![](files/infoQ.gif)
ran-binding protein 10 isoform 3 [Homo sapiens]
List of domain hits
![](files/help.png)
Name | Accession | Description | Interval | E-value | |||
SPRY super family | cl02614 | SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ... |
77-163 | 2.50e-47 | |||
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. The actual alignment was detected with superfamily member cd12909: Pssm-ID: 470632 Cd Length: 144 Bit Score: 162.31 E-value: 2.50e-47
|
|||||||
CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
481-578 | 5.94e-16 | |||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) : Pssm-ID: 214806 Cd Length: 99 Bit Score: 73.48 E-value: 5.94e-16
|
|||||||
CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
235-289 | 1.44e-13 | |||
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: 67.98 E-value: 1.44e-13
|
|||||||
LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
201-228 | 2.55e-03 | |||
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: 35.87 E-value: 2.55e-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 ... |
77-163 | 2.50e-47 | |||
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: 162.31 E-value: 2.50e-47
|
|||||||
CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
481-578 | 5.94e-16 | |||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) Pssm-ID: 214806 Cd Length: 99 Bit Score: 73.48 E-value: 5.94e-16
|
|||||||
CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
235-289 | 1.44e-13 | |||
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: 67.98 E-value: 1.44e-13
|
|||||||
CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
235-291 | 2.31e-13 | |||
C-terminal to LisH motif; Alpha-helical motif of unknown function. Pssm-ID: 128914 Cd Length: 58 Bit Score: 64.90 E-value: 2.31e-13
|
|||||||
CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
502-573 | 4.65e-12 | |||
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: 63.74 E-value: 4.65e-12
|
|||||||
LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
201-228 | 2.55e-03 | |||
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: 35.87 E-value: 2.55e-03
|
|||||||
LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
201-223 | 3.40e-03 | |||
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: 34.99 E-value: 3.40e-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 ... |
77-163 | 2.50e-47 | |||
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: 162.31 E-value: 2.50e-47
|
|||||||
CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
481-578 | 5.94e-16 | |||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) Pssm-ID: 214806 Cd Length: 99 Bit Score: 73.48 E-value: 5.94e-16
|
|||||||
SPRY_RanBP_like | cd12885 | SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ... |
88-162 | 6.73e-16 | |||
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: 74.62 E-value: 6.73e-16
|
|||||||
CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
235-289 | 1.44e-13 | |||
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: 67.98 E-value: 1.44e-13
|
|||||||
CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
235-291 | 2.31e-13 | |||
C-terminal to LisH motif; Alpha-helical motif of unknown function. Pssm-ID: 128914 Cd Length: 58 Bit Score: 64.90 E-value: 2.31e-13
|
|||||||
CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
502-573 | 4.65e-12 | |||
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: 63.74 E-value: 4.65e-12
|
|||||||
SPRYD3 | cd12908 | SPRY domain-containing protein 3; This family contains SPRY domain-containing protein 3 ... |
80-134 | 7.99e-05 | |||
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: 43.44 E-value: 7.99e-05
|
|||||||
LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
201-228 | 2.55e-03 | |||
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: 35.87 E-value: 2.55e-03
|
|||||||
LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
201-223 | 3.40e-03 | |||
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: 34.99 E-value: 3.40e-03
|
|||||||
Blast search parameters | ||||
|