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Search results 5001 to 5100 out of 5471 for Tyr

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0.019s

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Hits by Strain

Type Details Score
Protein
Q8BVT9
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
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Protein
S4R2G0
Organism: Mus musculus/domesticus
Length: 841  
Fragment?: false
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Protein
G3UXG7
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: false
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Protein
Q3U1V3
Organism: Mus musculus/domesticus
Length: 689  
Fragment?: false
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Protein
A2A7S7
Organism: Mus musculus/domesticus
Length: 564  
Fragment?: false
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Protein
E9Q024
Organism: Mus musculus/domesticus
Length: 73  
Fragment?: false
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Protein
E9QQ25
Organism: Mus musculus/domesticus
Length: 3262  
Fragment?: false
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Protein
G5E8J9
Organism: Mus musculus/domesticus
Length: 929  
Fragment?: false
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Protein
D3Z007
Organism: Mus musculus/domesticus
Length: 517  
Fragment?: false
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Protein
E0CY42
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: true
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Protein
Q3V344
Organism: Mus musculus/domesticus
Length: 313  
Fragment?: false
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Protein
D3YUF5
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
B7ZMN9
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
Q3UVM5
Organism: Mus musculus/domesticus
Length: 626  
Fragment?: false
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Protein
Q8BJJ2
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: false
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Protein
E9PWQ6
Organism: Mus musculus/domesticus
Length: 973  
Fragment?: false
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Protein
S4R215
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
E9Q260
Organism: Mus musculus/domesticus
Length: 995  
Fragment?: false
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Protein
F2Z3Z9
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
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Protein
N0E4C0
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: false
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Protein
F2Z490
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
Q8C8R9
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: true
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Protein
G3XA66
Organism: Mus musculus/domesticus
Length: 298  
Fragment?: true
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Protein
Q8K2E5
Organism: Mus musculus/domesticus
Length: 1052  
Fragment?: false
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Protein
A0A140LJ30
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Protein
A0A494BBD3
Organism: Mus musculus/domesticus
Length: 775  
Fragment?: true
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Protein
Q3UJJ9
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: false
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Protein
A0A338P6E0
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
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Protein
F6ZQR2
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: true
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Protein
F8VPK5
Organism: Mus musculus/domesticus
Length: 1388  
Fragment?: false
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Protein
A0A0G2JDR5
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
G3UZJ5
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: true
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Protein
N0E634
Organism: Mus musculus/domesticus
Length: 39  
Fragment?: true
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Protein
Z4YL33
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: false
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Protein
E9Q2P5
Organism: Mus musculus/domesticus
Length: 1275  
Fragment?: false
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Protein
Q3TAT8
Organism: Mus musculus/domesticus
Length: 499  
Fragment?: false
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Protein
A2AUL9
Organism: Mus musculus/domesticus
Length: 653  
Fragment?: false
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Protein
D3Z3F4
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
A0A087WRH4
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
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Protein
Q3UKP8
Organism: Mus musculus/domesticus
Length: 1430  
Fragment?: false
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Protein
E9QKJ7
Organism: Mus musculus/domesticus
Length: 1188  
Fragment?: false
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Protein
D3YTP3
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
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Protein
Q9CW82
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: true
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Protein
G3UZX4
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: false
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Protein
A2AI69
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
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Protein
F7AEX1
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
Q3THP3
Organism: Mus musculus/domesticus
Length: 607  
Fragment?: false
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Protein
A2JY28
Organism: Mus musculus/domesticus
Length: 997  
Fragment?: false
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Protein
V9GXG6
Organism: Mus musculus/domesticus
Length: 55  
Fragment?: true
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Protein
F7BWC1
Organism: Mus musculus/domesticus
Length: 125  
Fragment?: true
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Protein
Q2M2N5
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
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Protein
Q91YS0
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: true
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Protein
N0E4C5
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
Q3US12
Organism: Mus musculus/domesticus
Length: 393  
Fragment?: false
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Protein
D3YVW0
Organism: Mus musculus/domesticus
Length: 286  
Fragment?: false
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Protein
N0E636
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: false
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Protein
Q8BX21
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: true
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Protein
Q3UZD6
Organism: Mus musculus/domesticus
Length: 1052  
Fragment?: false
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Protein
N0E463
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
G3UWU5
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
A0A087WSE3
Organism: Mus musculus/domesticus
Length: 3010  
Fragment?: true
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Protein
H3BJH6
Organism: Mus musculus/domesticus
Length: 688  
Fragment?: true
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Protein
Q9DBV8
Organism: Mus musculus/domesticus
Length: 1008  
Fragment?: false
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Protein
Q5U4H6
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
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Protein
B2RQQ7
Organism: Mus musculus/domesticus
Length: 1713  
Fragment?: false
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Protein
Q9DAG7
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: false
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Publication
17346243 | -
First Author: Higuchi S
Year: 2007
Journal: Clin Sci (Lond)
Title: Angiotensin II signal transduction through the AT1 receptor: novel insights into mechanisms and pathophysiology.
Volume: 112
Issue: 8
Pages: 417-28
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Publication
2666134 | -
First Author: Jakobi R
Year: 1989
Journal: Eur J Biochem
Title: Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta.
Volume: 183
Issue: 1
Pages: 227-33
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Publication
1856204 | -
First Author: Voss H
Year: 1991
Journal: J Biol Chem
Title: Structure of the gene encoding human casein kinase II subunit beta.
Volume: 266
Issue: 21
Pages: 13706-11
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Publication
8027080 | -
First Author: Reed JC
Year: 1994
Journal: J Biol Chem
Title: Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein kinase II.
Volume: 269
Issue: 27
Pages: 18192-200
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Publication
7737972 | -
First Author: Bidwai AP
Year: 1995
Journal: J Biol Chem
Title: Cloning and disruption of CKB1, the gene encoding the 38-kDa beta subunit of Saccharomyces cerevisiae casein kinase II (CKII). Deletion of CKII regulatory subunits elicits a salt-sensitive phenotype.
Volume: 270
Issue: 18
Pages: 10395-404
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Publication
12764229 | -
First Author: Manjasetty BA
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate.
Volume: 100
Issue: 12
Pages: 6992-7
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Publication
1549128 | -
First Author: Imai Y
Year: 1992
Journal: Mol Cell Biol
Title: Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases involved in the mating response.
Volume: 12
Issue: 4
Pages: 1827-34
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Publication
15166216 | -
First Author: Sansen S
Year: 2004
Journal: J Biol Chem
Title: Structural basis for inhibition of Aspergillus niger xylanase by triticum aestivum xylanase inhibitor-I.
Volume: 279
Issue: 34
Pages: 36022-8
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Publication
9096349 | -
First Author: Conway G
Year: 1997
Journal: Proc Natl Acad Sci U S A
Title: Jak1 kinase is required for cell migrations and anterior specification in zebrafish embryos.
Volume: 94
Issue: 7
Pages: 3082-7
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Publication
19660986 | -
First Author: Lai X
Year: 2009
Journal: Comput Biol Chem
Title: A multi-level model accounting for the effects of JAK2-STAT5 signal modulation in erythropoiesis.
Volume: 33
Issue: 4
Pages: 312-24
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Publication
19596999 | J:244680
First Author: Chang BY
Year: 2009
Journal: J Immunol
Title: JAK3 inhibition significantly attenuates psoriasiform skin inflammation in CD18 mutant PL/J mice.
Volume: 183
Issue: 3
Pages: 2183-92
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Publication
7526154 | -
First Author: Colamonici O
Year: 1994
Journal: Mol Cell Biol
Title: Direct binding to and tyrosine phosphorylation of the alpha subunit of the type I interferon receptor by p135tyk2 tyrosine kinase.
Volume: 14
Issue: 12
Pages: 8133-42
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Publication
1848670 | J:14190
First Author: Wilks AF
Year: 1991
Journal: Mol Cell Biol
Title: Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase.
Volume: 11
Issue: 4
Pages: 2057-65
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Publication
12133952 | -
First Author: Usacheva A
Year: 2002
Journal: J Immunol
Title: Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors.
Volume: 169
Issue: 3
Pages: 1302-8
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Publication
32750333 | -
First Author: Gruber CN
Year: 2020
Journal: Immunity
Title: Complex Autoinflammatory Syndrome Unveils Fundamental Principles of JAK1 Kinase Transcriptional and Biochemical Function.
Volume: 53
Issue: 3
Pages: 672-684.e11
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Publication
16239216 | -
First Author: Staerk J
Year: 2005
Journal: J Biol Chem
Title: JAK1 and Tyk2 activation by the homologous polycythemia vera JAK2 V617F mutation: cross-talk with IGF1 receptor.
Volume: 280
Issue: 51
Pages: 41893-9
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Protein Domain
IPR016251 | Tyr_kinase_non-rcpt_Jak/Tyk2
Type: Family
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 [].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 kinases Jak and Tyk2:Jak1 appears to be required in early development for specific cell migrations (epiboly), for the expression of the homeobox protein goosecoid and for the formation of anterior structures [].Jak2 plays a role in leptin signalling and in the control of body weight. It is involved in interleukin-3, and probably interleukin-23, signal transduction [].Jak3 is involved in the interleukin-2 and interleukin-4 signalling pathway. It phosphorylates STAT6, IRS1, IRS2 and PI3K [].Tyk2 is probably involved in intracellular signal transduction by being involved in the initiation of type I IFN signalling. It phosphorylates the interferon-alpha/beta receptor alpha chain [].
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Protein Domain
IPR020776 | Tyr_kinase_non-rcpt_Jak1
Type: Family
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 [].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 represents the non-receptor tyrosine kinase JAK1, which is involved in the IFN-alpha/beta/gamma signal pathway. Jak1 acts as the kinase partner for the interleukin (IL)-2 receptor []and interleukin (IL)-10 receptor []. It directly phosphorylates STAT but also activates STAT signalling through the transactivation of other JAK kinases associated with signalling receptors [, ].JAK1 was initially cloned using a PCR-based strategy utilising degenerateprimers corresponding to conserved motifs within the catalytic domain of protein-tyrosine kinases []. In common with JAK2 and TYK2, and by contrastwith JAK3, JAK1 appears to be ubiquitously expressed.
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Protein
P52332
Organism: Mus musculus/domesticus
Length: 1153  
Fragment?: false
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Protein
Q3U8P8
Organism: Mus musculus/domesticus
Length: 1126  
Fragment?: false
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Protein
Q3URU8
Organism: Mus musculus/domesticus
Length: 1153  
Fragment?: false
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Protein
B1ASP2
Organism: Mus musculus/domesticus
Length: 1153  
Fragment?: false
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Protein
Q9QVP9
Organism: Mus musculus/domesticus
Length: 1009  
Fragment?: false
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Protein
P34152
Organism: Mus musculus/domesticus
Length: 1052  
Fragment?: false
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Protein
A0A5F8MPY3
Organism: Mus musculus/domesticus
Length: 1093  
Fragment?: false
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Protein
Q8C2G0
Organism: Mus musculus/domesticus
Length: 967  
Fragment?: false
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Protein
K7QD41
Organism: Mus musculus/domesticus
Length: 1009  
Fragment?: false
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Protein
K7Q751
Organism: Mus musculus/domesticus
Length: 1068  
Fragment?: false
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Protein
E9Q2A6
Organism: Mus musculus/domesticus
Length: 967  
Fragment?: false
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Protein
Q3UDE9
Organism: Mus musculus/domesticus
Length: 1005  
Fragment?: false
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Publication
- | J:94790
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Mouse Synonym Curation
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Protein
P13745
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
B2RU80
Organism: Mus musculus/domesticus
Length: 1998  
Fragment?: false
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Protein
Q64455
Organism: Mus musculus/domesticus
Length: 1238  
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