| + |
VPS33B | form complex 
binding
|
CHEVI complex |
0.788 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261830 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29778605 |
It has been recently suggested that VPS33B and VIPAR comprise two subunits of a novel multi-subunit tethering complex (named "CHEVI") |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEVI complex | up-regulates 
|
Platelet_aggregation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261833 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27319744 |
VPS33B association with VIPAS39, α-tubulin, and SEC22B was identified by co-immunoprecipitation, mass spectra, and immunoblotting in human embryonic kidney 293T (HEK293T) cells. Also, pull-down experiments revealed that VIPAS39 bound to intact VPS33B; in contrast, α-tubulin and SEC22B separately interacted with the sec1-like domains of VPS33B. Vps33b deficiency in megakaryocytes disturbs the redistribution of Vipas39 and Sec22b to proplatelets, and interrupted the co-localization of Sec22b with Vwf-positive vesicles |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VIPAS39 | form complex
binding
|
CHEVI complex |
0.788 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261831 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29778605 |
It has been recently suggested that VPS33B and VIPAR comprise two subunits of a novel multi-subunit tethering complex (named "CHEVI") |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEVI complex | up-regulates activity 
relocalization
|
SEC22B |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261832 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27319744 |
VPS33B association with VIPAS39, α-tubulin, and SEC22B was identified by co-immunoprecipitation, mass spectra, and immunoblotting in human embryonic kidney 293T (HEK293T) cells. Also, pull-down experiments revealed that VIPAS39 bound to intact VPS33B; in contrast, α-tubulin and SEC22B separately interacted with the sec1-like domains of VPS33B. Vps33b deficiency in megakaryocytes disturbs the redistribution of Vipas39 and Sec22b to proplatelets, and interrupted the co-localization of Sec22b with Vwf-positive vesicles |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CHEVI complex
CPX-6241