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E3 ubiquitin-protein ligase COP1 isoform X19 [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||||
PLN00181 super family | cl31831 | protein SPA1-RELATED; Provisional |
210-563 | 9.81e-104 | ||||||
protein SPA1-RELATED; Provisional The actual alignment was detected with superfamily member PLN00181: Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 332.05 E-value: 9.81e-104
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RING_Ubox super family | cl17238 | RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ... |
132-155 | 4.39e-12 | ||||||
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. 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. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates. The actual alignment was detected with superfamily member cd16504: Pssm-ID: 473075 [Multi-domain] Cd Length: 47 Bit Score: 60.72 E-value: 4.39e-12
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Name | Accession | Description | Interval | E-value | ||||||
PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
210-563 | 9.81e-104 | ||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 332.05 E-value: 9.81e-104
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
277-523 | 7.56e-37 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 139.01 E-value: 7.56e-37
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
264-542 | 3.88e-33 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 131.57 E-value: 3.88e-33
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RING-HC_COP1 | cd16504 | RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ... |
132-155 | 4.39e-12 | ||||||
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger. Pssm-ID: 438167 [Multi-domain] Cd Length: 47 Bit Score: 60.72 E-value: 4.39e-12
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
358-398 | 1.55e-04 | ||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.22 E-value: 1.55e-04
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zf-C3HC4_2 | pfam13923 | Zinc finger, C3HC4 type (RING finger); |
135-155 | 2.69e-04 | ||||||
Zinc finger, C3HC4 type (RING finger); Pssm-ID: 404756 [Multi-domain] Cd Length: 40 Bit Score: 38.57 E-value: 2.69e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
359-398 | 1.03e-03 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 1.03e-03
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Name | Accession | Description | Interval | E-value | ||||||
PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
210-563 | 9.81e-104 | ||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 332.05 E-value: 9.81e-104
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
277-523 | 7.56e-37 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 139.01 E-value: 7.56e-37
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
264-542 | 3.88e-33 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 131.57 E-value: 3.88e-33
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
262-523 | 1.72e-31 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.56 E-value: 1.72e-31
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
264-523 | 8.86e-31 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 122.06 E-value: 8.86e-31
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
341-542 | 1.24e-26 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 112.31 E-value: 1.24e-26
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
277-483 | 8.75e-26 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 110.00 E-value: 8.75e-26
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
280-482 | 1.46e-22 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 98.18 E-value: 1.46e-22
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
341-523 | 6.98e-22 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.44 E-value: 6.98e-22
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
362-523 | 1.72e-21 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 95.09 E-value: 1.72e-21
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
277-400 | 2.50e-12 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.17 E-value: 2.50e-12
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RING-HC_COP1 | cd16504 | RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ... |
132-155 | 4.39e-12 | ||||||
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger. Pssm-ID: 438167 [Multi-domain] Cd Length: 47 Bit Score: 60.72 E-value: 4.39e-12
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
381-523 | 6.48e-06 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 48.75 E-value: 6.48e-06
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
358-398 | 1.55e-04 | ||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.22 E-value: 1.55e-04
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zf-C3HC4_2 | pfam13923 | Zinc finger, C3HC4 type (RING finger); |
135-155 | 2.69e-04 | ||||||
Zinc finger, C3HC4 type (RING finger); Pssm-ID: 404756 [Multi-domain] Cd Length: 40 Bit Score: 38.57 E-value: 2.69e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
359-398 | 1.03e-03 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 1.03e-03
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
444-482 | 1.22e-03 | ||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 36.91 E-value: 1.22e-03
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RING-HC_BRCA1 | cd16498 | RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ... |
136-155 | 1.90e-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: 38.05 E-value: 1.90e-03
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RING-HC_TRIM40-C-V | cd16583 | RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ... |
129-155 | 2.79e-03 | ||||||
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. Pssm-ID: 438245 [Multi-domain] Cd Length: 63 Bit Score: 36.35 E-value: 2.79e-03
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RING-HC | cd16449 | HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ... |
134-155 | 5.01e-03 | ||||||
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates. Pssm-ID: 438113 [Multi-domain] Cd Length: 41 Bit Score: 35.15 E-value: 5.01e-03
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RING-HC_ScPSH1-like | cd16568 | RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ... |
135-155 | 8.85e-03 | ||||||
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain. Pssm-ID: 438230 [Multi-domain] Cd Length: 54 Bit Score: 34.65 E-value: 8.85e-03
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Blast search parameters | ||||
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