| + |
NAA16 | form complex 
binding
|
NatA- NAA10-NAA16 variant |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281465 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16638120|30054468|19480662 |
Immunoprecipitation coupled to mass spectrometry identified both endogenous hNaa15p and hNaa16p as distinct interaction partners of hNaa10p in HEK293 cells, thus demonstrating the presence of both hNaa15p-hNaa10p and hNaa16p-hNaa10p complexes. The hNaa16p-hNaa10p complex acetylates NatA type N-termini in vitro. hNaa16p is ribosome associated, supporting its potential role in cotranslational Nalpha-terminal acetylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NAA10 | form complex
binding
|
NatA- NAA10-NAA16 variant |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281466 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16638120|30054468|19480662 |
Immunoprecipitation coupled to mass spectrometry identified both endogenous hNaa15p and hNaa16p as distinct interaction partners of hNaa10p in HEK293 cells, thus demonstrating the presence of both hNaa15p-hNaa10p and hNaa16p-hNaa10p complexes. The hNaa16p-hNaa10p complex acetylates NatA type N-termini in vitro. hNaa16p is ribosome associated, supporting its potential role in cotranslational Nalpha-terminal acetylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NatA- NAA10-NAA16 variant | up-regulates 
|
Protein_acetylation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281467 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21351257 |
About 80% of soluble human proteins are N-terminally acetylated by 1 of 3 major Nα-terminal acetyltransferase complexes, hNatA, hNatB and hNatC, which differ in their subunit composition and substrate specificity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
NatA- NAA10-NAA16 variant