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 1280980824 215 VSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQR 269
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1280980824 215 VSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQR 269
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56

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 1280980824  215 VSRWLEEVGFGKYAGVFEMHEVDEEALPLLTI-EDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1280980824 215 VSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQR 269
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1280980824  215 VSRWLEEVGFGKYAGVFEMHEVDEEALPLLTI-EDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66

SAM domain (Sterile alpha motif);

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                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280980824 211 NTNAVSRWLEEVGFGKYAGVFEMHEVD-EEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:pfam07647   5 SLESVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.

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                  ....*....|....*....|....*....|....*....|....*....|...
gi 1280980824 219 LEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09520    11 LAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELN 63

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280980824 215 VSRWLEEVGFGKYAGVFEM-HEVDEEALPLLTIEDLK----EIGVLsvGSRRKLYNAIQRLR 271
Cdd:cd09515     9 VAKWLKKEGFSKYVDLLCNkHRIDGKVLLSLTEEDLRspplEIKVL--GDIKRLWLAIRKLQ 68

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 1280980824 206 RLEDENTNAVSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDL-KEIGVLSVGSRRKLYNAIQRLRGEE 274
Cdd:cd09505     1 SLQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLsKDLKIESLGHRNKILRKIEELKMKS 70

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 1280980824 212 TNAVSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRL 270
Cdd:cd09506     7 VDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1280980824 215 VSRWLEEV-GFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQR 269
Cdd:cd09509     9 VAQFIKSLdGCAEYAEVFREQEIDGQALLLLTEDDLLKGMGLKLGPALKIYNHIVK 64

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 1280980824 215 VSRW-LEEV--------GFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09582     1 VLRWsVDEVaefvqslpGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.

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                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1280980824 214 AVSRWLEEVGFGKYAGVF-EMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09546     5 SVGEWLEAIKMGRYTEIFmENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMR 63

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.

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                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1280980824 212 TNAVSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRL 270
Cdd:cd09507     7 TEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1280980824 211 NTNAVSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVlSVGSRRKLYNAIQRLR 271
Cdd:cd09585     8 DTPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGI-PLGPRKKILNYIRRRF 67

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.

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                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1280980824 214 AVSRWLEEVGFGKYAGVFEMHEVDE-EALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09547     5 TVSDWLDSIKMGQYKNNFMAAGFTTlDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLR 63

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.

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                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1280980824 212 TNAVSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRL 270
Cdd:cd09576     7 TDEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL 65

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.

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                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1280980824 214 AVSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09497     6 AIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQ 63

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.

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                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1280980824 215 VSRWLEEVGFGKYAGVFEMHEVDE-EALP--LLTIEDLKEIGVLSVGSRRKLYNAIQRL 270
Cdd:cd09499     5 VGQWLESIGLPQYESKLLLNGFDDvDFLGsgVMEDQDLKEIGITDEQHRQIILQAARSL 63

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1280980824 212 TNAVSRWLEEVGFGKYAGVFEMHEVDE-EALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09527     2 SNIVYDWLRTLQLEQYAEKFVDNGYDDlEVCKQIGDPDLDAIGVMNPAHRKRILEAVRRLK 62

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.

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                  ....*....|....*....|....*....|....*....|....*....
gi 1280980824 215 VSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKE-IGvLSVGSRRK 262
Cdd:cd09501     9 VQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQdLG-MSSGLLRK 56

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.

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gi 1280980824 214 AVSRWLEEVGFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLRG 272
Cdd:cd09524     7 SISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLIS 65

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1280980824 213 NAVSRWLEEVGFGKYAGVFEMHEVD--EEALPLlTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09498     8 NDLLEWLSLLGLPQYHKVLVENGYDsiDFVTDL-TWEDLQDIGITKLGHQKKLMLAIKKLK 67

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.

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                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1280980824 214 AVSRWLEEVGFGKYAGVFEMHEVDE-EALPLLTIEDLKEIGVLSVGSRRKLYNAIQ 268
Cdd:cd09542     6 SVSEWLESIRMKRYILHFRSAGLDTmECVLELTAEDLTQMGITLPGHQKRILCSIQ 61

SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1280980824 214 AVSRWLEEVGFGKYAGVFEMHEVDE-EALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLRGE 273
Cdd:cd09548     9 SVGEWLEAIKMERYKDNFTAAGYNSlESVARMTIEDVMSLGITLVGHQKKIMSSIQTMRAQ 69

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280980824 213 NAVSRWLEEVGFGKYAGVFEMHEVDE-EALPLLTIEDLKEIGVLSVGSRRKLYNAIQRLR 271
Cdd:cd09549     8 GSVGEWLEALDLCRYKDNFAAAGYGSlEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.

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                  ....*....|....*....|....*....|....*....|....*...
gi 1280980824 223 GFGKYAGVFEMHEVDEEALPLLTIEDLKEIGVLSVGSRRKLYNAIQRL 270
Cdd:cd09521    16 ELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEV 63