+ |
PRKCB |
phosphorylation
|
DAB2 |
0.301 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249026 |
Ser24 |
QAAPKAPsKKEKKKG |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
10542228 |
We have mapped the TPA-induced DOC-2/DAB2 protein phosphorylation site to Ser24, which appears to modulate the DOC-2/DAB2 inhibition of AP-1 transcription activity. Results indicate that phosphorylation of Ser24 is mediated by PKCbetaII, PKC_, and PKCdelta, but not CKII. This suggests that the PKC phosphorylation of Ser24 in DOC-2/DAB2 may be an underlying mechanisms for its tumor-suppressive function. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PRKCD |
phosphorylation
|
DAB2 |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249028 |
Ser24 |
QAAPKAPsKKEKKKG |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
10542228 |
We have mapped the TPA-induced DOC-2/DAB2 protein phosphorylation site to Ser24, which appears to modulate the DOC-2/DAB2 inhibition of AP-1 transcription activity. Results indicate that phosphorylation of Ser24 is mediated by PKCbetaII, PKC_, and PKCdelta, but not CKII. This suggests that the PKC phosphorylation of Ser24 in DOC-2/DAB2 may be an underlying mechanisms for its tumor-suppressive function. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PRKCD | down-regulates
phosphorylation
|
DAB2 |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127198 |
Ser24 |
QAAPKAPsKKEKKKG |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
15280374 |
Mutational analysis revealed that a dab2 ser(24) phosphorylation mutant (s24a) abrogated the inhibitory function of dab2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-71764 |
Ser24 |
QAAPKAPsKKEKKKG |
Homo sapiens |
|
pmid |
sentence |
10542228 |
Mutational analysis revealed that a dab2 ser(24) phosphorylation mutant (s24a) abrogated the inhibitory function of dab2. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCG |
phosphorylation
|
DAB2 |
0.303 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249027 |
Ser24 |
QAAPKAPsKKEKKKG |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
10542228 |
We have mapped the TPA-induced DOC-2/DAB2 protein phosphorylation site to Ser24, which appears to modulate the DOC-2/DAB2 inhibition of AP-1 transcription activity. Results indicate that phosphorylation of Ser24 is mediated by PKCbetaII, PKC_, and PKCdelta, but not CKII. This suggests that the PKC phosphorylation of Ser24 in DOC-2/DAB2 may be an underlying mechanisms for its tumor-suppressive function. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
VHL | up-regulates quantity by expression
transcriptional regulation
|
DAB2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255602 |
|
|
Homo sapiens |
Renal Cell Carcinoma Cell |
pmid |
sentence |
15824735 |
three of the nine targets had been identified previously as candidate TSGs (DOC-2/DAB2, CDKN1C and SPARC) and all were upregulated by wild-type pVHL. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DAB2 | up-regulates activity
binding
|
DAB2IP |
0.537 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254744 |
|
|
Homo sapiens |
|
pmid |
sentence |
27858941 |
In prostate cancer cells, DAB2IP was shown to be recruited by the adaptor protein DAB2/DOC2 to promote Ras inactivation and inhibition of MAPK signaling upon receptor stimulation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DAB2 | down-regulates
binding
|
LRP6 |
0.509 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196925 |
|
|
Homo sapiens |
|
pmid |
sentence |
22491013 |
Wnt stimulation induces the casein kinase 2 (ck2)-dependent phosphorylation of lrp6 at s1579, promoting its binding to dab2 and internalization with clathrin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AP-2 complex | up-regulates activity
binding
|
DAB2 |
0.49 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260391 |
|
|
Homo sapiens |
HFF-1 Cell, HeLa Cell |
pmid |
sentence |
11247302 |
Dab2 is alternatively spliced and its localization depends on a region of the protein that contains two DPF motifs that are present in the p96 Dab2 protein and absent in the p67 splice variant. This region is sufficient to confer Dab2 binding to the alpha‐adaptin subunit of the clathrin adaptor protein, AP‐2.|These findings suggest that in addition to previously reported signal-transduction functions, Dab2 could also act as an adaptor protein that may regulate protein trafficking. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |