putative Ran GTPase binding protein [Schizosaccharomyces pombe]
Protein Classification
topless-related protein; LisH domain-containing protein( domain architecture ID 10191541)
topless-related protein may act as transcription corepressor| LIS1 homology (LisH) domain-containing protein similar to Arabidopsis thaliana protein TONNEAU 1a/1b involved in the control of the dynamic organization of the cortical cytoskeleton
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| SPRY_RanBP9_10 | cd12909 | SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ... |
94-230 | 3.09e-78 | |||
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells. : Pssm-ID: 293966 Cd Length: 144 Bit Score: 240.50 E-value: 3.09e-78
|
|||||||
| CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
373-467 | 1.18e-14 | |||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) : Pssm-ID: 214806 Cd Length: 99 Bit Score: 69.63 E-value: 1.18e-14
|
|||||||
| CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
300-353 | 2.31e-08 | |||
C-terminal to LisH motif; Alpha-helical motif of unknown function. : Pssm-ID: 128914 Cd Length: 58 Bit Score: 50.26 E-value: 2.31e-08
|
|||||||
| LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
268-291 | 1.85e-04 | |||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. : Pssm-ID: 462501 Cd Length: 25 Bit Score: 38.45 E-value: 1.85e-04
|
|||||||
| Name | Accession | Description | Interval | E-value | ||||
| SPRY_RanBP9_10 | cd12909 | SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ... |
94-230 | 3.09e-78 | ||||
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells. Pssm-ID: 293966 Cd Length: 144 Bit Score: 240.50 E-value: 3.09e-78
|
||||||||
| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
113-231 | 1.04e-32 | ||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 120.53 E-value: 1.04e-32
|
||||||||
| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
113-231 | 8.75e-28 | ||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 107.00 E-value: 8.75e-28
|
||||||||
| CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
373-467 | 1.18e-14 | ||||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) Pssm-ID: 214806 Cd Length: 99 Bit Score: 69.63 E-value: 1.18e-14
|
||||||||
| CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
300-353 | 2.31e-08 | ||||
C-terminal to LisH motif; Alpha-helical motif of unknown function. Pssm-ID: 128914 Cd Length: 58 Bit Score: 50.26 E-value: 2.31e-08
|
||||||||
| LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
268-291 | 1.85e-04 | ||||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. Pssm-ID: 462501 Cd Length: 25 Bit Score: 38.45 E-value: 1.85e-04
|
||||||||
| LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
264-291 | 5.84e-04 | ||||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. Pssm-ID: 128913 Cd Length: 34 Bit Score: 37.41 E-value: 5.84e-04
|
||||||||
| CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
301-462 | 2.03e-03 | ||||
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif. Pssm-ID: 402305 [Multi-domain] Cd Length: 143 Bit Score: 38.71 E-value: 2.03e-03
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| SPRY_RanBP9_10 | cd12909 | SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ... |
94-230 | 3.09e-78 | ||||
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells. Pssm-ID: 293966 Cd Length: 144 Bit Score: 240.50 E-value: 3.09e-78
|
||||||||
| SPRY_RanBP_like | cd12885 | SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ... |
99-229 | 3.93e-57 | ||||
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate. Pssm-ID: 293943 Cd Length: 132 Bit Score: 185.56 E-value: 3.93e-57
|
||||||||
| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
113-231 | 1.04e-32 | ||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 120.53 E-value: 1.04e-32
|
||||||||
| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
113-231 | 8.75e-28 | ||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 107.00 E-value: 8.75e-28
|
||||||||
| SPRYD3 | cd12908 | SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ... |
108-228 | 5.17e-23 | ||||
SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 (SPRYD3). In humans, it is highly expressed in most tissues, including brain, kidney, heart, intestine, skeletal muscle, and testis. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes. Pssm-ID: 293965 Cd Length: 171 Bit Score: 95.44 E-value: 5.17e-23
|
||||||||
| SPRY_SSH4_like | cd12910 | SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ... |
100-230 | 1.89e-21 | ||||
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor of SHR3 null mutation protein 4) and similar proteins. SSH4 is a component of the endosome-vacuole trafficking pathway that regulates nutrient transport and may be involved in processes determining whether plasma membrane proteins are degraded or routed to the plasma membrane. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. In yeast, SSH4 and the homologous protein EAR1 (endosomal adapter of RSP5) recruit Rsp5p, an essential ubiquitin ligase of the Nedd4 family, and assist it in its function at multivesicular bodies by directing the ubiquitylation of specific cargoes. Pssm-ID: 293967 Cd Length: 192 Bit Score: 91.65 E-value: 1.89e-21
|
||||||||
| SPRY | cd11709 | SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ... |
113-227 | 3.40e-20 | ||||
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome. Pssm-ID: 293931 Cd Length: 118 Bit Score: 85.95 E-value: 3.40e-20
|
||||||||
| SPRY_DDX1 | cd12873 | SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ... |
114-232 | 9.79e-20 | ||||
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay. Pssm-ID: 293933 Cd Length: 155 Bit Score: 85.70 E-value: 9.79e-20
|
||||||||
| SPRY_RNF123 | cd12882 | SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ... |
107-229 | 7.82e-19 | ||||
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1). Pssm-ID: 293940 Cd Length: 128 Bit Score: 82.37 E-value: 7.82e-19
|
||||||||
| SPRY_Ash2 | cd12872 | SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ... |
100-233 | 6.20e-18 | ||||
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis. Pssm-ID: 293932 Cd Length: 150 Bit Score: 80.64 E-value: 6.20e-18
|
||||||||
| SPRY_hnRNP | cd12884 | SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ... |
99-232 | 1.92e-15 | ||||
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Pssm-ID: 293942 Cd Length: 177 Bit Score: 74.16 E-value: 1.92e-15
|
||||||||
| CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
373-467 | 1.18e-14 | ||||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) Pssm-ID: 214806 Cd Length: 99 Bit Score: 69.63 E-value: 1.18e-14
|
||||||||
| SPRY_SOCS3 | cd12876 | SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ... |
66-215 | 9.29e-14 | ||||
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression. Pssm-ID: 293936 Cd Length: 185 Bit Score: 69.50 E-value: 9.29e-14
|
||||||||
| SPRY2_RyR | cd12878 | SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ... |
114-229 | 4.75e-12 | ||||
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1 Pssm-ID: 240458 Cd Length: 133 Bit Score: 63.09 E-value: 4.75e-12
|
||||||||
| SPRY_like | cd12886 | SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ... |
114-229 | 1.75e-08 | ||||
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). Pssm-ID: 293944 Cd Length: 129 Bit Score: 52.89 E-value: 1.75e-08
|
||||||||
| CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
300-353 | 2.31e-08 | ||||
C-terminal to LisH motif; Alpha-helical motif of unknown function. Pssm-ID: 128914 Cd Length: 58 Bit Score: 50.26 E-value: 2.31e-08
|
||||||||
| SPRY_HECT_like | cd13735 | SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ... |
99-229 | 1.62e-07 | ||||
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at the N-terminus of the HECT (homologous to the E6AP carboxyl terminus) protein, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). HECT E3 binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. It has a prominent role in protein trafficking and immune response, and is involved in crucial signaling pathways implicated in tumorigenesis. Pssm-ID: 293970 [Multi-domain] Cd Length: 150 Bit Score: 50.60 E-value: 1.62e-07
|
||||||||
| SPRY_HERC1 | cd12881 | SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ... |
122-216 | 7.55e-07 | ||||
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined. Pssm-ID: 293939 Cd Length: 162 Bit Score: 48.88 E-value: 7.55e-07
|
||||||||
| SPRY_SOCS_Fbox | cd12875 | SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ... |
66-215 | 9.69e-07 | ||||
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis. Pssm-ID: 293935 Cd Length: 169 Bit Score: 48.61 E-value: 9.69e-07
|
||||||||
| LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
268-291 | 1.85e-04 | ||||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. Pssm-ID: 462501 Cd Length: 25 Bit Score: 38.45 E-value: 1.85e-04
|
||||||||
| LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
264-291 | 5.84e-04 | ||||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. Pssm-ID: 128913 Cd Length: 34 Bit Score: 37.41 E-value: 5.84e-04
|
||||||||
| CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
301-462 | 2.03e-03 | ||||
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif. Pssm-ID: 402305 [Multi-domain] Cd Length: 143 Bit Score: 38.71 E-value: 2.03e-03
|
||||||||
| SPRY_RING | cd12883 | SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ... |
113-229 | 4.31e-03 | ||||
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development. Pssm-ID: 293941 Cd Length: 121 Bit Score: 37.33 E-value: 4.31e-03
|
||||||||
| Blast search parameters | ||||
|
