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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948284472 299 PLLWSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSIRLGPALKIYENHVKVLQRSH 367
Cdd:cd09583    1 PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQQSH 69

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 948284472 299 PLLWSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSIRLGPALKIYENHVKVLQRSH 367
Cdd:cd09583    1 PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQQSH 69

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948284472  302 WSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDvLTGLSI-RLGPALKIYeNHVKVL 363
Cdd:pfam00536   3 WSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDD-LLKLGVtLLGHRKKIL-YAIQRL 63

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 948284472 299 PLLWSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSIRLGPALKIYENHVKVLQRSH 367
Cdd:cd09583    1 PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQQSH 69

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 948284472 299 PLLWSVADVARYFTSV-GFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSIRLGPALKIY 356
Cdd:cd09582    1 VLRWSVDEVAEFVQSLpGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIY 59

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948284472 296 SQDPLLWSVADVARYFTSVGfpEQALA-----FRTQEIDGKSLLLMQRSDVLTGLSIRLGPALKI 355
Cdd:cd09578    1 SKDPSTWSVEDVVQFIKEAD--PQALAphvdlFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKL 63

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*
gi 948284472 302 WSVADVARYFTSV-GFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSIRLGPALKI 355
Cdd:cd09579    4 WTVDDVCSFIGSLpGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKI 58

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.

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                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 948284472   299 PLLWSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSI-RLGPALKI 355
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKI 58

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948284472  302 WSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDvLTGLSI-RLGPALKIYeNHVKVL 363
Cdd:pfam00536   3 WSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDD-LLKLGVtLLGHRKKIL-YAIQRL 63

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.

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                 ....*....|....*....|....*....|....*....|....*....|.
gi 948284472 301 LWSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDvLTGLSI-RLG 350
Cdd:cd09506    4 EWTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKED-LTELGVtRVG 53

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.

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                 ....*....|....*....|....*....|....*....|....*....|..
gi 948284472 306 DVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDvLTGLSI-RLGPALKIY 356
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDED-LKELGItSPGHRKKIL 51

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.

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                 ....*....|....*....|....*....|....*....|....*.
gi 948284472 302 WSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSI 347
Cdd:cd09505    5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKI 50

SAM domain (Sterile alpha motif);

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948284472  299 PLLWSVADVARYFTSVGFPEQALAFRTQEIDGKSLLLMQRSDVLTGLSI-RLGPALKIYeNHVKVLQ 364
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGItSVGHRRKIL-KKIQELK 66