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Details on Person UniProt:P61956-1 SUMO2
| Class:Id | ReferenceIsoform:8967209 |
|---|---|
| _chainChangeLog | chain:1-93 added on Fri February 17 2017;propeptide:94-95 added on Fri February 17 2017 |
| _displayName | UniProt:P61956-1 SUMO2 |
| _timestamp | 2026-02-20 21:44:50 |
| chain | chain:1-93 propeptide:94-95 |
| checksum | F8F0426849BEF08B |
| comment | FUNCTION Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond 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, CBX4 or ZNF451 (PubMed:26524494). 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 (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).SUBUNIT Interacts with SAE2 and UBE2I. Interacts with ZNF451. Identified in a complex with ZNF451 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 and SOBP (via SIM domains). Interacts with MTA1 (PubMed:21965678). Interacts with HINT1 (By similarity). Interacts with GCNA (via SIM domains); this interaction allows the GCNA recruitment to DPCs sites (PubMed:30914427). Interacts with TINCR (via SUMO-interacting motif); the interaction increases TINCR protein stability (PubMed:36369429).SUBUNIT (Microbial infection) Interacts with Epstein-barr virus BGLF4.INTERACTION Broadly expressed.PTM Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.PTM Cleavage of precursor form by SENP1 or SENP2 is necessary for function.PTM Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.SIMILARITY Belongs to the ubiquitin family. SUMO subfamily.ONLINE INFORMATION SUMO protein entry |
| created | [InstanceEdit:8964659] Weiser, JD |
| description | recommendedName: fullName evidence="24"Small ubiquitin-related modifier 2 shortName evidence="24"SUMO-2 alternativeName: fullName evidence="22"HSMT3 alternativeName: fullName evidence="25"SMT3 homolog 2 alternativeName: fullName evidence="20"SUMO-3 alternativeName: fullName evidence="23"Sentrin-2 alternativeName: fullName evidence="24"Ubiquitin-like protein SMT3B shortName evidence="20"Smt3B |
| geneName | SUMO2 SMT3B SMT3H2 |
| identifier | P61956 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Alternative splicing Host-virus interaction Isopeptide bond Nucleus Proteomics identification Reference proteome Ubl conjugation Ubl conjugation pathway |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | SUMO2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8960151] ENSEMBL:ENSG00000188612 SUMO2 [Homo sapiens] |
| secondaryIdentifier | SUMO2_HUMAN B2R4I2 P55855 Q32Q42 Q6IPZ6 Q96HK1 |
| sequenceLength | 95 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | P61956-1 |
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No pathways have been reviewed or authored by UniProt:P61956-1 SUMO2 (8967209)
