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Search results 4401 to 4500 out of 5471 for Tyr

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Type Details Score
Protein
D3YXM1
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
Q1MX40
Organism: Mus musculus/domesticus
Length: 571  
Fragment?: false
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Protein
G3X905
Organism: Mus musculus/domesticus
Length: 564  
Fragment?: false
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Protein
Q3TMJ2
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: false
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Publication
11851389 | -
First Author: Attwood PV
Year: 2002
Journal: Acc Chem Res
Title: Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes.
Volume: 35
Issue: 2
Pages: 113-20
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Publication
12434148 | -
First Author: Yang J
Year: 2002
Journal: Nat Struct Biol
Title: Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP.
Volume: 9
Issue: 12
Pages: 940-4
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Publication
21749650 | -
First Author: Simões I
Year: 2011
Journal: FEBS J
Title: Shewasin A, an active pepsin homolog from the bacterium Shewanella amazonensis.
Volume: 278
Issue: 17
Pages: 3177-86
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Publication
2646860 | -
 
First Author: Hunkapiller T
Year: 1989
Journal: Adv Immunol
Title: Diversity of the immunoglobulin gene superfamily.
Volume: 44
Pages: 1-63
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Publication
1417831 | -
First Author: Terman BI
Year: 1992
Journal: Biochem Biophys Res Commun
Title: Identification of the KDR tyrosine kinase as a receptor for vascular endothelial cell growth factor.
Volume: 187
Issue: 3
Pages: 1579-86
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Publication
2157969 | -
First Author: Lee KH
Year: 1990
Journal: Mol Cell Biol
Title: Isolation and characterization of the alpha platelet-derived growth factor receptor from rat olfactory epithelium.
Volume: 10
Issue: 5
Pages: 2237-46
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Publication
8386825 | J:4693
First Author: Galland F
Year: 1993
Journal: Oncogene
Title: The FLT4 gene encodes a transmembrane tyrosine kinase related to the vascular endothelial growth factor receptor.
Volume: 8
Issue: 5
Pages: 1233-40
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Publication
14500499 | -
First Author: Verma A
Year: 2003
Journal: Infect Immun
Title: Identification of two eukaryote-like serine/threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1.
Volume: 71
Issue: 10
Pages: 5772-84
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Publication
12034833 | -
First Author: Nikolskaya AN
Year: 2002
Journal: Nucleic Acids Res
Title: A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family.
Volume: 30
Issue: 11
Pages: 2453-9
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Publication
7389358 | -
   
Year: 1980
Journal: Contrib Nephrol
Title: Disturbances of water and electrolyte metabolism.
Volume: 21
Pages: 1-152
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Publication
18045056 | -
First Author: Uckun FM
Year: 2007
Journal: Anticancer Agents Med Chem
Title: Targeting JAK3 tyrosine kinase-linked signal transduction pathways with rationally-designed inhibitors.
Volume: 7
Issue: 6
Pages: 612-23
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Protein Domain
IPR020775 | Tyr_kinase_non-rcpt_Jak3
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 JAK3, which is involved in the interleukin-2 and interleukin-4 signalling pathway. Jak3 phosphorylates STAT6, IRS1, IRS2 and PI3K [].
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Protein Domain
IPR000340 | Dual-sp_phosphatase_cat-dom
Type: Domain
Description: Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [, ]. The PTP superfamily can be divided into four subfamilies []:(1) pTyr-specific phosphatases(2) dual specificity phosphatases (dTyr and dSer/dThr)(3) Cdc25 phosphatases (dTyr and/or dThr)(4) LMW (low molecular weight) phosphatasesBased on their cellular localisation, PTPases are also classified as:Receptor-like, which are transmembrane receptors that contain PTPase domains []Non-receptor (intracellular) PTPases []All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel β-sheet with flanking α-helices containing a β-loop-α-loop that encompasses the PTP signature motif []. Functional diversity between PTPases is endowed by regulatory domains and subunits. This entry represents dual specificity protein-tyrosine phosphatases. Ser/Thr and Tyr dual specificity phosphatases are a group of enzymes with both Ser/Thr () and tyrosine specific protein phosphatase () activity able to remove both the serine/threonine or tyrosine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylatedunder the action of a kinase. Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. The crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), has been determined at 2.1 angstrom resolution []. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region"connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.These proteins may also have inactive phosphatase domains, and dependent on the domain composition this loss of catalytic activity has different effects on protein function. Inactive single domain phosphatases can still specifically bind substrates, and protect again dephosphorylation, while the inactive domains of tandem phosphatases can be further subdivided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. There is a region of higher conservation common to both classes, suggesting a new regulatory centre [].
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Protein Domain
IPR001824 | Tyr_kinase_rcpt_3_CS
Type: Conserved_site
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 [].A number of growth factors stimulate mitogenesis by interacting with a family of cell surface receptors which possess an intrinsic, ligand-sensitive, protein tyrosine kinase activity []. These receptor tyrosine kinases (RTK) all share the same topology: an extracellular ligand-binding domain, a single transmembrane region and a cytoplasmic kinase domain. However they can be classified into at least five groups. The class III RTK's are characterised by the presence of five to seven immunoglobulin-like domains []in their extracellular section. Their kinase domain differs from that of other RTK's by the insertion of a stretch of 70 to 100 hydrophilic residues in the middle of this domain. The receptors currently known to belong to class III are:Platelet-derived growth factor receptor (PDGF-R). PDGF-R exists as a homo- or heterodimer of two related chains: alpha and beta [].Macrophage colony stimulating factor receptor (CSF-1-R) (also known as the fms oncogene).Stem cell factor (mast cell growth factor) receptor (also known as the kit oncogene).Vascular endothelial growth factor (VEGF) receptors Flt-1 and Flk-1/KDR [].Fl cytokine receptor Flk-2/Flt-3 [].The putative receptor Flt-4 [].This entry represents a short, conserved region found within these proteins.
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Protein
Q9D7P7
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein
O88741
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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Protein
P27038
Organism: Mus musculus/domesticus
Length: 513  
Fragment?: false
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Protein
Q8K1R7
Organism: Mus musculus/domesticus
Length: 984  
Fragment?: false
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Protein
Q9Z265
Organism: Mus musculus/domesticus
Length: 546  
Fragment?: false
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Protein
O55222
Organism: Mus musculus/domesticus
Length: 452  
Fragment?: false
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Protein
Q8K592
Organism: Mus musculus/domesticus
Length: 568  
Fragment?: false
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Protein
P27040
Organism: Mus musculus/domesticus
Length: 536  
Fragment?: false
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Protein
Q9JI10
Organism: Mus musculus/domesticus
Length: 497  
Fragment?: false
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Protein
Q9CQS5
Organism: Mus musculus/domesticus
Length: 547  
Fragment?: false
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Protein
Q9JI11
Organism: Mus musculus/domesticus
Length: 487  
Fragment?: false
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Protein
Q7M6U3
Organism: Mus musculus/domesticus
Length: 1450  
Fragment?: false
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Protein
P35761
Organism: Mus musculus/domesticus
Length: 856  
Fragment?: false
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Protein
O88570
Organism: Mus musculus/domesticus
Length: 24  
Fragment?: true
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Protein
Q3TZ08
Organism: Mus musculus/domesticus
Length: 647  
Fragment?: true
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Protein
Q3UPT4
Organism: Mus musculus/domesticus
Length: 750  
Fragment?: false
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Protein
Q14B83
Organism: Mus musculus/domesticus
Length: 777  
Fragment?: false
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Protein
Q3U4B8
Organism: Mus musculus/domesticus
Length: 732  
Fragment?: false
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Protein
Q3URY8
Organism: Mus musculus/domesticus
Length: 636  
Fragment?: false
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Protein
A0A1B0GSB8
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
Q8K006
Organism: Mus musculus/domesticus
Length: 593  
Fragment?: true
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Protein
Q14B82
Organism: Mus musculus/domesticus
Length: 653  
Fragment?: false
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Protein
A2A5H8
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: true
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Protein
Q543W6
Organism: Mus musculus/domesticus
Length: 546  
Fragment?: false
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Protein
A2AI38
Organism: Mus musculus/domesticus
Length: 513  
Fragment?: false
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Protein
F6YT88
Organism: Mus musculus/domesticus
Length: 613  
Fragment?: true
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Protein
A0A2I3BQE0
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
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Protein
Q9JLM7
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
Q05BG3
Organism: Mus musculus/domesticus
Length: 780  
Fragment?: false
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Protein
Q91X01
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
Q3UTV3
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: true
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Protein
Q69Z43
Organism: Mus musculus/domesticus
Length: 1005  
Fragment?: true
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Protein
Q6P912
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
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Protein
A0A140LIP1
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
A0A1W2P6L1
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
Q3UEX4
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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Protein
A0A571BD42
Organism: Mus musculus/domesticus
Length: 667  
Fragment?: false
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Protein
A2AJ28
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
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Protein
Q8BRV4
Organism: Mus musculus/domesticus
Length: 513  
Fragment?: false
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Protein
B1AWI7
Organism: Mus musculus/domesticus
Length: 1033  
Fragment?: false
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Protein
Q6PD96
Organism: Mus musculus/domesticus
Length: 830  
Fragment?: false
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Protein
Q8R1P8
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: true
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Protein
Q3TM51
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: true
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Protein
E9Q1T3
Organism: Mus musculus/domesticus
Length: 780  
Fragment?: false
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Protein
Q8BY97
Organism: Mus musculus/domesticus
Length: 815  
Fragment?: false
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Protein
Q3UY30
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: true
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Protein
A0A338P7E9
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
Q8C774
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
Q8BHT4
Organism: Mus musculus/domesticus
Length: 515  
Fragment?: false
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Protein
E9Q6Q5
Organism: Mus musculus/domesticus
Length: 658  
Fragment?: false
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Protein
D3Z5W7
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: true
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Protein
Q9CQG8
Organism: Mus musculus/domesticus
Length: 561  
Fragment?: false
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Protein
Q3TPW2
Organism: Mus musculus/domesticus
Length: 773  
Fragment?: false
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Publication
9074797 | -
First Author: Armstrong RN
Year: 1997
Journal: Chem Res Toxicol
Title: Structure, catalytic mechanism, and evolution of the glutathione transferases.
Volume: 10
Issue: 1
Pages: 2-18
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Publication
10783391 | J:70880
First Author: Board PG
Year: 2000
Journal: J Biol Chem
Title: Identification, characterization, and crystal structure of the Omega class glutathione transferases.
Volume: 275
Issue: 32
Pages: 24798-806
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Publication
9045797 | -
First Author: Vuilleumier S
Year: 1997
Journal: J Bacteriol
Title: Bacterial glutathione S-transferases: what are they good for?
Volume: 179
Issue: 5
Pages: 1431-41
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Protein
P35991
Organism: Mus musculus/domesticus
Length: 659  
Fragment?: false
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Protein
P14234
Organism: Mus musculus/domesticus
Length: 517  
Fragment?: false
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Protein
P70451
Organism: Mus musculus/domesticus
Length: 823  
Fragment?: false
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Protein
P09581
Organism: Mus musculus/domesticus
Length: 977  
Fragment?: false
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Protein
Q3UFB7
Organism: Mus musculus/domesticus
Length: 799  
Fragment?: false
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Protein
P20444
Organism: Mus musculus/domesticus
Length: 672  
Fragment?: false
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Protein
O09127
Organism: Mus musculus/domesticus
Length: 1004  
Fragment?: false
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Protein
P05622
Organism: Mus musculus/domesticus
Length: 1098  
Fragment?: false
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Protein
Q00342
Organism: Mus musculus/domesticus
Length: 1000  
Fragment?: false
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Protein
Q60629
Organism: Mus musculus/domesticus
Length: 876  
Fragment?: false
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Protein
P05532
Organism: Mus musculus/domesticus
Length: 979  
Fragment?: false
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Protein
Q62190
Organism: Mus musculus/domesticus
Length: 1378  
Fragment?: false
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Protein
P35546
Organism: Mus musculus/domesticus
Length: 1115  
Fragment?: false
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Protein
P16056
Organism: Mus musculus/domesticus
Length: 1379  
Fragment?: false
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Protein
P16879
Organism: Mus musculus/domesticus
Length: 822  
Fragment?: false
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Protein
P68404
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
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Protein
P24604
Organism: Mus musculus/domesticus
Length: 630  
Fragment?: false
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Protein
P26618
Organism: Mus musculus/domesticus
Length: 1089  
Fragment?: false
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Protein
P97793
Organism: Mus musculus/domesticus
Length: 1621  
Fragment?: false
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Protein
P42682
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
P35918
Organism: Mus musculus/domesticus
Length: 1345  
Fragment?: false
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Protein
Q02858
Organism: Mus musculus/domesticus
Length: 1122  
Fragment?: false
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Protein
P35969
Organism: Mus musculus/domesticus
Length: 1333  
Fragment?: false
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Protein
P35917
Organism: Mus musculus/domesticus
Length: 1363  
Fragment?: false
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Protein
Q64434
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: false
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Protein
E0CYA3
Organism: Mus musculus/domesticus
Length: 739  
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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