three malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 2 (SFMBT2); 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. SFMBT2 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 third 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 568912457  21 HFFTVGMRLETLHISDPFHIYPASVTKVFNSKFFQVAIDDLRPEADKPTMLCHADSLGILPVQWCLKNGVNLAPPKGYSG 100
Cdd:cd20116    1 HSFTVGMKLEVVDPREPFHICPASVTKVFNNHYFQVTVDDLRPEASENSMLCHADSLGILPVQWCLKNGVNLTPPKGYSG 80

                         90
                 ....*....|...
gi 568912457 101 QDFNWVDYHKQRQ 113
Cdd:cd20116   81 QDFDWADYQKQCG 93

SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT1,2 (Sex comb on midleg, Malignant Brain Tumor) subfamily proteins (also known as Sfmbt1,2 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain four MBT repeats and DUF5388 domain. The MBT repeats of the human sfmbt1 protein are responsible for association with the nuclear matrix and for selective binding of H3 histone N-terminal tails, while the exact function of the SAM domain is unclear.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912457 617 EEKLILESNPLEWSVTDVVRFIKLTDCAPLARIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIERVKVAFYAQ 696
Cdd:cd09581    3 EERLKLDSNPLFWSVDDVVRFIKSTDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVKVAFYEQ 82

                 ...
gi 568912457 697 YAS 699
Cdd:cd09581   83 FAN 85

three malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 2 (SFMBT2); 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. SFMBT2 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 third 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 568912457  21 HFFTVGMRLETLHISDPFHIYPASVTKVFNSKFFQVAIDDLRPEADKPTMLCHADSLGILPVQWCLKNGVNLAPPKGYSG 100
Cdd:cd20116    1 HSFTVGMKLEVVDPREPFHICPASVTKVFNNHYFQVTVDDLRPEASENSMLCHADSLGILPVQWCLKNGVNLTPPKGYSG 80

                         90
                 ....*....|...
gi 568912457 101 QDFNWVDYHKQRQ 113
Cdd:cd20116   81 QDFDWADYQKQCG 93

SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT1,2 (Sex comb on midleg, Malignant Brain Tumor) subfamily proteins (also known as Sfmbt1,2 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain four MBT repeats and DUF5388 domain. The MBT repeats of the human sfmbt1 protein are responsible for association with the nuclear matrix and for selective binding of H3 histone N-terminal tails, while the exact function of the SAM domain is unclear.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912457 617 EEKLILESNPLEWSVTDVVRFIKLTDCAPLARIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIERVKVAFYAQ 696
Cdd:cd09581    3 EERLKLDSNPLFWSVDDVVRFIKSTDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVKVAFYEQ 82

                 ...
gi 568912457 697 YAS 699
Cdd:cd09581   83 FAN 85

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 568912457   107 DYHKQRQAEEAPHFCFKNA---FSRGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPmPDIIVDMDSMDI 183
Cdd:smart00561   2 DYLEETGARAAPVELFKQPvdsPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDK-YDFWCHADSPDI 80

                           90
                   ....*....|....*.
gi 568912457   184 FPVGWCEANSYPLTTP 199
Cdd:smart00561  81 FPVGWCEKNGHPLQPP 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 568912457     8 PCFFlKDHADLQSHFFTVGMRLETLHISDPFHIYPASVTKVFNSkFFQVAIDDLRpeaDKPTMLCHADSLGILPVQWCLK 87
Cdd:smart00561  14 VELF-KQPVDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGY-RLLLHFDGWD---DKYDFWCHADSPDIFPVGWCEK 88

                   ....*...
gi 568912457    88 NGVNLAPP 95
Cdd:smart00561  89 NGHPLQPP 96

SAM / Pointed domain; A subfamily of the SAM domain

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912457   612 SSQSDEEKLILESNPLEWSVTDVVRFI----KLTDCAPLarIFQEQDIDGQALLLLTlptvQECMELKLGPA 679
Cdd:smart00251   3 NFEKEQKRLGIPADPQLWTEDHVLEWLewavKEFSLSPI--DFSKFDMSGKELCSMS----KEEFLERAPFG 68

three malignant brain tumor (MBT) repeat found in Scm-like with four MBT domains protein 2 (SFMBT2); 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. SFMBT2 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 third 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 568912457  21 HFFTVGMRLETLHISDPFHIYPASVTKVFNSKFFQVAIDDLRPEADKPTMLCHADSLGILPVQWCLKNGVNLAPPKGYSG 100
Cdd:cd20116    1 HSFTVGMKLEVVDPREPFHICPASVTKVFNNHYFQVTVDDLRPEASENSMLCHADSLGILPVQWCLKNGVNLTPPKGYSG 80

                         90
                 ....*....|...
gi 568912457 101 QDFNWVDYHKQRQ 113
Cdd:cd20116   81 QDFDWADYQKQCG 93

SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT1,2 (Sex comb on midleg, Malignant Brain Tumor) subfamily proteins (also known as Sfmbt1,2 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain four MBT repeats and DUF5388 domain. The MBT repeats of the human sfmbt1 protein are responsible for association with the nuclear matrix and for selective binding of H3 histone N-terminal tails, while the exact function of the SAM domain is unclear.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912457 617 EEKLILESNPLEWSVTDVVRFIKLTDCAPLARIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIERVKVAFYAQ 696
Cdd:cd09581    3 EERLKLDSNPLFWSVDDVVRFIKSTDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVKVAFYEQ 82

                 ...
gi 568912457 697 YAS 699
Cdd:cd09581   83 FAN 85

third 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 third 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 568912457  23 FTVGMRLETLHISDPFHIYPASVTKVFNSKFFQVAIDDLRPEADKP-TMLCHADSLGILPVQWCLKNGVNLAPPKGYSGQ 101
Cdd:cd20095    1 FKVGMKLEALHPKNPSTICPATVTKVFNEYYFLVEIDDLRPEESEKiTFVCHANSPGIFPVGWCAKNGLRLTPPPGYPKS 80

                         90
                 ....*....|
gi 568912457 102 DFNWVDYHKQ 111
Cdd:cd20095   81 EFDWDSYLKL 90

third 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 third 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 568912457  21 HFFTVGMRLETLHISDPFHIYPASVTKVFNSKFFQVAIDDLRPE-ADKPTMLCHADSLGILPVQWCLKNGVNLAPPKGYS 99
Cdd:cd20115    1 HCFSEGMKLEAVDPAAPFTISPATVAKVFNEKFFLVEMDDLRPEeAGAHSFVCHRDSPGIFPVQWSLKNGLHLSPPPGYP 80

                         90
                 ....*....|..
gi 568912457 100 GQDFNWVDYHKQ 111
Cdd:cd20115   81 GQDFDWADYLKQ 92

fourth 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 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMPDIIVDMDSMDIFPVGWCEANSYPLTTPYKASSKSKR 208
Cdd:cd20117    2 CFKENMKLEAVNPICPEEICVATVTKVKGSYLWLQLEGSKKPIPECIVHVESMDIFPVGWCETNGYPLLHPRKARVNKQR 81

                 ....*....
gi 568912457 209 KTVHFKMEK 217
Cdd:cd20117   82 KIAVVQPEK 90

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912457 626 PLEWSVTDVVRFIKLTD-CAPLARIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIER 688
Cdd:cd09509    1 PSKWSVDDVAQFIKSLDgCAEYAEVFREQEIDGQALLLLTEDDLLKGMGLKLGPALKIYNHIVK 64

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912457 128 RGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20100    1 HGFKVGMKLEAVDLMEPRLICVATVTRVVGRLLRVHFDGWDDEF-DQWVDCDSPDIYPVGWCELVGYPLQPP 71

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 568912457     8 PCFFlKDHADLQSHFFTVGMRLETLHISDPFHIYPASVTKVFNSkFFQVAIDDLRpeaDKPTMLCHADSLGILPVQWCLK 87
Cdd:smart00561  14 VELF-KQPVDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGY-RLLLHFDGWD---DKYDFWCHADSPDIFPVGWCEK 88

                   ....*...
gi 568912457    88 NGVNLAPP 95
Cdd:smart00561  89 NGHPLQPP 96

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912457 128 RGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETpMPDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20103    3 HGFEVGMKLEAVDKRNPRLIRVATVADVEDYRVKLHFDGWPD-IYDFWVDDDSPDIHPPGWCSKTGHPLEPP 73

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETpMPDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20101    5 GFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSE-CYDFWVNADSPDIFPVGWCEKTGHKLQPP 74

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 568912457 127 SRGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETpMPDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20102    1 PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDD-SYDYWCDPDSPYIHPVGWCEENGKTLQPP 72

third malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt) and similar proteins; dSfmbt, also called Scm-like with four MBT domain-containing protein 1, is a Polycomb group repressor involved in epigenetic regulation of gene expression. dSfmbt 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 third 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912457  23 FTVGMRLETLhisDPF---HIYPASVTKVFNSKFFQVAIDDLRPEADKPTMLC-HADSLGILPVQWCLKNGVNLAPPKGY 98
Cdd:cd20125    1 FKEGMKLEAV---DPLnlsAICVATVMKVLRFGYLMIRIDSYEPDASGSDWFCyHESSPCIFPAGFCEVNNITLTPPNGY 77

                         90       100
                 ....*....|....*....|
gi 568912457  99 SGQDFNWVDYHKQRQAEEAP 118
Cdd:cd20125   78 DGRTFTWEGYLRQTGATAAP 97

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912457 122 FKNAFSRGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20138    1 FKVKPPHGFQKNMKLEVVDKRNPMLIRVATVADTDDHRVKVHFDGWNNCY-DYWIDADSPDIHPAGWCAKTGHPLQPP 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 568912457 127 SRGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20130    3 NHGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEY-DQWVDCESPDIYPVGWCELTGYQLQPP 74

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 568912457 122 FKNAFSRGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTPYK 201
Cdd:cd20139    1 FKLRPPHGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNY-DFWVDADSPDIHPVGWCDKTGHALQVPLG 79

                 ..
gi 568912457 202 AS 203
Cdd:cd20139   80 AS 81

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGL-ETPMPDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20093    3 GFKPGMKLEVPNKNNPDTYWVATVVMTCGPLLRLRYVGYeDDRSADFWCDLSSGDVHPIGWCAQNGKPLQPP 74

SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin and Atherin-like subfamily proteins is a putative protein-protein and/or protein-lipid interaction domain. In addition to the C-terminal SAM domain, the majority of proteins belonging to this group also have PHD (or Zn finger) domain. As potential members of the polycomb group, these proteins may be involved in regulation of some key regulatory genes during development. Atherin can be recruited by Ruk/CIN85 kinase-binding proteins via its SH3 domains thus participating in the signal transferring kinase cascades. Also, atherin was found associated with low density lipids (LDL) in atherosclerotic lesions in human. It was suggested that atherin plays an essential role in atherogenesis via immobilization of LDL in the arterial wall. SAM domains of atherins are predicted to form polymers. Inhibition of polymer formation could be a potential antiatherosclerotic therapy.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568912457 626 PLEWSVTDVVRFIKLTDCAPLARIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIERVKV 691
Cdd:cd09583    1 PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQ 66

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
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568912457  72 CHADSLGILPVQWCLKNGVNLAPPKGYSGQDFNWVDYHKQRQAEEAPHFCF 122
Cdd:cd20101   51 VNADSPDIFPVGWCEKTGHKLQPPKGYTSETFSWSAYLKLTKAQAAPKHLF 101

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20133    5 GFKVGMRLEGIDPEHPSLFCVLSVAEVQGYRLRLHFDGYSECY-DFWVNADSPDIHPVGWCEKTGHKLLPP 74

SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a protein-protein interaction domain. Phylogenetic analysis suggests that proteins of this subfamily are most closely related to SAM-Ph1,2,3 subfamily of Polycomb group. They are predicted transcriptional repressors in photoreceptor cells and pinealocytes of vertebrates. SAM domain containing protein 11 is also known as Mr-s (major retinal SAM) protein. In mouse, it is predominantly expressed in developing retinal photoreceptors and in adult pineal gland. The SAM domain is involved in homooligomerization of whole proteins (it was shown based on immunoprecipitation assay and mutagenesis), however its repression activity is not due to SAM/SAM interactions but to the C-terminal region.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912457 627 LEWSVTDVVRFI-KLTDCAPLARIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIER 688
Cdd:cd09579    2 RKWTVDDVCSFIgSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQVAK 64

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 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20132    5 GFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCY-DFWVNADSPDIHPVGWCEKTGHKLHPP 74

second malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein sex comb on midleg (Scm) and similar proteins; 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 second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912457 127 SRGFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20110    3 SNLFKVGMKLEAVDRKNPHLICPATVGAVKDDQIFVTFDGWRGAF-DYWCRYDSRDIFPVGWCARSGHPLQPP 74

third 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 third 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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912457 130 FSKNMKLEAVNPVNPGEVCVATVVSV-KGRLLWLHLEGLETPMPD--IIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20099    1 FKVGMKLEAVDPLNLSSICVATVRKVlRFGYLVIGIDGPSADDGSdwFCCHASSPFIFPVGFAEKNGIELTPP 73

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVS-VKGRLLwLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP--YKASSk 205
Cdd:cd20135    5 GFRVGMKLEAVDKKNPSFICVATITDmVDNRLL-IHFDNWDESY-DYWCDASSPYIHPVGYCQEHGRTLTTPpgYKDPK- 81

                         90
                 ....*....|....
gi 568912457 206 skrktvHFKMEKQL 219
Cdd:cd20135   82 ------HFSWEKYL 89

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 568912457  23 FTVGMRLETLhisDPFHIYPASVTKVFNSKFFQVAID-DLRPEadkptmlCH-----ADSLGILPVQWCLKNGVNLAPPK 96
Cdd:cd20133    6 FKVGMRLEGI---DPEHPSLFCVLSVAEVQGYRLRLHfDGYSE-------CYdfwvnADSPDIHPVGWCEKTGHKLLPPK 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 568912457  97 GYSGQDFNWVDYHKQRQAEEAPhfcfKNAF 126
Cdd:cd20133   76 GYKDGEFNWSSYLKTCKAQAAP----KNLF 101

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGLETPMpDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20134    5 GFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTY-DYWCDPSSPYIHPVGWCQKQGKPLTPP 74

third malignant brain tumor (MBT) repeat found in MBT domain-containing protein 1 (MBTD1); MBTD1 is a putative Polycomb group (PcG) protein that specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. MBTD1 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 third 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912457 130 FSKNMKLEAVNPVNPGEVCVATVVSV-KGRLLWLHLEGLETPMPD--IIVDMDSMDIFPVGWCEANSYPLTTP--YKASS 204
Cdd:cd20126    1 FKEGMKLEAIDPLNLSTICVATVRKVlANGYLMIGIDGSEAADGSdwFCYHATSPSIFPVGFCEINMIELTPPrgYKKPF 80

                 .
gi 568912457 205 K 205
Cdd:cd20126   81 K 81

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568912457 129 GFSKNMKLEAVNPVNPGEVCVATVVSVKGRLLWLHLEGL-ETPMPDIIVDMDSMDIFPVGWCEANSYPLTTP 199
Cdd:cd20111    3 GFSPGMKLEVAVRTDPNTYWVATIITTCGQLLLLRYDGYgEDRRADFWCDIMTADLHPIGWCEQNGKTLRPP 74