Tripeptidyl-peptidase 1; Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (By similarity). Requires substrates with an unsubstituted N-terminus (By similarity).

Tumor protein p53-inducible nuclear protein 2; Dual regulator of transcription and autophagy. Positively regulates autophagy and is required for autophagosome formation and processing. May act as a scaffold protein that recruits MAP1LC3A, GABARAP and GABARAPL2 and brings them to the autophagosome membrane by interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase class III complex, they trigger autophagosome development. Acts as a transcriptional activator of THRA.

Nuclear transition protein 2; Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction. The histone H2AB1-H2BC1/TH2B dimer is required for loading of TNP2 onto chromatin. Belongs to the nuclear transition protein 2 family.

TERF1-interacting nuclear factor 2; Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly (By similarity).

Telomeric repeat-binding factor 2; Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA- binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'- TTAGGG-3' repeats added [...]

TSSK6-activating co-chaperone protein; Co-chaperone that facilitates HSP-mediated activation of TSSK6.

Vacuole membrane protein 1; Stress-induced protein that, when overexpressed, promotes formation of intracellular vacuoles followed by cell death (By similarity). May be involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis. Involved in cell-cell adhesion. Plays an essential role in formation of cell junctions. Plays a role in the initial stages of the autophagic process through its interaction with BECN1. Required for autophagosome formation (By similarity); Belongs to the VMP1 family.

Inactive C-alpha-formylglycine-generating enzyme 2; Lacks formylglycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1. Belongs to the sulfatase-modifying factor family.

Telomeric repeat-binding factor 2-interacting protein 1; Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)- mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology- directed repair ( [...]