SCUBA

NAA10 — N-alpha-acetyltransferase 10, NatA catalytic subunit

NAA10 belongs to a gene co-expression module in 5 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

NAA10's module in each cell type

Cell typeModuleShares the module with
EndothelialVascular Tone Regulation
Endothelial cell development
ADAMTS6, ATP1A1, ATP1B3, ATP5PF, CALD1, CAVIN3, CCDC3, CD81 +13 moreView in SCUBA
Gamma-delta T cellsProtein Homeostasis Chaperones
Housekeeping
ATXN10, DYNLRB1, GMFG, HIGD1A, POLR2J, PPIA, PPIB, PRDX2 +6 more
Innate lymphoid cellsEndosomal Trafficking Signaling
Immune regulation
ARF1, CCDC85B, CKLF, COMMD8, FAM50A, GDE1, HAX1, IL27RA +16 moreView in SCUBA
MacrophagesMitochondrial Biogenesis
Mitochondrial & OxPhos
AIMP1, ATP5F1D, ATP5MC1, C1QBP, CCT2, CCT3, CCT7, CHCHD1 +38 moreView in SCUBA
Mucosal-associated invariant T cellT cell Surface Signaling
TCR Signaling
CD37, ICAM3, LIME1, MFNG, MZT2A, PLSCR3, SIGIRR

About the gene

SynonymsARD1, ARD1A, DXS707, TE2
ChromosomeX: 153929225-153935080
Predicted locationIntracellular
Essential geneYes
Protein classDisease related genes, Enzymes, Essential proteins, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins
Molecular functionAcyltransferase, Transferase

Function

Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity. Acetylates amino termini that are devoid of initiator methionine. The alpha (N-terminal) acetyltransferase activity may be important for vascular, hematopoietic and neuronal growth and development. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration. Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development. Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX. Acetylates HIST1H4A. Acts as a negative regulator of sister chromatid cohesion during mitosis.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.