| + |
TSG101 | form complex 
binding
|
ESCRT-I complex, VPS37A-UBAP1 variant |
0.877 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280924 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22405001 |
Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VPS28 | form complex
binding
|
ESCRT-I complex, VPS37A-UBAP1 variant |
0.91 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280927 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22405001 |
Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VPS37A | form complex
binding
|
ESCRT-I complex, VPS37A-UBAP1 variant |
0.877 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280925 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22405001 |
Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBAP1 | form complex
binding
|
ESCRT-I complex, VPS37A-UBAP1 variant |
0.845 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280926 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22405001 |
Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-0 complex | up-regulates quantity 
binding
|
ESCRT-I complex, VPS37A-UBAP1 variant |
0.617 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280931 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
ESCRT-I is a soluble hetero-tetramer consisting of Vps23/TSG101, Vps28, Vps37(A–D) and Mvb12(A,B) or ubiquitin-associated protein 1 (UBAP1) (Figure 2). Its efficient recruitment from the cytoplasm to endosomes requires protein–protein interactions with the ESCRT-0 complex. UBAP1-containing ESCRT-I appears to be more specific for MVB sorting, whereas Mvb12A/B-containing ESCRT-I also functions during HIV budding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-I complex, VPS37A-UBAP1 variant | up-regulates quantity
binding
|
ESCRT-II complex |
0.688 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280932 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
At the opposite end of the ESCRT-I rod, Vps28 binds to the GLUE domain of the ESCRT-II protein Vps36/Eap45 and thereby interacts with the ESCRT-II complex. In addition to cargo sorting, ESCRT-I together with ESCRT-II is capable of budding membranes into the lumen of giant unilamellar vesicles. The rigid architecture and size of ESCRT-I and ESCRT-II (see below) may help to stabilize the bud neck of a growing vesicle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-I complex, VPS37A-UBAP1 variant | up-regulates 
|
Multivesicular_body_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280935 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
In vivo and in vitro data suggest a key role for the ESCRT-III complex in all ESCRT-mediated membrane remodeling (budding and scission) reactions, although the mechanism is not understood. Hence, ESCRT-III filaments may have a dual role during MVB sorting: cargo sequestration within the site of MVB vesicle formation and membrane budding/scission. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESCRT-I complex, VPS37A-UBAP1 variant | up-regulates
|
Membrane_fusion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280938 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22361144 |
In vivo and in vitro data suggest a key role for the ESCRT-III complex in all ESCRT-mediated membrane remodeling (budding and scission) reactions, although the mechanism is not understood. Hence, ESCRT-III filaments may have a dual role during MVB sorting: cargo sequestration within the site of MVB vesicle formation and membrane budding/scission. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
ESCRT-I complex, VPS37A-UBAP1 variant
CPX-7181