RING/U-box superfamily protein [Arabidopsis thaliana]
Protein Classification
RING finger protein( domain architecture ID 106764)
RING finger protein may function as an E3 ubiquitin protein ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| SIP5-like super family | cl48856 | SNF1-interacting protein 5 and similar proteins; Sip5 plays a role in the regulation of SNF1 ... |
10-110 | 2.84e-29 | |||
SNF1-interacting protein 5 and similar proteins; Sip5 plays a role in the regulation of SNF1 kinase. It may negatively regulate SNF1 kinase under glucose-limiting conditions, by promoting the interaction of the REG1/GLC7 phosphatase complex with the kinase. It interacts directly with SNF1 kinase and the Reg1 component of the phosphatase complex. Sip5 also physically interacts with the N-terminus of Std1, an accessory subunit of the SNF1 kinase protein complex, in the absence of glucose. This prevents aggregation of Std1 and keeps it bound to SNF1, the catalytic subunit, keeping the SNF1 complex in an active state. Upon addition of glucose, Vhs1 kinase phosphorylates Sip5, inhibiting its binding to Std1. Once Sip5 is released, the N-terminal asparagine-rich part of Std1 aggregates, and Std1 exits the nucleus and localizes to cytoplasmic granules. SNF1 kinase is inactive in this state. The actual alignment was detected with superfamily member cd24139: Pssm-ID: 467940 Cd Length: 200 Bit Score: 112.76 E-value: 2.84e-29
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| Name | Accession | Description | Interval | E-value | |||
| SIP5-like | cd24139 | SNF1-interacting protein 5 and similar proteins; Sip5 plays a role in the regulation of SNF1 ... |
10-110 | 2.84e-29 | |||
SNF1-interacting protein 5 and similar proteins; Sip5 plays a role in the regulation of SNF1 kinase. It may negatively regulate SNF1 kinase under glucose-limiting conditions, by promoting the interaction of the REG1/GLC7 phosphatase complex with the kinase. It interacts directly with SNF1 kinase and the Reg1 component of the phosphatase complex. Sip5 also physically interacts with the N-terminus of Std1, an accessory subunit of the SNF1 kinase protein complex, in the absence of glucose. This prevents aggregation of Std1 and keeps it bound to SNF1, the catalytic subunit, keeping the SNF1 complex in an active state. Upon addition of glucose, Vhs1 kinase phosphorylates Sip5, inhibiting its binding to Std1. Once Sip5 is released, the N-terminal asparagine-rich part of Std1 aggregates, and Std1 exits the nucleus and localizes to cytoplasmic granules. SNF1 kinase is inactive in this state. Pssm-ID: 467940 Cd Length: 200 Bit Score: 112.76 E-value: 2.84e-29
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| Name | Accession | Description | Interval | E-value | |||
| SIP5-like | cd24139 | SNF1-interacting protein 5 and similar proteins; Sip5 plays a role in the regulation of SNF1 ... |
10-110 | 2.84e-29 | |||
SNF1-interacting protein 5 and similar proteins; Sip5 plays a role in the regulation of SNF1 kinase. It may negatively regulate SNF1 kinase under glucose-limiting conditions, by promoting the interaction of the REG1/GLC7 phosphatase complex with the kinase. It interacts directly with SNF1 kinase and the Reg1 component of the phosphatase complex. Sip5 also physically interacts with the N-terminus of Std1, an accessory subunit of the SNF1 kinase protein complex, in the absence of glucose. This prevents aggregation of Std1 and keeps it bound to SNF1, the catalytic subunit, keeping the SNF1 complex in an active state. Upon addition of glucose, Vhs1 kinase phosphorylates Sip5, inhibiting its binding to Std1. Once Sip5 is released, the N-terminal asparagine-rich part of Std1 aggregates, and Std1 exits the nucleus and localizes to cytoplasmic granules. SNF1 kinase is inactive in this state. Pssm-ID: 467940 Cd Length: 200 Bit Score: 112.76 E-value: 2.84e-29
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| RING-HC_RNF152 | cd16548 | RING finger, HC subclass, found in RING finger protein 152 (RNF152) and similar proteins; ... |
58-102 | 2.61e-03 | |||
RING finger, HC subclass, found in RING finger protein 152 (RNF152) and similar proteins; RNF152 is a lysosome-anchored E3 ubiquitin-protein ligase involved in apoptosis. It is polyubiquitinated through K48 linkage. It negatively regulates the activation of the mTORC1 pathway by targeting RagA GTPase for K63-linked ubiquitination. It interacts with and ubiquitinates RagA in an amino-acid-sensitive manner. The ubiquitination of RagA recruits its inhibitor GATOR1, a GAP complex for Rag GTPases, to the Rag complex, thereby inactivating mTORC1 signaling. RNF152 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal transmembrane domain, both of which are responsible for its E3 ligase activity. Pssm-ID: 438210 [Multi-domain] Cd Length: 46 Bit Score: 35.74 E-value: 2.61e-03
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| RING-HC_BRCA1 | cd16498 | RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ... |
58-104 | 3.81e-03 | |||
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. Pssm-ID: 438161 [Multi-domain] Cd Length: 94 Bit Score: 36.51 E-value: 3.81e-03
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| RING-HC_RNF183-like | cd16556 | RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar ... |
58-104 | 3.84e-03 | |||
RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar proteins; RNF183 is an E3 ubiquitin-protein ligase that is upregulated during intestinal inflammation and is negatively regulated by miR-7. It promotes intestinal inflammation by increasing the ubiquitination and degradation of inhibitor of kappa B, thereby resulting in secondary activation of the Nuclear factor-kappaB (NF-kB) pathway. The interaction between RNF183-mediated ubiquitination and miRNA may be an important novel epigenetic mechanism in the pathogenesis of inflammatory bowel disease (IBD). The biological function of RNF223 and RNF225 remains unclear. Members of this family contain an N-terminal C3HC4-type RING-HC finger. Pssm-ID: 438218 [Multi-domain] Cd Length: 57 Bit Score: 35.42 E-value: 3.84e-03
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| RING-HC_malin | cd16516 | RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in ... |
58-103 | 7.15e-03 | |||
RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in French), also known as NHL repeat-containing protein 1 (NHLRC1), or EPM2B, is a nuclear E3 ubiquitin-protein ligase that ubiquitinates and promotes the degradation of laforin (EPM2A encoding protein phosphatase). Malin and laforin operate as a functional complex that play key roles in regulating cellular functions such as glycogen metabolism, unfolded cellular stress response, and proteolytic processes. They act as pro-survival factors that negatively regulate the Hipk2-p53 cell death pathway. They also negatively regulate cellular glucose uptake by preventing plasma membrane targeting of glucose transporters. Moreover, they degrade polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase. Furthermore, they, together with Hsp70, form a new functional complex that suppress the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Defects in either malin or laforin may cause Lafora disease (LD), a fatal form of teenage-onset autosomal recessive progressive myoclonus epilepsy. In addition, malin may have function, independent of laforin, in lysosomal biogenesis and/or lysosomal glycogen disposal. Malin contains six NHL-repeat protein-protein interaction domains and a C3HC4-type RING-HC finger. Pssm-ID: 438179 [Multi-domain] Cd Length: 52 Bit Score: 34.41 E-value: 7.15e-03
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| RING-HC_TRIM32_C-VII | cd16587 | RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ... |
58-101 | 8.63e-03 | |||
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs. Pssm-ID: 438249 [Multi-domain] Cd Length: 51 Bit Score: 34.30 E-value: 8.63e-03
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