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Search results 101 to 125 out of 125 for Cd2bp2

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0.017s
Type Details Score
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Protein
Organism: Mus musculus/domesticus
Length: 1044  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1291  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 721  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1122  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1285  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 787  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 721  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 877  
Fragment?: true
Publication
First Author: Nishizawa K
Year: 1998
Journal: Proc Natl Acad Sci U S A
Title: Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation.
Volume: 95
Issue: 25
Pages: 14897-902
Publication
First Author: Freund C
Year: 1999
Journal: Nat Struct Biol
Title: The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences.
Volume: 6
Issue: 7
Pages: 656-60
Publication
First Author: Freund C
Year: 2002
Journal: EMBO J
Title: Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules.
Volume: 21
Issue: 22
Pages: 5985-95
Protein Domain
Type: Domain
Description: The glycine-tyrosine-phenylalanine (GYF) domain is an around 60-amino acid domain which contains a conserved GP[YF]xxxx[MV]xxWxxx[GN]YF motif. It was identified in the human intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two tandem PPPGHR segments within the cytoplasmic region of CD2. Binding experiments and mutational analyses have demonstrated the critical importance of the GYF tripeptide in ligand binding. A GYF domain is also found in several other eukaryotic proteins of unknown function []. It has been proposed that the GYF domain found in these proteins could also be involved in proline-rich sequence recognition [].Resolution of the structure of the CD2BP2 GYF domain by NMR spectroscopy revealed a compact domain with a β-β-α-β-beta topology, where the single α-helix is tilted away from the twisted, anti-parallel β-sheet. The conserved residues of the GYF domain create a contiguous patch of predominantly hydrophobic nature which forms an integral part of the ligand-binding site []. There is limited homology within the C-terminal 20-30 amino acids of various GYF domains, supporting the idea that this part of the domain is structurally but not functionally important [].
Protein
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: true
Publication
First Author: Berr A
Year: 2010
Journal: Plant Cell
Title: Arabidopsis SET DOMAIN GROUP2 is required for H3K4 trimethylation and is crucial for both sporophyte and gametophyte development.
Volume: 22
Issue: 10
Pages: 3232-48
Publication
First Author: Springer NM
Year: 2003
Journal: Plant Physiol
Title: Comparative analysis of SET domain proteins in maize and Arabidopsis reveals multiple duplications preceding the divergence of monocots and dicots.
Volume: 132
Issue: 2
Pages: 907-25
Protein Domain
Type: Homologous_superfamily
Description: The glycine-tyrosine-phenylalanine (GYF) domain is an around 60-amino acid domain which contains a conserved GP[YF]xxxx[MV]xxWxxx[GN]YF motif. It was identified in the human intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two tandem PPPGHR segments within the cytoplasmic region of CD2. Binding experiments and mutational analyses have demonstrated the critical importance of the GYF tripeptide in ligand binding. A GYF domain is also found in several other eukaryotic proteins of unknown function []. It has been proposed that the GYF domain found in these proteins could also be involved in proline-rich sequence recognition [].Resolution of the structure of the CD2BP2 GYF domain by NMR spectroscopy revealed a compact domain with a β-β-α-β-beta topology, where the single α-helix is tilted away from the twisted, anti-parallel β-sheet. The conserved residues of the GYF domain create a contiguous patch of predominantly hydrophobic nature which forms an integral part of the ligand-binding site []. There is limited homology within the C-terminal 20-30 amino acids of various GYF domains, supporting the idea that this part of the domain is structurally but not functionally important [].This entry also matches Arabidopsis histone methyltransferases ATXR3/SDG2 and ATXR7/SDG25, which contain two partial GYF domains towards the N terminus []. Histone methyltransferase ATXR7 is involved in regulation of flowering time []. It is specifically required for the trimethylation of 'Lys-4' of histone H3 (H3K4me3) at the FLC locus, it prevents the trimethylation on 'Lys-27' (H3K27me3) at the same locus. ATXR3 is also required for H3K4 trimethylation and is crucial for both sporophyte and gametophyte development in plants [, ].
Protein
Organism: Mus musculus/domesticus
Length: 174  
Fragment?: true
Publication
First Author: Guo L
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: SET DOMAIN GROUP2 is the major histone H3 lysine [corrected] 4 trimethyltransferase in Arabidopsis.
Volume: 107
Issue: 43
Pages: 18557-62
Publication
First Author: Tamada Y
Year: 2009
Journal: Plant Cell
Title: ARABIDOPSIS TRITHORAX-RELATED7 is required for methylation of lysine 4 of histone H3 and for transcriptional activation of FLOWERING LOCUS C.
Volume: 21
Issue: 10
Pages: 3257-69
Protein
Organism: Mus musculus/domesticus
Length: 2248  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2243  
Fragment?: false