Ubiquitin-like (UBL) modifications are post-translational modifications that, like ubiquitylation, play various roles in regulating various cellular processes. These modifications involve the attachment of UBL proteins to target substrates, often through a series of enzymatic reactions like ubiquitylation. The SUMOylation (Small Ubiquitin-like Modifier) process involves the E1 activating enzyme (SAE1/SAE2), the E2 conjugating enzyme (Ubc9), and various E3 ligases. SUMOylation typically occurs on specific lysine (K) residues within target proteins within ψ-K-x-E motifs, where ψ represents a hydrophobic residue, K is the target lysine, x can be any amino acid, and E is the acceptor residue for the carboxyl group of the C-terminal glycine of SUMO. SUMOylation can regulate transcription, DNA repair, and protein localization. For example, SUMOylation of DNA repair factors like PCNA (Proliferating Cell Nuclear Antigen) enhances their recruitment to damaged DNA sites. NEDDylation (Neural precursor cell Expressed, Developmentally Downregulated 8) involves the E1 activating enzyme (APPBP1/UBA3), the E2 conjugating enzyme (Ubc12), and various E3 ligases, such as DCN1, which facilitates NEDDylation. NEDDylation occurs on specific lysine (K) residues within target proteins. NEDDylation primarily regulates the degradation of specific proteins through the Cullin-RING E3 ubiquitin ligases (CRLs). By NEDDylating Cullin subunits of CRLs, NEDDylation activates these complexes, leading to targeted protein ubiquitylation and degradation. ISGylation involves the attachment of ISG15 (Interferon-Stimulated Gene 15) protein to specific lysine (K) residues. ISGylation is catalysed by the E1 activating enzyme (UBA7), the E2 conjugating enzyme (UbcH8), and various E3 ligases. ISGylation is induced by interferon signalling and is involved in antiviral responses and immune regulation through modulating the activity and stability of target proteins. ATG8/LC3 Phosphatidylethanolamine Conjugation (Autophagy-related Protein 8) involves the E1 activating enzyme (Atg7), the E2 conjugating enzyme (Atg3), and the formation of lipidated ATG8/LC3-II. ATG8/LC3 conjugation is important for autophagy where ATG8/LC3 is conjugated to phosphatidylethanolamine (PE) and inserted into autophagic membranes, facilitating cargo engulfment and autophagosome formation. UFM1ylation (Ubiquitin-fold Modifier 1) involves the E1 activating enzyme (Uba5), the E2 conjugating enzyme (Ufc1), and the E3 ligase Ufl1. UFM1ylation is linked to the endoplasmic reticulum (ER) and regulates ER homeostasis, modifying proteins involved in ER function and protein secretion, thereby aiding in maintaining ER integrity. FATylation (Fatty acylation) is catalysed by the E1 activating enzyme (UBA5), the E2 conjugating enzyme (ATG10), and the E3 ligase (ZDHHC20) and is a lipidation modification that regulates protein localization to membranes. For example, FATylation occurs on the G protein subunit Gα(q), influencing GPCR signalling. Conversely, FAT10ylation (HLA-F Adjacent Transcript 10) involves the E1 activating enzyme (UBE1L), the E2 conjugating enzyme (UBC6), and the E3 ligases (UBE3C and HOIP) and is implicated in immune regulation and protein turnover. It targets proteins for proteasomal degradation and modulates immune responses. Finally, Rub1ylation (Related to Ubiquitin 1) involves the E1 activating enzyme (Ula1), the E2 conjugating enzyme (Ubc1), and various E3 ligases and is a modification like ubiquitylation that regulates the activity and stability of target proteins. We offer a comprehensive product range of research tools for studying ubiquitin like modifiers, including PIAS2 antibodies, PIAS3 antibodies, ISG15 antibodies, PIAS1 antibodies, and SENP6 antibodies. Explore our full ubiquitin like modifiers product range below and discover more, for less.