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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569   9 HFDWDKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVD 88
Cdd:cd20105    1 HFSWDKYLKETGAVPAPVHCFKQSYTPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594591569  89 SSDIQPVGTCEQGGDLLQPPLGYTLNTSSWPMFLLRVLTGSELAPAVFFKE 139
Cdd:cd20105   81 SSEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPVRIFHK 131

second malignant brain tumor (MBT) repeat found in the Polycomb protein sex comb on midleg family; The Sex comb on midleg (Scm) family of Polycomb proteins includes Drosophila melanogaster Scm protein, as well as two vertebrate homologs of Scm, Polycomb protein sex comb on midleg homolog 1 (SCMH1) and sex comb on midleg-like protein 2 (SCML2). Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Both SCMH1 and SCML2 are components of PRC1, which acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. Members of this family contain two 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594591569 144 PLQNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPPG 218
Cdd:cd20092    1 PEKNMFKVGMKLEAVDRKNPQLICPATVGDVDGDEIHISFDGWRGAFDYWCRYDSRDIFPVGWCKKTGHPLQPPG 75

first malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1; Sex comb on midleg homolog 1 (SCMH1) is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. It contains two 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 first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569   9 HFDWDKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVD 88
Cdd:cd20105    1 HFSWDKYLKETGAVPAPVHCFKQSYTPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594591569  89 SSDIQPVGTCEQGGDLLQPPLGYTLNTSSWPMFLLRVLTGSELAPAVFFKE 139
Cdd:cd20105   81 SSEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPVRIFHK 131

second malignant brain tumor (MBT) repeat found in the Polycomb protein sex comb on midleg family; The Sex comb on midleg (Scm) family of Polycomb proteins includes Drosophila melanogaster Scm protein, as well as two vertebrate homologs of Scm, Polycomb protein sex comb on midleg homolog 1 (SCMH1) and sex comb on midleg-like protein 2 (SCML2). Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Both SCMH1 and SCML2 are components of PRC1, which acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. Members of this family contain two 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594591569 144 PLQNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPPG 218
Cdd:cd20092    1 PEKNMFKVGMKLEAVDRKNPQLICPATVGDVDGDEIHISFDGWRGAFDYWCRYDSRDIFPVGWCKKTGHPLQPPG 75

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569    13 DKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDI 92
Cdd:smart00561   1 EDYLEETGARAAPVELFKQPVDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPDI 80

                           90
                   ....*....|....*.
gi 594591569    93 QPVGTCEQGGDLLQPP 108
Cdd:smart00561  81 FPVGWCEKNGHPLQPP 96

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591569   44 MKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPL 109
Cdd:pfam02820   1 MKLEAVDPLNPSLICVATVVKVLGGRLRLRFDGWDDSYDFWCHADSPDIHPVGWCEKNGHPLQPPK 66

first malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1; Sex comb on midleg homolog 1 (SCMH1) is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. It contains two 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 first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569   9 HFDWDKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVD 88
Cdd:cd20105    1 HFSWDKYLKETGAVPAPVHCFKQSYTPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594591569  89 SSDIQPVGTCEQGGDLLQPPLGYTLNTSSWPMFLLRVLTGSELAPAVFFKE 139
Cdd:cd20105   81 SSEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPVRIFHK 131

first malignant brain tumor (MBT) repeat found in the sex comb on midleg family; The sex comb on midleg (Scm) family of Polycomb proteins includes Drosophila melanogaster Scm protein, as well as two vertebrate homologs of Scm, sex comb on midleg homolog 1 (SCMH1) and sex comb on midleg-like protein 2 (SCML2). Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Both SCMH1 and SCML2 are components of PRC1, which acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. Members of this family contain two 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 first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  31 QSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLG 110
Cdd:cd20091    1 QSPIPPVNEFKVGMKLEAQDPRNLTSTCIATVVGIQGPRLRLRLDGSDNKNDFWRLVDSSDIHPVGWCEKNGGLLQPPLG 80

                         90
                 ....*....|....*..
gi 594591569 111 YTLNTSSWPMFLLRVLT 127
Cdd:cd20091   81 FRMNPSSWPMFLQKTLN 97

first malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein sex comb on midleg and similar proteins; Sex comb on midleg (Scm) is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Scm contains two 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 first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  31 QSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLG 110
Cdd:cd20107    1 QAQNPPKNEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEKNGGMLQPPLG 80

                         90
                 ....*....|....*.
gi 594591569 111 YTLNTSSWPMFLLRVL 126
Cdd:cd20107   81 FRMNASSWPMFLLKTL 96

second malignant brain tumor (MBT) repeat found in sex comb on midleg-like protein 2 (SCML2) and similar proteins; SCML2 is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. SCML2 contains two 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594591569 144 PLQNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPPG 218
Cdd:cd20109    1 PPLNNFKVGMKLEAIDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCRLTGDVLQPPG 75

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569   126 LTGSELAPAVFFKEEPPRPlQNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVG 205
Cdd:smart00561   6 ETGARAAPVELFKQPVDSP-PNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPDIFPVG 84

                           90
                   ....*....|..
gi 594591569   206 WCRLTGDVLQPP 217
Cdd:smart00561  85 WCEKNGHPLQPP 96

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569    13 DKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDI 92
Cdd:smart00561   1 EDYLEETGARAAPVELFKQPVDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPDI 80

                           90
                   ....*....|....*.
gi 594591569    93 QPVGTCEQGGDLLQPP 108
Cdd:smart00561  81 FPVGWCEKNGHPLQPP 96

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594591569 147 NNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPP 217
Cdd:cd20102    2 HGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPP 72

first 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 first MBT repeat that contains the semi-aromatic cage and may bind methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  35 PPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLN 114
Cdd:cd20101    1 FNKNGFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSECYDFWVNADSPDIFPVGWCEKTGHKLQPPKGYTSE 80

                         90       100
                 ....*....|....*....|...
gi 594591569 115 TSSWPMFLlrVLTGSELAPAVFF 137
Cdd:cd20101   81 TFSWSAYL--KLTKAQAAPKHLF 101

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).

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594591569 149 FIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWS-GAFDYWCDYDSRDIFPVGWCR 208
Cdd:cd20088    1 FKVGMKLEAVDPLNPSEICVATVVKVVGGRLLLHFDGWDpSRYDFWCDVDSPDIHPVGWCE 61

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594591569 149 FIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPP 217
Cdd:cd20136    5 FQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAP 73

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  37 TNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLNTS 116
Cdd:cd20102    1 PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPPKGYSPGNF 80

                 ..
gi 594591569 117 SW 118
Cdd:cd20102   81 SW 82

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594591569 149 FIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPP 217
Cdd:cd20135    6 FRVGMKLEAVDKKNPSFICVATITDMVDNRLLIHFDNWDESYDYWCDASSPYIHPVGYCQEHGRTLTTP 74

first 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 first MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594591569 146 QNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPP 217
Cdd:cd20132    3 KNGFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCYDFWVNADSPDIHPVGWCEKTGHKLHPP 74

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569 137 FKEEPPRPLQNNfivgMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQP 216
Cdd:cd20138    1 FKVKPPHGFQKN----MKLEVVDKRNPMLIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPAGWCAKTGHPLQP 76

                 .
gi 594591569 217 P 217
Cdd:cd20138   77 P 77

first 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 first MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  38 NEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLNTSS 117
Cdd:cd20133    4 NGFKVGMRLEGIDPEHPSLFCVLSVAEVQGYRLRLHFDGYSECYDFWVNADSPDIHPVGWCEKTGHKLLPPKGYKDGEFN 83

                 ....*
gi 594591569 118 WPMFL 122
Cdd:cd20133   84 WSSYL 88

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569 137 FKEEPPrplqNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQP 216
Cdd:cd20139    1 FKLRPP----HGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQV 76

                 .
gi 594591569 217 P 217
Cdd:cd20139   77 P 77

fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2); L3MBTL2, also called L(3)mbt-like protein 2, is a putative Polycomb group (PcG) protein that binds to monomethylated and dimethylated 'Lys-20' on histone H4 and also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. L3MBTL2 orchestrates ubiquitin signalling by dictating the sequential recruitment of RNF8 and RNF168 after DNA damage. It is an integral component of the polycomb repressive complex 1.6 (PRC1.6) and has been implicated in transcriptional repression and chromatin compaction. L3MBTL2 contains 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594591569 147 NNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPP 217
Cdd:cd20130    4 HGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGYQLQPP 74

first 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 first MBT repeat that contains the semi-aromatic cage and may bind methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  29 FRQSKTPP--TNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQ 106
Cdd:cd20131    1 FQDSQAVThnKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQ 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 594591569 107 PPLGYTLNTSSWPMFLLrvLTGSELAPAVFF 137
Cdd:cd20131   81 PPKGYKEEEFSWSQYLR--STRAQAAPKHLF 109

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  39 EFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGY-TLNTSS 117
Cdd:cd20136    4 EFQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAPQGYpNPEKFS 83

                 ....*
gi 594591569 118 WPMFL 122
Cdd:cd20136   84 WTEYL 88

fourth malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family; The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. 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 does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594591569 149 FIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSG-AFDYWCDYDSRDIFPVGWCRLTGDVLQPPGKI 220
Cdd:cd20096    1 FERGMKLEAVNPENPNQICVATITKVVGPLLWLHLDSEKKlSPNIIVDVESTDIFPVGWCESNGYPLVTPRKY 73

first malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family; The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. 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 first MBT repeat that contains a partially conserved semi-aromatic cage.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  38 NEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDG--SDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLNT 115
Cdd:cd20093    2 SGFKPGMKLEVPNKNNPDTYWVATVVMTCGPLLRLRYVGyeDDRSADFWCDLSSGDVHPIGWCAQNGKPLQPPADIKEKE 81

                         90
                 ....*....|...
gi 594591569 116 SSWPMFLLRVLTG 128
Cdd:cd20093   82 LDWAEFLIKELTG 94

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594591569  36 PTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLG 110
Cdd:cd20137    1 PPHGFQVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLG 75

fourth malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family; The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. 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 does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594591569  40 FKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWrLVD--SSDIQPVGTCEQGGDLLQPPLGY 111
Cdd:cd20096    1 FERGMKLEAVNPENPNQICVATITKVVGPLLWLHLDSEKKLSPNI-IVDveSTDIFPVGWCESNGYPLVTPRKY 73

first malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1; Sex comb on midleg homolog 1 (SCMH1) is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. It contains two 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 first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569 117 SWPMFLLRvlTGSELAPAVFFKEEPPRPLqNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDY 196
Cdd:cd20105    3 SWDKYLKE--TGAVPAPVHCFKQSYTPPV-NEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLV 79

                         90       100
                 ....*....|....*....|.
gi 594591569 197 DSRDIFPVGWCRLTGDVLQPP 217
Cdd:cd20105   80 DSSEIQPIGNCEKNGGMLQPP 100

second 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 second MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594591569  39 EFKIGMKLEARDPRNIDSVCVASVIGITGARLRLR-LDGSDNKNDFWRLVDSSDIQPVGTCEQGG 102
Cdd:cd20098   14 PFKVGMRLEVVDKMCISRTRVAVVEEVVGGRLRLQyVDSEDDDDDFWCHMKSPLIHPVGWSQAVG 78

first malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 1 (SFMBT1); SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT1 contains 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 first MBT repeat that contains a partially conserved semi-aromatic cage.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591569  38 NEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDG--SDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLNT 115
Cdd:cd20111    2 NGFSPGMKLEVAVRTDPNTYWVATIITTCGQLLLLRYDGygEDRRADFWCDIMTADLHPIGWCEQNGKTLRPPEGIRDKL 81

                         90
                 ....*....|...
gi 594591569 116 SSWPMFLLRVLTG 128
Cdd:cd20111   82 SDWEEFLAQTLTG 94

first malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein sex comb on midleg and similar proteins; Sex comb on midleg (Scm) is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Scm contains two 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 first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594591569 139 EEPPRplqNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPP 217
Cdd:cd20107    3 QNPPK---NEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEKNGGMLQPP 78