sex comb on midleg-like protein 1 isoform X4 [Macaca mulatta]
Protein Classification
SAM domain-containing protein; Smaug family SAM domain-containing protein( domain architecture ID 10176023)
SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation| Smaug family sterile alpha motif (SAM) domain-containing protein such as mammalian Smaug which is a translational repressor that forms cytoplasmic foci similar to stress granules
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SAM_Scm | cd09578 | SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ... |
290-361 | 5.82e-33 | ||
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex comb on midleg) subfamily of Polycomb group is a protein-protein interaction domain. Proteins of this subfamily are transcriptional repressors associated with PRC1 complex. This group includes invertebrate Scm protein and chordate Scm homolog 1 and Scm-like 1, 2, 3 proteins. Most have a SAM domain, two MBT repeats, and a DUF3588 domain, except Scm-like 4 proteins which do not have MBT repeats. Originally the Scm protein was described in Drosophila as a regulator required for proper spatial expression of homeotic genes. It plays a major role during early embryogenesis. SAM domains of Scm proteins can interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with SAM domains of Ph (polyhomeotic) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Mammalian Scmh1 protein is known be indispensible member of PRC1 complex; it plays a regulatory role for the complex during meiotic prophase of male sperm cells, and is particularly involved in regulation of chromatin modification at the XY chromatin domain of the pachytene spermatocytes. : Pssm-ID: 188977 Cd Length: 72 Bit Score: 117.52 E-value: 5.82e-33
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| Name | Accession | Description | Interval | E-value | ||
| SAM_Scm | cd09578 | SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ... |
290-361 | 5.82e-33 | ||
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex comb on midleg) subfamily of Polycomb group is a protein-protein interaction domain. Proteins of this subfamily are transcriptional repressors associated with PRC1 complex. This group includes invertebrate Scm protein and chordate Scm homolog 1 and Scm-like 1, 2, 3 proteins. Most have a SAM domain, two MBT repeats, and a DUF3588 domain, except Scm-like 4 proteins which do not have MBT repeats. Originally the Scm protein was described in Drosophila as a regulator required for proper spatial expression of homeotic genes. It plays a major role during early embryogenesis. SAM domains of Scm proteins can interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with SAM domains of Ph (polyhomeotic) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Mammalian Scmh1 protein is known be indispensible member of PRC1 complex; it plays a regulatory role for the complex during meiotic prophase of male sperm cells, and is particularly involved in regulation of chromatin modification at the XY chromatin domain of the pachytene spermatocytes. Pssm-ID: 188977 Cd Length: 72 Bit Score: 117.52 E-value: 5.82e-33
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
293-361 | 5.07e-06 | ||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 43.82 E-value: 5.07e-06
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| SAM_1 | pfam00536 | SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
294-360 | 3.06e-05 | ||
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains. Pssm-ID: 425739 Cd Length: 64 Bit Score: 41.49 E-value: 3.06e-05
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| Name | Accession | Description | Interval | E-value | ||
| SAM_Scm | cd09578 | SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ... |
290-361 | 5.82e-33 | ||
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex comb on midleg) subfamily of Polycomb group is a protein-protein interaction domain. Proteins of this subfamily are transcriptional repressors associated with PRC1 complex. This group includes invertebrate Scm protein and chordate Scm homolog 1 and Scm-like 1, 2, 3 proteins. Most have a SAM domain, two MBT repeats, and a DUF3588 domain, except Scm-like 4 proteins which do not have MBT repeats. Originally the Scm protein was described in Drosophila as a regulator required for proper spatial expression of homeotic genes. It plays a major role during early embryogenesis. SAM domains of Scm proteins can interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with SAM domains of Ph (polyhomeotic) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Mammalian Scmh1 protein is known be indispensible member of PRC1 complex; it plays a regulatory role for the complex during meiotic prophase of male sperm cells, and is particularly involved in regulation of chromatin modification at the XY chromatin domain of the pachytene spermatocytes. Pssm-ID: 188977 Cd Length: 72 Bit Score: 117.52 E-value: 5.82e-33
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| SAM_Polycomb | cd09509 | SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ... |
293-358 | 3.72e-16 | ||
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. Pssm-ID: 188908 Cd Length: 64 Bit Score: 72.13 E-value: 3.72e-16
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| SAM_Scm-like-4MBT1,2 | cd09581 | SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of ... |
293-361 | 1.14e-09 | ||
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. Pssm-ID: 188980 Cd Length: 85 Bit Score: 54.76 E-value: 1.14e-09
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| SAM_Ph1,2,3 | cd09577 | SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ... |
293-361 | 2.03e-08 | ||
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Pssm-ID: 188976 Cd Length: 69 Bit Score: 50.48 E-value: 2.03e-08
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
293-361 | 5.07e-06 | ||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 43.82 E-value: 5.07e-06
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| SAM_Scm-like-3MBT3,4 | cd09582 | SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ... |
293-360 | 5.51e-06 | ||
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma. Pssm-ID: 188981 Cd Length: 66 Bit Score: 43.42 E-value: 5.51e-06
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| SAM_1 | pfam00536 | SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
294-360 | 3.06e-05 | ||
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains. Pssm-ID: 425739 Cd Length: 64 Bit Score: 41.49 E-value: 3.06e-05
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| SAM_Scm-like-4MBT | cd09580 | SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of ... |
293-360 | 3.59e-05 | ||
SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT (Sex comb on midleg like, Malignant Brain Tumor) subfamily proteins of the polycomb group is a putative protein-protein interaction domain. Additionally to the SAM domain, most of the proteins of this subfamily have 4 MBT repeats. In Drosophila SAM-Scm-like-4MBT protein (known as dSfmbt) is a member of Pho repressive complex (PhoRC). Additionally to dSfmbt, the PhoRC complex includes Pho or Pho-like proteins. This complex is responsible for HOX (Homeobox) gene silencing: Pho or Pho-like proteins bind DNA and dSmbt binds methylated histones. dSmbt can interact with mono- and di-methylated histones H3 and H4 (however this activity has been shown for the MBT repeats, while exact function of the SAM domain is unclear). Besides interaction with histones, dSmbt can interact with Scm (a member of PRC complex), but this interaction also seems to be SAM domain independent. Pssm-ID: 188979 Cd Length: 67 Bit Score: 41.20 E-value: 3.59e-05
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| SAM_Atherin-like | cd09583 | SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ... |
293-363 | 4.52e-04 | ||
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. Pssm-ID: 188982 Cd Length: 69 Bit Score: 38.41 E-value: 4.52e-04
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| SAM_WDSUB1 | cd09505 | SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ... |
292-363 | 1.03e-03 | ||
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding. Pssm-ID: 188904 Cd Length: 72 Bit Score: 37.30 E-value: 1.03e-03
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