+ |
CD3D | form complex
binding
|
CD3 |
0.725 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255295 |
|
|
Homo sapiens |
|
pmid |
sentence |
12507424 |
The T cell receptor-CD3 complex (TCR-CD3) serves a critical role in the differentiation, survival, and function of T cells, and receptor triggering elicits a complex set of biological responses that serve to protect the organism from infectious agents. The receptor is composed of six different chains that form the TCR heterodimer responsible for ligand recognition, as well as the CD3γε, CD3δε, and ζζ signaling modules. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM13 | down-regulates quantity by destabilization
polyubiquitination
|
CD3D |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271644 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17314412 |
RFP2, a gene frequently lost in various malignancies, encodes a protein with RING finger, B-box, and coiled-coil domains that belongs to the RBCC/TRIM family of proteins.Rfp2 Regulates the Stability of the ERAD Substrate CD3-δ. In summary, these experiments demonstrate that Rfp2 functions as a RING-dependent ERAD E3 ubiquitin ligase and regulates the degradation of the ER substrate, CD3-δ. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LCK | up-regulates activity
phosphorylation
|
CD3D |
0.552 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259929 |
|
|
Mus musculus |
T-lymphocyte |
pmid |
sentence |
2470098 |
Last, we demonstrate directly that members of the CD3 complex, including the gamma, delta, and epsilon chains, as well as a putative zeta subunit, can be phosphorylated at tyrosine residues by the CD4/CD8.p56lck complex. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
AMFR | down-regulates quantity by destabilization
polyubiquitination
|
CD3D |
0.486 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272670 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11724934 |
Gp78 specifically recruits MmUBC7, a ubiquitin-conjugating enzyme (E2) implicated in ER-associated degradation (ERAD), through a region distinct from the RING finger. gp78 can target itself for proteasomal degradation in a RING finger- and MmUBC7-dependent manner. Importantly, gp78 can also mediate degradation of CD3-delta, a well-characterized ERAD substrate. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |