+ |
CSNK2A1 | up-regulates
phosphorylation
|
CD5 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-62303 |
Ser482 |
SSMQPDNsSDSDYDL |
Homo sapiens |
|
pmid |
sentence |
9834084 |
In this study, we use jurkat t cell transfectants of cd5 cytoplasmic tail mutants to reveal phosphorylation sites relevant to signal transduction. Our results show that casein kinase ii (ckii) is responsible for the constitutive phosphorylation of cd5 molecules at a cluster of three serine residues located at the extreme c terminus (s458, s459, and s461) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-62307 |
Ser483 |
SMQPDNSsDSDYDLH |
Homo sapiens |
|
pmid |
sentence |
9834084 |
In this study, we use jurkat t cell transfectants of cd5 cytoplasmic tail mutants to reveal phosphorylation sites relevant to signal transduction. Our results show that casein kinase ii (ckii) is responsible for the constitutive phosphorylation of cd5 molecules at a cluster of three serine residues located at the extreme c terminus (s458, s459, and s461) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-62311 |
Ser485 |
QPDNSSDsDYDLHGA |
Homo sapiens |
|
pmid |
sentence |
9834084 |
In this study, we use jurkat t cell transfectants of cd5 cytoplasmic tail mutants to reveal phosphorylation sites relevant to signal transduction. Our results show that casein kinase ii (ckii) is responsible for the constitutive phosphorylation of cd5 molecules at a cluster of three serine residues located at the extreme c terminus (s458, s459, and s461) |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PRKCB |
phosphorylation
|
CD5 |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249073 |
Thr434 |
MSFHRNHtATVRSHA |
Homo sapiens |
|
pmid |
sentence |
11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249075 |
Thr436 |
FHRNHTAtVRSHAEN |
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCA |
phosphorylation
|
CD5 |
0.345 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249070 |
Thr434 |
MSFHRNHtATVRSHA |
Homo sapiens |
|
pmid |
sentence |
11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249071 |
Thr436 |
FHRNHTAtVRSHAEN |
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCA | up-regulates
phosphorylation
|
CD5 |
0.345 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-85175 |
Thr434 |
MSFHRNHtATVRSHA |
Homo sapiens |
|
pmid |
sentence |
11123317 |
Cd5 is a good pkc substrate. Phosphorylation of cd5 is necessary for cd5-mediated lipid second messenger generation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-85179 |
Thr436 |
FHRNHTAtVRSHAEN |
Homo sapiens |
|
pmid |
sentence |
11123317 |
Cd5 is a good pkc substrate. Phosphorylation of cd5 is necessary for cd5-mediated lipid second messenger generation. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCG |
phosphorylation
|
CD5 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249072 |
Thr434 |
MSFHRNHtATVRSHA |
Homo sapiens |
|
pmid |
sentence |
11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249074 |
Thr436 |
FHRNHTAtVRSHAEN |
Homo sapiens |
|
pmid |
sentence |
11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCG | up-regulates
phosphorylation
|
CD5 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-85183 |
Thr436 |
FHRNHTAtVRSHAEN |
Homo sapiens |
|
pmid |
sentence |
11123317 |
Cd5 is a good pkc substrate. Phosphorylation of cd5 is necessary for cd5-mediated lipid second messenger generation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FYN |
phosphorylation
|
CD5 |
0.505 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251151 |
Tyr453 |
ASHVDNEySQPPRNS |
in vitro |
|
pmid |
sentence |
11298344 |
Tyrosine-mutated CD5 molecules have been used to show that residues Y429 and Y463 are targeted in vivo by protein tyrosine kinases following cell stimulation with anti-CD3 mAb or pervanadate. This is in agreement with data from direct in vitro kinase assays using purified recombinant Lck and Fyn protein tyrosine kinases. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251152 |
Tyr487 |
DNSSDSDyDLHGAQR |
in vitro |
|
pmid |
sentence |
11298344 |
Tyrosine-mutated CD5 molecules have been used to show that residues Y429 and Y463 are targeted in vivo by protein tyrosine kinases following cell stimulation with anti-CD3 mAb or pervanadate. This is in agreement with data from direct in vitro kinase assays using purified recombinant Lck and Fyn protein tyrosine kinases. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
LCK | up-regulates activity
phosphorylation
|
CD5 |
0.558 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-106799 |
Tyr453 |
ASHVDNEySQPPRNS |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
11298344 |
Tyrosine phosphorylation of cd5 requires lck activity. We propose that t cell activation mediates cd5 tyrosine phosphorylation at residues y429 and y463 mainly through the activation of lck |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-106803 |
Tyr487 |
DNSSDSDyDLHGAQR |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
11298344 |
Tyrosine phosphorylation of cd5 requires lck activity. We propose that t cell activation mediates cd5 tyrosine phosphorylation at residues y429 and y463 mainly through the activation of lck |
|
Publications: |
2 |
Organism: |
Homo Sapiens |