(Q27548762)

http://www.ebi.ac.uk/interpro/protein/P07347

GNAT domain, protein family

1 reference

based on heuristic

inferred from protein domain or family

found in taxon

Saccharomyces cerevisiae S288c

1 reference

25 May 2022

1 reference

25 May 2022

peptide-glutamate-N-acetyltransferase activity

1 reference

14 February 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

1 reference

14 February 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

IEA

acyltransferase activity

1 reference

14 February 2019

peptide-serine-N-acetyltransferase activity

IEA

1 reference

14 February 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

4 references

14 February 2019

ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

14 February 2019

The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

14 February 2019

Functional organization of the yeast proteome by systematic analysis of protein complexes

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

14 February 2019

Proteome survey reveals modularity of the yeast cell machinery

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

identical protein binding

IPI

1 reference

14 February 2019

ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

peptide alpha-N-acetyltransferase activity

IPI

1 reference

27 March 2018

The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides

http://www.ebi.ac.uk/QuickGO/annotations?protein=P07347&geneProductId=UniProtKB:P07347

1 reference

14 February 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

1 reference

27 March 2018

The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides

http://www.ebi.ac.uk/QuickGO/annotations?protein=P07347&geneProductId=UniProtKB:P07347

1 reference

14 February 2019

Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail.

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

N-terminal protein amino acid propionylation

IMP

1 reference

14 February 2019

Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

N-terminal peptidyl-glutamic acid acetylation

IMP

1 reference

14 February 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

N-terminal peptidyl-serine acetylation

IBA

1 reference

14 February 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P07347

N-terminal protein amino acid acetylation

IBA

1 reference

InterPro Release 71.0

http://www.ebi.ac.uk/interpro/protein/P07347

Identifiers

1 reference

20 March 2022

1 reference

25 May 2022

1 reference