Stress activated transcription factor atfs-1 [Caenorhabditis elegans]
Protein Classification
bZIP transcription factor( domain architecture ID 10200220)
basic leucine zipper (bZIP) transcription factor similar to Homo sapiens cyclic AMP-dependent transcription factors, ATF-4 and ATF-5
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| bZIP_ATF4 | cd14692 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ... |
407-469 | 5.30e-21 | ||
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. : Pssm-ID: 269840 [Multi-domain] Cd Length: 63 Bit Score: 86.09 E-value: 5.30e-21
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| Name | Accession | Description | Interval | E-value | ||
| bZIP_ATF4 | cd14692 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ... |
407-469 | 5.30e-21 | ||
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269840 [Multi-domain] Cd Length: 63 Bit Score: 86.09 E-value: 5.30e-21
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| bZIP_2 | pfam07716 | Basic region leucine zipper; |
411-458 | 2.43e-11 | ||
Basic region leucine zipper; Pssm-ID: 462244 [Multi-domain] Cd Length: 51 Bit Score: 58.38 E-value: 2.43e-11
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| BRLZ | smart00338 | basic region leucin zipper; |
406-468 | 8.91e-10 | ||
basic region leucin zipper; Pssm-ID: 197664 [Multi-domain] Cd Length: 65 Bit Score: 54.49 E-value: 8.91e-10
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| Name | Accession | Description | Interval | E-value | ||
| bZIP_ATF4 | cd14692 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ... |
407-469 | 5.30e-21 | ||
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269840 [Multi-domain] Cd Length: 63 Bit Score: 86.09 E-value: 5.30e-21
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| bZIP_2 | pfam07716 | Basic region leucine zipper; |
411-458 | 2.43e-11 | ||
Basic region leucine zipper; Pssm-ID: 462244 [Multi-domain] Cd Length: 51 Bit Score: 58.38 E-value: 2.43e-11
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| BRLZ | smart00338 | basic region leucin zipper; |
406-468 | 8.91e-10 | ||
basic region leucin zipper; Pssm-ID: 197664 [Multi-domain] Cd Length: 65 Bit Score: 54.49 E-value: 8.91e-10
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| bZIP | cd14686 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
411-459 | 5.24e-09 | ||
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 52.16 E-value: 5.24e-09
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| bZIP_XBP1 | cd14691 | Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ... |
406-467 | 7.15e-07 | ||
Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a DNA-binding and dimerization domain; XBP1, a member of the Basic leucine zipper (bZIP) family, is the key transcription factor that orchestrates the unfolded protein response (UPR). It is the most conserved component of the UPR and is critical for cell fate determination in response to ER stress. The inositol-requiring enzyme 1 (IRE1)-XBP1 pathway is one of the three major sensors at the ER membrane that initiates the UPR upon activation. IRE1, a type I transmembrane protein kinase and endoribonuclease, oligomerizes upon ER stress leading to its increased activity. It splices the XBP1 mRNA, producing a variant that translocates to the nucleus and activates its target genes, which are involved in protein folding, degradation, and trafficking. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269839 [Multi-domain] Cd Length: 58 Bit Score: 46.05 E-value: 7.15e-07
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| bZIP_ATF2 | cd14687 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ... |
411-466 | 2.83e-06 | ||
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269835 [Multi-domain] Cd Length: 61 Bit Score: 44.44 E-value: 2.83e-06
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| bZIP_1 | pfam00170 | bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ... |
411-467 | 4.28e-05 | ||
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region. Pssm-ID: 395118 [Multi-domain] Cd Length: 60 Bit Score: 41.21 E-value: 4.28e-05
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| bZIP_Zip1 | cd14705 | Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ... |
408-463 | 1.42e-03 | ||
Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of fungal bZIP transcription factors including Schizosaccharomyces pombe Zip1, Saccharomyces cerevisiae Methionine-requiring protein 28 (Met28p), and Neurospora crassa cys-3, among others. Zip1 is required for the production of key proteins involved in sulfur metabolism and also plays a role in cadmium response. Met28p acts as a cofactor of Met4p, a transcriptional activator of the sulfur metabolic network; it stabilizes DNA:Met4 complexes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269853 [Multi-domain] Cd Length: 55 Bit Score: 36.74 E-value: 1.42e-03
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