). BAHCC1 may function as a transcriptional regulator. The biological function of TNRC18 remains unclear. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410468 Cd Length: 67 Bit Score: 122.05 E-value: 1.16e-32
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Tudor_TNRC18 | cd20469 | Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ... |
1977-2043 | 9.12e-32 | ||||
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar proteins; TNRC18, also called long CAG trinucleotide repeat-containing gene 79 protein (CAGL79), is a protein that in humans is encoded by the TNRC18 gene. Its biological function remains unclear. TNRC18 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410540 Cd Length: 67 Bit Score: 119.45 E-value: 9.12e-32
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BAH | cd04370 | BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ... |
2517-2679 | 1.49e-22 | ||||
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions. Pssm-ID: 239835 [Multi-domain] Cd Length: 123 Bit Score: 95.15 E-value: 1.49e-22
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BAH | smart00439 | Bromo adjacent homology domain; |
2519-2679 | 7.03e-13 | ||||
Bromo adjacent homology domain; Pssm-ID: 214664 [Multi-domain] Cd Length: 121 Bit Score: 67.32 E-value: 7.03e-13
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BAH | pfam01426 | BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ... |
2518-2679 | 4.82e-10 | ||||
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction. Pssm-ID: 460207 Cd Length: 120 Bit Score: 59.24 E-value: 4.82e-10
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BAH_polybromo | cd04717 | BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ... |
2520-2566 | 4.08e-06 | ||||
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions. Pssm-ID: 240068 Cd Length: 121 Bit Score: 47.96 E-value: 4.08e-06
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Tudor_53BP1 | cd20383 | Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ... |
1983-2034 | 3.85e-05 | ||||
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410454 Cd Length: 52 Bit Score: 43.02 E-value: 3.85e-05
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Tudor_3 | pfam18115 | DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ... |
1985-2037 | 5.94e-05 | ||||
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2. Pssm-ID: 436284 Cd Length: 50 Bit Score: 42.55 E-value: 5.94e-05
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BAH_plant_3 | cd04713 | BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ... |
2502-2643 | 1.16e-04 | ||||
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions. Pssm-ID: 240064 Cd Length: 146 Bit Score: 44.76 E-value: 1.16e-04
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Tudor_SpCrb2-like_rpt1 | cd20395 | first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ... |
1984-2037 | 2.73e-03 | ||||
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and similar proteins; Crb2, also called RAD9 protein homolog, or checkpoint mediator protein crb2, is a DNA repair protein essential for cell cycle arrest at the G1 and G2 stages following DNA damage by X-, and UV-irradiation, or inactivation of DNA ligase. Crb2 contains two Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Pssm-ID: 410466 Cd Length: 50 Bit Score: 38.11 E-value: 2.73e-03
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