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Search results 3501 to 3600 out of 5471 for Tyr

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0.021s

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Hits by Pathway

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Hits by Strain

Type Details Score
Protein
A0A140LHR2
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
F8WIS9
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
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Protein
A0A494BAS3
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
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Protein
Q8BRS2
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: false
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Protein
A0A3B2WB60
Organism: Mus musculus/domesticus
Length: 307  
Fragment?: false
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Protein
Q9CSF4
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
Q8BKY7
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: false
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Protein
Q8K2L2
Organism: Mus musculus/domesticus
Length: 732  
Fragment?: true
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Protein
Q60515
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: true
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Protein
Q5SVI2
Organism: Mus musculus/domesticus
Length: 529  
Fragment?: false
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Protein
A0A0G2JGS4
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: false
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Protein
A0A0J9YTX8
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: true
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Protein
Q3TRX1
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: true
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Protein
Q5SVI3
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q8C8P0
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: false
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Protein
Q9CV04
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
E9Q696
Organism: Mus musculus/domesticus
Length: 520  
Fragment?: false
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Protein
Q3UMT5
Organism: Mus musculus/domesticus
Length: 825  
Fragment?: true
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Protein
E9Q1V9
Organism: Mus musculus/domesticus
Length: 488  
Fragment?: false
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Protein
F6TDC5
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: true
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Protein
Q5SVI1
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
Q3U350
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
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Protein
Q80TN1
Organism: Mus musculus/domesticus
Length: 487  
Fragment?: true
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Protein
Q3UG22
Organism: Mus musculus/domesticus
Length: 567  
Fragment?: false
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Protein
E9PVU4
Organism: Mus musculus/domesticus
Length: 49  
Fragment?: false
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Protein
Q5SVJ0
Organism: Mus musculus/domesticus
Length: 666  
Fragment?: false
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Protein
Q6PF82
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: true
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Protein
Q3TT60
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
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Protein
A0A087WP73
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: true
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Protein
E9Q1W0
Organism: Mus musculus/domesticus
Length: 512  
Fragment?: false
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Protein
A0A087WQ75
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
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Protein
H9H9R6
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
Q3TR46
Organism: Mus musculus/domesticus
Length: 436  
Fragment?: true
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Protein
A0A2I3BQP6
Organism: Mus musculus/domesticus
Length: 565  
Fragment?: false
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Protein
Q5SVI9
Organism: Mus musculus/domesticus
Length: 479  
Fragment?: false
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Protein
Q3TPM5
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
A0A494BB87
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: false
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Protein
E9Q3I6
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
E9Q5L9
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: false
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Protein
E9Q1T1
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: false
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Protein
A0A494B9X6
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
A0A3Q4EGN8
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: false
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Protein
Q3TJ05
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Protein
D3Z4A5
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: true
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Protein
Q3TXG1
Organism: Mus musculus/domesticus
Length: 579  
Fragment?: false
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Protein
A0A3Q4L2X0
Organism: Mus musculus/domesticus
Length: 504  
Fragment?: true
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Protein
Q8CD05
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: true
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Protein
Q05CL1
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q3UIJ5
Organism: Mus musculus/domesticus
Length: 1037  
Fragment?: false
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Protein
A0A0U1RNS2
Organism: Mus musculus/domesticus
Length: 61  
Fragment?: true
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Protein
H3BJC9
Organism: Mus musculus/domesticus
Length: 927  
Fragment?: false
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Protein
A0PJK0
Organism: Mus musculus/domesticus
Length: 405  
Fragment?: true
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Protein
D6RI32
Organism: Mus musculus/domesticus
Length: 588  
Fragment?: false
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Protein
Q5SVJ1
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
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Protein
D6RGU6
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: false
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Protein
Q3UIB2
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
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Protein
A0A2I3BQC5
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: false
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Protein
Q6P243
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
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Protein
A0A3B2W7L2
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: true
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Protein
Q3U2H3
Organism: Mus musculus/domesticus
Length: 367  
Fragment?: true
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Protein
Q8BK42
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
Q3UDT1
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
Q6ZWS7
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
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Protein
A0A494BBG0
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
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Protein
Q3UWD6
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: true
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Protein
Q91YV1
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
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Protein
Q68EG2
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
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Protein
Q543C0
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: false
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Protein
G1C1N8
Organism: Mus musculus/domesticus
Length: 59  
Fragment?: true
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Protein
Q3TV45
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Publication
11709088 | -
First Author: Parker PJ
Year: 2001
Journal: Biochem Soc Trans
Title: AGC protein kinase phosphorylation and protein kinase C.
Volume: 29
Issue: Pt 6
Pages: 860-3
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Publication
15209375 | -
First Author: Mora A
Year: 2004
Journal: Semin Cell Dev Biol
Title: PDK1, the master regulator of AGC kinase signal transduction.
Volume: 15
Issue: 2
Pages: 161-70
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Publication
2115088 | -
First Author: Cooper JB
Year: 1990
Journal: J Mol Biol
Title: X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.
Volume: 214
Issue: 1
Pages: 199-222
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Publication
2115087 | -
First Author: Sielecki AR
Year: 1990
Journal: J Mol Biol
Title: Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
Volume: 214
Issue: 1
Pages: 143-70
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Publication
19758436 | -
 
First Author: Rawlings ND
Year: 2009
Journal: BMC Genomics
Title: Pepsin homologues in bacteria.
Volume: 10
Pages: 437
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Publication
11782538 | -
First Author: Banerjee R
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine.
Volume: 99
Issue: 2
Pages: 990-5
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Publication
24179 | -
First Author: Tang J
Year: 1978
Journal: Nature
Title: Structural evidence for gene duplication in the evolution of the acid proteases.
Volume: 271
Issue: 5646
Pages: 618-21
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Publication
27872247 | -
First Author: Gao H
Year: 2017
Journal: Plant Physiol
Title: Two Membrane-Anchored Aspartic Proteases Contribute to Pollen and Ovule Development.
Volume: 173
Issue: 1
Pages: 219-239
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Publication
10716174 | -
First Author: Ilyin VA
Year: 2000
Journal: Protein Sci
Title: 2.9 A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site.
Volume: 9
Issue: 2
Pages: 218-31
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Publication
11285229 | -
First Author: Newlon MG
Year: 2001
Journal: EMBO J
Title: A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.
Volume: 20
Issue: 7
Pages: 1651-62
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Publication
11728710 | -
First Author: Galperin MY
Year: 2001
Journal: FEMS Microbiol Lett
Title: MHYT, a new integral membrane sensor domain.
Volume: 205
Issue: 1
Pages: 17-23
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Publication
25217636 | -
First Author: Rodriguez F
Year: 2014
Journal: J Biol Chem
Title: Crystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iron and calcium-containing active site.
Volume: 289
Issue: 45
Pages: 30889-99
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Publication
11065377 | -
 
First Author: Schlüter A
Year: 2000
Journal: Microbiology
Title: The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation.
Volume: 146 ( Pt 11)
Pages: 2987-96
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Publication
11810255 | -
First Author: Van Dommelen A
Year: 2002
Journal: Mol Genet Genomics
Title: Cloning and characterisation of the Azospirillum brasilense glnD gene and analysis of a glnD mutant.
Volume: 266
Issue: 5
Pages: 813-20
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Publication
8163536 | -
First Author: Law CL
Year: 1994
Journal: J Biol Chem
Title: Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex.
Volume: 269
Issue: 16
Pages: 12310-9
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Publication
1874735 | -
First Author: Taniguchi T
Year: 1991
Journal: J Biol Chem
Title: Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis.
Volume: 266
Issue: 24
Pages: 15790-6
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Publication
14656470 | -
First Author: di Clemente N
Year: 2003
Journal: Mol Cell Endocrinol
Title: Components of the anti-Müllerian hormone signaling pathway in gonads.
Volume: 211
Issue: 1-2
Pages: 9-14
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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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Publication
12138094 | -
First Author: Pandini G
Year: 2002
Journal: J Biol Chem
Title: Insulin/insulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved.
Volume: 277
Issue: 42
Pages: 39684-95
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Publication
16831875 | -
First Author: Slaaby R
Year: 2006
Journal: J Biol Chem
Title: Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR splice variant.
Volume: 281
Issue: 36
Pages: 25869-74
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Publication
8276809 | -
First Author: Van Horn DJ
Year: 1994
Journal: J Biol Chem
Title: Direct activation of the phosphatidylinositol 3'-kinase by the insulin receptor.
Volume: 269
Issue: 1
Pages: 29-32
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Publication
16732286 | -
First Author: Barton WA
Year: 2006
Journal: Nat Struct Mol Biol
Title: Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex.
Volume: 13
Issue: 6
Pages: 524-32
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Publication
16849318 | -
First Author: Macdonald PR
Year: 2006
Journal: J Biol Chem
Title: Structure of the extracellular domain of Tie receptor tyrosine kinases and localization of the angiopoietin-binding epitope.
Volume: 281
Issue: 38
Pages: 28408-14
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Publication
9275185 | -
First Author: Diener K
Year: 1997
Journal: Proc Natl Acad Sci U S A
Title: Activation of the c-Jun N-terminal kinase pathway by a novel protein kinase related to human germinal center kinase.
Volume: 94
Issue: 18
Pages: 9687-92
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Publication
7659156 | -
First Author: Hatada MH
Year: 1995
Journal: Nature
Title: Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor.
Volume: 377
Issue: 6544
Pages: 32-8
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Publication
22266942 | -
First Author: Engel P
Year: 2012
Journal: Nature
Title: Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.
Volume: 482
Issue: 7383
Pages: 107-10
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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
IPR016149 | Casein_kin_II_reg-sub_N
Type: Homologous_superfamily
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 [].Casein kinase, a ubiquitous, well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Ser or Thr in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits [, ]. However, some species (e.g., mammals) possess 2 related forms of the alpha-subunit (alpha and alpha'), while others (e.g., fungi) possess 2 related beta-subunits (beta and beta') []. The alpha-subunit is the catalytic unit and contains regions characteristic of serine/threonine protein kinases. The beta-subunit is believed to be regulatory, possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif []. The beta subunit is a highly conserved protein of about 25kDa that contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc []. The mammalian beta-subunit gene promoter shares common features with those of other mammalian protein kinases and is closely related to the promoter of the regulatory subunit of cAMP-dependent protein kinase [].This superfamily represents the N-terminal α-helical domain, which has an orthogonal bundle topology.
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Protein Domain
IPR018941 | Tyr_kin_Tie2_Ig-like_dom-1_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 [].Angiogenesis is a physiological process whereby new blood vessels are formed from existing ones. It is essential for tissue repair and regeneration during wound healing but also plays important roles in many pathological processes including tumor growth and metastasis [, ]. Angiogenesis is regulated in part by the receptor protein tyrosine kinase Tie2 and its ligands, the angiopoietins. The angiopoietin-binding site is harbord by the N-terminal two immunoglobulin-like (Ig-like) domains of Tie2 [].The angiopoietin-1 receptor contains the Tie-2 Ig-like domain. This protein is a tyrosine-kinase transmembrane receptor for angiopoietin 1. It probably regulates endothelial cell proliferation, differentiation and guides the proper patterning of endothelial cells during blood vessel formation.Tie2 contains not two but three immunoglobulin domains. They fold together with the three epidermal growth factor domains to form a compact, arrowhead-shaped structure [].
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Protein Domain
IPR016246 | Tyr_kinase_insulin-like_rcpt
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 [].This entry represents the insulin receptor, as well as related insulin-like receptors. The insulin receptor binds insulin and has a tyrosine-protein kinase activity, and mediates the metabolic functions of insulin. Binding to insulin stimulates the association of the receptor with downstream mediators, including IRS1 and phosphatidylinositol 3'-kinase (PI3K). The insulin receptor can activate PI3K either directly by binding to the p85 regulatory subunit, or indirectly via IRS1. When the insulin receptor is present in a hybrid receptor with IGF1R (insulin growth factor receptor), it binds IGF1 (insulin growth factor 1) [, , ].
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