nuclear factor interleukin-3-regulated protein isoform X1 [Rattus norvegicus]
Protein Classification
bZIP transcription factor( domain architecture ID 10200232)
basic leucine zipper (bZIP) transcription factor binds to the promoter regions of genes to control their expression
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| Vert_IL3-reg_TF | pfam06529 | Vertebrate interleukin-3 regulated transcription factor; This family includes vertebrate ... |
130-461 | 0e+00 | ||||||
Vertebrate interleukin-3 regulated transcription factor; This family includes vertebrate transcription factors, some of which are regulated by IL-3/adenovirus E4 promoter binding protein. Others were found to strongly repress transcription in a DNA-binding-site-dependent manner. : Pssm-ID: 368956 Cd Length: 332 Bit Score: 648.03 E-value: 0e+00
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| bZIP_NFIL3 | cd14694 | Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): ... |
72-131 | 1.85e-31 | ||||||
Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain; NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. 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: 269842 Cd Length: 60 Bit Score: 114.73 E-value: 1.85e-31
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| Name | Accession | Description | Interval | E-value | ||||||
| Vert_IL3-reg_TF | pfam06529 | Vertebrate interleukin-3 regulated transcription factor; This family includes vertebrate ... |
130-461 | 0e+00 | ||||||
Vertebrate interleukin-3 regulated transcription factor; This family includes vertebrate transcription factors, some of which are regulated by IL-3/adenovirus E4 promoter binding protein. Others were found to strongly repress transcription in a DNA-binding-site-dependent manner. Pssm-ID: 368956 Cd Length: 332 Bit Score: 648.03 E-value: 0e+00
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| bZIP_NFIL3 | cd14694 | Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): ... |
72-131 | 1.85e-31 | ||||||
Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain; NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. 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: 269842 Cd Length: 60 Bit Score: 114.73 E-value: 1.85e-31
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| bZIP_2 | pfam07716 | Basic region leucine zipper; |
76-123 | 1.52e-14 | ||||||
Basic region leucine zipper; Pssm-ID: 462244 [Multi-domain] Cd Length: 51 Bit Score: 67.63 E-value: 1.52e-14
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| BRLZ | smart00338 | basic region leucin zipper; |
71-123 | 4.02e-08 | ||||||
basic region leucin zipper; Pssm-ID: 197664 [Multi-domain] Cd Length: 65 Bit Score: 49.87 E-value: 4.02e-08
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| VPA1267_fam | NF040697 | VPA1267 family protein; Members of this family occur in mobile elements, as for VPA1267 found ... |
68-133 | 5.89e-03 | ||||||
VPA1267 family protein; Members of this family occur in mobile elements, as for VPA1267 found in pathogenicity island 6 of Vibrio parahaemolyticus RIMD2210633. Pssm-ID: 468661 [Multi-domain] Cd Length: 143 Bit Score: 37.21 E-value: 5.89e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| Vert_IL3-reg_TF | pfam06529 | Vertebrate interleukin-3 regulated transcription factor; This family includes vertebrate ... |
130-461 | 0e+00 | ||||||
Vertebrate interleukin-3 regulated transcription factor; This family includes vertebrate transcription factors, some of which are regulated by IL-3/adenovirus E4 promoter binding protein. Others were found to strongly repress transcription in a DNA-binding-site-dependent manner. Pssm-ID: 368956 Cd Length: 332 Bit Score: 648.03 E-value: 0e+00
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| bZIP_NFIL3 | cd14694 | Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): ... |
72-131 | 1.85e-31 | ||||||
Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain; NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. 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: 269842 Cd Length: 60 Bit Score: 114.73 E-value: 1.85e-31
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| bZIP_HLF | cd14695 | Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a ... |
72-123 | 1.43e-14 | ||||||
Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a DNA-binding and dimerization domain; HLF, also called vitellogenin gene-binding protein (VBP) in birds, is a circadian clock-controlled Basic leucine zipper (bZIP) transcription factor which is a direct transcriptional target of CLOCK/BMAL1. It is implicated, together with bZIPs DBP and TEF, in the regulation of genes involved in the metabolism of endobiotic and xenobiotic agents. Triple knockout mice display signs of early aging and suffer premature death, likely due to impaired defense against xenobiotic stress. A leukemogenic translocation results in the chimeric fusion protein E2A-HLF that results in a rare form of pro-B-cell acute lymphoblastic leukemia (ALL). 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: 269843 [Multi-domain] Cd Length: 60 Bit Score: 67.96 E-value: 1.43e-14
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| bZIP_2 | pfam07716 | Basic region leucine zipper; |
76-123 | 1.52e-14 | ||||||
Basic region leucine zipper; Pssm-ID: 462244 [Multi-domain] Cd Length: 51 Bit Score: 67.63 E-value: 1.52e-14
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| bZIP | cd14686 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
76-123 | 2.16e-08 | ||||||
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: 50.24 E-value: 2.16e-08
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| BRLZ | smart00338 | basic region leucin zipper; |
71-123 | 4.02e-08 | ||||||
basic region leucin zipper; Pssm-ID: 197664 [Multi-domain] Cd Length: 65 Bit Score: 49.87 E-value: 4.02e-08
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| bZIP_BmCbz-like | cd14813 | Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and ... |
76-123 | 1.02e-07 | ||||||
Basic leucine zipper (bZIP) domain of Bombyx mori chorion b-ZIP transcription factor and similar bZIP domains; Bombyx mori chorion b-ZIP transcription factor, is encoded by the Cbz gene. 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: 269875 [Multi-domain] Cd Length: 52 Bit Score: 48.52 E-value: 1.02e-07
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| bZIP_GCN4 | cd12193 | Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and ... |
79-123 | 4.45e-06 | ||||||
Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and dimerization domain; GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain. In amino acid-deprived cells, GCN4 is up-regulated leading to transcriptional activation of genes encoding amino acid biosynthetic enzymes. 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: 269833 [Multi-domain] Cd Length: 54 Bit Score: 43.71 E-value: 4.45e-06
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| bZIP_CEBP | cd14693 | Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar ... |
76-121 | 1.60e-05 | ||||||
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar proteins: a DNA-binding and dimerization domain; CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. 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: 269841 [Multi-domain] Cd Length: 60 Bit Score: 42.16 E-value: 1.60e-05
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| bZIP_CEBPG | cd14713 | Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein gamma (CEBPG): a ... |
76-126 | 2.56e-05 | ||||||
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein gamma (CEBPG): a DNA-binding and dimerization domain; CEBPG is an important regulator of cellular senescence; mouse embryonic fibroblasts deficient of CEBPG proliferated poorly, entered senescence prematurely, and expressed elevated levels of proinflammatory genes. It is also the primary transcription factor that regulates antioxidant and DNA repair transcripts in normal bronchial epithelial cells. In a subset of AML patients with CEBPA hypermethylation, CEBPG is significantly overexpressed. CEBPG is the shortest CEBP protein and it lacks a transactivation domain. It acts as a regulator and buffering reservoir against the transcriptional activities of other CEBP proteins. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. 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: 269861 Cd Length: 61 Bit Score: 41.68 E-value: 2.56e-05
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| bZIP_CREB1 | cd14690 | Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) ... |
79-123 | 1.04e-04 | ||||||
Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 1 (CREB1) and similar proteins: a DNA-binding and dimerization domain; CREB1 is a Basic leucine zipper (bZIP) transcription factor that plays a role in propagating signals initiated by receptor activation through the induction of cAMP-responsive genes. Because it responds to many signal transduction pathways, CREB1 is implicated to function in many processes including learning, memory, circadian rhythm, immune response, and reproduction, among others. 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: 269838 [Multi-domain] Cd Length: 55 Bit Score: 39.92 E-value: 1.04e-04
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| bZIP_Zip1 | cd14705 | Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ... |
78-123 | 3.10e-04 | ||||||
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: 38.67 E-value: 3.10e-04
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| bZIP_XBP1 | cd14691 | Basic leucine zipper (bZIP) domain of X-box binding protein 1 (XBP1) and similar proteins: a ... |
79-126 | 3.85e-04 | ||||||
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: 38.34 E-value: 3.85e-04
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| bZIP_1 | pfam00170 | bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ... |
78-123 | 2.87e-03 | ||||||
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: 36.20 E-value: 2.87e-03
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| bZIP_CEBPD | cd14714 | Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein delta (CEBPD): a ... |
76-124 | 3.24e-03 | ||||||
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein delta (CEBPD): a DNA-binding and dimerization domain; CEBPD is an inflammatory response gene that is induced by Toll-like receptor 4 (TLR4) and is essential in the expression of many lipopolysaccharide (LPS)-induced genes and the clearance of bacterial infection. Its expression is increased in response to various extracellular stimuli and it induces growth arrest and apoptosis in cancer cells. It is thought to function as a tumor suppressor and its expression is found reduced by site-specific methylation in many cancers including breast, cervical, and hepatocellular carcinoma. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. 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: 269862 Cd Length: 65 Bit Score: 36.13 E-value: 3.24e-03
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| VPA1267_fam | NF040697 | VPA1267 family protein; Members of this family occur in mobile elements, as for VPA1267 found ... |
68-133 | 5.89e-03 | ||||||
VPA1267 family protein; Members of this family occur in mobile elements, as for VPA1267 found in pathogenicity island 6 of Vibrio parahaemolyticus RIMD2210633. Pssm-ID: 468661 [Multi-domain] Cd Length: 143 Bit Score: 37.21 E-value: 5.89e-03
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| bZIP_ATF4 | cd14692 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ... |
79-123 | 7.97e-03 | ||||||
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: 34.86 E-value: 7.97e-03
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| bZIP_CEBPB | cd14712 | Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein beta (CEBPB): a ... |
70-124 | 8.76e-03 | ||||||
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein beta (CEBPB): a DNA-binding and dimerization domain; CEBPB is a key regulator of metabolism, adipocyte differentiation, myogenesis, and macrophage activation. It is expressed as three distinct isoforms from an intronless gene through alternative translation initiation: CEBPB1 (or liver-enriched activator protein 1, LAP1); CEBPB2 (OR LAP2); and CEBPB3 (or liver-enriched inhibitory protein, LIP). LAP1/2 function as transcriptional activators while LIP is a repressor due to its lack of a transactivation domain. The relative expression of LAP and LIP has effects on inflammation, ER stress, and insulin resistance. CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate many cellular processes. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. 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: 269860 Cd Length: 71 Bit Score: 35.07 E-value: 8.76e-03
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