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Search results 501 to 531 out of 531 for Jak1

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0.018s

Type

Details

Score

Publication

25825724 | J:220454

First Author:	Hammarén HM
Year:	2015
Journal:	Proc Natl Acad Sci U S A
Title:	ATP binding to the pseudokinase domain of JAK2 is critical for pathogenic activation.
Volume:	112
Issue:	15
Pages:	4642-7

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Publication

25129481 | J:227596

First Author:	Xing L
Year:	2014
Journal:	Nat Med
Title:	Alopecia areata is driven by cytotoxic T lymphocytes and is reversed by JAK inhibition.
Volume:	20
Issue:	9
Pages:	1043-9

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Publication

28708884 | J:247362

First Author:	Murakami K
Year:	2017
Journal:	PLoS One
Title:	A Jak1/2 inhibitor, baricitinib, inhibits osteoclastogenesis by suppressing RANKL expression in osteoblasts in vitro.
Volume:	12
Issue:	7
Pages:	e0181126

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Publication

29016674 | J:247148

First Author:	Wilbers RHP
Year:	2017
Journal:	PLoS One
Title:	Re-evaluation of IL-10 signaling reveals novel insights on the contribution of the intracellular domain of the IL-10R2 chain.
Volume:	12
Issue:	10
Pages:	e0186317

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Publication

27802075 | J:247177

First Author:	Raje V
Year:	2017
Journal:	Endocrinology
Title:	Kinase Inactive Tyrosine Kinase (Tyk2) Supports Differentiation of Brown Fat Cells.
Volume:	158
Issue:	1
Pages:	148-157

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Publication

31748225 | J:298335

First Author:	Hwang JY
Year:	2019
Journal:	Immunohorizons
Title:	Dissociating STAT4 and STAT5 Signaling Inhibitory Functions of SOCS3: Effects on CD8 T Cell Responses.
Volume:	3
Issue:	11
Pages:	547-558

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Publication

26956044 | J:309327

First Author:	Hsu TI
Year:	2016
Journal:	Oncotarget
Title:	Positive feedback regulation between IL10 and EGFR promotes lung cancer formation.
Volume:	7
Issue:	15
Pages:	20840-54

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Publication

34535769 | J:312446

First Author:	Heltemes-Harris LM
Year:	2021
Journal:	Oncogene
Title:	Identification of mutations that cooperate with defects in B cell transcription factors to initiate leukemia.
Volume:	40
Issue:	43
Pages:	6166-6179

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Publication

10848598 | J:124518

First Author:	Pang Q
Year:	2000
Journal:	Mol Cell Biol
Title:	The Fanconi anemia protein FANCC binds to and facilitates the activation of STAT1 by gamma interferon and hematopoietic growth factors.
Volume:	20
Issue:	13
Pages:	4724-35

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Publication

31680865 | J:332408

First Author:	Sims SG
Year:	2019
Journal:	Front Cell Neurosci
Title:	Janus Kinase 1 Is Required for Transcriptional Reprograming of Murine Astrocytes in Response to Endoplasmic Reticulum Stress.
Volume:	13

Pages:	446

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Publication

15364614 | J:162844

First Author:	Dawn B
Year:	2004
Journal:	Cardiovasc Res
Title:	IL-6 plays an obligatory role in late preconditioning via JAK-STAT signaling and upregulation of iNOS and COX-2.
Volume:	64
Issue:	1
Pages:	61-71

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Publication

32818015 | J:310337

First Author:	Chen X
Year:	2020
Journal:	Mol Vis
Title:	Interleukin-6 promotes proliferative vitreoretinopathy by inducing epithelial-mesenchymal transition via the JAK1/STAT3 signaling pathway.
Volume:	26

Pages:	517-529

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Publication

2156206 | J:10367

First Author:	Krolewski JJ
Year:	1990
Journal:	Oncogene
Title:	Identification and chromosomal mapping of new human tyrosine kinase genes.
Volume:	5
Issue:	3
Pages:	277-82

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Protein Domain

IPR016045 | Tyr_kinase_non-rcpt_TYK2_N

Type:

Domain

Description:

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].TYK2 was first identified by low-stringency hybridisation screening of ahuman lymphoid cDNA library with the catalytic domain of proto-oncogene c-fms []. Mouse and puffer fish orthlogues have also been identified. In common with JAK1 and JAK2, and by contrast with JAK3, TYK2 appears to be ubiquitously expressed. This entry represents the N-terminal region of TYK2.

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Protein Domain

IPR020693 | Tyr_kinase_non-rcpt_Jak2

Type:

Family

Description:

Janus kinases (JAKs) are tyrosine kinases that function in membrane-proximal signalling events initiated by a variety of extracellular factors binding to cell surface receptors []. Many type I and II cytokine receptors lack a protein tyrosine kinase domain and rely on JAKs to initiate the cytoplasmic signal transduction cascade. Ligand binding induces oligomerisation of the receptors, which then activates the cytoplasmic receptor-associated JAKs. These subsequently phosphorylate tyrosine residues along the receptor chains with which they are associated. The phosphotyrosine residues are a target for a variety of SH2 domain-containing transducer proteins. Amongst these are the signal transducers and activators of transcription (STAT) proteins, which, after binding to the receptor chains, are phosphorylated by the JAK proteins. Phosphorylation enables the STAT proteins to dimerise and translocate into the nucleus, where they alter the expression of cytokine-regulated genes. This system is known as the JAK-STAT pathway.Four mammalian JAK family members have been identified: JAK1, JAK2, JAK3, and TYK2. They are relatively large kinases of approximately 1150 amino acids, with molecular weights of ~120-130kDa. Their amino acid sequences are characterised by the presence of 7 highly conserved domains, termed JAK homology (JH) domains. The C-terminal domain (JH1) is responsible for the tyrosine kinase function. The next domain in the sequence (JH2) is known as the tyrosine kinase-like domain, as its sequence shows high similarity to functional kinases but does not possess any catalytic activity. Although the function of this domain is not well established, there is some evidence for a regulatory role on the JH1 domain, thus modulating catalytic activity. The N-terminal portion of the JAKs (spanning JH7 to JH3) is important for receptor association and non-catalytic activity, and consists of JH3-JH4, which is homologous to the SH2 domain, and lastly JH5-JH7, which is a FERM domain.This entry represents the non-receptor tyrosine kinase JAK2 []. JAK2 was initially cloned using a PCR-based strategy utilising primers corresponding to conserved motifs within the catalytic domain of protein-tyrosine kinases []. In common with JAK1 and TYK2, and by contrast with JAK3, JAK2 appears to be ubiquitously expressed.

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Publication

9208871 | J:41587

First Author:	Pestka S
Year:	1997
Journal:	Semin Oncol
Title:	The interferon receptors.
Volume:	24
Issue:	3 Suppl 9
Pages:	S9-18-S9-40

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Protein

Q3UZ30

Organism:	Mus musculus/domesticus
Length:	333
Fragment?:	true

•

Protein

Q9R117

Organism:	Mus musculus/domesticus
Length:	1184
Fragment?:	false

•

Protein

Q2M4G5

Organism:	Mus musculus/domesticus
Length:	1180
Fragment?:	false

•

Protein

E9QJS1

Organism:	Mus musculus/domesticus
Length:	1207
Fragment?:	false

•

Protein

Q3U447

Organism:	Mus musculus/domesticus
Length:	1207
Fragment?:	false

•

Protein

Q3TDN4

Organism:	Mus musculus/domesticus
Length:	1159
Fragment?:	true

•

Protein

Q3TIS9

Organism:	Mus musculus/domesticus
Length:	1184
Fragment?:	false

•

Protein

A0A494BBB9

Organism:	Mus musculus/domesticus
Length:	638
Fragment?:	true

•

Protein

Q62120

Organism:	Mus musculus/domesticus
Length:	1132
Fragment?:	false

•

Protein

Q62137

Organism:	Mus musculus/domesticus
Length:	1100
Fragment?:	false

•

Protein

P97423

Organism:	Mus musculus/domesticus
Length:	1081
Fragment?:	false

•

Protein

A0A0R4J0R7

Organism:	Mus musculus/domesticus
Length:	1100
Fragment?:	false

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

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Publication

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

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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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