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FLASH GENE
Symbol UBE2D1 contributors: mct - updated : 31-01-2023
HGNC name ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)
HGNC id 12474
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • a conserved UBC domain of 150 AA harboring the cysteine residue required for enzyme-ubiquitin thioester formation
  • six transmembrane spanning segments with intracellular N and C termini and a REXXE motif ressembling a motif involved in yeast transport
  • HOMOLOGY
    interspecies homolog to yeast UBC4/5
    Homologene
    FAMILY
    CATEGORY enzyme
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,endosome
    intracellular,cytoplasm,cytosolic
    intracellular,nucleus,nucleoplasm
    text
  • located in recycling endosomes
  • localized to the cytoplasm
  • basic FUNCTION
  • involved in the degradation of cellular proteins
  • mediating the E6-AP dependent ubiquitination of TP53
  • regulates DAPK3 accumulation in promyelocytic leukemia protein nuclear body (PML-NB)by interacting with DAPK3 and stimulating its ubiquitination
  • catalytically active UBE2D1 is required for IRF3 activation by viral infection
  • critical regulators of the stability of BIRC2 protein following destabilizing stimuli such as TNFSF12 or CD40 signalling or IAP antagonists
  • promiscuous E2 enzyme with an innate preference for forming polyubiquitin chains through lysine 11 (K11), lysine 48 (K48), and lysine 63 (K63) of Ubiquitin
  • BIRC2 and UBE2D1 promote K11-linked polyubiquitination of RIPK1 in TNF signalling
  • CELLULAR PROCESS cell cycle
    protein, degradation
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component component of a complex with UBE1, UBE2D1, UBE2DG1, CBL ubiquitination complex
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • DAPK3-binding partner (induced ubiquitination of DAPK3)
  • TRIM21 is an E3 ligase dependent on the ubiquitin conjugation enzymes UBE2D1 and UBE2E1
  • UBE2N and UBE2D1 had distinct effects on the conformational dynamics of STUB1, suggesting different roles of the STUB1-E2 interaction in the ubiquitination of substrates and interaction with chaperones
  • interacting with MYLIP (MYLIP-UBE2D1 complex is an important determinant of LDLR activity)
  • OTUB1 is a Lys48-specific deubiquitinating enzyme that forms a complex with E2 ubiquitin (Ub)-conjugating enzymes including UBE2N and UBE2D1
  • preferentially binds to the monoubiquitinated OTUB1 via UB interaction with its backside donor Ub-interacting surface
  • MARCH1 likely undergoes lysine-independent ubiquitination by an as yet unidentified E3 ubiquitin ligase that, together with UBE2D1, regulates MARCH1 expression
  • CNPY2 inhibits MYLIP-mediated AR protein degradation in prostate cancer cells, and decreased the ubiquitination activity of MYLIP by inhibition of interaction between MYLIP and UBE2D1, an E2 ubiquitin ligase
  • NEDD8 acts as a nexus that binds disparate cullin elements and the RING-activated ubiquitin-linked UBE2D1
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    cancerdigestivestomach
    silencing of UBE2D1 inhibited cell migration in gastric cancer, decreasing ubiquitination of SMAD4
    ANIMAL & CELL MODELS