SPRY domain-containing SOCS box protein 3 isoform a [Mus musculus]
Protein Classification
SPRY domain-containing protein; PRY/SPRY domain-containing protein( domain architecture ID 10191362)
SPRY (SPla and the RYanodine receptor) domain-containing protein similar to yeast SSH4 (suppressor of SHR3 null mutation protein 4); the SPRY domain is a protein interaction module found in proteins implicated in important biological pathways, including those that regulate innate and adaptive immunity| PRY/SPRY domain-containing family protein, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| SPRY_SOCS3 | cd12876 | SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ... |
104-286 | 8.18e-121 | ||||
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: 346.07 E-value: 8.18e-121
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| SOCS super family | cl02533 | SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ... |
276-312 | 1.41e-07 | ||||
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions. The actual alignment was detected with superfamily member cd03717: Pssm-ID: 470605 Cd Length: 39 Bit Score: 47.21 E-value: 1.41e-07
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| Name | Accession | Description | Interval | E-value | ||||
| SPRY_SOCS3 | cd12876 | SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ... |
104-286 | 8.18e-121 | ||||
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: 346.07 E-value: 8.18e-121
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
147-257 | 1.07e-12 | ||||
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: 64.24 E-value: 1.07e-12
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
149-265 | 1.07e-12 | ||||
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: 64.29 E-value: 1.07e-12
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| SOCS_SOCS_like | cd03717 | SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ... |
276-312 | 1.41e-07 | ||||
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. These intracellular proteins regulate the responses of immune cells to cytokines. Identified as negative regulators of the cytokine-JAK-STAT pathway, they seem to play a role in many immunological and pathological processes. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. Related SOCS boxes are also present in Rab40-like proteins and insect proteins of unknown function that also contain a NEUZ (domain in neuralized proteins) domain. Pssm-ID: 239687 Cd Length: 39 Bit Score: 47.21 E-value: 1.41e-07
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| SOCS_box | smart00969 | The SOCS box acts as a bridge between specific substrate- binding domains and more generic ... |
276-312 | 6.29e-04 | ||||
The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases; Pssm-ID: 198037 Cd Length: 34 Bit Score: 36.62 E-value: 6.29e-04
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| SOCS_box | pfam07525 | SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ... |
276-310 | 3.67e-03 | ||||
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases. Pssm-ID: 462192 Cd Length: 39 Bit Score: 34.83 E-value: 3.67e-03
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| Name | Accession | Description | Interval | E-value | ||||
| SPRY_SOCS3 | cd12876 | SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ... |
104-286 | 8.18e-121 | ||||
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: 346.07 E-value: 8.18e-121
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| SPRY | cd11709 | SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ... |
147-268 | 1.04e-21 | ||||
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: 89.03 E-value: 1.04e-21
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| SPRY_SOCS_Fbox | cd12875 | SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ... |
135-268 | 2.57e-18 | ||||
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: 81.35 E-value: 2.57e-18
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
147-257 | 1.07e-12 | ||||
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: 64.24 E-value: 1.07e-12
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
149-265 | 1.07e-12 | ||||
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: 64.29 E-value: 1.07e-12
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| SPRY_Fbox | cd12907 | SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, ... |
135-258 | 2.17e-11 | ||||
SPRY domain in the F-box family Fbxo45; Fbxo45 is a novel synaptic E3 and ubiquitin ligase, related to the suppressor of cytokine signaling (SOCS) proteins and located N-terminal to a SPRY (SPla and the ryanodine receptor) domain. Fbxo45 induces 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. F-box motifs are found in proteins that function as the substrate recognition component of SCF E3 complexes. Pssm-ID: 293964 Cd Length: 175 Bit Score: 62.02 E-value: 2.17e-11
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| SPRY_SOCS1-2-4 | cd12906 | SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4); ... |
135-256 | 4.69e-10 | ||||
SPRY domain in the suppressor of cytokine signaling 1, 2, 4 families (SOCS1, SOCS2, SOCS4); 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 only SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4). They are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation, thus contributing to protection against the cytotoxic effect of iNOS in activated macrophages. It has been shown that SPSB1 and SPSB4 induce the degradation of iNOS more strongly than SPSB2. The Drosophila melanogaster SPSB1 homolog, GUSTAVUS, interacts with the DEAD box RNA helicase Vasa. 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: 293963 Cd Length: 174 Bit Score: 58.02 E-value: 4.69e-10
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| SPRY_RanBP_like | cd12885 | SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ... |
151-256 | 1.40e-09 | ||||
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: 55.75 E-value: 1.40e-09
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| SPRY_like | cd12886 | SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ... |
147-257 | 5.24e-09 | ||||
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: 54.05 E-value: 5.24e-09
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| SPRY_DDX1 | cd12873 | SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ... |
133-257 | 1.82e-08 | ||||
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: 52.96 E-value: 1.82e-08
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| SPRY_RanBP9_10 | cd12909 | SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ... |
147-256 | 2.37e-08 | ||||
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: 52.52 E-value: 2.37e-08
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| SPRYD7 | cd12880 | SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also ... |
133-256 | 9.60e-08 | ||||
SPRY domain-containing protein 7; This family contains SPRY domain-containing protein 7 (also known as SPRY domain-containing protein 7 or CLL deletion region gene 6 protein homolog or CLLD6 or chronic lymphocytic leukemia deletion region gene 6 protein homolog). In humans, CLLD6 is highly expressed in heart, skeletal muscle, and testis as well as cancer cell lines. It also has cross-species conservation, suggesting that it is likely to carry out important cellular processes. Pssm-ID: 293938 Cd Length: 160 Bit Score: 51.05 E-value: 9.60e-08
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| SOCS_SOCS_like | cd03717 | SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ... |
276-312 | 1.41e-07 | ||||
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. These intracellular proteins regulate the responses of immune cells to cytokines. Identified as negative regulators of the cytokine-JAK-STAT pathway, they seem to play a role in many immunological and pathological processes. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. Related SOCS boxes are also present in Rab40-like proteins and insect proteins of unknown function that also contain a NEUZ (domain in neuralized proteins) domain. Pssm-ID: 239687 Cd Length: 39 Bit Score: 47.21 E-value: 1.41e-07
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| SPRY_PRY_TRIM67_9 | cd12889 | PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ... |
107-256 | 3.38e-07 | ||||
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. Pssm-ID: 293947 Cd Length: 172 Bit Score: 49.55 E-value: 3.38e-07
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| SPRY_PRY_C-II | cd13734 | PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ... |
118-234 | 5.85e-07 | ||||
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as MID2) and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. Their coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. Pssm-ID: 293969 [Multi-domain] Cd Length: 166 Bit Score: 48.82 E-value: 5.85e-07
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| SPRY_PRY_TRIM65 | cd12896 | PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ... |
118-234 | 1.00e-06 | ||||
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM65 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not been characterized. Pssm-ID: 293953 [Multi-domain] Cd Length: 182 Bit Score: 48.60 E-value: 1.00e-06
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| SOCS | cd03587 | SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ... |
276-312 | 3.65e-06 | ||||
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions. Pssm-ID: 239641 Cd Length: 41 Bit Score: 43.23 E-value: 3.65e-06
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| SPRY_PRY_C-I_2 | cd12891 | PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ... |
109-234 | 5.17e-06 | ||||
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, TRIM16-like, TRIM25-like, TRIM47-like, TRIM65 and RNF135, and stonustoxin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM14, TRIM16 and TRIM25, TRIM47 as well as RING finger protein RNF135 and stonustoxin, a secreted poisonous protein of the stonefish Synanceja horrida. TRIM16 (also known as estrogen-responsive B box protein or EBBP) has E3 ubiquitin ligase activity. It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function. TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100), is highly expressed in kidney tubular cells, but low expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. RNF135 ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Stonustoxin (STNX) is a hypotensive and lethal protein factor that also possesses other biological activities such as species-specific hemolysis (due to its ability to form pores in the cell membrane) and platelet aggregation, edema-induction, and endothelium-dependent vasorelaxation (mediated by the nitric oxide pathway and activation of potassium channels). The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. Pssm-ID: 293949 [Multi-domain] Cd Length: 167 Bit Score: 46.09 E-value: 5.17e-06
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| SPRY_Ash2 | cd12872 | SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ... |
147-256 | 8.09e-06 | ||||
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: 45.20 E-value: 8.09e-06
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| SPRY_hnRNP | cd12884 | SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ... |
182-258 | 1.43e-05 | ||||
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: 44.89 E-value: 1.43e-05
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| SPRY_HERC1 | cd12881 | SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ... |
150-258 | 1.44e-04 | ||||
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: 41.95 E-value: 1.44e-04
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| SPRY_PRY_RNF135 | cd12902 | PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ... |
141-234 | 3.41e-04 | ||||
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of the RING finger protein RNF135 (also known as Riplet/RNF135), which ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Normally, RIG-I is activated by TRIM25 in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. However, RNF135, consisting of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs and showing sequence similarity to TRIM25, acts as an alternative factor that promotes RIG-I activation independent of TRIM25. Pssm-ID: 293959 [Multi-domain] Cd Length: 168 Bit Score: 40.96 E-value: 3.41e-04
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| SOCS_box | smart00969 | The SOCS box acts as a bridge between specific substrate- binding domains and more generic ... |
276-312 | 6.29e-04 | ||||
The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases; Pssm-ID: 198037 Cd Length: 34 Bit Score: 36.62 E-value: 6.29e-04
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| SOCS_box | pfam07525 | SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ... |
276-310 | 3.67e-03 | ||||
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases. Pssm-ID: 462192 Cd Length: 39 Bit Score: 34.83 E-value: 3.67e-03
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| SOCS | smart00253 | suppressors of cytokine signalling; suppressors of cytokine signalling |
276-309 | 6.67e-03 | ||||
suppressors of cytokine signalling; suppressors of cytokine signalling Pssm-ID: 128549 Cd Length: 43 Bit Score: 34.19 E-value: 6.67e-03
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