Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly- SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Interacts with HIPK1, HIPK2, PPM1J, RASD2 and TCF3 Interacts with NR2C1; the interaction promotes its sumoylation. Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with DNMT1. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with human herpesvirus 6 IE2. Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation (Probable). Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML- RARA oncoprotein. Interacts with IPO13. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus. Belongs to the ubiquitin-conjugating enzyme family. Note: This description may include information from UniProtKB.
Molecular Function: protein binding; enzyme binding; ubiquitin protein ligase binding; transcription factor binding; HLH domain binding; SUMO ligase activity; ATP binding; ligase activity
Biological Process: ubiquitin-dependent protein catabolic process; mitosis; positive regulation of I-kappaB kinase/NF-kappaB cascade; viral reproduction; protein modification process; protein ubiquitination; negative regulation of transcription from RNA polymerase II promoter; post-translational protein modification; chromosome segregation; protein sumoylation; cellular protein metabolic process; cell division; negative regulation of transcription, DNA-dependent
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.