WD repeat, SAM and U-box domain-containing protein 1 [Rattus norvegicus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
3-311 | 8.47e-75 | |||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 240.58 E-value: 8.47e-75
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| SAM_WDSUB1 | cd09505 | SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ... |
328-399 | 4.35e-34 | |||||
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: 122.43 E-value: 4.35e-34
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| U-box | pfam04564 | U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ... |
404-476 | 1.67e-32 | |||||
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues. : Pssm-ID: 398320 [Multi-domain] Cd Length: 73 Bit Score: 118.18 E-value: 1.67e-32
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| Name | Accession | Description | Interval | E-value | |||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
3-311 | 8.47e-75 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 240.58 E-value: 8.47e-75
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
4-309 | 1.01e-60 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 200.25 E-value: 1.01e-60
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| SAM_WDSUB1 | cd09505 | SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ... |
328-399 | 4.35e-34 | |||||
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: 122.43 E-value: 4.35e-34
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| U-box | pfam04564 | U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ... |
404-476 | 1.67e-32 | |||||
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues. Pssm-ID: 398320 [Multi-domain] Cd Length: 73 Bit Score: 118.18 E-value: 1.67e-32
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| RING-Ubox_WDSUB1-like | cd16655 | U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ... |
405-460 | 1.46e-30 | |||||
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis. Pssm-ID: 438317 [Multi-domain] Cd Length: 55 Bit Score: 112.60 E-value: 1.46e-30
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
407-470 | 1.41e-22 | |||||
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination. Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 90.76 E-value: 1.41e-22
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
332-396 | 3.44e-16 | |||||
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: 72.71 E-value: 3.44e-16
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| SAM_2 | pfam07647 | SAM domain (Sterile alpha motif); |
332-394 | 3.21e-13 | |||||
SAM domain (Sterile alpha motif); Pssm-ID: 429573 Cd Length: 66 Bit Score: 64.21 E-value: 3.21e-13
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
230-267 | 1.69e-07 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 47.31 E-value: 1.69e-07
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
230-267 | 1.22e-06 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 45.03 E-value: 1.22e-06
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| PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
55-179 | 4.63e-06 | |||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 49.31 E-value: 4.63e-06
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| UFD2 | COG5113 | Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ... |
366-471 | 9.31e-05 | |||||
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227444 [Multi-domain] Cd Length: 929 Bit Score: 44.97 E-value: 9.31e-05
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| Name | Accession | Description | Interval | E-value | |||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
3-311 | 8.47e-75 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 240.58 E-value: 8.47e-75
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
4-315 | 3.15e-61 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 205.15 E-value: 3.15e-61
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
4-309 | 1.01e-60 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 200.25 E-value: 1.01e-60
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
3-270 | 1.50e-60 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 203.60 E-value: 1.50e-60
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
19-314 | 1.35e-48 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 171.63 E-value: 1.35e-48
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
50-317 | 1.53e-48 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 168.28 E-value: 1.53e-48
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
3-217 | 4.85e-38 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 140.16 E-value: 4.85e-38
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| SAM_WDSUB1 | cd09505 | SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ... |
328-399 | 4.35e-34 | |||||
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: 122.43 E-value: 4.35e-34
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| U-box | pfam04564 | U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ... |
404-476 | 1.67e-32 | |||||
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues. Pssm-ID: 398320 [Multi-domain] Cd Length: 73 Bit Score: 118.18 E-value: 1.67e-32
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| RING-Ubox_WDSUB1-like | cd16655 | U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ... |
405-460 | 1.46e-30 | |||||
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis. Pssm-ID: 438317 [Multi-domain] Cd Length: 55 Bit Score: 112.60 E-value: 1.46e-30
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
172-318 | 7.85e-24 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 100.87 E-value: 7.85e-24
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
407-470 | 1.41e-22 | |||||
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination. Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 90.76 E-value: 1.41e-22
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| RING-Ubox_CHIP | cd16654 | U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ... |
404-474 | 2.99e-16 | |||||
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase. Pssm-ID: 438316 [Multi-domain] Cd Length: 71 Bit Score: 72.99 E-value: 2.99e-16
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
332-396 | 3.44e-16 | |||||
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: 72.71 E-value: 3.44e-16
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| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
405-457 | 3.74e-16 | |||||
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain. Pssm-ID: 438326 [Multi-domain] Cd Length: 53 Bit Score: 72.21 E-value: 3.74e-16
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
146-314 | 2.00e-15 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 78.03 E-value: 2.00e-15
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| RING-Ubox | cd16453 | U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ... |
408-452 | 3.85e-15 | |||||
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. Pssm-ID: 438117 [Multi-domain] Cd Length: 44 Bit Score: 69.12 E-value: 3.85e-15
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| RING-Ubox_LubX-like_rpt2 | cd23150 | second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ... |
405-471 | 2.58e-13 | |||||
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one. Pssm-ID: 438512 [Multi-domain] Cd Length: 69 Bit Score: 64.79 E-value: 2.58e-13
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| SAM_2 | pfam07647 | SAM domain (Sterile alpha motif); |
332-394 | 3.21e-13 | |||||
SAM domain (Sterile alpha motif); Pssm-ID: 429573 Cd Length: 66 Bit Score: 64.21 E-value: 3.21e-13
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| SAM_superfamily | cd09487 | SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
336-392 | 6.55e-13 | |||||
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. Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 63.03 E-value: 6.55e-13
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| SAM_1 | pfam00536 | SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
332-394 | 1.97e-12 | |||||
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: 61.90 E-value: 1.97e-12
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| RING-Ubox_LubX-like_rpt1 | cd23149 | first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ... |
408-463 | 5.85e-12 | |||||
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one. Pssm-ID: 438511 [Multi-domain] Cd Length: 55 Bit Score: 60.58 E-value: 5.85e-12
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| SAM_HD | cd09508 | SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ... |
332-394 | 6.88e-11 | |||||
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon). Pssm-ID: 188907 Cd Length: 70 Bit Score: 57.71 E-value: 6.88e-11
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| SAM_Ste11_fungal | cd09534 | SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ... |
332-394 | 7.11e-11 | |||||
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator. Pssm-ID: 188933 Cd Length: 62 Bit Score: 57.60 E-value: 7.11e-11
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| SAM_SARM1-like_repeat1 | cd09501 | SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
332-395 | 1.38e-10 | |||||
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. Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 56.93 E-value: 1.38e-10
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| SAM_SGMS1-like | cd09515 | SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ... |
329-395 | 2.05e-10 | |||||
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. Pssm-ID: 188914 Cd Length: 70 Bit Score: 56.49 E-value: 2.05e-10
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| SAM_DGK-delta-eta | cd09507 | SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ... |
329-393 | 3.71e-09 | |||||
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. Pssm-ID: 188906 Cd Length: 65 Bit Score: 52.80 E-value: 3.71e-09
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| SAM_BOI-like_fungal | cd09535 | SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ... |
332-394 | 2.77e-08 | |||||
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation). Pssm-ID: 188934 Cd Length: 65 Bit Score: 50.25 E-value: 2.77e-08
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| SPL-RING_NSE2 | cd16651 | SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ... |
408-469 | 7.63e-08 | |||||
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity. Pssm-ID: 438313 [Multi-domain] Cd Length: 67 Bit Score: 49.18 E-value: 7.63e-08
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| SAM_Neurabin-like | cd09512 | SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
329-395 | 9.50e-08 | |||||
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions. Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 48.80 E-value: 9.50e-08
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| SAM_Polycomb | cd09509 | SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ... |
332-377 | 1.01e-07 | |||||
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: 48.63 E-value: 1.01e-07
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
230-267 | 1.69e-07 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 47.31 E-value: 1.69e-07
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
270-308 | 3.75e-07 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 46.54 E-value: 3.75e-07
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| SAM_DGK-eta | cd09576 | SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ... |
329-393 | 1.12e-06 | |||||
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. Pssm-ID: 188975 Cd Length: 65 Bit Score: 45.73 E-value: 1.12e-06
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
230-267 | 1.22e-06 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 45.03 E-value: 1.22e-06
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| SAM_Ph1,2,3 | cd09577 | SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ... |
332-394 | 1.61e-06 | |||||
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: 45.47 E-value: 1.61e-06
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| SAM_Ste50-like_fungal | cd09533 | SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ... |
336-394 | 1.83e-06 | |||||
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity. Pssm-ID: 188932 Cd Length: 58 Bit Score: 45.00 E-value: 1.83e-06
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| SAM_MLTK | cd09529 | SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ... |
332-393 | 2.29e-06 | |||||
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a protein-protein interaction domain. Besides SAM domain, these proteins have N-terminal protein tyrosine kinase domain and leucine-zipper motif. Proteins of this group act as mitogen-activated protein triple kinase in a number of MAPK cascades. They can be activated by autophosphorylation in response to stress signals. MLTK-alpha is known to phosphorylate histone H3. In mammals, MLTKs participate in the activation of the JNK/SAPK, p38, ERK5 pathways, the transcriptional factor NF-kB, in the regulation of the cell cycle checkpoint, and in the induction of apoptosis in a hepatoma cell line. Some members of this subfamily are proto-oncogenes, thus MLTK-alpha is involved in neoplasmic cell transformation and/or skin cancer development in athymic nude mice. Based on in vivo coprecipitation experiments in mammalian cells, it has been demonstrated that MLTK proteins might form homodimers/oligomers via their SAM domains. Pssm-ID: 188928 Cd Length: 71 Bit Score: 45.19 E-value: 2.29e-06
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| SAM_DGK-delta | cd09575 | SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ... |
329-393 | 2.55e-06 | |||||
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-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-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta. Pssm-ID: 188974 Cd Length: 65 Bit Score: 44.94 E-value: 2.55e-06
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
46-82 | 2.67e-06 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.84 E-value: 2.67e-06
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
272-308 | 2.79e-06 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.87 E-value: 2.79e-06
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| SAM_aveugle-like | cd09510 | SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like ... |
332-398 | 3.00e-06 | |||||
SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis. Pssm-ID: 188909 Cd Length: 75 Bit Score: 44.99 E-value: 3.00e-06
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| PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
55-179 | 4.63e-06 | |||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 49.31 E-value: 4.63e-06
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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 ... |
329-371 | 5.60e-06 | |||||
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: 43.90 E-value: 5.60e-06
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
3-38 | 1.24e-05 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 42.30 E-value: 1.24e-05
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| RING-Ubox1_NOSIP | cd16661 | U-box domain 1, a modified RING finger, found in nitric oxide synthase-interacting protein ... |
410-449 | 1.41e-05 | |||||
U-box domain 1, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies, including cleft lip/palate, cyclopia, and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting the nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the first U-box domain. Pssm-ID: 438323 Cd Length: 46 Bit Score: 42.31 E-value: 1.41e-05
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| SAM_GAREM | cd09525 | SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ... |
333-394 | 2.98e-05 | |||||
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and regulator of Erk/MARK) protein subfamily (also known as FAM59A) is a putative protein-protein interaction domain. SAM domain is a widespread domain in signaling proteins. Proteins of this group have SAM at the C-terminus. Human GAREM protein is known to play a role in regulation of the EGF (Epidermal Growth Factor) receptor and of Gab or insulin preceptor substrate-1 family proteins. Grb2 (Growth factor receptor-bound) protein was identified as a binding partner of human GAREM. Proline-rich motifs and phosphorylation of two conserved tyrosines in GAREM are important for the interaction with the SH3 domains of Grb2 protein; however these motifs and residues do not belong to the SAM domain. Pssm-ID: 188924 Cd Length: 67 Bit Score: 41.75 E-value: 2.98e-05
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| SAM_Atherin-like | cd09583 | SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ... |
331-381 | 4.15e-05 | |||||
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: 41.49 E-value: 4.15e-05
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
3-38 | 5.09e-05 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.41 E-value: 5.09e-05
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
50-82 | 7.11e-05 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.02 E-value: 7.11e-05
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| SAM_Shank1,2,3 | cd09506 | SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ... |
332-393 | 8.59e-05 | |||||
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. Pssm-ID: 188905 Cd Length: 66 Bit Score: 40.38 E-value: 8.59e-05
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| UFD2 | COG5113 | Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ... |
366-471 | 9.31e-05 | |||||
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227444 [Multi-domain] Cd Length: 929 Bit Score: 44.97 E-value: 9.31e-05
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| SAM_CNK1,2,3-suppressor | cd09511 | SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ... |
329-394 | 1.54e-04 | |||||
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction. Pssm-ID: 188910 Cd Length: 69 Bit Score: 39.97 E-value: 1.54e-04
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
98-125 | 1.67e-04 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.83 E-value: 1.67e-04
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| Frtz | pfam11768 | WD repeat-containing and planar cell polarity effector protein Fritz; Fritz is a probable ... |
87-167 | 3.15e-04 | |||||
WD repeat-containing and planar cell polarity effector protein Fritz; Fritz is a probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. In Drosophila melanogaster, fritz regulates both the location and the number of wing cell prehair initiation sites. Pssm-ID: 432059 Cd Length: 544 Bit Score: 43.34 E-value: 3.15e-04
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| SAM_SGMS1 | cd09514 | SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ... |
332-394 | 3.59e-04 | |||||
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism. Pssm-ID: 188913 Cd Length: 72 Bit Score: 39.00 E-value: 3.59e-04
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| PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
205-329 | 4.60e-04 | |||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 42.77 E-value: 4.60e-04
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| SAM_BICC1 | cd09520 | SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ... |
335-396 | 4.85e-04 | |||||
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. Pssm-ID: 188919 Cd Length: 65 Bit Score: 38.43 E-value: 4.85e-04
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| SAM_PNT-ERG_FLI-1 | cd08531 | Sterile alpha motif (SAM)/Pointed domain of ERG (Ets related gene) and FLI-1 (Friend leukemia ... |
332-369 | 6.36e-04 | |||||
Sterile alpha motif (SAM)/Pointed domain of ERG (Ets related gene) and FLI-1 (Friend leukemia integration 1) transcription factors; SAM Pointed domain of ERG/FLI-1 subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. The ERG and FLI regulators are involved in endothelial cell differentiation, bone morphogenesis and neural crest development. They are proto-oncogenes implicated in cancer development such as myeloid leukemia, Ewing's sarcoma and erythroleukemia. Members of this subfamily are potential targets for cancer therapy. Pssm-ID: 188877 Cd Length: 75 Bit Score: 38.16 E-value: 6.36e-04
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| Ge1_WD40 | pfam16529 | WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ... |
139-217 | 6.95e-04 | |||||
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions. Pssm-ID: 465162 [Multi-domain] Cd Length: 328 Bit Score: 41.67 E-value: 6.95e-04
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
98-125 | 7.54e-04 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 7.54e-04
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| SAM_Ste50_fungal | cd09536 | SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal ... |
332-387 | 8.39e-04 | |||||
SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and Ras-associated UBQ superfamily domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response, and contribute to cell wall integrity in vegetative cells. Ste50 of S.cerevisiae acts as an adaptor protein between G protein and MAP triple kinase Ste11. Ste50 proteins are able to form homooligomers, binding each other via their SAM domains, as well as heterodimers and heterogeneous complexes with SAM domain or SAM homodimers of MAPKKK Ste11 protein kinase. Pssm-ID: 188935 Cd Length: 74 Bit Score: 37.79 E-value: 8.39e-04
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| SAM_Scm | cd09578 | SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ... |
331-383 | 9.33e-04 | |||||
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: 37.79 E-value: 9.33e-04
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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 ... |
332-394 | 9.36e-04 | |||||
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: 37.64 E-value: 9.36e-04
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| SP-RING-like | cd16452 | SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ... |
408-444 | 1.03e-03 | |||||
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Pssm-ID: 438116 [Multi-domain] Cd Length: 45 Bit Score: 36.85 E-value: 1.03e-03
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| SAM_PNT-ERG | cd08540 | Sterile alpha motif (SAM)/Pointed domain of ERG transcription factor; SAM Pointed domain of ... |
332-371 | 1.11e-03 | |||||
Sterile alpha motif (SAM)/Pointed domain of ERG transcription factor; SAM Pointed domain of ERG subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It may participate in formation of homodimers or heterodimers with ETS-2, Fli-1, ER81, and Pu-1. However, dimeric forms are inactive and SAM Pointed domain is not essential for dimerization, since ER81 and Pu-1 do not have it. In mouse, a regulator of this type binds the ESET histone H3-specific methyltransferase (human homolog is SETDB1), which leads to modification of the local chromatin structure through histone methylation. ERG regulators are involved in endothelial cell differentiation, bone morphogenesis and neural crest development. The Erg gene is a proto-oncogene. It is a target of chromosomal translocations resulting in fusions with other neighboring genes. Chimeric proteins were found in solid tumors such as myeloid leukemia or Ewing's sarcoma. Members of this subfamily are potential targets for cancer therapy. Pssm-ID: 176090 Cd Length: 75 Bit Score: 37.64 E-value: 1.11e-03
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| SAM_tumor-p63,p73 | cd09503 | SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 ... |
337-394 | 1.19e-03 | |||||
SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 transcriptional factors is a putative protein-protein interaction domain and lipid-binding domain. p63 and p73 are homologs to the tumor suppressor p53. They have a C-terminal SAM domain in their longest spliced alpha forms, while p53 doesn't have it. p63 or p73 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 and p73 play a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for p63/p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Pssm-ID: 188902 Cd Length: 65 Bit Score: 37.30 E-value: 1.19e-03
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| SAM_Samd7,11 | cd09579 | SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a ... |
329-390 | 1.27e-03 | |||||
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. Pssm-ID: 188978 Cd Length: 68 Bit Score: 37.43 E-value: 1.27e-03
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| SAM_Samd3 | cd09526 | SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ... |
329-366 | 1.32e-03 | |||||
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 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. Exact function of proteins belonging to this subfamily is unknown. Pssm-ID: 188925 Cd Length: 66 Bit Score: 37.34 E-value: 1.32e-03
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| SAM_VTS1_fungal | cd09556 | SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily ... |
335-399 | 1.33e-03 | |||||
SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily proteins is RNA binding domain located in the C-terminal region. SAM interacts with stem-loop structures of mRNA. Proteins of this subfamily participate in regulation of transcript stability and degradation, and also may be involved in vacuolar protein transport regulation. VTS1 protein of S.cerevisiae induces mRNA degradation via the major deadenylation-dependent mRNA decay pathway; VTS1 recruits CCR4/POP2/NOT deadenylase complex to target mRNA. The recruitment is the initial step resulting in poly(A) tail removal transcripts. Potentially SAM domain may be responsible not only for RNA binding but also for deadenylase binding. Pssm-ID: 188955 Cd Length: 69 Bit Score: 37.28 E-value: 1.33e-03
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| RING-Ubox_RNF37 | cd16660 | U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ... |
405-438 | 1.57e-03 | |||||
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain. Pssm-ID: 438322 Cd Length: 53 Bit Score: 36.52 E-value: 1.57e-03
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| SAM_PNT | pfam02198 | Sterile alpha motif (SAM)/Pointed domain; |
330-369 | 1.82e-03 | |||||
Sterile alpha motif (SAM)/Pointed domain; Pssm-ID: 460486 Cd Length: 83 Bit Score: 37.27 E-value: 1.82e-03
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| SAM_PNT | smart00251 | SAM / Pointed domain; A subfamily of the SAM domain |
330-369 | 2.59e-03 | |||||
SAM / Pointed domain; A subfamily of the SAM domain Pssm-ID: 128547 Cd Length: 82 Bit Score: 36.86 E-value: 2.59e-03
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| RING-Ubox_UBE4B | cd16658 | U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ... |
404-475 | 2.72e-03 | |||||
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus. Pssm-ID: 438320 Cd Length: 74 Bit Score: 36.49 E-value: 2.72e-03
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| SAM_ASZ1 | cd09521 | SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ... |
345-393 | 2.97e-03 | |||||
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. Pssm-ID: 188920 Cd Length: 64 Bit Score: 36.11 E-value: 2.97e-03
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| SAM_USH1G_HARP | cd09517 | SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ... |
341-398 | 3.29e-03 | |||||
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans. Pssm-ID: 188916 Cd Length: 66 Bit Score: 36.16 E-value: 3.29e-03
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| SAM_STIM-1,2-like | cd09504 | SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
332-391 | 5.42e-03 | |||||
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane. Pssm-ID: 188903 Cd Length: 74 Bit Score: 35.77 E-value: 5.42e-03
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| SAM_Samd9_Samd9L | cd09528 | SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ... |
330-377 | 5.86e-03 | |||||
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification. Pssm-ID: 188927 Cd Length: 64 Bit Score: 35.47 E-value: 5.86e-03
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| SAM_3 | pfam18016 | SAM domain (Sterile alpha motif); |
333-371 | 6.10e-03 | |||||
SAM domain (Sterile alpha motif); Pssm-ID: 436214 Cd Length: 65 Bit Score: 35.32 E-value: 6.10e-03
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