senescence-associated E3 ubiquitin ligase 1 [Arabidopsis thaliana]
Protein Classification
U-box domain-containing protein( domain architecture ID 11616232)
U-box domain-containing protein contains a modified RING finger and functions as an E3 ubiquitin 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 | |||||
| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
24-81 | 3.06e-23 | |||||
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: 93.01 E-value: 3.06e-23
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| PLN03200 super family | cl33659 | cellulose synthase-interactive protein; Provisional |
137-387 | 2.28e-05 | |||||
cellulose synthase-interactive protein; Provisional The actual alignment was detected with superfamily member PLN03200: Pssm-ID: 215629 [Multi-domain] Cd Length: 2102 Bit Score: 48.17 E-value: 2.28e-05
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| Name | Accession | Description | Interval | E-value | |||||
| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
24-81 | 3.06e-23 | |||||
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: 93.01 E-value: 3.06e-23
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
26-94 | 9.48e-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: 89.22 E-value: 9.48e-22
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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 ... |
23-98 | 6.32e-12 | |||||
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: 61.56 E-value: 6.32e-12
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| PLN03200 | PLN03200 | cellulose synthase-interactive protein; Provisional |
137-387 | 2.28e-05 | |||||
cellulose synthase-interactive protein; Provisional Pssm-ID: 215629 [Multi-domain] Cd Length: 2102 Bit Score: 48.17 E-value: 2.28e-05
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| SRP1 | COG5064 | Karyopherin (importin) alpha [Intracellular trafficking and secretion]; |
152-459 | 2.56e-05 | |||||
Karyopherin (importin) alpha [Intracellular trafficking and secretion]; Pssm-ID: 227396 [Multi-domain] Cd Length: 526 Bit Score: 47.58 E-value: 2.56e-05
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| Adaptin_N | pfam01602 | Adaptin N terminal region; This family consists of the N terminal region of various alpha, ... |
142-345 | 3.67e-03 | |||||
Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles. Pssm-ID: 396262 [Multi-domain] Cd Length: 523 Bit Score: 40.68 E-value: 3.67e-03
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| Name | Accession | Description | Interval | E-value | |||||
| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
24-81 | 3.06e-23 | |||||
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: 93.01 E-value: 3.06e-23
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
26-94 | 9.48e-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: 89.22 E-value: 9.48e-22
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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 ... |
25-81 | 3.47e-16 | |||||
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: 72.92 E-value: 3.47e-16
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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 ... |
27-76 | 1.60e-12 | |||||
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: 62.19 E-value: 1.60e-12
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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 ... |
23-98 | 6.32e-12 | |||||
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: 61.56 E-value: 6.32e-12
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| RING-Ubox_CHIP | cd16654 | U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ... |
25-98 | 8.62e-10 | |||||
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: 55.27 E-value: 8.62e-10
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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 ... |
27-93 | 2.41e-09 | |||||
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: 54.19 E-value: 2.41e-09
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| RING-Ubox_RNF37 | cd16660 | U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ... |
25-76 | 4.48e-09 | |||||
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: 52.70 E-value: 4.48e-09
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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 ... |
26-97 | 7.25e-09 | |||||
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: 52.85 E-value: 7.25e-09
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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 ... |
27-81 | 6.56e-08 | |||||
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: 49.79 E-value: 6.56e-08
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| PLN03200 | PLN03200 | cellulose synthase-interactive protein; Provisional |
137-387 | 2.28e-05 | |||||
cellulose synthase-interactive protein; Provisional Pssm-ID: 215629 [Multi-domain] Cd Length: 2102 Bit Score: 48.17 E-value: 2.28e-05
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| SRP1 | COG5064 | Karyopherin (importin) alpha [Intracellular trafficking and secretion]; |
152-459 | 2.56e-05 | |||||
Karyopherin (importin) alpha [Intracellular trafficking and secretion]; Pssm-ID: 227396 [Multi-domain] Cd Length: 526 Bit Score: 47.58 E-value: 2.56e-05
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| PLN03200 | PLN03200 | cellulose synthase-interactive protein; Provisional |
252-460 | 6.15e-05 | |||||
cellulose synthase-interactive protein; Provisional Pssm-ID: 215629 [Multi-domain] Cd Length: 2102 Bit Score: 47.02 E-value: 6.15e-05
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| SP-RING-like | cd16452 | SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ... |
27-69 | 1.96e-04 | |||||
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: 39.55 E-value: 1.96e-04
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| RING-HC_BAR | cd16497 | RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ... |
27-74 | 1.15e-03 | |||||
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability, as well as functioning in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This model corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s). Pssm-ID: 438160 [Multi-domain] Cd Length: 52 Bit Score: 37.49 E-value: 1.15e-03
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| RING-Ubox_PRP19 | cd16656 | U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ... |
27-80 | 1.62e-03 | |||||
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment. Pssm-ID: 438318 Cd Length: 54 Bit Score: 37.16 E-value: 1.62e-03
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| Adaptin_N | pfam01602 | Adaptin N terminal region; This family consists of the N terminal region of various alpha, ... |
142-345 | 3.67e-03 | |||||
Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles. Pssm-ID: 396262 [Multi-domain] Cd Length: 523 Bit Score: 40.68 E-value: 3.67e-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 ... |
25-98 | 4.25e-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: 4.25e-03
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| RING-HC_TRIM25_C-IV | cd16597 | RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ... |
28-70 | 4.61e-03 | |||||
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. Pssm-ID: 438259 [Multi-domain] Cd Length: 71 Bit Score: 36.52 E-value: 4.61e-03
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| RING-HC_TRIM39_C-IV | cd16601 | RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ... |
27-69 | 5.23e-03 | |||||
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are 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 region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. Pssm-ID: 438263 [Multi-domain] Cd Length: 44 Bit Score: 35.54 E-value: 5.23e-03
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| PLN03200 | PLN03200 | cellulose synthase-interactive protein; Provisional |
128-391 | 5.56e-03 | |||||
cellulose synthase-interactive protein; Provisional Pssm-ID: 215629 [Multi-domain] Cd Length: 2102 Bit Score: 40.47 E-value: 5.56e-03
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