Reactome: A Curated Pathway Database
Results 1 to 10 of 17
Pathways (6) Reactions (6) Proteins (1) Others (4)
Protein: UniProt:Q9UBE0 SAE1 (Homo sapiens)
Last changed: 2014-11-26 10:20:21

Pathway: Metabolism of proteins (Homo sapiens)
Protein metabolism comprises the pathways of translation, post-translational modification and protein folding
Last changed: 2014-11-21 19:49:01

Pathway: Post-translational protein modification (Homo sapiens)
After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the internal peptide bond cleavages that activate proenzymes, the attachment of oligosaccharide moieties to membrane-bound and secreted proteins, the attachment of lipid o
Last changed: 2014-11-21 19:49:01

Pathway: SUMOylation (Homo sapiens)
Small Ubiquitin-like MOdifiers (SUMOs) are a family of 3 proteins (SUMO1,2,3) that are reversibly conjugated to lysine residues of target proteins via a glycine-lysine isopeptide bond (reviewed in Hay 2013, Hannoun et al. 2010, Gareau and Lima 2010, Wilkinson and Henley 2010, Wang and Dasso 2009). Proteomic methods have yielded estimates of hundreds of target proteins. Targets are mostly located in the
Last changed: 2014-11-21 19:49:01

Pathway: SUMO is transferred from E1 to E2 (UBE2I, UBC9) (Homo sapiens)
SUMO is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010). UBC9 is the only known E2 enzyme for SUMO and on certain substrates such as RanGAP1 may act without the requirement of an E3 ligase
Last changed: 2014-11-21 19:49:01

Pathway: Processing and activation of SUMO (Homo sapiens)
The initial translation products of SUMO1, SUMO2, and SUMO3 are precursors that have extra amino acid residues at the C-terminus (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010, Hay 2007). SUMO1 has 4 extra residues, SUMO2 has 2 extra residues, and SUMO3 has 11 extra residues. Proteolytic cleavage by SUMO peptidases (SENPs) removes the propeptide
Last changed: 2014-11-21 19:49:01

Pathway: SUMO is conjugated to E1 (UBA2:SAE1) (Homo sapiens)
The UBA2:SAE1 complex catalyzes the formation of a thioester linkage between the C-terminal glycine of the mature SUMO and a cysteine residue (cysteine-173) in UBA2 (SAE2) (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010). During the process the C-terminal glycine residue of SUMO is reacted with ATP to yield pyrophosphate and a transient intermediat
Last changed: 2014-11-21 19:49:01

Reaction: Transfer of SUMO2 from E1 to UBE2I (UBC9) (Homo sapiens)
SUMO2 is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (Tatham et al. 2001, Werner et al. 2009)
Last changed: 2014-11-21 19:49:01

Reaction: Transfer of SUMO3 from E1 to UBE2I (UBC9) (Homo sapiens)
SUMO3 is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (Tatham et al. 2001, Werner et al. 2009)
Last changed: 2014-11-21 19:49:01

Reaction: Conjugation of SUMO3 to UBA2:SAE1 (Homo sapiens)
The UBA2:SAE1 complex catalyzes the formation of a thioester bond between SUMO3 and cysteine-173 of UBA2 (Tatham et al. 2001, Werner et al. 2009). ATP reacts with the C-terminal glycine residue of SUMO3 to yield pyrophosphate and a transient intermediate, SUMO3 adenylate, which then reacts with the thiol group of the cysteine residue on UBA2
Last changed: 2014-11-21 19:49:01

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