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Search results 901 to 982 out of 982 for Stat5a

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Type Details Score
Publication
12759342 | J:120649
First Author: Naylor MJ
Year: 2003
Journal: J Biol Chem
Title: The neuropeptide galanin augments lobuloalveolar development.
Volume: 278
Issue: 31
Pages: 29145-52
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Publication
8584036 | J:29717
First Author: Kazansky AV
Year: 1995
Journal: Mol Endocrinol
Title: Regulation of mammary gland factor/Stat5a during mammary gland development.
Volume: 9
Issue: 11
Pages: 1598-609
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Publication
8943349 | J:36543
First Author: Meinke A
Year: 1996
Journal: Mol Cell Biol
Title: Activation of different Stat5 isoforms contributes to cell-type-restricted signaling in response to interferons.
Volume: 16
Issue: 12
Pages: 6937-44
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Publication
9300676 | J:42622
First Author: Pericle F
Year: 1997
Journal: J Immunol
Title: Immunocompromised tumor-bearing mice show a selective loss of STAT5a/b expression in T and B lymphocytes.
Volume: 159
Issue: 6
Pages: 2580-5
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Publication
10022878 | J:53081
First Author: John S
Year: 1999
Journal: Mol Cell Biol
Title: The significance of tetramerization in promoter recruitment by Stat5.
Volume: 19
Issue: 3
Pages: 1910-8
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Publication
12730671 | J:83052
First Author: Li M
Year: 2003
Journal: Oncogene
Title: Chemoprevention of mammary carcinogenesis in a transgenic mouse model by alpha-difluoromethylornithine (DFMO) in the diet is associated with decreased cyclin D1 activity.
Volume: 22
Issue: 17
Pages: 2568-72
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Publication
12611881 | J:83274
First Author: Bagheri-Yarmand R
Year: 2003
Journal: J Biol Chem
Title: Activating transcription factor 4 overexpression inhibits proliferation and differentiation of mammary epithelium resulting in impaired lactation and accelerated involution.
Volume: 278
Issue: 19
Pages: 17421-9
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Publication
12732616 | J:83342
First Author: Wang RA
Year: 2003
Journal: J Cell Biol
Title: Essential functions of p21-activated kinase 1 in morphogenesis and differentiation of mammary glands.
Volume: 161
Issue: 3
Pages: 583-92
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Publication
14713198 | J:87259
First Author: Petridou B
Year: 2003
Journal: Transgenic Res
Title: Heterogeneous inducible mammary-specific expression of Jab/SOCS1 in lactating transgenic mice is associated with no obvious phenotype, even at the cellular level.
Volume: 12
Issue: 6
Pages: 693-706
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Publication
15963848 | J:99030
First Author: Moore MA
Year: 2005
Journal: Exp Hematol
Title: Converging pathways in leukemogenesis and stem cell self-renewal.
Volume: 33
Issue: 7
Pages: 719-37
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Publication
16684815 | J:110357
First Author: Lavens D
Year: 2006
Journal: J Cell Sci
Title: A complex interaction pattern of CIS and SOCS2 with the leptin receptor.
Volume: 119
Issue: Pt 11
Pages: 2214-24
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Publication
18653779 | J:139964
First Author: Muraoka-Cook RS
Year: 2008
Journal: Mol Endocrinol
Title: Prolactin and ErbB4/HER4 signaling interact via Janus kinase 2 to induce mammary epithelial cell gene expression differentiation.
Volume: 22
Issue: 10
Pages: 2307-21
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Publication
26601851 | J:235905
First Author: White UA
Year: 2016
Journal: Am J Physiol Endocrinol Metab
Title: The modulation of adiponectin by STAT5-activating hormones.
Volume: 310
Issue: 2
Pages: E129-36
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Protein
A2A5D3
Organism: Mus musculus/domesticus
Length: 125  
Fragment?: true
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Protein
A2A5D4
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Protein
Q71UV3
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: true
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Protein
P42232
Organism: Mus musculus/domesticus
Length: 786  
Fragment?: false
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Publication
15169911 | J:90883
First Author: Wagner KU
Year: 2004
Journal: Mol Cell Biol
Title: Impaired alveologenesis and maintenance of secretory mammary epithelial cells in Jak2 conditional knockout mice.
Volume: 24
Issue: 12
Pages: 5510-20
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Publication
19920132 | J:159955
First Author: Hewitt SC
Year: 2010
Journal: J Biol Chem
Title: Estrogen-mediated regulation of Igf1 transcription and uterine growth involves direct binding of estrogen receptor alpha to estrogen-responsive elements.
Volume: 285
Issue: 4
Pages: 2676-85
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Publication
12813461 | J:84340
First Author: Bierie B
Year: 2003
Journal: Oncogene
Title: Activation of beta-catenin in prostate epithelium induces hyperplasias and squamous transdifferentiation.
Volume: 22
Issue: 25
Pages: 3875-87
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Publication
9207075 | J:41784
First Author: Udy GB
Year: 1997
Journal: Proc Natl Acad Sci U S A
Title: Requirement of STAT5b for sexual dimorphism of body growth rates and liver gene expression.
Volume: 94
Issue: 14
Pages: 7239-44
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Publication
16886906 | J:116529
First Author: Starzynski RR
Year: 2006
Journal: Biochem J
Title: STAT5 proteins are involved in down-regulation of iron regulatory protein 1 gene expression by nitric oxide.
Volume: 400
Issue: 2
Pages: 367-75
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Publication
10752065 | J:62399
 
First Author: Waxman DJ
Year: 2000
Journal: Novartis Found Symp
Title: Growth hormone pulse-activated STAT5 signalling: a unique regulatory mechanism governing sexual dimorphism of liver gene expression.
Volume: 227
Pages: 61-74; discussion 75-81
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Publication
8943338 | J:36545
First Author: Lécine P
Year: 1996
Journal: Mol Cell Biol
Title: Elf-1 and Stat5 bind to a critical element in a new enhancer of the human interleukin-2 receptor alpha gene.
Volume: 16
Issue: 12
Pages: 6829-40
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Publication
10361113 | J:55735
First Author: Ilaria RL Jr
Year: 1999
Journal: Blood
Title: Dominant negative mutants implicate STAT5 in myeloid cell proliferation and neutrophil differentiation.
Volume: 93
Issue: 12
Pages: 4154-66
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Publication
10454585 | J:56954
First Author: Matsumoto A
Year: 1999
Journal: Mol Cell Biol
Title: Suppression of STAT5 functions in liver, mammary glands, and T cells in cytokine-inducible SH2-containing protein 1 transgenic mice.
Volume: 19
Issue: 9
Pages: 6396-407
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Protein
Q99ML3
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Publication
12209125 | -
First Author: Levy DE
Year: 2002
Journal: Nat Rev Mol Cell Biol
Title: Stats: transcriptional control and biological impact.
Volume: 3
Issue: 9
Pages: 651-62
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Publication
14668806 | -
First Author: Shuai K
Year: 2003
Journal: Nat Rev Immunol
Title: Regulation of JAK-STAT signalling in the immune system.
Volume: 3
Issue: 11
Pages: 900-11
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Publication
23977103 | -
First Author: Takakuma K
Year: 2013
Journal: PLoS One
Title: Novel multiplexed assay for identifying SH2 domain antagonists of STAT family proteins.
Volume: 8
Issue: 8
Pages: e71646
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Protein Domain
IPR001217 | STAT
Type: Family
Description: The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus []. Binding of these factors to cell-surface receptors leads to receptor autophosphorylation at a tyrosine, the phosphotyrosine being recognised by the STAT SH2 domain, which mediates the recruitment of STAT proteins from the cytosol and their association with the activated receptor. The STAT proteins are then activated by phosphorylation via members of the JAK family of protein kinases, causing them to dimerise and translocated to the nucleus, where they bind to specific promoter sequences in target genes. In mammals, STATs comprise a family of seven structurally and functionally related proteins: Stat1, Stat2, Stat3, Stat4, Stat5a and Stat5b, Stat6. STAT proteins play a critical role in regulating innate and acquired host immune responses. Dysregulation of at least two STAT signalling cascades (i.e. Stat3 and Stat5) is associated with cellular transformation.Signalling through the JAK/STAT pathway is initiated when a cytokine binds to its corresponding receptor. This leads to conformational changes in the cytoplasmic portion of the receptor, initiating activation of receptor associated members of the JAK family of kinases. The JAKs, in turn, mediate phosphorylation at the specific receptor tyrosine residues, which then serve as docking sites for STATs and other signalling molecules. Once recruited to the receptor, STATs also become phosphorylated by JAKs, on a single tyrosine residue. Activated STATs dissociate from the receptor, dimerise, translocate to the nucleus and bind to members of the GAS (gamma activated site) family of enhancers.The seven STAT proteins identified in mammals range in size from 750 and 850 amino acids. The chromosomal distribution of these STATs, as well as the identification of STATs in more primitive eukaryotes, suggest that this family arose from a single primordial gene. STATs share 6 structurally and functionally conserved domains including: an N-terminal domain (ND) that strengthens interactions between STAT dimers on adjacent DNA-binding sites; a coiled-coil STAT domain (CCD) that is implicated in protein-protein interactions; a DNA-binding domain (DBD) with an immunoglobulin-like fold similar to p53 tumour suppressor protein; an EF-hand-like linker domain connecting the DNA-binding and SH2 domains; an SH2 domain () that acts as a phosphorylation-dependent switch to control receptor recognition and DNA-binding; and a C-terminal transactivation domain [, , ]. The crystal structure of the N terminus of Stat4 reveals a dimer. The interface of this dimer is formed by a ring-shaped element consisting of five short helices. Several studies suggest that this N-terminal dimerisation promotes cooperativity of binding to tandem GAS elements and with the transcriptional coactivator CBP/p300.
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Protein
P42230
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
A0A087WSQ5
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: true
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Protein
D3YU28
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Protein
B2C3G8
Organism: Mus musculus/domesticus
Length: 797  
Fragment?: false
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Publication
23028142 | J:188260
First Author: Chen CC
Year: 2012
Journal: Genes Dev
Title: Autocrine prolactin induced by the Pten-Akt pathway is required for lactation initiation and provides a direct link between the Akt and Stat5 pathways.
Volume: 26
Issue: 19
Pages: 2154-68
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Publication
12039028 | -
First Author: Kisseleva T
Year: 2002
Journal: Gene
Title: Signaling through the JAK/STAT pathway, recent advances and future challenges.
Volume: 285
Issue: 1-2
Pages: 1-24
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Publication
9630226 | -
First Author: Chen X
Year: 1998
Journal: Cell
Title: Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.
Volume: 93
Issue: 5
Pages: 827-39
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Publication
15780933 | -
First Author: Mao X
Year: 2005
Journal: Mol Cell
Title: Structural bases of unphosphorylated STAT1 association and receptor binding.
Volume: 17
Issue: 6
Pages: 761-71
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Publication
18433722 | -
First Author: Ren Z
Year: 2008
Journal: Biochem Biophys Res Commun
Title: Crystal structure of unphosphorylated STAT3 core fragment.
Volume: 374
Issue: 1
Pages: 1-5
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Protein
Q3UZ79
Organism: Mus musculus/domesticus
Length: 277  
Fragment?: true
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Publication
15053873 | -
First Author: Soler-Lopez M
Year: 2004
Journal: Mol Cell
Title: Structure of an activated Dictyostelium STAT in its DNA-unbound form.
Volume: 13
Issue: 6
Pages: 791-804
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Protein Domain
IPR012345 | STAT_TF_DNA-bd_N
Type: Homologous_superfamily
Description: The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus []. Binding of these factors to cell-surface receptors leads to receptor autophosphorylation at a tyrosine, the phosphotyrosine being recognised by the STAT SH2 domain, which mediates the recruitment of STAT proteins from the cytosol and their association with the activated receptor. The STAT proteins are then activated by phosphorylation via members of the JAK family of protein kinases, causing them to dimerise and translocated to the nucleus, where they bind to specific promoter sequences in target genes. In mammals, STATs comprise a family of seven structurally and functionally related proteins: Stat1, Stat2, Stat3, Stat4, Stat5a and Stat5b, Stat6. STAT proteins play a critical role in regulating innate and acquired host immune responses. Dysregulation of at least two STAT signalling cascades (i.e. Stat3 and Stat5) is associated with cellular transformation.Signalling through the JAK/STAT pathway is initiated when a cytokine binds to its corresponding receptor. This leads to conformational changes in the cytoplasmic portion of the receptor, initiating activation of receptor associated members of the JAK family of kinases. The JAKs, in turn, mediate phosphorylation at the specific receptor tyrosine residues, which then serve as docking sites for STATs and other signalling molecules. Once recruited to the receptor, STATs also become phosphorylated by JAKs, on a single tyrosine residue. Activated STATs dissociate from the receptor, dimerise, translocate to the nucleus and bind to members of the GAS (gamma activated site) family of enhancers.The seven STAT proteins identified in mammals range in size from 750 and 850 amino acids. The chromosomal distribution of these STATs, as well as the identification of STATs in more primitive eukaryotes, suggest that this family arose from a single primordial gene. STATs share 6 structurally and functionally conserved domains including: an N-terminal domain (ND) that strengthens interactions between STAT dimers on adjacent DNA-binding sites; a coiled-coil STAT domain (CCD) that is implicated in protein-protein interactions; a DNA-binding domain (DBD) with an immunoglobulin-like fold similar to p53 tumour suppressor protein; an EF-hand-like linker domain connecting the DNA-binding and SH2 domains; an SH2 domain () that acts as a phosphorylation-dependent switch to control receptor recognition and DNA-binding; and a C-terminal transactivation domain [, , ]. The crystal structure of the N terminus of Stat4 reveals a dimer. The interface of this dimer is formed by a ring-shaped element consisting of five short helices. Several studies suggest that this N-terminal dimerisation promotes cooperativity of binding to tandem GAS elements and with the transcriptional coactivator CBP/p300.This superfamily represents the N terminus part of the p53-like DNA-binding domain of STAT proteins. Both the DNA-binding domain and the linker domain help determine DNA-specificity.
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Protein Domain
IPR015347 | STAT_TF_homologue_coiled-coil
Type: Domain
Description: The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus []. Binding of these factors to cell-surface receptors leads to receptor autophosphorylation at a tyrosine, the phosphotyrosine being recognised by the STAT SH2 domain, which mediates the recruitment of STAT proteins from the cytosol and their association with the activated receptor. The STAT proteins are then activated by phosphorylation via members of the JAK family of protein kinases, causing them to dimerise and translocated to the nucleus, where they bind to specific promoter sequences in target genes. In mammals, STATs comprise a family of seven structurally and functionally related proteins: Stat1, Stat2, Stat3, Stat4, Stat5a and Stat5b, Stat6. STAT proteins play a critical role in regulating innate and acquired host immune responses. Dysregulation of at least two STAT signalling cascades (i.e. Stat3 and Stat5) is associated with cellular transformation.Signalling through the JAK/STAT pathway is initiated when a cytokine binds to its corresponding receptor. This leads to conformational changes in the cytoplasmic portion of the receptor, initiating activation of receptor associated members of the JAK family of kinases. The JAKs, in turn, mediate phosphorylation at the specific receptor tyrosine residues, which then serve as docking sites for STATs and other signalling molecules. Once recruited to the receptor, STATs also become phosphorylated by JAKs, on a single tyrosine residue. Activated STATs dissociate from the receptor, dimerise, translocate to the nucleus and bind to members of the GAS (gamma activated site) family of enhancers.The seven STAT proteins identified in mammals range in size from 750 and 850 amino acids. The chromosomal distribution of these STATs, as well as the identification of STATs in more primitive eukaryotes, suggest that this family arose from a single primordial gene. STATs share 6 structurally and functionally conserved domains including: an N-terminal domain (ND) that strengthens interactions between STAT dimers on adjacent DNA-binding sites; a coiled-coil STAT domain (CCD) that is implicated in protein-protein interactions; a DNA-binding domain (DBD) with an immunoglobulin-like fold similar to p53 tumour suppressor protein; an EF-hand-like linker domain connecting the DNA-binding and SH2 domains; an SH2 domain () that acts as a phosphorylation-dependent switch to control receptor recognition and DNA-binding; and a C-terminal transactivation domain [, , ]. The crystal structure of the N terminus of Stat4 reveals a dimer. The interface of this dimer is formed by a ring-shaped element consisting of five short helices. Several studies suggest that this N-terminal dimerisation promotes cooperativity of binding to tandem GAS elements and with the transcriptional coactivator CBP/p300.This entry represents a domain found in Dictyostelium STAT proteins. This domain adopts a structure consisting of four long α-helices, folded into a coiled coil. It is responsible for nuclear export of the protein [].
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Protein Domain
IPR015988 | STAT_TF_coiled-coil
Type: Homologous_superfamily
Description: The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus []. Binding of these factors to cell-surface receptors leads to receptor autophosphorylation at a tyrosine, the phosphotyrosine being recognised by the STAT SH2 domain, which mediates the recruitment of STAT proteins from the cytosol and their association with the activated receptor. The STAT proteins are then activated by phosphorylation via members of the JAK family of protein kinases, causing them to dimerise and translocated to the nucleus, where they bind to specific promoter sequences in target genes. In mammals, STATs comprise a family of seven structurally and functionally related proteins: Stat1, Stat2, Stat3, Stat4, Stat5a and Stat5b, Stat6. STAT proteins play a critical role in regulating innate and acquired host immune responses. Dysregulation of at least two STAT signalling cascades (i.e. Stat3 and Stat5) is associated with cellular transformation.Signalling through the JAK/STAT pathway is initiated when a cytokine binds to its corresponding receptor. This leads to conformational changes in the cytoplasmic portion of the receptor, initiating activation of receptor associated members of the JAK family of kinases. The JAKs, in turn, mediate phosphorylation at the specific receptor tyrosine residues, which then serve as docking sites for STATs and other signalling molecules. Once recruited to the receptor, STATs also become phosphorylated by JAKs, on a single tyrosine residue. Activated STATs dissociate from the receptor, dimerise, translocate to the nucleus and bind to members of the GAS (gamma activated site) family of enhancers.The seven STAT proteins identified in mammals range in size from 750 and 850 amino acids. The chromosomal distribution of these STATs, as well as the identification of STATs in more primitive eukaryotes, suggest that this family arose from a single primordial gene. STATs share 6 structurally and functionally conserved domains including: an N-terminal domain (ND) that strengthens interactions between STAT dimers on adjacent DNA-binding sites; a coiled-coil STAT domain (CCD) that is implicated in protein-protein interactions; a DNA-binding domain (DBD) with an immunoglobulin-like fold similar to p53 tumour suppressor protein; an EF-hand-like linker domain connecting the DNA-binding and SH2 domains; an SH2 domain () that acts as a phosphorylation-dependent switch to control receptor recognition and DNA-binding; and a C-terminal transactivation domain [, , ]. The crystal structure of the N terminus of Stat4 reveals a dimer. The interface of this dimer is formed by a ring-shaped element consisting of five short helices. Several studies suggest that this N-terminal dimerisation promotes cooperativity of binding to tandem GAS elements and with the transcriptional coactivator CBP/p300.This entry represents a domain consisting of four long helices that forms a bundle with a left-handed twist (coiled coil), in a right-handed superhelix.
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Protein Domain
IPR013801 | STAT_TF_DNA-bd
Type: Domain
Description: The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus []. Binding of these factors to cell-surface receptors leads to receptor autophosphorylation at a tyrosine, the phosphotyrosine being recognised by the STAT SH2 domain, which mediates the recruitment of STAT proteins from the cytosol and their association with the activated receptor. The STAT proteins arethen activated by phosphorylation via members of the JAK family of protein kinases, causing them to dimerise and translocated to the nucleus, where they bind to specific promoter sequences in target genes. In mammals, STATs comprise a family of seven structurally and functionally related proteins: Stat1, Stat2, Stat3, Stat4, Stat5a and Stat5b, Stat6. STAT proteins play a critical role in regulating innate and acquired host immune responses. Dysregulation of at least two STAT signalling cascades (i.e. Stat3 and Stat5) is associated with cellular transformation.Signalling through the JAK/STAT pathway is initiated when a cytokine binds to its corresponding receptor. This leads to conformational changes in the cytoplasmic portion of the receptor, initiating activation of receptor associated members of the JAK family of kinases. The JAKs, in turn, mediate phosphorylation at the specific receptor tyrosine residues, which then serve as docking sites for STATs and other signalling molecules. Once recruited to the receptor, STATs also become phosphorylated by JAKs, on a single tyrosine residue. Activated STATs dissociate from the receptor, dimerise, translocate to the nucleus and bind to members of the GAS (gamma activated site) family of enhancers.The seven STAT proteins identified in mammals range in size from 750 and 850 amino acids. The chromosomal distribution of these STATs, as well as the identification of STATs in more primitive eukaryotes, suggest that this family arose from a single primordial gene. STATs share 6 structurally and functionally conserved domains including: an N-terminal domain (ND) that strengthens interactions between STAT dimers on adjacent DNA-binding sites; a coiled-coil STAT domain (CCD) that is implicated in protein-protein interactions; a DNA-binding domain (DBD) with an immunoglobulin-like fold similar to p53 tumour suppressor protein; an EF-hand-like linker domain connecting the DNA-binding and SH2 domains; an SH2 domain () that acts as a phosphorylation-dependent switch to control receptor recognition and DNA-binding; and a C-terminal transactivation domain [, , ]. The crystal structure of the N terminus of Stat4 reveals a dimer. The interface of this dimer is formed by a ring-shaped element consisting of five short helices. Several studies suggest that this N-terminal dimerisation promotes cooperativity of binding to tandem GAS elements and with the transcriptional coactivator CBP/p300.This entry represents the DNA-binding domain, which has an immunoglobulin-like structural fold.
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Protein Domain
IPR013800 | STAT_TF_alpha
Type: Domain
Description: The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus []. Binding of these factors to cell-surface receptors leads to receptor autophosphorylation at a tyrosine, the phosphotyrosine being recognised by the STAT SH2 domain, which mediates the recruitment of STAT proteins from the cytosol and their association with the activated receptor. The STAT proteins are then activated by phosphorylation via members of the JAK family of protein kinases, causing them to dimerise and translocated to the nucleus, where they bind to specific promoter sequences in target genes. In mammals, STATs comprise a family of seven structurally and functionally related proteins: Stat1, Stat2, Stat3, Stat4, Stat5a and Stat5b, Stat6. STAT proteins play a critical role in regulating innate and acquired host immune responses. Dysregulation of at least two STAT signalling cascades (i.e. Stat3 and Stat5) is associated with cellular transformation.Signalling through the JAK/STAT pathway is initiated when a cytokine binds to its corresponding receptor. This leads to conformational changes in the cytoplasmic portion of the receptor, initiating activation of receptor associated members of the JAK family of kinases. The JAKs, in turn, mediate phosphorylation at the specific receptor tyrosine residues, which then serve as docking sites for STATs and other signalling molecules. Once recruited to the receptor, STATs also become phosphorylated by JAKs, on a single tyrosine residue. Activated STATs dissociate from the receptor, dimerise, translocate to the nucleus and bind to members of the GAS (gamma activated site) family of enhancers.The seven STAT proteins identified in mammals range in size from 750 and 850 amino acids. The chromosomal distribution of these STATs, as well as the identification of STATs in more primitive eukaryotes, suggest that this family arose from a single primordial gene. STATs share 6 structurally and functionally conserved domains including: an N-terminal domain (ND) that strengthens interactions between STAT dimers on adjacent DNA-binding sites; a coiled-coil STAT domain (CCD) that is implicated in protein-protein interactions; a DNA-binding domain (DBD) with an immunoglobulin-like fold similar to p53 tumour suppressor protein; an EF-hand-like linker domain connecting the DNA-binding and SH2 domains; an SH2 domain () that acts as a phosphorylation-dependent switch to control receptor recognition and DNA-binding; and a C-terminal transactivation domain [, , ]. The crystal structure of the N terminus of Stat4 reveals a dimer. The interface of this dimer is formed by a ring-shaped element consisting of five short helices. Several studies suggest that this N-terminal dimerisation promotes cooperativity of binding to tandem GAS elements and with the transcriptional coactivator CBP/p300.This entry represents the all-alpha helical domain, which consists of four long helices arranged in a bundle with a left-handed twist (coiled-coil), which in turn forms a right-handed superhelix.
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Protein Domain
IPR013799 | STAT_TF_prot_interaction
Type: Domain
Description: The STAT protein (Signal Transducers and Activators of Transcription) family contains transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors, hence they act as signal transducers in the cytoplasm and transcription activators in the nucleus []. Binding of these factors to cell-surface receptors leads to receptor autophosphorylation at a tyrosine, the phosphotyrosine being recognised by the STAT SH2 domain, which mediates the recruitment of STAT proteins from the cytosol and their association with the activated receptor. The STAT proteins are then activated by phosphorylation via members of the JAK family of protein kinases, causing them to dimerise and translocated to the nucleus, where they bind to specific promoter sequences in target genes. In mammals, STATs comprise a family of seven structurally and functionally related proteins: Stat1, Stat2, Stat3, Stat4, Stat5a and Stat5b, Stat6. STAT proteins play a critical role in regulating innate and acquired host immune responses. Dysregulation of at least two STAT signalling cascades (i.e. Stat3 and Stat5) is associated with cellular transformation.Signalling through the JAK/STAT pathway is initiated when a cytokine binds to its corresponding receptor. This leads to conformational changes in the cytoplasmic portion of the receptor, initiating activation of receptor associated members of the JAK family of kinases. The JAKs, in turn, mediate phosphorylation at the specific receptor tyrosine residues, which then serve as docking sites for STATs and other signalling molecules. Once recruited to the receptor, STATs also become phosphorylated by JAKs, on a singletyrosine residue. Activated STATs dissociate from the receptor, dimerise, translocate to the nucleus and bind to members of the GAS (gamma activated site) family of enhancers.The seven STAT proteins identified in mammals range in size from 750 and 850 amino acids. The chromosomal distribution of these STATs, as well as the identification of STATs in more primitive eukaryotes, suggest that this family arose from a single primordial gene. STATs share 6 structurally and functionally conserved domains including: an N-terminal domain (ND) that strengthens interactions between STAT dimers on adjacent DNA-binding sites; a coiled-coil STAT domain (CCD) that is implicated in protein-protein interactions; a DNA-binding domain (DBD) with an immunoglobulin-like fold similar to p53 tumour suppressor protein; an EF-hand-like linker domain connecting the DNA-binding and SH2 domains; an SH2 domain () that acts as a phosphorylation-dependent switch to control receptor recognition and DNA-binding; and a C-terminal transactivation domain [, , ]. The crystal structure of the N terminus of Stat4 reveals a dimer. The interface of this dimer is formed by a ring-shaped element consisting of five short helices. Several studies suggest that this N-terminal dimerisation promotes cooperativity of binding to tandem GAS elements and with the transcriptional coactivator CBP/p300.This entry represents the N-terminal domain, which is responsible for protein interactions. This domain has a multi-helical structure that can be subdivided into two structural sub-domains.
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Protein
P42225
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
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Protein
Q9WVL2
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: false
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Protein
P42227
Organism: Mus musculus/domesticus
Length: 770  
Fragment?: false
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Protein
P42228
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
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Protein
P52633
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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Protein
Q3U5W1
Organism: Mus musculus/domesticus
Length: 858  
Fragment?: true
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Protein
Q9QXJ2
Organism: Mus musculus/domesticus
Length: 922  
Fragment?: false
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Protein
Q8C3V4
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
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Protein
B7ZC18
Organism: Mus musculus/domesticus
Length: 744  
Fragment?: false
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Protein
Q9QZE4
Organism: Mus musculus/domesticus
Length: 925  
Fragment?: false
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Protein
Q8R4D4
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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Protein
Q3ULI4
Organism: Mus musculus/domesticus
Length: 770  
Fragment?: false
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Protein
Q3TW11
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
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Protein
Q3U5Q4
Organism: Mus musculus/domesticus
Length: 770  
Fragment?: false
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Protein
Q6GU23
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
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Protein
Q4G0C1
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: false
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Protein
E9QJX9
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: false
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Protein
Q8C8M3
Organism: Mus musculus/domesticus
Length: 755  
Fragment?: false
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Protein
Q8C497
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
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Protein
Q3U098
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: true
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Protein
Q3U6S9
Organism: Mus musculus/domesticus
Length: 770  
Fragment?: false
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Protein
Q9D323
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
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Protein
Q3UDU1
Organism: Mus musculus/domesticus
Length: 931  
Fragment?: false
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Protein
A0A087WSP5
Organism: Mus musculus/domesticus
Length: 755  
Fragment?: false
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Protein
Q99K94
Organism: Mus musculus/domesticus
Length: 712  
Fragment?: false
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Protein
Q3V157
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: false
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Protein
Q8CD97
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: true
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Protein
Q91Y52
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: true
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Protein
A0A087WRI1
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
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Protein
Q6P1X8
Organism: Mus musculus/domesticus
Length: 441  
Fragment?: false
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Protein
Q8C2A4
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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Protein
Q8CFJ6
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
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Protein
Q8CFQ1
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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