fos-related antigen 1 isoform 5 [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
bZIP super family | cl21462 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
34-66 | 3.71e-14 | |||
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. The actual alignment was detected with superfamily member cd14721: Pssm-ID: 473870 [Multi-domain] Cd Length: 62 Bit Score: 63.53 E-value: 3.71e-14
|
|||||||
PRK13729 super family | cl42933 | conjugal transfer pilus assembly protein TraB; Provisional |
35-148 | 3.98e-03 | |||
conjugal transfer pilus assembly protein TraB; Provisional The actual alignment was detected with superfamily member PRK13729: Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 36.72 E-value: 3.98e-03
|
|||||||
Name | Accession | Description | Interval | E-value | |||
bZIP_Fos | cd14721 | Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ... |
34-66 | 3.71e-14 | |||
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization domain; Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are four Fos proteins: c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2. In addition, FosB also exists as smaller splice variants FosB2 and deltaFosB2. They all contain an N-terminal region and a bZIP domain. c-Fos and FosB also contain a C-terminal transactivation domain which is absent in Fra-1/2 and the smaller FosB variants. Fos proteins can only heterodimerize with Jun and other AP-1 proteins, but cannot homodimerize. Fos:Jun heterodimers are more stable and can bind DNA with more affinity that Jun:Jun homodimers. Fos proteins can enhance the trans-activating and transforming properties of Jun proteins. 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: 269869 [Multi-domain] Cd Length: 62 Bit Score: 63.53 E-value: 3.71e-14
|
|||||||
PRK13729 | PRK13729 | conjugal transfer pilus assembly protein TraB; Provisional |
35-148 | 3.98e-03 | |||
conjugal transfer pilus assembly protein TraB; Provisional Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 36.72 E-value: 3.98e-03
|
|||||||
Prefoldin_2 | pfam01920 | Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
35-67 | 6.32e-03 | |||
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 34.51 E-value: 6.32e-03
|
|||||||
Name | Accession | Description | Interval | E-value | |||
bZIP_Fos | cd14721 | Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ... |
34-66 | 3.71e-14 | |||
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization domain; Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are four Fos proteins: c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2. In addition, FosB also exists as smaller splice variants FosB2 and deltaFosB2. They all contain an N-terminal region and a bZIP domain. c-Fos and FosB also contain a C-terminal transactivation domain which is absent in Fra-1/2 and the smaller FosB variants. Fos proteins can only heterodimerize with Jun and other AP-1 proteins, but cannot homodimerize. Fos:Jun heterodimers are more stable and can bind DNA with more affinity that Jun:Jun homodimers. Fos proteins can enhance the trans-activating and transforming properties of Jun proteins. 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: 269869 [Multi-domain] Cd Length: 62 Bit Score: 63.53 E-value: 3.71e-14
|
|||||||
bZIP_Fos_like | cd14699 | Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ... |
34-63 | 1.24e-05 | |||
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. 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: 269847 [Multi-domain] Cd Length: 59 Bit Score: 41.09 E-value: 1.24e-05
|
|||||||
bZIP_ATF3 | cd14722 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar ... |
34-66 | 1.00e-03 | |||
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar proteins: a DNA-binding and dimerization domain; ATF-3 is a Basic leucine zipper (bZIP) transcription factor that is induced by various stress signals such as cytokines, genetoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. Mice deficient with ATF3 display increased susceptibility to endotoxic shock induced death. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. 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: 269870 Cd Length: 62 Bit Score: 35.90 E-value: 1.00e-03
|
|||||||
PRK13729 | PRK13729 | conjugal transfer pilus assembly protein TraB; Provisional |
35-148 | 3.98e-03 | |||
conjugal transfer pilus assembly protein TraB; Provisional Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 36.72 E-value: 3.98e-03
|
|||||||
Prefoldin_2 | pfam01920 | Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
35-67 | 6.32e-03 | |||
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 34.51 E-value: 6.32e-03
|
|||||||
Fungal_TACC | pfam12709 | Fungal Transforming acidic coiled-coil (TACC) proteins; TACC proteins are present in different ... |
36-62 | 9.71e-03 | |||
Fungal Transforming acidic coiled-coil (TACC) proteins; TACC proteins are present in different organizms, ranging from yeasts to mammals. Schizosaccharomyces pombe has one TACC protein, known as Alp7 or Mia1p. Alp7/TACC consists of two domains: the N-terminal half that contains the nuclear localization signal (NLS) and has no homology to the other TACC members, and the C-terminal half, which consists of the conserved coiled-coil TACC domain. Alp7/TACC forms a complex with Alp14/TOG and localizes to microtubules, SPBs and kinetochores. This complex is necessary for mitotic and meiotic spindle assembly and proper chromosome segregation. The homolog from S. cerevisiae, Slk19, also has a role in spindle assembly and stability, and it is required for proper chromosome segregation. Pssm-ID: 403801 [Multi-domain] Cd Length: 77 Bit Score: 33.41 E-value: 9.71e-03
|
|||||||
Blast search parameters | ||||
|