| + |
CSNK2A1 | up-regulates 
phosphorylation
|
CLIP1 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167168 |
Ser1364 |
DDLNNYDsDDQEKQS |
Homo sapiens |
|
| pmid |
sentence |
| 20664522 |
Herein, we have identified polo-like kinase 1 (plk1) and casein kinase 2 (ck2) as two kinases of clip-170 and mapped s195 and s1318 as their respective phosphorylation sites.Plk1- and ck2-associated phosphorylations of clip-170 are involved in the timely formation of kinetochore-microtubule attachments in mitosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
CLIP1 |
0.701 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167172 |
Ser195 |
LTKTASEsISNLSEA |
Homo sapiens |
|
| pmid |
sentence |
| 20664522 |
Furthermore, we provide evidence that plk1 phosphorylation of clip-170 at s195 enhances its association with ck2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity 
phosphorylation
|
CLIP1 |
0.701 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264575 |
Ser312 |
ASLKRSPsASSLSSM |
in vitro |
|
| pmid |
sentence |
| 24451569 |
Plk1 phosphorylates CLIP-170 and regulates its binding to microtubules for chromosome alignment|Here, we show that phosphorylation at Ser312 in the third serine-rich region of CLIP-170 is increased during mitosis. Polo-like kinase 1 (Plk1) is responsible for this phosphorylation during the mitotic phase of dividing cells. In vitro analysis using a purified CLIP-170 N-terminal fragment showed that phosphorylation by Plk1 diminishes CLIP-170 binding to the MT ends |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCA | down-regulates
phosphorylation
|
CLIP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165857 |
Ser312 |
ASLKRSPsASSLSSM |
Homo sapiens |
|
| pmid |
sentence |
| 20519438 |
Furthermore, by using phosphoproteomic analysis, we determined that s309 and s311 of clip-170 are phosphorylated in cells and mapped s311 as a protein kinase a (pka) phosphorylation site.phosphorylation of s311 may be critical for establishing the ?folded Back? Conformation of clip-170clip-170 open and folded back conformations represent active and inactive modes of the protein, respectively |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRRK1 | up-regulates activity
phosphorylation
|
CLIP1 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275469 |
Thr1430 |
EMFGHWAtNCNDDET |
|
|
| pmid |
sentence |
| 25413345 |
LRRK1 phosphorylates CLIP-170 at Thr1384, located in its C-terminal zinc knuckle motif, and this promotes the association of CLIP-170 with dynein-dynactin complexes. |
|
| Publications: |
1 |
| + |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
CLIP1 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275471 |
Thr287 |
KIGFPSTtPAKAKAN |
|
|
| pmid |
sentence |
| 19687009 |
Cdc2 phosphorylates T287|CLIP-170, the founding member of microtubule “plus ends tracking” proteins, is involved in many critical microtubule-related functions, including recruitment of dynactin to the microtubule plus ends and formation of kinetochore-microtubule attachments during metaphase. |These results demonstrate that Cdc2-mediated phosphorylation of CLIP-170 is essential for the normal function of this protein during cell cycle progression. |
|
| Publications: |
1 |
| + |
CDK1 | up-regulates activity
phosphorylation
|
CLIP1 |
0.488 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275470 |
Thr287 |
KIGFPSTtPAKAKAN |
|
|
| pmid |
sentence |
| 19687009 |
Cdc2 phosphorylates T287|CLIP-170, the founding member of microtubule “plus ends tracking” proteins, is involved in many critical microtubule-related functions, including recruitment of dynactin to the microtubule plus ends and formation of kinetochore-microtubule attachments during metaphase. |These results demonstrate that Cdc2-mediated phosphorylation of CLIP-170 is essential for the normal function of this protein during cell cycle progression. |
|
| Publications: |
1 |
| + |
CLIP1 | up-regulates activity
binding
|
DCTN1 |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252164 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15381688 |
MT-unbound CLIP-170 can adopt a folded conformation through an intramolecular interaction of its terminal domains. Binding to MTs correlates with the unfolding of CLIP-170, which allows the interaction of the COOH-terminal domain with its binding partners, such as dynactin, resulting in their recruitment to the MT tip. The NH2 terminus of p150Glued binds directly to the COOH terminus of CLIP-170 through its second metal-binding motif. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLIP1 | up-regulates
binding
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264830 |
|
|
|
|
| pmid |
sentence |
| 17889670 |
Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264832 |
|
|
|
|
| pmid |
sentence |
| 17889670 |
Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170) |
|
| Publications: |
2 |
| + |
MTOR | up-regulates activity
phosphorylation
|
CLIP1 |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279231 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12742166 |
By contrast to the phosphorylation of p150 Glued by PKA, inhibition of mTOR by rapamycin inhibited the ability of CLIP-170 to bind to microtubules, suggesting that phosphorylation by mTOR promotes CLIP-170 microtubule binding.|The new study confirms this physical interaction in animal cells and suggests that mTOR phosphorylates CLIP-170 on some, but not all, of the sites that are phosphorylated in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLASP1 | up-regulates activity
binding
|
CLIP1 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265091 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15631994 |
CLIP-associating protein (CLASP) 1 and CLASP2 are mammalian microtubule (MT) plus-end binding proteins, which associate with CLIP-170 and CLIP-115.|We demonstrate that the middle part of CLASPs binds directly to EB1 and to MTs. | Both EB1- and cortex-binding domains of CLASP are required to promote MT stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLASP2 | up-regulates activity
binding
|
CLIP1 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264827 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 19638411 |
CLASPs were originally identified as CLIP-170-interacting proteins and later found to be required for microtubule stabilisation at the cortical regions of epithelial cells|the C-terminal region of CLASP2 is known to interact with CLIP-170 |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PAFAH1B1 | up-regulates activity
binding
|
CLIP1 |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252166 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11940666 |
Here we demonstrate colocalization and direct interaction between CLIP-170 and LIS1. In mammalian cells, LIS1 recruitment to kinetochores is dynein/dynactin dependent, and recruitment there of CLIP-170 is dependent on its site of binding to LIS1, located in the distal zinc finger motif. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CLIP1
- 
- 