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PHD finger protein 20-like protein 1 isoform X14 [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
Tudor_PHF20L1 | cd20454 | Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; ... |
86-143 | 1.24e-38 | |||
Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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: 410525 Cd Length: 59 Bit Score: 135.87 E-value: 1.24e-38
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MBT_PHF20L1-like | cd20104 | malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ... |
13-72 | 6.76e-29 | |||
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues. : Pssm-ID: 439094 [Multi-domain] Cd Length: 60 Bit Score: 108.86 E-value: 6.76e-29
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PHD20L1_u1 | pfam16660 | PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but ... |
318-383 | 4.02e-27 | |||
PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but highly conserved sequence on a set of higher eukaryotic PHD finger protein 20-like protein 1 like proteins. The function is not known. : Pssm-ID: 465222 Cd Length: 68 Bit Score: 104.24 E-value: 4.02e-27
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DUF3776 super family | cl13990 | Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is ... |
197-310 | 6.69e-08 | |||
Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The actual alignment was detected with superfamily member pfam12618: Pssm-ID: 463645 Cd Length: 110 Bit Score: 50.99 E-value: 6.69e-08
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Name | Accession | Description | Interval | E-value | |||
Tudor_PHF20L1 | cd20454 | Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; ... |
86-143 | 1.24e-38 | |||
Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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: 410525 Cd Length: 59 Bit Score: 135.87 E-value: 1.24e-38
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MBT_PHF20L1-like | cd20104 | malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ... |
13-72 | 6.76e-29 | |||
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues. Pssm-ID: 439094 [Multi-domain] Cd Length: 60 Bit Score: 108.86 E-value: 6.76e-29
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PHD20L1_u1 | pfam16660 | PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but ... |
318-383 | 4.02e-27 | |||
PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but highly conserved sequence on a set of higher eukaryotic PHD finger protein 20-like protein 1 like proteins. The function is not known. Pssm-ID: 465222 Cd Length: 68 Bit Score: 104.24 E-value: 4.02e-27
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TUDOR | smart00333 | Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ... |
86-139 | 1.95e-08 | |||
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished). Pssm-ID: 197660 Cd Length: 57 Bit Score: 50.74 E-value: 1.95e-08
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DUF3776 | pfam12618 | Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is ... |
197-310 | 6.69e-08 | |||
Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is approximately 100 amino acids in length. Pssm-ID: 463645 Cd Length: 110 Bit Score: 50.99 E-value: 6.69e-08
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MBT | smart00561 | Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2; Present in Drosophila Scm, l(3)mbt, ... |
3-68 | 1.57e-07 | |||
Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2; Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2. These proteins are involved in transcriptional regulation. Pssm-ID: 214723 Cd Length: 96 Bit Score: 49.56 E-value: 1.57e-07
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Tudor_2 | pfam18104 | Jumonji domain-containing protein 2A Tudor domain; This is the tudor domain found in histone ... |
90-123 | 6.96e-07 | |||
Jumonji domain-containing protein 2A Tudor domain; This is the tudor domain found in histone demethylase Jumonji domain-containing protein 2A (JMJD2A). Structure and function analysis indicate that this domain can recognize equally well two unrelated histone peptides, H3K4me3 and H4K20me3, by means of two very different binding mechanisms. JMJD2 also known as KDM4, is a conserved iron (II)-dependent jumonji-domain demethylase subfamily that is essential during development. Vertebrate KDM4A-C proteins contain a conserved double tudor domain (DTD). Pssm-ID: 465651 Cd Length: 35 Bit Score: 45.87 E-value: 6.96e-07
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MBT | pfam02820 | mbt repeat; The function of this repeat is unknown, but is found in a number of nuclear ... |
18-67 | 1.37e-05 | |||
mbt repeat; The function of this repeat is unknown, but is found in a number of nuclear proteins such as drosophila sex comb on midleg protein. The repeat is found in up to four copies as in Swiss:Q9UHJ3. The repeat contains a completely conserved glutamate at its amino terminus that may be important for function. Pssm-ID: 460712 Cd Length: 66 Bit Score: 42.88 E-value: 1.37e-05
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Name | Accession | Description | Interval | E-value | |||
Tudor_PHF20L1 | cd20454 | Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; ... |
86-143 | 1.24e-38 | |||
Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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: 410525 Cd Length: 59 Bit Score: 135.87 E-value: 1.24e-38
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MBT_PHF20L1-like | cd20104 | malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ... |
13-72 | 6.76e-29 | |||
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues. Pssm-ID: 439094 [Multi-domain] Cd Length: 60 Bit Score: 108.86 E-value: 6.76e-29
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PHD20L1_u1 | pfam16660 | PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but ... |
318-383 | 4.02e-27 | |||
PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but highly conserved sequence on a set of higher eukaryotic PHD finger protein 20-like protein 1 like proteins. The function is not known. Pssm-ID: 465222 Cd Length: 68 Bit Score: 104.24 E-value: 4.02e-27
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Tudor_PHF20-like | cd20386 | Tudor domain found in PHD finger protein 20 (PHF20), PHF20-like protein 1 (PHF20L1), and ... |
87-136 | 3.03e-23 | |||
Tudor domain found in PHD finger protein 20 (PHF20), PHF20-like protein 1 (PHF20L1), and similar proteins; PHF20, also called Glioma-expressed antigen 2, hepatocellular carcinoma-associated antigen 58, novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds to Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53-mediated signaling. PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Both PHF20 and PHF20L1 contain an N-terminal malignant brain tumor (MBT) domain, a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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: 410457 [Multi-domain] Cd Length: 50 Bit Score: 92.65 E-value: 3.03e-23
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Tudor_PHF20 | cd20453 | Tudor domain found in PHD finger protein 20 (PHF20) and similar proteins; PHF20, also called ... |
87-139 | 1.04e-20 | |||
Tudor domain found in PHD finger protein 20 (PHF20) and similar proteins; PHF20, also called Glioma-expressed antigen 2, hepatocellular carcinoma-associated antigen 58, novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds to Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53-mediated signaling. PHF20 contains an N-terminal malignant brain tumor (MBT) domain, a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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: 410524 Cd Length: 53 Bit Score: 85.68 E-value: 1.04e-20
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MBT | cd20088 | malignant brain tumor (MBT) repeat; The MBT repeat is a protein module that recognizes ... |
13-72 | 2.60e-13 | |||
malignant brain tumor (MBT) repeat; The MBT repeat is a protein module that recognizes methylated lysine residues on histones and are thought to affect a variety of chromatin processes, including transcription. It exists as tandem repeats and is found in a number of nuclear proteins such as Drosophila sex comb on midleg protein. In the human genome, there are at least 9 MBT repeat proteins, each containing two, three or four MBT repeats. MBT repeat proteins use a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine (monomethyllysine and/or dimethyllysine). Pssm-ID: 439080 Cd Length: 61 Bit Score: 64.58 E-value: 2.60e-13
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Tudor_SF | cd04508 | Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ... |
90-134 | 1.51e-10 | |||
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain. Pssm-ID: 410449 [Multi-domain] Cd Length: 47 Bit Score: 56.44 E-value: 1.51e-10
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TUDOR | smart00333 | Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ... |
86-139 | 1.95e-08 | |||
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished). Pssm-ID: 197660 Cd Length: 57 Bit Score: 50.74 E-value: 1.95e-08
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DUF3776 | pfam12618 | Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is ... |
197-310 | 6.69e-08 | |||
Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is approximately 100 amino acids in length. Pssm-ID: 463645 Cd Length: 110 Bit Score: 50.99 E-value: 6.69e-08
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MBT | smart00561 | Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2; Present in Drosophila Scm, l(3)mbt, ... |
3-68 | 1.57e-07 | |||
Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2; Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2. These proteins are involved in transcriptional regulation. Pssm-ID: 214723 Cd Length: 96 Bit Score: 49.56 E-value: 1.57e-07
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Tudor_2 | pfam18104 | Jumonji domain-containing protein 2A Tudor domain; This is the tudor domain found in histone ... |
90-123 | 6.96e-07 | |||
Jumonji domain-containing protein 2A Tudor domain; This is the tudor domain found in histone demethylase Jumonji domain-containing protein 2A (JMJD2A). Structure and function analysis indicate that this domain can recognize equally well two unrelated histone peptides, H3K4me3 and H4K20me3, by means of two very different binding mechanisms. JMJD2 also known as KDM4, is a conserved iron (II)-dependent jumonji-domain demethylase subfamily that is essential during development. Vertebrate KDM4A-C proteins contain a conserved double tudor domain (DTD). Pssm-ID: 465651 Cd Length: 35 Bit Score: 45.87 E-value: 6.96e-07
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Tudor_53BP1 | cd20383 | Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ... |
89-134 | 3.36e-06 | |||
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: 44.18 E-value: 3.36e-06
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Tudor_SpSPF30-like | cd20446 | Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar ... |
87-136 | 5.08e-06 | |||
Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar proteins; SpSPF30, also called survival of motor neuron-related-splicing factor 30, is necessary for spliceosome assembly. It 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: 410517 Cd Length: 56 Bit Score: 44.02 E-value: 5.08e-06
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Tudor_LBR | cd20381 | Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral ... |
87-135 | 5.86e-06 | |||
Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral nuclear envelope inner membrane (INM) protein or LMN2R, is a nuclear envelope protein that anchors the lamina and the heterochromatin to the inner nuclear membrane, in cellular senescence induced by excess thymidine. It is also important for cholesterol biosynthesis. LBR can interact with chromodomain proteins and DNA. It 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: 410452 Cd Length: 51 Bit Score: 43.45 E-value: 5.86e-06
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MBT_L3MBTL1-like_rpt3 | cd20103 | third malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like ... |
9-67 | 1.20e-05 | |||
third malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family; The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues. Pssm-ID: 439093 Cd Length: 73 Bit Score: 43.42 E-value: 1.20e-05
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MBT | pfam02820 | mbt repeat; The function of this repeat is unknown, but is found in a number of nuclear ... |
18-67 | 1.37e-05 | |||
mbt repeat; The function of this repeat is unknown, but is found in a number of nuclear proteins such as drosophila sex comb on midleg protein. The repeat is found in up to four copies as in Swiss:Q9UHJ3. The repeat contains a completely conserved glutamate at its amino terminus that may be important for function. Pssm-ID: 460712 Cd Length: 66 Bit Score: 42.88 E-value: 1.37e-05
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MBT_dSfmbt-like_rpt4 | cd20100 | fourth malignant brain tumor (MBT) repeat found in the Drosophila melanogaster Polycomb ... |
13-67 | 3.24e-05 | |||
fourth malignant brain tumor (MBT) repeat found in the Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt)-like family; The dSfmbt-like family includes Drosophila melanogaster Scm-like with four MBT domain-containing protein 1 (dSfmbt), as well as its two vertebrate homologs, MBT domain-containing protein 1 (MBTD1) and Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). dSfmbt is a Polycomb group (PcG) repressor involved in epigenetic regulation of gene expression. MBTD1 and L3MBTL2, also called L(3)mbt-like protein 2, are putative PcG proteins that specifically bind to monomethylated and dimethylated 'Lys-20' on histone H4. L3MBTL2 also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues. Pssm-ID: 439090 Cd Length: 71 Bit Score: 42.28 E-value: 3.24e-05
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MBT_L3MBTL1-like_rpt2 | cd20102 | second malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like ... |
12-67 | 3.46e-05 | |||
second malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family; The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues. Pssm-ID: 439092 Cd Length: 90 Bit Score: 42.61 E-value: 3.46e-05
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MBT_L3MBTL1_rpt3 | cd20137 | third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein ... |
9-67 | 4.34e-05 | |||
third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1); L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL1 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues. Pssm-ID: 439127 Cd Length: 75 Bit Score: 41.73 E-value: 4.34e-05
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Tudor_3 | pfam18115 | DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ... |
93-136 | 6.35e-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: 40.62 E-value: 6.35e-05
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Tudor_JMJD2_rpt2 | cd20392 | second Tudor domain found in Jumonji domain-containing protein 2 (JMJD2) family of histone ... |
88-133 | 7.05e-05 | |||
second Tudor domain found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; JMJD2 proteins, also called lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains only three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD domain, a noncanonical extended PHD domain, and tandem Tudor domains. The model corresponds to the second 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. JMJD2D is not included in this model, since it lacks both the PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth. Pssm-ID: 410463 Cd Length: 56 Bit Score: 40.70 E-value: 7.05e-05
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Tudor_ZGPAT | cd20384 | Tudor domain found in zinc finger CCCH-type with G patch domain-containing protein (ZGPAT) and ... |
83-120 | 1.04e-04 | |||
Tudor domain found in zinc finger CCCH-type with G patch domain-containing protein (ZGPAT) and similar proteins; ZGPAT, also called ZIP, G patch domain-containing protein 6 (GPATC6), GPATCH6, zinc finger CCCH domain-containing protein 9 (ZC3HDC9), ZC3H9, or zinc finger and G patch domain-containing protein, is a transcription repressor that specifically binds the 5'-GGAG[GA]A[GA]A-3' consensus sequence. It represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. It 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: 410455 Cd Length: 55 Bit Score: 40.29 E-value: 1.04e-04
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Tudor_PCL | cd20385 | Tudor domain found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ... |
86-122 | 1.27e-04 | |||
Tudor domain found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins; The PCL family includes PHD finger protein1 (PHF1) and its homologs, metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are accessory components of the Polycomb repressive complex 2 (PRC2) core complex. Members contain an N-terminal Tudor domain followed by two PHD domains, and a C-terminal MTF2 domain. PCL proteins specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD domain-containing proteins, the first PHD domains of PCL proteins do not display histone H3K4 binding affinity and they do not affect the binding of the Tudor domain to histones. Pssm-ID: 410456 Cd Length: 54 Bit Score: 39.93 E-value: 1.27e-04
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Tudor_TDRD3 | cd20413 | Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ... |
87-122 | 2.42e-04 | |||
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In the nucleus, it acts as a coactivator; it recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In the cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 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: 410484 Cd Length: 53 Bit Score: 39.25 E-value: 2.42e-04
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Tudor_SMN_SPF30-like | cd21182 | Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ... |
90-123 | 3.06e-04 | |||
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single 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: 410549 Cd Length: 50 Bit Score: 38.77 E-value: 3.06e-04
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MBT_L3MBTL4_rpt3 | cd20139 | fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein ... |
8-68 | 5.11e-04 | |||
fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4); L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues. Pssm-ID: 439129 Cd Length: 82 Bit Score: 39.08 E-value: 5.11e-04
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MBT_L3MBTL1_rpt2 | cd20134 | second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein ... |
9-84 | 7.65e-04 | |||
second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1); L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL1 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues. Pssm-ID: 439124 Cd Length: 93 Bit Score: 39.05 E-value: 7.65e-04
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Agenet | smart00743 | Tudor-like domain present in plant sequences; Domain in plant sequences with possible ... |
86-126 | 1.27e-03 | |||
Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions. Pssm-ID: 214798 Cd Length: 59 Bit Score: 37.30 E-value: 1.27e-03
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MBT_L3MBTL4_rpt2 | cd20136 | second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein ... |
13-84 | 2.23e-03 | |||
second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4); L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues. Pssm-ID: 439126 Cd Length: 92 Bit Score: 37.67 E-value: 2.23e-03
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MBT_L3MBTL3_rpt2 | cd20135 | second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein ... |
13-68 | 2.29e-03 | |||
second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3); L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues. Pssm-ID: 439125 Cd Length: 93 Bit Score: 37.48 E-value: 2.29e-03
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Tudor-knot | pfam11717 | RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ... |
13-66 | 3.54e-03 | |||
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is required for binding to RNA. The know influences the loop conformation of the helical turn Ht2 - residues 61-6 3- that is located at the side opposite the knot in the tudor domain-chromodomain; stabilization of Ht2 is essential for RNA binding. Pssm-ID: 432022 [Multi-domain] Cd Length: 55 Bit Score: 36.03 E-value: 3.54e-03
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MBT_L3MBTL3_rpt3 | cd20138 | third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein ... |
4-67 | 4.83e-03 | |||
third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3); L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues. Pssm-ID: 439128 Cd Length: 78 Bit Score: 36.06 E-value: 4.83e-03
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CBD_RBP1_like | cd18641 | chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; ... |
26-58 | 7.33e-03 | |||
chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; Retinoblastoma-binding protein 1 (RBP1), also termed AT-rich interaction domain 4A, is a ubiquitously expressed nuclear protein. RBP1 is a tumor and leukemia suppressor that binds both methylated histone tails and DNA, and is involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndromes. The chromo barrel domain of RBP1 has been reported to recognize histone H4K20me3 weakly, and this binding is enhanced by the simultaneous binding of DNA. RBP1 binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation; pRB represses transcription by recruiting RBP1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. Pssm-ID: 350843 [Multi-domain] Cd Length: 59 Bit Score: 35.33 E-value: 7.33e-03
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