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Search results 901 to 1000 out of 1010 for Stat5a

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Type Details Score
Genotype
Genotype
Symbol: Stat5a/Stat5a Stat5b/Stat5b
Background: involves: 129 * C57BL/6
Zygosity: cx
Has Mutant Allele: true
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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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Publication
8976384 | J:37320
First Author: Chen KS
Year: 1996
Journal: Cytogenet Cell Genet
Title: Cloning and chromosomal localization of the rat Stat5 and Yy1 genes.
Volume: 74
Issue: 4
Pages: 277-80
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Publication
11909942 | J:98590
First Author: Zirngibl RA
Year: 2002
Journal: Mol Cell Biol
Title: Enhanced endotoxin sensitivity in fps/fes-null mice with minimal defects in hematopoietic homeostasis.
Volume: 22
Issue: 8
Pages: 2472-86
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Publication
36773294 | J:333452
First Author: Mandarano AH
Year: 2023
Journal: Cell Rep
Title: DRAK2 contributes to type 1 diabetes by negatively regulating IL-2 sensitivity to alter regulatory T cell development.
Volume: 42
Issue: 2
Pages: 112106
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Publication
21106534 | J:175322
First Author: Dhennin-Duthille I
Year: 2011
Journal: J Biol Chem
Title: The tumor suppressor hTid1 inhibits STAT5b activity via functional interaction.
Volume: 286
Issue: 7
Pages: 5034-42
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Publication
14556656 | J:86061
First Author: Hiai H
Year: 2003
Journal: Cancer Sci
Title: Pre-B lymphomas in SL/Kh mice: a multifactorial disease model.
Volume: 94
Issue: 10
Pages: 847-50
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Publication
27721401 | J:239246
First Author: Tsuruyama T
Year: 2017
Journal: Oncogene
Title: Hotspots of MLV integration in the hematopoietic tumor genome.
Volume: 36
Issue: 9
Pages: 1169-1175
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Publication
32966801 | J:297407
First Author: Hennighausen L
Year: 2020
Journal: Cell Rep
Title: Activation of the SARS-CoV-2 Receptor Ace2 through JAK/STAT-Dependent Enhancers during Pregnancy.
Volume: 32
Issue: 13
Pages: 108199
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Publication
12456789 | J:125450
First Author: Grimm SL
Year: 2002
Journal: Mol Endocrinol
Title: Disruption of steroid and prolactin receptor patterning in the mammary gland correlates with a block in lobuloalveolar development.
Volume: 16
Issue: 12
Pages: 2675-91
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Publication
11804960 | J:108582
First Author: Riedlinger G
Year: 2002
Journal: Biol Reprod
Title: Bcl-x is not required for maintenance of follicles and corpus luteum in the postnatal mouse ovary.
Volume: 66
Issue: 2
Pages: 438-44
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Publication
18577706 | J:138893
First Author: Cohen PA
Year: 2008
Journal: Blood
Title: STAT3- and STAT5-dependent pathways competitively regulate the pan-differentiation of CD34pos cells into tumor-competent dendritic cells.
Volume: 112
Issue: 5
Pages: 1832-43
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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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Publication
16837552 | J:114489
First Author: Muraoka-Cook RS
Year: 2006
Journal: Mol Biol Cell
Title: The intracellular domain of ErbB4 induces differentiation of mammary epithelial cells.
Volume: 17
Issue: 9
Pages: 4118-29
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Publication
19596786 | J:152606
First Author: Muraoka-Cook RS
Year: 2009
Journal: Mol Cell Biol
Title: ErbB4 splice variants Cyt1 and Cyt2 differ by 16 amino acids and exert opposing effects on the mammary epithelium in vivo.
Volume: 29
Issue: 18
Pages: 4935-48
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Publication
11773439 | J:197519
First Author: Aoki N
Year: 2002
Journal: Mol Endocrinol
Title: A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus.
Volume: 16
Issue: 1
Pages: 58-69
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Publication
10482620 | J:76636
First Author: Stegalkina SS
Year: 1999
Journal: J Virol
Title: Transcription originating in the long terminal repeats of the endogenous mouse mammary tumor virus MTV-3 is activated in Stat5a-null mice and picks Up hitchhiking exons.
Volume: 73
Issue: 10
Pages: 8669-76
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Publication
17890450 | J:129993
First Author: Bessette K
Year: 2008
Journal: Blood
Title: A Stat5b transgene is capable of inducing CD8+ lymphoblastic lymphoma in the absence of normal TCR/MHC signaling.
Volume: 111
Issue: 1
Pages: 344-50
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Publication
25548153 | J:331322
First Author: Ji Y
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: miR-155 augments CD8+ T-cell antitumor activity in lymphoreplete hosts by enhancing responsiveness to homeostatic γc cytokines.
Volume: 112
Issue: 2
Pages: 476-81
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Publication
37030590 | J:338933
First Author: Kanagaratham C
Year: 2023
Journal: J Allergy Clin Immunol
Title: IgG:FcγRIIb signals block effector programs of IgE:FcεRI-activated mast cells but spare survival pathways.
Volume: 152
Issue: 2
Pages: 453-468
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Publication
12049767 | J:77170
First Author: Boussadia O
Year: 2002
Journal: Mech Dev
Title: E-cadherin is a survival factor for the lactating mouse mammary gland.
Volume: 115
Issue: 1-2
Pages: 53-62
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Publication
10331984 | J:54980
First Author: Luetteke NC
Year: 1999
Journal: Development
Title: Targeted inactivation of the EGF and amphiregulin genes reveals distinct roles for EGF receptor ligands in mouse mammary gland development.
Volume: 126
Issue: 12
Pages: 2739-50
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Publication
17071600 | J:114569
First Author: Williams TM
Year: 2006
Journal: Am J Pathol
Title: Stromal and epithelial caveolin-1 both confer a protective effect against mammary hyperplasia and tumorigenesis: Caveolin-1 antagonizes cyclin D1 function in mammary epithelial cells.
Volume: 169
Issue: 5
Pages: 1784-801
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Publication
11287618 | J:68832
First Author: Hoffmeyer A
Year: 2001
Journal: Mol Cell Biol
Title: Gadd45gamma is dispensable for normal mouse development and T-cell proliferation.
Volume: 21
Issue: 9
Pages: 3137-43
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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
10523632 | J:84535
First Author: Senis Y
Year: 1999
Journal: Mol Cell Biol
Title: Targeted disruption of the murine fps/fes proto-oncogene reveals that Fps/Fes kinase activity is dispensable for hematopoiesis.
Volume: 19
Issue: 11
Pages: 7436-46
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Publication
11875116 | J:75082
First Author: Shillingford JM
Year: 2002
Journal: Mol Endocrinol
Title: Jak2 is an essential tyrosine kinase involved in pregnancy-mediated development of mammary secretory epithelium.
Volume: 16
Issue: 3
Pages: 563-70
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Publication
36232979 | J:330902
 
First Author: Kim U
Year: 2022
Journal: Int J Mol Sci
Title: Mammary-Enriched Transcription Factors Synergize to Activate the Wap Super-Enhancer for Mammary Gland Development.
Volume: 23
Issue: 19
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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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Publication
26250110 | J:356929
First Author: Yoo KH
Year: 2015
Journal: Nucleic Acids Res
Title: Loss of EZH2 results in precocious mammary gland development and activation of STAT5-dependent genes.
Volume: 43
Issue: 18
Pages: 8774-89
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Publication
22348097 | J:347891
First Author: Tsuruyama T
Year: 2012
Journal: PLoS One
Title: In vitro murine leukemia retroviral integration and structure fluctuation of target DNA.
Volume: 7
Issue: 2
Pages: e31533
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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
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
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
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: LĂ©cine 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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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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