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Search results 401 to 500 out of 773 for Nfat5

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Hits by Pathway

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Type Details Score
Publication
30232334 | J:267623
First Author: Essig K
Year: 2018
Journal: Nat Commun
Title: Roquin targets mRNAs in a 3'-UTR-specific manner by different modes of regulation.
Volume: 9
Issue: 1
Pages: 3810
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Publication
17846422 | J:125198
First Author: Magnúsdóttir E
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Epidermal terminal differentiation depends on B lymphocyte-induced maturation protein-1.
Volume: 104
Issue: 38
Pages: 14988-93
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Publication
36068919 | J:360478
First Author: Xu J
Year: 2023
Journal: Mol Ther
Title: NLRC3 expression in macrophage impairs glycolysis and host immune defense by modulating the NF-κB-NFAT5 complex during septic immunosuppression.
Volume: 31
Issue: 1
Pages: 154-173
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Publication
19436108 | J:150581
First Author: Chen S
Year: 2009
Journal: J Clin Invest
Title: Tonicity-dependent induction of Sgk1 expression has a potential role in dehydration-induced natriuresis in rodents.
Volume: 119
Issue: 6
Pages: 1647-58
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Publication
26436647 | J:227488
First Author: Ying W
Year: 2015
Journal: J Clin Invest
Title: MicroRNA-223 is a crucial mediator of PPARγ-regulated alternative macrophage activation.
Volume: 125
Issue: 11
Pages: 4149-59
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Publication
22287635 | J:197721
First Author: Ortells MC
Year: 2012
Journal: Nucleic Acids Res
Title: Transcriptional regulation of gene expression during osmotic stress responses by the mammalian target of rapamycin.
Volume: 40
Issue: 10
Pages: 4368-84
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Publication
26220925 | J:227285
First Author: Izumi Y
Year: 2015
Journal: Physiol Genomics
Title: RNA-Seq analysis of high NaCl-induced gene expression.
Volume: 47
Issue: 10
Pages: 500-13
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Publication
31033226 | J:304483
First Author: Wang H
Year: 2019
Journal: Physiol Rep
Title: Sickle cell disease up-regulates vasopressin, aquaporin 2, urea transporter A1, Na-K-Cl cotransporter 2, and epithelial Na channels in the mouse kidney medulla despite compromising urinary concentration ability.
Volume: 7
Issue: 8
Pages: e14066
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Publication
24990897 | J:214240
First Author: Zhou X
Year: 2014
Journal: Am J Physiol Renal Physiol
Title: Leishmania infantum-chagasi activates SHP-1 and reduces NFAT5/TonEBP activity in the mouse kidney inner medulla.
Volume: 307
Issue: 5
Pages: F516-24
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Publication
24990896 | J:214241
First Author: Quadri S
Year: 2014
Journal: Am J Physiol Renal Physiol
Title: Regulation of (pro)renin receptor expression in mIMCD via the GSK-3β-NFAT5-SIRT-1 signaling pathway.
Volume: 307
Issue: 5
Pages: F593-600
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Publication
12651950 | -
First Author: Arnesano F
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.
Volume: 100
Issue: 7
Pages: 3814-9
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Publication
15380510 | -
First Author: Aggarwal BB
Year: 2004
Journal: Cancer Cell
Title: Nuclear factor-kappaB: the enemy within.
Volume: 6
Issue: 3
Pages: 203-8
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Publication
14671122 | -
First Author: Misaghi S
Year: 2004
Journal: J Virol
Title: Structural and functional analysis of human cytomegalovirus US3 protein.
Volume: 78
Issue: 1
Pages: 413-23
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Publication
15513926 | -
First Author: Dransart E
Year: 2005
Journal: J Biol Chem
Title: Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors.
Volume: 280
Issue: 6
Pages: 4674-83
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Publication
15290350 | -
First Author: Pepe I
Year: 2004
Journal: Amino Acids
Title: Biochemical mechanisms for a possible involvement of the transglutaminase activity in the pathogenesis of the polyglutamine diseases: minireview article.
Volume: 26
Issue: 4
Pages: 431-4
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Publication
15102497 | -
First Author: Gurevich VV
Year: 2004
Journal: Trends Pharmacol Sci
Title: The molecular acrobatics of arrestin activation.
Volume: 25
Issue: 2
Pages: 105-11
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Publication
14756796 | -
First Author: Maamar H
Year: 2004
Journal: Mol Microbiol
Title: Cellulolysis is severely affected in Clostridium cellulolyticum strain cipCMut1.
Volume: 51
Issue: 2
Pages: 589-98
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Protein Domain
IPR014756 | Ig_E-set
Type: Homologous_superfamily
Description: The immunoglobulin (Ig) like fold, which consists of a β-sandwich of seven or more strands in two sheets with a greek-key topology, is one of the most common protein modules found in animals. Many different unrelated proteins share an Ig-like fold, which is often involved in interactions, commonly with other Ig-like domains via their β-sheets []. Of these, the "early"set (E set) domains are possibly related to the immunoglobulin () and/or fibronectin type III () Ig-like protein superfamilies. Ig-like E set domains include:C-terminal domain of certain transcription factors, such as the pro-inflammatory transcription factor NF-kappaB, and the T-cell transcription factors NFAT1 and NFAT5 [].Ig-like domains of sugar-utilising enzymes, such as galactose oxidase (C-terminal domain), sialidase (linker domain), and maltogenic amylase (N-terminal domain).C-terminal domain of arthropod haemocyanin, where many loops are inserted into the fold. These proteins act as dioxygen-transporting proteins.C-terminal domain of class II viral fusion proteins. These envelope glycoproteins are responsible for membrane fusion with target cells during viral invasion.Cytomegaloviral US (unique short) proteins. These type I membrane proteins help suppress the host immune response by modulating surface expression of MHC class I molecules [].Molybdenium-containing oxidoreductase-like dimerisation domain found in enzymes such as sulphite reductase.ML domains found in cholesterol-binding epididymal secretory protein E1, and in a major house-dust mite allergen; ML domains are implicated in lipid recognition, particularly the recognition of pathogen-related products.Rho-GDI-like signalling proteins, which regulate the activity of small G proteins [].Cytoplasmic domain of inward rectifier potassium channels such as Girk1 and Kirbac1.1. These channels act as regulators of excitability in eukaryotic cells.N-terminal domain of transglutaminases, including coagulation factor XIII; many loops are inserted into the fold in these proteins. These proteins act to catalyse the cross-linking of various protein substrates [].Filamin repeat rod domain found in proteins such as the F-actin cross-linking gelation factor ABP-120. These proteins interact with a variety of cellular proteins, acting as signalling scaffolds [].Arrestin family of proteins, which contain a tandem repeat of two elaborated Ig-like domains contacting each other head-to-head. These proteins are key to the redirection of GPCR signals to alternative pathways [].C-terminal domain of arginine-specific cysteine proteases, such as Gingipain-R, which act as major virulence factors of Porphyromonas gingivalis (Bacteroides gingivalis).Copper-resistance proteins, such as CopC, which act as copper-trafficking proteins [].Cellulosomal scaffoldin proteins, such as CipC module x2.1. These proteins act as scaffolding proteins of cellulosomes, which contain cellulose-degrading enzymes [].Quinohaemoprotein amine dehydrogenases (A chain), which contain a tandem repeat of two Ig-like domains. These proteins function in electron transfer reactions.Internalin Ig-like domains, which are truncated and fused to a leucine-rich repeat domain. These proteins are required for host cell invasion of Listeria species.
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Protein
O88188
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q9JHF9
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
Q8C4B4
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
O35075
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
M0QWG6
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: false
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Protein
A0A087WQZ9
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: false
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Protein
M0QWR1
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: false
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Protein
F7BA91
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: true
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Protein
Q64HC9
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: false
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Protein
Q14AM4
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
Q921U5
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
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Protein
Q3TBA1
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: true
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Publication
15516996 | -
First Author: Feng Y
Year: 2004
Journal: Nat Cell Biol
Title: The many faces of filamin: a versatile molecular scaffold for cell motility and signalling.
Volume: 6
Issue: 11
Pages: 1034-8
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Protein
O55057
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
P02816
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: false
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Protein
Q9D4H1
Organism: Mus musculus/domesticus
Length: 924  
Fragment?: false
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Protein
Q99PT1
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: false
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Protein
Q61599
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: false
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Protein
Q62160
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
Q3U095
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
Q52KP5
Organism: Mus musculus/domesticus
Length: 543  
Fragment?: false
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Protein
G5E897
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
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Protein
Q9Z0J0
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q9Z2R6
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
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Protein
A0A1L1SQH9
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: false
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Protein
Q99N75
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
S4R2R1
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: false
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Protein
Q76I99
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
B1AQD9
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: false
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Protein
E9PZX5
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
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Protein
Q8BSK6
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: false
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Protein
A0A3B2WCS7
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: false
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Protein
Q3UWC0
Organism: Mus musculus/domesticus
Length: 532  
Fragment?: false
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Protein
F7CZG3
Organism: Mus musculus/domesticus
Length: 871  
Fragment?: true
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Protein
Q3V299
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
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Protein
Q3UU48
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: false
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Protein
Q9JJ37
Organism: Mus musculus/domesticus
Length: 65  
Fragment?: true
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Protein
Q3URU9
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
Q8K3J6
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
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Protein
Q6Y684
Organism: Mus musculus/domesticus
Length: 61  
Fragment?: false
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Protein
F6T0L5
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: true
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Protein
A0A2I3BS02
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
E0CZE1
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
D3Z617
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Protein
Q8C984
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
Q3U3W7
Organism: Mus musculus/domesticus
Length: 790  
Fragment?: true
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Protein
Q7TPQ2
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
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Protein
Q3TXQ4
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q7TMG2
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: true
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Protein
E0CX47
Organism: Mus musculus/domesticus
Length: 564  
Fragment?: false
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Protein
Q3KQH7
Organism: Mus musculus/domesticus
Length: 555  
Fragment?: false
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Protein
V9GZF6
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: true
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Protein
Q8K2U5
Organism: Mus musculus/domesticus
Length: 516  
Fragment?: true
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Protein
G3UXE8
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: false
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Protein
D3Z433
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
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Protein
D3Z4E7
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: false
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Protein
A0A0G2JDM9
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: true
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Protein
E0CYW5
Organism: Mus musculus/domesticus
Length: 543  
Fragment?: false
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Protein
Q8BT78
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: true
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Protein
Q3U8F7
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
D3YWL7
Organism: Mus musculus/domesticus
Length: 50  
Fragment?: true
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Protein
Q8VCY2
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: true
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Protein
D6RG50
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
D3Z6W0
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
F6X333
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: true
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Protein
A0A0N4SV85
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: false
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Protein
A0A2I3BQN2
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: true
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Protein
A0A0N4SVH4
Organism: Mus musculus/domesticus
Length: 89  
Fragment?: true
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Protein
B9EKK6
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: false
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Protein
A0A0R4J0E5
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
E9PY98
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: true
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Protein
F7AVL7
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
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Protein
E9PX96
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: false
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Protein
A0A0N4SV27
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: true
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Protein
B1AQD7
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
D6RE32
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: false
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Protein
Q3U3C2
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q3TDQ8
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
Q64367
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
Q9D2X6
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
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Protein
Q3SXH3
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
E9PXC9
Organism: Mus musculus/domesticus
Length: 542  
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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom