leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
682-744
9.82e-38
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 (TSC22D2), also called transforming growth factor beta-stimulated clone 22 domain family member 2, or TSC22-related-inducible leucine zipper protein 4 (TILZ4), may participate in the regulation of cell growth. It interacts with pyruvate kinase isoform M2 (PKM2) and WD repeat domain 77 (WDR77). The model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D2. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
:
Pssm-ID: 409279 Cd Length: 63 Bit Score: 134.71 E-value: 9.82e-38
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
682-744
9.82e-38
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 (TSC22D2), also called transforming growth factor beta-stimulated clone 22 domain family member 2, or TSC22-related-inducible leucine zipper protein 4 (TILZ4), may participate in the regulation of cell growth. It interacts with pyruvate kinase isoform M2 (PKM2) and WD repeat domain 77 (WDR77). The model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D2. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409279 Cd Length: 63 Bit Score: 134.71 E-value: 9.82e-38
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
198-387
1.92e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.68 E-value: 1.92e-03
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
273-374
2.33e-03
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 41.33 E-value: 2.33e-03
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
682-744
9.82e-38
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 (TSC22D2), also called transforming growth factor beta-stimulated clone 22 domain family member 2, or TSC22-related-inducible leucine zipper protein 4 (TILZ4), may participate in the regulation of cell growth. It interacts with pyruvate kinase isoform M2 (PKM2) and WD repeat domain 77 (WDR77). The model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D2. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409279 Cd Length: 63 Bit Score: 134.71 E-value: 9.82e-38
leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 ...
673-738
1.27e-29
leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 (TSC22D4), also called TSC22-related-inducible leucine zipper protein 2 (TILZ2), or Tsc-22-like protein THG-1, is a transcriptional repressor that acts as a molecular determinant of insulin signalling and glucose handling. It also functions in hepatic lipid handling by regulating hepatic very-low-density-lipoprotein (VLDL) release and lipogenic gene expression. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D4. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409281 Cd Length: 74 Bit Score: 111.95 E-value: 1.27e-29
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
682-730
1.02e-26
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; The TGF-beta-stimulated clone-22 domain (TSC22D) family includes TSC22D1-4 and similar proteins. They have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. All family members contain a conserved leucine zipper (ZIP) domain located at the C-terminus. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409276 Cd Length: 49 Bit Score: 102.64 E-value: 1.02e-26
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 ...
678-748
5.62e-26
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409278 Cd Length: 79 Bit Score: 101.76 E-value: 5.62e-26
leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 ...
682-741
2.56e-23
leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 (TSC22D3) is also called DSIP-immunoreactive peptide, protein DIP, delta sleep-inducing peptide immunoreactor, glucocorticoid-induced leucine zipper protein (GILZ), TSC-22-like protein, or TSC-22-related protein (TSC-22R). It protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, it plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, it inhibits anti-CD3-induced NFKB1 nuclear translocation. TSC22D3 contains a leucine zipper motif, a Pro/Glu rich domain, and three potential phosphorylation sites. This model corresponds to the leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409280 Cd Length: 81 Bit Score: 94.25 E-value: 2.56e-23
leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding ...
683-730
2.28e-17
leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding protein, and similar proteins; The family includes TGF-beta-stimulated clone-22 domain (TSC22D) leucine zipper transcription factors, TSC22D1-4, as well as c-Myc-binding protein (MycBP). TSC22D proteins have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. Members of this family contain a conserved leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409275 Cd Length: 51 Bit Score: 76.40 E-value: 2.28e-17
leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called ...
682-734
5.57e-05
leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. This model corresponds to the conserved region that shows high sequence similarity with the leucine zipper (ZIP) domain located at the C-terminus of TGF-beta-stimulated clone-22 domain (TSC22D) family transcription factors. The first helix of ZIP is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.
Pssm-ID: 409277 [Multi-domain] Cd Length: 53 Bit Score: 41.38 E-value: 5.57e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
198-387
1.92e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.68 E-value: 1.92e-03
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
273-374
2.33e-03
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 41.33 E-value: 2.33e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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