| + |
NAA35 | form complex 
binding
|
NatC |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267234 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19398576 |
We here identify and characterize the human NatC (hNatC) complex, containing the catalytic subunit hMak3 and the auxiliary subunits hMak10 and hMak31. This complex associates with ribosomes, and hMak3 acetylates Met-Leu protein N termini in vitro, suggesting a model in which the human NatC complex functions in cotranslational N-terminal acetylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NAA30 | form complex
binding
|
NatC |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267233 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19398576 |
We here identify and characterize the human NatC (hNatC) complex, containing the catalytic subunit hMak3 and the auxiliary subunits hMak10 and hMak31. This complex associates with ribosomes, and hMak3 acetylates Met-Leu protein N termini in vitro, suggesting a model in which the human NatC complex functions in cotranslational N-terminal acetylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NatC | up-regulates 
|
Protein_acetylation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267236 |
|
|
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 |
| + |
NAA38 | form complex
binding
|
NatC |
0.672 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267235 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19398576 |
We here identify and characterize the human NatC (hNatC) complex, containing the catalytic subunit hMak3 and the auxiliary subunits hMak10 and hMak31. This complex associates with ribosomes, and hMak3 acetylates Met-Leu protein N termini in vitro, suggesting a model in which the human NatC complex functions in cotranslational N-terminal acetylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NatC
CPX-6275