DCN1-like protein 2a [Danio rerio]
DCN1-like protein 2( domain architecture ID 10199025)
DCN1-like protein 2 (DCNL2) contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and plays an essential role in the regulation of SCF (SKP1-CUL1-F-box protein)-type complexes activity
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Cullin_binding | pfam03556 | Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ... |
136-246 | 3.98e-52 | |||
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices. : Pssm-ID: 460971 Cd Length: 117 Bit Score: 165.45 E-value: 3.98e-52
|
|||||||
UBA_DCNL2 | cd14412 | UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in ... |
2-48 | 6.17e-30 | |||
UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1, a protein that plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. At this point, DCNL2 may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that is responsible for the binding to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. : Pssm-ID: 270595 Cd Length: 47 Bit Score: 106.32 E-value: 6.17e-30
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Cullin_binding | pfam03556 | Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ... |
136-246 | 3.98e-52 | |||
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices. Pssm-ID: 460971 Cd Length: 117 Bit Score: 165.45 E-value: 3.98e-52
|
|||||||
UBA_DCNL2 | cd14412 | UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in ... |
2-48 | 6.17e-30 | |||
UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1, a protein that plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. At this point, DCNL2 may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that is responsible for the binding to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Pssm-ID: 270595 Cd Length: 47 Bit Score: 106.32 E-value: 6.17e-30
|
|||||||
UBA_4 | pfam14555 | UBA-like domain; |
9-49 | 1.95e-08 | |||
UBA-like domain; Pssm-ID: 464207 Cd Length: 43 Bit Score: 49.37 E-value: 1.95e-08
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Cullin_binding | pfam03556 | Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ... |
136-246 | 3.98e-52 | |||
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices. Pssm-ID: 460971 Cd Length: 117 Bit Score: 165.45 E-value: 3.98e-52
|
|||||||
UBA_DCNL2 | cd14412 | UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in ... |
2-48 | 6.17e-30 | |||
UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1, a protein that plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. At this point, DCNL2 may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that is responsible for the binding to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Pssm-ID: 270595 Cd Length: 47 Bit Score: 106.32 E-value: 6.17e-30
|
|||||||
UBA_DCNL1 | cd14411 | UBA-like domain found in DCN1-like protein 1 (DCNL1) and similar proteins; DCNL1 (defective in ... |
1-51 | 1.16e-22 | |||
UBA-like domain found in DCN1-like protein 1 (DCNL1) and similar proteins; DCNL1 (defective in cullin neddylation protein 1-like protein 1), also called DCUN1 domain-containing protein 1, is encoded by squamous cell carcinoma-related oncogene SCCRO (DCUN1D1). It interacts with known cullin isoforms as well as ROC1, Ubc12 and CAND1, the components of the neddylation pathway. It plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. DCNL1 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that binds to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Pssm-ID: 270594 Cd Length: 51 Bit Score: 87.52 E-value: 1.16e-22
|
|||||||
UBA_DCNL | cd14350 | UBA-like domain found in DCN1-like protein DCNL1, DCNL2 and similar proteins; DCNL1 (defective ... |
7-48 | 8.33e-21 | |||
UBA-like domain found in DCN1-like protein DCNL1, DCNL2 and similar proteins; DCNL1 (defective in cullin neddylation protein 1-like protein 1), also called DCUN1 domain-containing protein 1, is encoded by squamous cell carcinoma-related oncogene SCCRO (DCUN1D1). It interacts with known cullin isoforms as well as ROC1, Ubc12 and CAND1, the components of the neddylation pathway. It plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. DCNL1 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that binds to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1 and may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal UBA-like domain and a C-terminal cullin binding domain. Pssm-ID: 270535 Cd Length: 42 Bit Score: 82.30 E-value: 8.33e-21
|
|||||||
UBA_4 | pfam14555 | UBA-like domain; |
9-49 | 1.95e-08 | |||
UBA-like domain; Pssm-ID: 464207 Cd Length: 43 Bit Score: 49.37 E-value: 1.95e-08
|
|||||||
UBA_TAP-C_like | cd14273 | UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; ... |
15-45 | 5.97e-06 | |||
UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; This family includes nuclear RNA export factors (NXF1/NXF2), FAS-associated factors (FAF1/2), tyrosyl-DNA phosphodiesterase 2 (TDP2), OTU domain-containing proteins (OTU7A/OTU7B), NSFL1 cofactor p47, defective in cullin neddylation protein 1 (DCN1)-like protein (DCNL1/DCNL2), yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins. NXF proteins can stimulate nuclear export of mRNAs and facilitate the export of unspliced viral mRNA containing the constitutive transport element. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. Its biological function remains unclear. TDP2 is a 5'-Tyr-DNA phosphodiesterase required for the efficient repair of topoisomerase II-induced DNA double strand breaks. OTU7A and OTU7B are zinc finger proteins that function as deubiquitinating enzymes. p47 is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. DCNL1 plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. The biological function of DCNL2 remains unclear. Yeast DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity. Pssm-ID: 270459 Cd Length: 31 Bit Score: 42.00 E-value: 5.97e-06
|
|||||||
UBA_DCN1 | cd14352 | UBA-like domain found in yeast defective in cullin neddylation protein 1 (DCN1) and similar ... |
12-45 | 1.81e-04 | |||
UBA-like domain found in yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins; DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity. It contains an N-terminal ubiquitin-associated (UBA)-like domain and a unique C-terminal PONY domain that is essential for the neddylation function of DCN1. Pssm-ID: 270537 Cd Length: 36 Bit Score: 38.03 E-value: 1.81e-04
|
|||||||
UBA_p47 | cd14348 | UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX ... |
9-48 | 4.54e-04 | |||
UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX domain-containing protein 2C, is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. p47, together with p97, forms the p97-p47 complex that plays an important role in regulation of membrane fusion events. p47 contains an N-terminal ubiquitin-associated (UBA)-like domain, a central SEP (named after shp1, eyc and p47) domain, and a ubiquitin-like (UBX) domain. UBA-like domain is responsible for forming a highly stable complex with ubiquitin. SEP domain and UBX domain may involve in p47 trimerization or forms a stable complex with the p97 N-terminal domain. Pssm-ID: 270533 Cd Length: 40 Bit Score: 37.13 E-value: 4.54e-04
|
|||||||
Blast search parameters | ||||
|