Type |
Details |
Score |
Allele |
Name: |
CD2 cytoplasmic tail binding protein 2; endonuclease-mediated mutation 1, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
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 |
|
•
•
•
•
•
|