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6C95

The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex bound to HYPK

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005667cellular_componenttranscription regulator complex
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006474biological_processN-terminal protein amino acid acetylation
A0010698molecular_functionacetyltransferase activator activity
A0016020cellular_componentmembrane
A0016407molecular_functionacetyltransferase activity
A0016604cellular_componentnuclear body
A0030154biological_processcell differentiation
A0031415cellular_componentNatA complex
A0043022molecular_functionribosome binding
A0043066biological_processnegative regulation of apoptotic process
A0045893biological_processpositive regulation of DNA-templated transcription
A0050821biological_processprotein stabilization
B0004596molecular_functionprotein-N-terminal amino-acid acetyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006473biological_processprotein acetylation
B0006474biological_processN-terminal protein amino acid acetylation
B0006475biological_processinternal protein amino acid acetylation
B0008080molecular_functionN-acetyltransferase activity
B0008999molecular_functionprotein-N-terminal-alanine acetyltransferase activity
B0016020cellular_componentmembrane
B0016407molecular_functionacetyltransferase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0031415cellular_componentNatA complex
B0043022molecular_functionribosome binding
B0051276biological_processchromosome organization
B1990189molecular_functionprotein N-terminal-serine acetyltransferase activity
B1990190molecular_functionprotein-N-terminal-glutamate acetyltransferase activity
B2000719biological_processnegative regulation of maintenance of mitotic sister chromatid cohesion, centromeric
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0006457biological_processprotein folding
D0015630cellular_componentmicrotubule cytoskeleton
D0032991cellular_componentprotein-containing complex
D0043066biological_processnegative regulation of apoptotic process
D0044183molecular_functionprotein folding chaperone
D0050821biological_processprotein stabilization
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue IHP A 901
ChainResidue
ALYS416
BLYS78
ALYS419
AHIS420
ALYS447
ALYS450
ATYR451
AHOH1001
BHIS16
BLYS51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues33
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues33
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues33
DetailsRepeat: {"description":"TPR 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues32
DetailsRepeat: {"description":"TPR 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues33
DetailsRepeat: {"description":"TPR 7"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues33
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues151
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues57
DetailsRegion: {"description":"Interaction with NAA15","evidences":[{"source":"PubMed","id":"15496142","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues69
DetailsRegion: {"description":"Required for association with the NAA10-NAA15 complex","evidences":[{"source":"PubMed","id":"29754825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues45
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues15
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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