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Search results 501 to 600 out of 627 for Stat4

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Type Details Score
Allele
Stat4<em1Smoc> | MGI:7292610
Name: signal transducer and activator of transcription 4; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Allele
Stat4<em3Adiuj> | MGI:5787992
Name: signal transducer and activator of transcription 4; endonuclease-mediated mutation 3, MODEL-AD Center
Allele Type: Endonuclease-mediated
Attribute String: Not Specified
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Strain
MGI:5788000 | C57BL/6J-Stat4<em3Adiuj>/J
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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GO Term
GO:0007260 | tyrosine phosphorylation of STAT protein
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GO Term
GO:0042509 | regulation of tyrosine phosphorylation of STAT protein
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Protein Coding Gene
MGI:1924885 | Socs6
Type: protein_coding_gene
Organism: mouse, laboratory
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HT Experiment
GSE38808 | The Transcription Factor T-bet Is Induced by Multiple Pathways and Prevents an Endogenous Th2 Cell Program during Th1 Cell Responses
Series Id: E-GEOD-38808
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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GO Term
GO:0042532 | negative regulation of tyrosine phosphorylation of STAT protein
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Publication
10320373 | J:54604
First Author: Diefenbach A
Year: 1999
Journal: Science
Title: Requirement for type 2 NO synthase for IL-12 signaling in innate immunity.
Volume: 284
Issue: 5416
Pages: 951-5
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Publication
10817963 | J:62426
First Author: Takeda K
Year: 2000
Journal: Cytokine Growth Factor Rev
Title: STAT family of transcription factors in cytokine-mediated biological responses.
Volume: 11
Issue: 3
Pages: 199-207
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GO Term
GO:0042531 | positive regulation of tyrosine phosphorylation of STAT protein
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Publication
11114383 | J:65966
First Author: Oppmann B
Year: 2000
Journal: Immunity
Title: Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12.
Volume: 13
Issue: 5
Pages: 715-25
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Publication
18549798 | J:137735
First Author: Shi M
Year: 2008
Journal: Immunity
Title: Janus-kinase-3-dependent signals induce chromatin remodeling at the Ifng locus during T helper 1 cell differentiation.
Volume: 28
Issue: 6
Pages: 763-73
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Publication
34471108 | J:310403
First Author: Hoefig KP
Year: 2021
Journal: Nat Commun
Title: Defining the RBPome of primary T helper cells to elucidate higher-order Roquin-mediated mRNA regulation.
Volume: 12
Issue: 1
Pages: 5208
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Publication
17306571 | J:118426
First Author: Nakahira M
Year: 2007
Journal: Immunity
Title: Regulation of signal transducer and activator of transcription signaling by the tyrosine phosphatase PTP-BL.
Volume: 26
Issue: 2
Pages: 163-76
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Publication
10064070 | J:332070
First Author: Yang J
Year: 1999
Journal: Eur J Immunol
Title: Induction of interferon-gamma production in Th1 CD4+ T cells: evidence for two distinct pathways for promoter activation.
Volume: 29
Issue: 2
Pages: 548-55
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Publication
10209051 | J:331608
First Author: Carter LL
Year: 1999
Journal: J Exp Med
Title: Lineage-specific requirement for signal transducer and activator of transcription (Stat)4 in interferon gamma production from CD4(+) versus CD8(+) T cells.
Volume: 189
Issue: 8
Pages: 1355-60
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Publication
29440505 | J:259420
First Author: Madera S
Year: 2018
Journal: J Immunol
Title: Cutting Edge: Divergent Requirement of T-Box Transcription Factors in Effector and Memory NK Cells.
Volume: 200
Issue: 6
Pages: 1977-1981
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Publication
14734615 | J:88973
First Author: Park WR
Year: 2004
Journal: Int Immunol
Title: A mechanism underlying STAT4-mediated up-regulation of IFN-gamma induction inTCR-triggered T cells.
Volume: 16
Issue: 2
Pages: 295-302
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Publication
20060330 | J:157633
First Author: Rao RR
Year: 2010
Journal: Immunity
Title: The mTOR kinase determines effector versus memory CD8+ T cell fate by regulating the expression of transcription factors T-bet and Eomesodermin.
Volume: 32
Issue: 1
Pages: 67-78
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Publication
25064073 | J:260275
First Author: Schmitt N
Year: 2014
Journal: Nat Immunol
Title: The cytokine TGF-β co-opts signaling via STAT3-STAT4 to promote the differentiation of human TFH cells.
Volume: 15
Issue: 9
Pages: 856-65
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Publication
29618525 | J:261485
First Author: Nabekura T
Year: 2018
Journal: J Immunol
Title: Crk Adaptor Proteins Regulate NK Cell Expansion and Differentiation during Mouse Cytomegalovirus Infection.
Volume: 200
Issue: 10
Pages: 3420-3428
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Publication
34795671 | J:315044
 
First Author: Schroeder JH
Year: 2021
Journal: Front Immunol
Title: Sustained Post-Developmental T-Bet Expression Is Critical for the Maintenance of Type One Innate Lymphoid Cells In Vivo.
Volume: 12
Pages: 760198
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Protein Domain
IPR035856 | STAT4_SH2
Type: Domain
Description: Signal transducer and activator of transcription 4 (STAT4) transduces interleukin-12, interleukin-23, and type I interferon cytokine signals in T cells and monocytes [, ]. It plays an important role in CD4+ Th1 lineage differentiation and IFN-gamma protein expression by CD4+ T cells []. It is crucial for both innate and adaptive immune responses to viral infection []. Variations of the STAT4 gene affect the susceptibility to autoimmune diseases [], such as systemic lupus erythematosus 11 (SLEB11) []and rheumatoid arthritis (RA) []. STAT proteins have a dual function: signal transduction and activation of transcription. When cytokines are boundto cell surface receptors, the associated Janus kinases (JAKs) are activated, leading to tyrosine phosphorylation of the given STAT proteins []. Phosphorylated STATs form dimers, translocate to the nucleus, and bind specific response elements to activate transcription of target genes []. STAT proteins contain an N-terminal domain (NTD), a coiled-coil domain (CCD), a DNA-binding domain (DBD), an α-helical linker domain (LD), an SH2 domain, and a transactivation domain (TAD). The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6 []. This entry represents the SH2 domain of STAT4.
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Publication
19001140 | J:141397
First Author: Watford WT
Year: 2008
Journal: J Exp Med
Title: Tpl2 kinase regulates T cell interferon-gamma production and host resistance to Toxoplasma gondii.
Volume: 205
Issue: 12
Pages: 2803-12
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Publication
28183532 | J:241140
First Author: Masuda T
Year: 2017
Journal: Am J Pathol
Title: Growth Factor Midkine Promotes T-Cell Activation through Nuclear Factor of Activated T Cells Signaling and Th1 Cell Differentiation in Lupus Nephritis.
Volume: 187
Issue: 4
Pages: 740-751
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Publication
12023369 | J:76845
First Author: Parham C
Year: 2002
Journal: J Immunol
Title: A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 and a novel cytokine receptor subunit, IL-23R.
Volume: 168
Issue: 11
Pages: 5699-708
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Publication
14768057 | J:87674
First Author: Schleicher U
Year: 2004
Journal: Eur J Immunol
Title: Control of Leishmania major in the absence of Tyk2 kinase.
Volume: 34
Issue: 2
Pages: 519-29
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Publication
30258450 | J:286049
 
First Author: Yin S
Year: 2018
Journal: Front Immunol
Title: Runx3 Mediates Resistance to Intracellular Bacterial Infection by Promoting IL12 Signaling in Group 1 ILC and NCR+ILC3.
Volume: 9
Pages: 2101
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Publication
20593019 | J:162009
First Author: Nowak M
Year: 2010
Journal: PLoS One
Title: Defective NKT cell activation by CD1d+ TRAMP prostate tumor cells is corrected by interleukin-12 with α-galactosylceramide.
Volume: 5
Issue: 6
Pages: e11311
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Publication
19124743 | J:143488
First Author: Ribeiro de Almeida C
Year: 2009
Journal: J Immunol
Title: Critical role for the transcription regulator CCCTC-binding factor in the control of Th2 cytokine expression.
Volume: 182
Issue: 2
Pages: 999-1010
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Publication
12706437 | J:105826
First Author: Chakir H
Year: 2003
Journal: Microbes Infect
Title: IL-12Rbeta2-deficient mice of a genetically resistant background are susceptible to Leishmania major infection and develop a parasite-specific Th2 immune response.
Volume: 5
Issue: 4
Pages: 241-9
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Publication
14688355 | J:87565
First Author: Lieberman LA
Year: 2004
Journal: J Immunol
Title: STAT1 plays a critical role in the regulation of antimicrobial effector mechanisms, but not in the development of Th1-type responses during toxoplasmosis.
Volume: 172
Issue: 1
Pages: 457-63
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Publication
16237058 | J:119357
First Author: Suto A
Year: 2005
Journal: J Immunol
Title: Murine plasmacytoid dendritic cells produce IFN-gamma upon IL-4 stimulation.
Volume: 175
Issue: 9
Pages: 5681-9
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Publication
12407025 | J:80122
First Author: Fujimoto M
Year: 2002
Journal: Int Immunol
Title: A regulatory role for suppressor of cytokine signaling-1 in T(h) polarization in vivo.
Volume: 14
Issue: 11
Pages: 1343-50
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Publication
26208884 | J:278579
First Author: Bouhamdan M
Year: 2015
Journal: Cell Signal
Title: MEK1 dependent and independent ERK activation regulates IL-10 and IL-12 production in bone marrow derived macrophages.
Volume: 27
Issue: 10
Pages: 2068-76
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Publication
21555485 | J:177293
First Author: Brigl M
Year: 2011
Journal: J Exp Med
Title: Innate and cytokine-driven signals, rather than microbial antigens, dominate in natural killer T cell activation during microbial infection.
Volume: 208
Issue: 6
Pages: 1163-77
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Publication
16920939 | J:139547
First Author: Aprahamian T
Year: 2006
Journal: J Immunol
Title: Simvastatin treatment ameliorates autoimmune disease associated with accelerated atherosclerosis in a murine lupus model.
Volume: 177
Issue: 5
Pages: 3028-34
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Publication
27920091 | J:246468
First Author: Driver JP
Year: 2017
Journal: Diabetes
Title: Interferon-γ Limits Diabetogenic CD8+ T-Cell Effector Responses in Type 1 Diabetes.
Volume: 66
Issue: 3
Pages: 710-721
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Publication
11313413 | J:69051
First Author: Ortmann R
Year: 2001
Journal: J Immunol
Title: A heritable defect in IL-12 signaling in B10.Q/J mice. I. In vitro analysis.
Volume: 166
Issue: 9
Pages: 5712-9
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Publication
17114431 | J:140600
First Author: Li Q
Year: 2006
Journal: J Immunol
Title: IL-12-programmed long-term CD8+ T cell responses require STAT4.
Volume: 177
Issue: 11
Pages: 7618-25
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Publication
11956247 | J:76087
First Author: O'Kelly J
Year: 2002
Journal: J Clin Invest
Title: Normal myelopoiesis but abnormal T lymphocyte responses in vitamin D receptor knockout mice.
Volume: 109
Issue: 8
Pages: 1091-9
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Publication
15778345 | J:110005
First Author: Arsenescu R
Year: 2005
Journal: J Immunol
Title: IL-12 induction of mRNA encoding substance P in murine macrophages from the spleen and sites of inflammation.
Volume: 174
Issue: 7
Pages: 3906-11
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Publication
28550203 | J:250655
First Author: Takahashi R
Year: 2017
Journal: J Immunol
Title: SOCS1 Is a Key Molecule That Prevents Regulatory T Cell Plasticity under Inflammatory Conditions.
Volume: 199
Issue: 1
Pages: 149-158
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Publication
11748115 | J:103357
First Author: Afanasyeva M
Year: 2001
Journal: Circulation
Title: Interleukin-12 receptor/STAT4 signaling is required for the development of autoimmune myocarditis in mice by an interferon-gamma-independent pathway.
Volume: 104
Issue: 25
Pages: 3145-51
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Publication
11441092 | J:331611
First Author: Zhu H
Year: 2001
Journal: J Immunol
Title: Unexpected characteristics of the IFN-gamma reporters in nontransformed T cells.
Volume: 167
Issue: 2
Pages: 855-65
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Publication
12902482 | J:84809
First Author: Corn RA
Year: 2003
Journal: J Immunol
Title: T cell-intrinsic requirement for NF-kappa B induction in postdifferentiation IFN-gamma production and clonal expansion in a Th1 response.
Volume: 171
Issue: 4
Pages: 1816-24
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Publication
20876105 | J:165405
First Author: Miyake T
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: IκBζ is essential for natural killer cell activation in response to IL-12 and IL-18.
Volume: 107
Issue: 41
Pages: 17680-5
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Publication
18263766 | J:134459
First Author: Page KM
Year: 2008
Journal: J Leukoc Biol
Title: Natural killer cells from protein kinase C theta-/- mice stimulated with interleukin-12 are deficient in production of interferon-gamma.
Volume: 83
Issue: 5
Pages: 1267-76
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Publication
22586032 | J:188872
First Author: Kwon MJ
Year: 2012
Journal: J Immunol
Title: Protein kinase C-θ promotes Th17 differentiation via upregulation of Stat3.
Volume: 188
Issue: 12
Pages: 5887-97
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Publication
24788550 | J:216101
First Author: Wachowicz K
Year: 2014
Journal: PLoS One
Title: Protein kinase C θ regulates the phenotype of murine CD4+ Th17 cells.
Volume: 9
Issue: 5
Pages: e96401
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Publication
28733487 | J:251010
First Author: Carson WF 4th
Year: 2017
Journal: J Immunol
Title: The STAT4/MLL1 Epigenetic Axis Regulates the Antimicrobial Functions of Murine Macrophages.
Volume: 199
Issue: 5
Pages: 1865-1874
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Publication
15778369 | J:97961
First Author: Takatori H
Year: 2005
Journal: J Immunol
Title: Stat5a inhibits IL-12-induced Th1 cell differentiation through the induction of suppressor of cytokine signaling 3 expression.
Volume: 174
Issue: 7
Pages: 4105-12
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Publication
15661872 | J:96424
First Author: Krymskaya L
Year: 2005
Journal: J Immunol
Title: Polarized development of memory cell-like IFN-gamma-producing cells in the absence of TCR zeta-chain.
Volume: 174
Issue: 3
Pages: 1188-95
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Publication
26059830 | J:242733
First Author: Schaller M
Year: 2015
Journal: J Leukoc Biol
Title: Epigenetic regulation of IL-12-dependent T cell proliferation.
Volume: 98
Issue: 4
Pages: 601-13
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Publication
11465102 | J:69512
First Author: Park WR
Year: 2001
Journal: Eur J Immunol
Title: CD28 costimulation is required not only to induce IL-12 receptor but also to render janus kinases/STAT4 responsive to IL-12 stimulation in TCR-triggered T cells.
Volume: 31
Issue: 5
Pages: 1456-64
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Publication
11698474 | J:72684
First Author: Matsumoto M
Year: 2001
Journal: J Immunol
Title: Inability of IL-12 to down-regulate IgE synthesis due to defective production of IFN-gamma in atopic NC/Nga mice.
Volume: 167
Issue: 10
Pages: 5955-62
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Publication
10975850 | J:64565
First Author: Elhofy A
Year: 2000
Journal: J Immunol
Title: Salmonella infection does not increase expression and activity of the high affinity IL-12 receptor.
Volume: 165
Issue: 6
Pages: 3324-32
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Publication
12036584 | J:76710
First Author: Waldvogel AS
Year: 2002
Journal: Gene
Title: Regulation of bovine IL-12R beta 2 subunit mRNA expression in bovine lymph node cells.
Volume: 289
Issue: 1-2
Pages: 61-7
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Publication
15187137 | J:90823
First Author: Mattner J
Year: 2004
Journal: J Immunol
Title: Protection against progressive leishmaniasis by IFN-beta.
Volume: 172
Issue: 12
Pages: 7574-82
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Publication
16949558 | J:116594
First Author: Frisancho-Kiss S
Year: 2006
Journal: Brain Res
Title: Sex differences in coxsackievirus B3-induced myocarditis: IL-12Rbeta1 signaling and IFN-gamma increase inflammation in males independent from STAT4.
Volume: 1126
Issue: 1
Pages: 139-47
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Publication
16520391 | J:123705
First Author: Usui T
Year: 2006
Journal: J Exp Med
Title: T-bet regulates Th1 responses through essential effects on GATA-3 function rather than on IFNG gene acetylation and transcription.
Volume: 203
Issue: 3
Pages: 755-66
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Publication
11359836 | J:128017
First Author: Nishikomori R
Year: 2001
Journal: J Immunol
Title: BALB/c mice bearing a transgenic IL-12 receptor beta 2 gene exhibit a nonhealing phenotype to Leishmania major infection despite intact IL-12 signaling.
Volume: 166
Issue: 11
Pages: 6776-83
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Publication
16951332 | J:138052
First Author: Suto A
Year: 2006
Journal: J Immunol
Title: IL-21 inhibits IFN-gamma production in developing Th1 cells through the repression of Eomesodermin expression.
Volume: 177
Issue: 6
Pages: 3721-7
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Publication
24958858 | J:212176
First Author: Kissick HT
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: Androgens alter T-cell immunity by inhibiting T-helper 1 differentiation.
Volume: 111
Issue: 27
Pages: 9887-92
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Publication
24935968 | J:217839
First Author: Köther K
Year: 2014
Journal: FASEB J
Title: MAPKAP kinase 3 suppresses Ifng gene expression and attenuates NK cell cytotoxicity and Th1 CD4 T-cell development upon influenza A virus infection.
Volume: 28
Issue: 10
Pages: 4235-46
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Publication
25994622 | J:284622
 
First Author: Wu W
Year: 2015
Journal: Sci Rep
Title: TLR ligand induced IL-6 counter-regulates the anti-viral CD8(+) T cell response during an acute retrovirus infection.
Volume: 5
Pages: 10501
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Publication
31434804 | J:289760
 
First Author: Xie MM
Year: 2019
Journal: JCI Insight
Title: Follicular regulatory T cells inhibit the development of granzyme B-expressing follicular helper T cells.
Volume: 4
Issue: 16
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Publication
29222089 | J:318905
 
First Author: Rapp M
Year: 2017
Journal: Sci Immunol
Title: Core-binding factor β and Runx transcription factors promote adaptive natural killer cell responses.
Volume: 2
Issue: 18
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Publication
37344599 | J:340087
First Author: Li J
Year: 2023
Journal: Nature
Title: Histone demethylase KDM5D upregulation drives sex differences in colon cancer.
Volume: 619
Issue: 7970
Pages: 632-639
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Protein
Q99ML3
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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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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Publication
24614195 | J:208402
First Author: Chen X
Year: 2014
Journal: Lab Invest
Title: Tapasin modification on the intracellular epitope HBcAg18-27 enhances HBV-specific CTL immune response and inhibits hepatitis B virus replication in vivo.
Volume: 94
Issue: 5
Pages: 478-90
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Publication
26793623 | J:286095
 
First Author: Ruiz J
Year: 2015
Journal: Front Cell Infect Microbiol
Title: Systemic Activation of TLR3-Dependent TRIF Signaling Confers Host Defense against Gram-Negative Bacteria in the Intestine.
Volume: 5
Pages: 105
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Publication
11786421 | J:73727
First Author: Maier J
Year: 2002
Journal: Am J Pathol
Title: Regulation of signal transducer and activator of transcription and suppressor of cytokine-signaling gene expression in the brain of mice with astrocyte-targeted production of interleukin-12 or experimental autoimmune encephalomyelitis.
Volume: 160
Issue: 1
Pages: 271-88
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Publication
15546392 | J:95527
 
First Author: Berenson LS
Year: 2004
Journal: Immunol Rev
Title: Issues in T-helper 1 development--resolved and unresolved.
Volume: 202
Pages: 157-74
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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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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
Q71UV3
Organism: Mus musculus/domesticus
Length: 183  
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
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
P42225
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: false
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Protein
P42232
Organism: Mus musculus/domesticus
Length: 786  
Fragment?: false
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Protein
P42230
Organism: Mus musculus/domesticus
Length: 793  
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
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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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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