probable E3 ubiquitin-protein ligase DTX2 isoform X1 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| DTC | pfam18102 | Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family ... |
480-614 | 1.56e-88 | |||||
Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family of proteins which comprises five members (DTX1, 2, 3, 4, and 3L). This conserved C-terminal region of about 150 residues of the Deltex family, is preceded by a RING E3 ligase domain in four of the members. Crystal structure of the Deltex C-terminal (DTC) domain reveals a fold composed of a central beta-sheet lined with two long parallel alpha-helices. : Pssm-ID: 465650 Cd Length: 133 Bit Score: 270.52 E-value: 1.56e-88
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| RING-H2_DTX2 | cd16672 | RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ... |
411-482 | 3.89e-47 | |||||
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins; DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals. : Pssm-ID: 438334 Cd Length: 72 Bit Score: 159.99 E-value: 3.89e-47
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| WWE | smart00678 | Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
21-105 | 9.39e-25 | |||||
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis; : Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 97.80 E-value: 9.39e-25
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| WWE | smart00678 | Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
110-181 | 1.10e-24 | |||||
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis; : Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 97.41 E-value: 1.10e-24
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| PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
166-394 | 2.55e-04 | |||||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.55e-04
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| Name | Accession | Description | Interval | E-value | |||||
| DTC | pfam18102 | Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family ... |
480-614 | 1.56e-88 | |||||
Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family of proteins which comprises five members (DTX1, 2, 3, 4, and 3L). This conserved C-terminal region of about 150 residues of the Deltex family, is preceded by a RING E3 ligase domain in four of the members. Crystal structure of the Deltex C-terminal (DTC) domain reveals a fold composed of a central beta-sheet lined with two long parallel alpha-helices. Pssm-ID: 465650 Cd Length: 133 Bit Score: 270.52 E-value: 1.56e-88
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| Deltex_C | cd09633 | Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in ... |
481-613 | 1.11e-80 | |||||
Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in the regulation of Notch signaling, and therefore may play roles in cell-to-cell communications that regulate mechanisms determining cell fate. They have a central RING-type zinc finger domain and contain a C-terminal domain, described here, that is also found in other domain architectures. Deltex-1 (DTX1) contains a RING finger and two WWE domains, indicating that it may be an E3 ubiquitin ligase. Human deltex 3-like, which contains an additional N-terminal domain (presumably with ubiquitin ligase activity) is also described as E3 ubiquitin-protein ligase DTX3L, B-lymphoma- and BAL-associated protein (BBAP), or rhysin-2. DTX3L mediates monoubiquitination of K91 of histone H4 in response to DNA damage. Pssm-ID: 193607 Cd Length: 131 Bit Score: 250.18 E-value: 1.11e-80
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| RING-H2_DTX2 | cd16672 | RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ... |
411-482 | 3.89e-47 | |||||
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins; DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals. Pssm-ID: 438334 Cd Length: 72 Bit Score: 159.99 E-value: 3.89e-47
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| WWE | smart00678 | Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
21-105 | 9.39e-25 | |||||
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis; Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 97.80 E-value: 9.39e-25
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| WWE | smart00678 | Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
110-181 | 1.10e-24 | |||||
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis; Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 97.41 E-value: 1.10e-24
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| WWE | pfam02825 | WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
21-97 | 2.07e-19 | |||||
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems. Pssm-ID: 460715 [Multi-domain] Cd Length: 66 Bit Score: 82.34 E-value: 2.07e-19
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| WWE | pfam02825 | WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
111-174 | 4.84e-19 | |||||
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems. Pssm-ID: 460715 [Multi-domain] Cd Length: 66 Bit Score: 81.19 E-value: 4.84e-19
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
166-394 | 2.55e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.55e-04
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| Name | Accession | Description | Interval | E-value | |||||
| DTC | pfam18102 | Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family ... |
480-614 | 1.56e-88 | |||||
Deltex C-terminal domain; This is the C-terminal domains found in members of the Deltex family of proteins which comprises five members (DTX1, 2, 3, 4, and 3L). This conserved C-terminal region of about 150 residues of the Deltex family, is preceded by a RING E3 ligase domain in four of the members. Crystal structure of the Deltex C-terminal (DTC) domain reveals a fold composed of a central beta-sheet lined with two long parallel alpha-helices. Pssm-ID: 465650 Cd Length: 133 Bit Score: 270.52 E-value: 1.56e-88
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| Deltex_C | cd09633 | Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in ... |
481-613 | 1.11e-80 | |||||
Domain found at the C-terminus of deltex-like; The deltex family of proteins is involved in the regulation of Notch signaling, and therefore may play roles in cell-to-cell communications that regulate mechanisms determining cell fate. They have a central RING-type zinc finger domain and contain a C-terminal domain, described here, that is also found in other domain architectures. Deltex-1 (DTX1) contains a RING finger and two WWE domains, indicating that it may be an E3 ubiquitin ligase. Human deltex 3-like, which contains an additional N-terminal domain (presumably with ubiquitin ligase activity) is also described as E3 ubiquitin-protein ligase DTX3L, B-lymphoma- and BAL-associated protein (BBAP), or rhysin-2. DTX3L mediates monoubiquitination of K91 of histone H4 in response to DNA damage. Pssm-ID: 193607 Cd Length: 131 Bit Score: 250.18 E-value: 1.11e-80
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| RING-H2_DTX2 | cd16672 | RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ... |
411-482 | 3.89e-47 | |||||
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins; DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals. Pssm-ID: 438334 Cd Length: 72 Bit Score: 159.99 E-value: 3.89e-47
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| RING-H2_DTX1_4 | cd16671 | RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), ... |
409-477 | 1.60e-30 | |||||
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase deltex1 (DTX1), deltex4 (DTX4), and similar proteins; DTX1 functions as a Notch downstream transcription regulator that mediates a Notch signal to block differentiation of neural progenitor cells. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 appears to promote B-cell development at the expense of T-cell development. It also promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1 and likely interacts with the intracellular domain of Notch as well. Both DTX1 and DTX4 contain two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. They also harbor two nuclear localization signals. Pssm-ID: 438333 Cd Length: 69 Bit Score: 113.80 E-value: 1.60e-30
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| RING-H2_DTX1-like | cd16459 | RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), ... |
411-477 | 7.66e-30 | |||||
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), Deltex4 (DTX4), and similar proteins; This subfamily contains the vertebrate homologs of Drosophila melanogaster Deltex, specifically DTX1, DTX2, and DTX4, and other similar proteins mainly from eumetazoa. The vertebrate homologs of Deltex are involved in Notch signaling and neurogenesis. Mammalian DTX1 is most closely related to the Drosophila Deltex. Both of them bind to SH3-domain containing protein Grb2 and further inhibit E2A. DTX1 functions as a Notch downstream transcription regulator. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1. So it likely interacts with the intracellular domain of Notch as well. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. In contrast to other DTXs, DTX3 does not contain two Notch-binding WWE domains at the N-terminus, but rather a short unique N-terminal domain. It does not interact with the intracellular domain of Notch. In addition, it has a different class of RING finger (C3HC4 type or RING-HC subclass), compared with the other DTXs which harbor a C3H2C3-type RING-H2 finger. Thus DTX3 is not included in this subfamily. Drosophila melanogaster Deltex also does not belong to this subfamily. Pssm-ID: 438122 [Multi-domain] Cd Length: 64 Bit Score: 111.84 E-value: 7.66e-30
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| WWE | smart00678 | Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
21-105 | 9.39e-25 | |||||
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis; Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 97.80 E-value: 9.39e-25
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| WWE | smart00678 | Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
110-181 | 1.10e-24 | |||||
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis; Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 97.41 E-value: 1.10e-24
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| WWE | pfam02825 | WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
21-97 | 2.07e-19 | |||||
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems. Pssm-ID: 460715 [Multi-domain] Cd Length: 66 Bit Score: 82.34 E-value: 2.07e-19
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| WWE | pfam02825 | WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
111-174 | 4.84e-19 | |||||
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems. Pssm-ID: 460715 [Multi-domain] Cd Length: 66 Bit Score: 81.19 E-value: 4.84e-19
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| RING-H2 | cd16448 | H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ... |
412-473 | 1.18e-06 | |||||
H2 subclass of RING (RING-H2) fingers 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 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). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger 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 serves as a scaffold 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: 438112 [Multi-domain] Cd Length: 43 Bit Score: 45.47 E-value: 1.18e-06
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| RING-H2_RNF32_rpt2 | cd16678 | second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ... |
411-476 | 4.32e-05 | |||||
second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the second RING-H2 finger. Pssm-ID: 438340 [Multi-domain] Cd Length: 61 Bit Score: 41.58 E-value: 4.32e-05
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| RING-H2_ASR1 | cd23120 | RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ... |
410-474 | 1.41e-04 | |||||
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger protein 1 (ASR1) and similar proteins; ASR1 is required for tolerance to alcohol. It signals alcohol stress to the nucleus. ASR1 contains a C3H2C3-type RING-H2 finger. Pssm-ID: 438482 [Multi-domain] Cd Length: 54 Bit Score: 39.83 E-value: 1.41e-04
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
166-394 | 2.55e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.55e-04
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| RING-HC_DTX3 | cd16711 | RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ... |
442-484 | 4.48e-03 | |||||
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain two N-terminal Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with the intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. Pssm-ID: 438371 [Multi-domain] Cd Length: 54 Bit Score: 35.86 E-value: 4.48e-03
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| Blast search parameters | ||||
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