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FLASH GENE
Symbol SUMO1 contributors: mct/ - updated : 29-09-2016
HGNC name SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae)
HGNC id 12502
Location 2q33.1      Physical location : 203.070.902 - 203.103.322
Synonym name
  • SMT3 suppressor of mif two 3 homolog 1 (yeast)
  • small ubiquitin related modifier 1
  • ubiquitin-homology domain protein PIC1
  • sentrin
  • GAP-modifying protein 1
  • Synonym symbol(s) PIC1, GMP1, SMT3, UBL1, SENP2, SMT3C, SMT3H3, SUMO-1, SUMO, OFC10, DAP1
    DNA
    TYPE functioning gene
    STRUCTURE 32.42 kb     5 Exon(s)
    MAPPING cloned Y linked N status confirmed
    RNA
    TRANSCRIPTS type messenger
    text variants 1 and 2 encode the same protein
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    5 - 1527 11.5 97 - 2008 18983974
    also called variant 1
    6 - 1078 - 101 - 2008 18983974
    also called variant 2
    4 - 1452 - 76 - 2008 18983974
    also called variant 3
    EXPRESSION
    Type ubiquitous
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestivesalivary gland   highly
    Endocrineparathyroid   highly
    Reproductivemale systemtestis  highly
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Blood / hematopoieticbone marrow  highly
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
    HOMOLOGY
    interspecies homolog to yeast S.cerevisiae smt3 (see SMT3H1)
    intraspecies homolog to SMT3H1
    Homologene
    FAMILY
  • SMT3 subfamily
  • superfamily of ubiquitin-like proteins
  • SUMO subfamily
  • CATEGORY regulatory , transport
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,cytoskeleton,microtubule,mitotic spindle
    intracellular,nucleus,nucleoplasm,nuclear bodies,nuclear speckles
    intracellular,nuclear envelope,pore
    text
  • localizes to the mitotic spindle and spindle midzone
  • basic FUNCTION
  • involved in posttranslational modifications of many proteins
  • protecting against both Fas/Apo-1 (TNFRSF6) or TNFR1 apoptosis, and antagonizing IKBA to generate protein resistant to degradation
  • involved in DNA repair topoisomerase mediated DNA damage
  • involved in NF-kappaB activation and may thus be involved in type 1 diabetes through apoptosis in pancreatic beta-cells
  • may control the activity of a repertoire of downstream effectors involved in palatogenesis
  • with other SUMO proteins, binding to lysine residues of target proteins and thereby modifying their stability, activity and subcellular localization
  • playing a role in meiotic chromosome synapsis
  • both SUMO1 and SUMO2 had the ability to enhance the solubility of MMP13, with the SUMO2 tag having a more significant effect
  • with SUMO2 and SUMO3 accumulate at DNA double-strand breaks sites in mammalian cells, with SUMO1 and SUMO2/3 accrual requiring the E3 ligase enzymes PIAS4 and PIAS1
  • covalently monoconjugated to proteins at lysine residues, thereby playing a critical role in many cellular processes, as mentioned earlier, through rapidly reversible changes in sumoylation status
  • plays an important role in modulation of NADPH oxidase complex (NOX) activity required for ROS generation
  • plays an essential role in ROS generation caused by NADPH oxidase activity
  • plays a key role in ROS generation by modifying NOX and inhibiting its enzymatic activity
  • is an important regulatory mechanism that indirectly represses the production of ROS to ameliorate cellular stress
  • CELLULAR PROCESS cell cycle, checkpoint
    cell life
    nucleotide, repair, recombination
    protein, degradation
    cell organization/biogenesis
    PHYSIOLOGICAL PROCESS immunity/defense , cellular trafficking transport
    text nucleo-cytoplasmic protein transport, stress response
    PATHWAY
    metabolism
    signaling
  • SUMO pathway critically regulates PRDM1 function during plasma cell differentiation
  • a component
  • non-covalent ternary complex formed by PIAS1, SUMO1, and UBE2I proteins involved in transcriptional regulation
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • covalently linked to PML and NFKBIA via a conjugation step, requiring the activating enzymes SAE1 (AOS1) and SAE2 (UBA2)
  • associating with RAD51 and RAD52 proteins in the double strand break RAD51/RAD52 repair pathway
  • conjugating with TOP2A, TOP2B in response to DNA damage
  • conjugating to PCNA
  • interacting wiht DDXP1, TP53
  • targeting RANBP2
  • sumoylating ETV6 after conjugation of ETV6 by UBE2I
  • physically interacts with KLF4 in a region that matches an acidic and hydrophobic residue-rich SUMO-interacting motif (SIM) consensus
  • decreases JNK and MAPK14 activities, downstream of intracellular ROS signaling molecule, and increases cell viability response to heat-shock
  • partially sumoylates CYBB at plasma membrane and negatively modulates the ROS generation from CYBB
  • SUMOylation strongly enhances NKX2-5 transcriptional activity and that AA K51 of NKX2-5 is a SUMOylation target
  • ATP2A2 binds to SUMO1 and to ubiquitin-conjugating enzyme E2I (UBE2I)
  • more extensive contacts among SUMO, UBE2I, and RANBP2 in complexes containing SUMO1 compared with SUMO2
  • SUMO modification of the GLP1R could be a contributing factor to reduced incretin responsiveness
  • importance of SUMO modification of PCNA in preventing replication fork collapse to DNA double-strand breaks and providing genome stability
  • direct interaction between PGRMC1 and SUMO1, and this interaction is increased by progesterone
  • SUMO1, or more likely, a sumoylated protein, acts as an allosteric regulator of DPP9
  • DPP9 and SUMO1 interact in a SIM-independent manner, suggesting a novel surface on SUMO1 for noncovalent interactions with downstream effectors
  • noncovalent interaction of DPP9 with SUMO1 leads to activation of the peptidase
  • UBA2 interacts with both SUMO1 and SUMO2, both DPP8 and DPP9 showed a strong preference toward SUMO1 binding
  • CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the transcriptional activity of ESR1
  • SUMO1 is involved in posttranslational modification of the lamin A tail
  • TRIM5 is a SUMO1 and SUMO2 substrate
  • AGO2 can be SUMOylated in mammalian cells by both SUMO1 and SUMO2
  • cell & other
    REGULATION
    activated by E1 enzymes
    Other conjugating with TOP1
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --low  
    in autism with duplicated UBE3A
    constitutional        
    haploinsufficiency leads to cleft lip and palate
    constitutional     --other  
    alterations in SUMO1 substrate conjugation may occur and global posttranslational modifications by ubiquitin may play an important role in the mechanisms underlying Alzheimer disease
    constitutional     --over  
    in isolated cardiomyocytes augmented contractility and accelerated Ca2+ decay
    Susceptibility to non-syndromic cleft lip with or without cleft palate (NSCLP)
    Variant & Polymorphism SNP significant correlations between a 4-SNP SUMO1 haplotype and NSCLP
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    cardiovascularaquiredheart failure
    targeting SUMO1 may provide a novel therapeutic strategy for the treatment of heart failure
    ANIMAL & CELL MODELS