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RNF4

Domain

The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate.

The RING-type zinc finger domain is required for the ubiquitination of polysumoylated substrates.

Function

E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.

Pathway

Protein modification; protein ubiquitination.

Post-translational modifications

Sumoylated; conjugated by one or two SUMO1 moieties.

Autoubiquitinated.

Tissue specificity

Widely expressed at low levels in many tissues; highly expressed in testis.

Cellular localization

  • Cytoplasm
  • Nucleus
  • Nucleus
  • PML body
  • Nucleus
  • Nucleoplasm

Alternative names

  • E3 ubiquitin-protein ligase RNF4
  • RING finger protein 4
  • RING-type E3 ubiquitin transferase RNF4
  • Small nuclear ring finger protein
  • Protein SNURF
  • RNF4
  • SNURF
  • RES4-26

Target type

Proteins

Molecular weight

21319Da