Enables the directed movement of sulfate ions (SO4 2-) into, out of, within or between cells.

Catalysis of the hydrolysis of peptide bonds. Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

The alteration of a histone by the covalent addition or removal of a chemical group.

Catalysis of the hydrolysis of peptide bonds. Similar to cathepsin L, but with much less activity on the terminal bond of Z-Phe-Arg-NHMec, and more activity on the terminal bond of Z-Val-Val-Arg-Xaa compounds.

The modification of histones by addition of methyl groups.

The insertion, deletion or substitution of nucleotides within nascent mRNA transcripts to produce mRNA molecules with sequences that differ from those coded genetically.

The modification of histones by addition of phosphoric groups.

Catalysis of the reaction: reduced riboflavin + NADP+ = riboflavin + NADPH + H+.

The modification of histones by addition of acetyl groups.

transcription from RNA polymerase III promoter

The synthesis of RNA from a DNA template by RNA polymerase III (Pol III), originating at a Pol III-specific promoter.

The modification of histones by addition of ubiquitin groups.

transcription initiation from RNA polymerase III promoter

transcription initiation from Pol III promoter

The modification of histones by removal of acetyl groups.

Interacting selectively with an antigen peptide, a fragment of a foreign protein derived by proteolysis within the cell.

Interacting selectively with an antigen peptide, a fragment of an exogenous foreign protein derived by endocytosis of the protein and proteolysis within the cell.

Catalysis of the release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.

Interacting selectively with a T cell receptor, the antigen-recognizing receptor on the surface of T cells.

The removal of one or more ubiquitin moieties from a protein.