SUMO1

Small ubiquitin-related modifier 1 ;
SUMO-1 ;
GAP-modifying protein 1 ;
GMP1 ;
SMT3 homolog 3 ;
Sentrin ;
Ubiquitin-homology domain protein PIC1 ;
Ubiquitin-like protein SMT3C ;
Smt3C ;
Ubiquitin-like protein UBL1 ;

caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.,function:Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalent attachment 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.,online information:SUMO protein entry,PTM:Cleavage of precursor form by SENP1 or SENP2 is necessary for function.,similarity:Belongs to the ubiquitin family. SUMO subfamily.,similarity:Contains 1 ubiquitin-like domain.,subunit:Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52.,

DNA metabolic process, DNA repair, proteolysis, response to DNA damage stimulus, macromolecule catabolic process,negative regulation of biosynthetic process, negative regulation of macromolecule biosynthetic process, negative regulation of macromolecule metabolic process, negative regulation of gene expression, negative regulation of transcription, protein sumoylation, modification-dependent protein catabolic process, protein catabolic process,negative regulation of cellular biosynthetic process, positive regulation of protein complex assembly, protein modification by small protein conjugation, regulation of protein localization, cellular response to stress, regulation of protein complex assembly, negative regulation of DNA binding, negative regulation of transcription factor activity,modification-dependent macromolecule catabolic process, regulation of cellular component biogenesis, negative regulation of molecular function, cellular protein catabolic process, cellular macromolecule catabolic process, regulation of transcription, negative regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process,regulation of transcription factor activity, regulation of binding, negative regulation of binding, regulation of DNA binding, positive regulation of cellular component organization, negative regulation of nitrogen compound metabolic process, proteolysis involved in cellular protein catabolic process, protein modification by small protein conjugation or removal,

Nucleus membrane . Nucleus speckle . Cytoplasm . Nucleus, PML body . Cell membrane . Nucleus . Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (PubMed:24651376). .