6C95
The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex bound to HYPK
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001525 | biological_process | angiogenesis |
A | 0003723 | molecular_function | RNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005667 | cellular_component | transcription regulator complex |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006474 | biological_process | N-terminal protein amino acid acetylation |
A | 0010698 | molecular_function | acetyltransferase activator activity |
A | 0016020 | cellular_component | membrane |
A | 0016407 | molecular_function | acetyltransferase activity |
A | 0016604 | cellular_component | nuclear body |
A | 0030154 | biological_process | cell differentiation |
A | 0031415 | cellular_component | NatA complex |
A | 0043022 | molecular_function | ribosome binding |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0050821 | biological_process | protein stabilization |
B | 0004596 | molecular_function | protein-N-terminal amino-acid acetyltransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005730 | cellular_component | nucleolus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006473 | biological_process | protein acetylation |
B | 0006474 | biological_process | N-terminal protein amino acid acetylation |
B | 0006475 | biological_process | internal protein amino acid acetylation |
B | 0008080 | molecular_function | N-acetyltransferase activity |
B | 0008999 | molecular_function | protein-N-terminal-alanine acetyltransferase activity |
B | 0016020 | cellular_component | membrane |
B | 0016407 | molecular_function | acetyltransferase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0031415 | cellular_component | NatA complex |
B | 0043022 | molecular_function | ribosome binding |
B | 0051276 | biological_process | chromosome organization |
B | 1990189 | molecular_function | protein N-terminal-serine acetyltransferase activity |
B | 1990190 | molecular_function | protein-N-terminal-glutamate acetyltransferase activity |
B | 2000719 | biological_process | negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005737 | cellular_component | cytoplasm |
D | 0006457 | biological_process | protein folding |
D | 0015630 | cellular_component | microtubule cytoskeleton |
D | 0032991 | cellular_component | protein-containing complex |
D | 0043066 | biological_process | negative regulation of apoptotic process |
D | 0044183 | molecular_function | protein folding chaperone |
D | 0050821 | biological_process | protein stabilization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue IHP A 901 |
Chain | Residue |
A | LYS416 |
B | LYS78 |
A | LYS419 |
A | HIS420 |
A | LYS447 |
A | LYS450 |
A | TYR451 |
A | HOH1001 |
B | HIS16 |
B | LYS51 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 1"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 36 |
Details | Repeat: {"description":"TPR 3"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 4"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 5"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 32 |
Details | Repeat: {"description":"TPR 6"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 7"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 8"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 151 |
Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 57 |
Details | Region: {"description":"Interaction with NAA15","evidences":[{"source":"PubMed","id":"15496142","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 69 |
Details | Region: {"description":"Required for association with the NAA10-NAA15 complex","evidences":[{"source":"PubMed","id":"29754825","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 45 |
Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 15 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |