| + |
PRKAA2 | down-regulates 
phosphorylation
|
BAIAP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195102 |
Ser366 |
KTLPRSSsMAAGLER |
Homo sapiens |
|
| pmid |
sentence |
| 22137581 |
Using this approach for ppp1r12c, baiap2, and cdc27, we found that mutation of a single serine to alanine (s452, s366, and s379 respectively) resulted in almost a complete loss of ampk phosphorylation in these proteins. Termination of irsp53 function is suggested to occur following cdc42 dissociation, kinase phosphorylation of t340 and t360, and subsequent 14-3-3 binding, which competes for sh3 partners, thus allowing filopodial retraction |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161810 |
Ser366 |
KTLPRSSsMAAGLER |
Homo sapiens |
|
| pmid |
sentence |
| 19933840 |
Using this approach for ppp1r12c, baiap2, and cdc27, we found that mutation of a single serine to alanine (s452, s366, and s379 respectively) resulted in almost a complete loss of ampk phosphorylation in these proteins. Termination of irsp53 function is suggested to occur following cdc42 dissociation, kinase phosphorylation of t340 and t360, and subsequent 14-3-3 binding, which competes for sh3 partners, thus allowing filopodial retraction |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MARK2 | down-regulates activity
phosphorylation
|
BAIAP2 |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278411 |
Ser366 |
KTLPRSSsMAAGLER |
Homo sapiens |
|
| pmid |
sentence |
| 21282462 |
Par1b directly phosphorylates IRSp53 on S366 in cell lysates and stimulates phosphorylation on S453/3/5 via an indirect mechanism.|These data are consistent with a scenario in which Par1b phosphorylation inhibits IRSp53 function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPK | down-regulates
phosphorylation
|
BAIAP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216572 |
Ser366 |
KTLPRSSsMAAGLER |
Homo sapiens |
|
| pmid |
sentence |
| 19933840 |
Using this approach for ppp1r12c, baiap2, and cdc27, we found that mutation of a single serine to alanine (s452, s366, and s379 respectively) resulted in almost a complete loss of ampk phosphorylation in these proteins. Termination of irsp53 function is suggested to occur following cdc42 dissociation, kinase phosphorylation of t340 and t360, and subsequent 14-3-3 binding, which competes for sh3 partners, thus allowing filopodial retraction |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216608 |
Ser366 |
KTLPRSSsMAAGLER |
Homo sapiens |
|
| pmid |
sentence |
| 22137581 |
Using this approach for ppp1r12c, baiap2, and cdc27, we found that mutation of a single serine to alanine (s452, s366, and s379 respectively) resulted in almost a complete loss of ampk phosphorylation in these proteins. Termination of irsp53 function is suggested to occur following cdc42 dissociation, kinase phosphorylation of t340 and t360, and subsequent 14-3-3 binding, which competes for sh3 partners, thus allowing filopodial retraction |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BAIAP2 | up-regulates activity 
binding
|
ENAH |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268423 |
|
|
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 11696321 |
We conclude that the interaction of Cdc42 with the partial CRIB motif of IRSp53 relieves an intramolecular, autoinhibitory interaction with the N terminus, allowing the recruitment of Mena to the IRSp53 SH3 domain. This IRSp53:Mena complex initiates actin filament assembly into filopodia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
CDC42 | up-regulates activity
binding
|
BAIAP2 |
0.866 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268424 |
|
|
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 11696321 |
We conclude that the interaction of Cdc42 with the partial CRIB motif of IRSp53 relieves an intramolecular, autoinhibitory interaction with the N terminus, allowing the recruitment of Mena to the IRSp53 SH3 domain. This IRSp53:Mena complex initiates actin filament assembly into filopodia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
BAIAP2 | up-regulates activity
binding
|
WASF2 |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265556 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11130076 |
Here we demonstrate that IRSp53, a substrate for insulin receptor with unknown function, is the 'missing link' between Rac and WAVE. Activated Rac binds to the amino terminus of IRSp53, and carboxy-terminal Src-homology-3 domain of IRSp53 binds to WAVE to form a trimolecular complex. From studies of ectopic expression, we found that IRSp53 is essential for Rac to induce membrane ruffling, probably because it recruits WAVE, which stimulates actin polymerization mediated by the Arp2/3 complex. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RAC1 | up-regulates activity
binding
|
BAIAP2 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265554 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 19171758 |
In this study, we report that Kank disrupts the function of active Rac1 through IRSp53. The binding between IRSp53 and Kank inhibits the association of active Rac1 with IRSp53 rather than the association of active cdc42 with IRSp53. Kank inhibits the formation of lamellipodia and membrane ruffles induced by active Rac1 in NIH3T3 cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Axon guidance |
| + |
BAIAP2 | up-regulates 
|
Neurite_outgrowth |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265555 |
|
|
Mus musculus |
N1E-115 Cell |
| pmid |
sentence |
| 19171758 |
Ectopic expression of IRSp53 in mouse neuroblastoma N1E115 cells induces neurite outgrowth . Kank inhibits IRSp53-mediated neurite outgrowth in N1E115 cells |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
KANK1 | down-regulates activity
binding
|
BAIAP2 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265553 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 19171758 |
In this study, we report that Kank disrupts the function of active Rac1 through IRSp53. The binding between IRSp53 and Kank inhibits the association of active Rac1 with IRSp53 rather than the association of active cdc42 with IRSp53. Kank inhibits the formation of lamellipodia and membrane ruffles induced by active Rac1 in NIH3T3 cells. Kank interacts with IRSp53 through their coiled-coil domains. Kank affected the interaction between IRSp53 and Rac1 and partially affected that between IRSp53 and cdc42 (Fig. 3). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RAC1 | up-regulates
binding
|
BAIAP2 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85302 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11130076 |
Here we demonstrate that irsp53, a substrate for insulin receptor with unknown function, is the 'missing link' between rac and wave. Activated rac binds to the amino terminus of irsp53, and carboxy-terminal src-homology-3 domain of irsp53 binds to wave to form a trimolecular complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
BAIAP2 | up-regulates
binding
|
WASF1 |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85299 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11130076 |
Here we demonstrate that irsp53, a substrate forinsulinreceptor with unknown function, is the 'missing link' between rac and wave. Activated rac binds to the amino terminus of irsp53, and carboxy-terminal src-homology-3 domain of irsp53 binds to wave to form a trimolecular complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
BAIAP2
- 
- 