AFG1-like ATPase; Putative mitochondrial ATPase. Plays a role in mitochondrial morphology and mitochondrial protein metabolism. Promotes degradation of excess nuclear-encoded complex IV subunits (COX4I1, COX5A and COX6A1) and normal activity of complexes III and IV of the respiratory chain. Mediates mitochondrial translocation of TP53 and its transcription-independent apoptosis in response to genotoxic stress (481 aa)

TP53-regulating kinase; Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates ’Ser-15’ of p53/TP53 protein and may therefore p [...] (253 aa)

Inactive phospholipid phosphatase 7; Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity (By similarity) (271 aa)

UPF0428 protein CXorf56; Chromosome X open reading frame 56; Spliceosomal C complex (208 aa)

Arpin; Regulates actin polymerization by inhibiting the actin- nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence; Belongs to the Arpin family (226 aa)

Potassium channel subfamily K member 9; pH-dependent, voltage-insensitive, background potassium channel protein; Potassium two pore domain channel subfamily K (374 aa)

Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily (386 aa)

Uncharacterized protein C12orf43; Chromosome 12 open reading frame 43 (252 aa)