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FLASH GENE
Symbol SUMO3 contributors: mct - updated : 27-09-2023
HGNC name SMT3 suppressor of mif two 3 homolog 1 (yeast)
HGNC id 11124
DNA
TYPE functioning gene
STRUCTURE 12.45 kb     4 Exon(s)
MAPPING cloned Y linked N status confirmed
Map cen - PFKL PFKL - C21orf2 - D21S154 - D21S170 - D21S171 - D21S1903 - SUMO3 - ITGB2 - D21S1897 - ADARB1 - COL18A1 - SLC19A1 - D21S44 - D21S112 - COL6A1 - LSS - COL6A2 - PCNT2 - S100B - qter
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
4 - 1831 - 103 - 2001 11451954
4 - 1854 - 141 - 2001 11451954
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Cardiovascularheart   moderately
Digestivestomach   moderately
Reproductivefemale systemuteruscervix moderately
 female systemovary  highly
Skin/Tegumentskin   moderately
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Blood / hematopoieticbone marrow   
Connectivebone   
Nervousperipherous   
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • a central ubiquitin domain
  • a conserved C terminal Gly-Gly residues
  • HOMOLOGY
    interspecies ortholog to yeast S.cerevisiae SMT3 (suppressor of mutations in centromeric protein MIF2)
    intraspecies homolog to CENPC
    homolog to SUMO2 (97p100)
    Homologene
    FAMILY
  • ubiquitin family
  • SUMO subfamily
  • CATEGORY regulatory
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm
    intracellular,nucleus,nucleoplasm,nuclear bodies,PML
    intracellular,nucleus,chromatin/chromosome,centromere
    intracellular,nucleus,chromatin/chromosome,kinetochore
    text
  • SUMO-2/3 localize to centromeres and condensed chromosomes
  • ARHGAP21 co-localizes with SUMO2/3 in the cytoplasm and membrane compartments
  • basic FUNCTION
  • involved in the function and/or structure of the eukaryotic kinetochore
  • ubiquitin-like protein that can be conjugated to other proteins in a manner analogous to ubiquitination
  • SUMO-2/3 conjugation and the ubiquitin-proteasome system are tightly integrated and act in a cooperative manner
  • with other SUMO proteins, binding to lysine residues of target proteins and thereby modifying their stability, activity and subcellular localization
  • with SUMO2 and SUMO1 accumulate at DNA double-strand breaks sites in mammalian cells, with SUMO1 and SUMO2/3 accrual requiring the E3 ligase enzymes PIAS4 and PIAS1
  • SUMO2 and SUMO3 can rapidly convert to be conjugated in response to a variety of cellular stresses
  • SUMO2 and SUMO3 are specific and essential negative regulators of a noncanonical mechanism of IFN induction
  • CELLULAR PROCESS protein, degradation
    PHYSIOLOGICAL PROCESS cellular trafficking transport
    PATHWAY
    metabolism
    signaling
    a component
  • kinetochore
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • targeting proteins
  • covalently binding and modifying RANGAP1 involved in nuclear transport
  • interacting with CENPE (CENPE was found to be modified specifically by SUMO-2/3 and to possess SUMO-2/3 polymeric chain-binding activity essential for kinetochore localization)
  • EGLN3 SUMOylation by SUMO2 or SUMO3 contributes to EGLN3-mediated repression of HIF1-dependent transcriptional activity
  • PES1 could be modified by the small ubiquitin-like modifier (SUMO) SUMO1, SUMO2 and SUMO3, and SUMOylation of PES1 was stimulated by estrogen (E2)
  • SENP2 genetically interacts with SUMO2 and SUMO3 pivotal for the development of three major trophoblast layers
  • SUMO3 modification of PIAS1 modulates AR cellular distribution and stability
  • TRIM28 binds NLRP3, promotes SUMO1, SUMO2 and SUMO3 modification of NLRP3, and thereby inhibits NLRP3 ubiquitination and proteasomal degradation
  • SUMO3 or SUMO3-modified proteins modulate likely the localization, stability, and RING ubiquitin ligase activity of TRIM55
  • cell & other
    REGULATION
    repressed by expression of SUMO3, can be down-regulated at the transcription level by cellular oxidative stress
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS