E3 ubiquitin-protein ligase RFWD2 (Protein name
), RFWD2_MOUSE from NCBI database.
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General Annotation
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Antigen Annotation
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3D
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Predicted Eptitope
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Vaild Sequence
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Gene name:
Rfwd2(Cop1);
Protein name:
E3 ubiquitin-protein ligase RFWD2;
Alternative:
RING finger and WD repeat domain protein 2;Constitutive photomorphogenesis protein 1 homolog(mCOP1);
Organism:
Mouse (Mus musculus).
General Annotation
Sub Unit:
Homodimer. Homodimerization is mediated by the coiled coil domain. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Isoform 2 does not interact with CUL4A but still binds to RBX1, suggesting that the interaction may be mediated by another culllin protein. Isoform 1 and isoform 2 interact with CUL5 but not with CUL1, CUL2 not CUL3. Interacts with bZIP transcription factors JUN, JUNB and JUND but not with FOS, ATF2 nor XBP1. Interacts with p53 (TP53).
Function:
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1.
Subcellular Location:
Nucleus speckle
Cytoplasm
In the nucleus, it forms nuclear speckles.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];SUBCELLULAR LOCATION;TISSUE SPECIFICITY;DOMAIN;MUTAGENESIS OF 113-ARG-LYS-114; 197-LYS--ARG-201; 205-LYS--LYS-208; 244-LEU--LEU-246 AND 358-ARG--LYS-360
Vaild Sequence:
