Human Sulfatase Modifying Factor 1 (SUMF1) is a 42kDa protein. SUMF1 is a Ca2+-binging member of the sulfatase-modifying factor family. SUMF1 is a soluble ER lumenal glycoprotein, it converts inactive sulfatases into an active form by transforming a catalytic site cysteine into a formylglycine residue. In the ER, SUMF1 can exist as either a monomer, or a disulfide-linked homodimer or a heterodimer with SUMF2. Three splice isoforms are known.
Small Ubiquitin-Related Modifier 1 (SUMO1) is an Ubiquitin-like protein that belongs to the ubiquitin family with SUMO subfamily. It is a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. SUMO1 functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. SUMO1 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO1 is not active until the last four amino acids of the carboxy-terminus are cleaved off. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins and may also regulate a network of genes involved in palate development.
Small ubiquitin-like modifier protein (SUMO) modification is a highly dynamic process, catalyzed by SUMO-specific activating (E1), conjugating (E2) and ligating (E3) enzymes, and reversed by a family of SUMO-specific proteases (SENPs). Small ubiquitin-like modifier 1 (SUMO1) is a member of the superfamily of ubiquitin-like proteins. Despite its structural similarity with ubiquitin, SUMO1 does not seem to play any role in protein degradation. SUMO1 plays an important role in modulation of NOX activity required for ROS generation. SUMO1 haploinsufficiency results in cleft lip and palate in animal models. SUMO1 gene variation in human non-syndromic cleft lip with or without cleft palate (NSCLP) development. SUMO-1 may be useful as a novel target for therapy in oral squamous cell carcinoma (SCC) as well as a clinical indicator for tumor recurrence together with Mdm2.
Small Ubiquitin-Related Modifier 2 (SUMO2) is an Ubiquitin-like protein that belongs to the ubiquitin family with SUMO subfamily. It is a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. SUMO2 can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptidebond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.
SUMO3 belongs to the SUMO protein family and operates like ubiquitin. Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polyer. Nevertheless unlike ubiquitin that targets proteins for degration; SUMO3 takes part in several cellular processess; such as nuclear transport; transcription regulation; apoptosis and protein stability. SUMO3 participates in amyloid beta generation and has a key role in the oneset or progression of Alzheimer's disease.
Small ubiquitin-like modifier (SUMO); also known as SUMO homologue and SMT3; is a member of the superfamily of ubiquitin-like polypeptides that become covalently attached to various intracellular target proteins as a way to alter their function; location; and/or half-life. Small ubiquitin-like modifiers include SUMO1; SUMO2; SUMO3; and SUMO4. Except for SUMO4; all other SUMOs are ubiquitously expressed; including in the brain. In human; SUMO2 and SUMO3 are two highly homologous proteins; collectively called SUMO2/3. Several studies suggest that SUMO3 are associated with pathogenesis in several neurological diseases; including Alzheimer's disease; Parkinson's disease; and cerebral ischemia/stroke.
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