Protein: UBE4_CAEEL
Sequence: MIEDEKAGLQPMDISDASVFFFQADVESKDFLTSLFDCEGKSDDRMLRYADAIIDVQNLNFDVSPQCLQSNIAEIITKFVLLSQDGSRRGLSRSFNFIDPDIIAGCREEDAIEFLLINFVRCHHELGKSGTSNCYKKTLESTRKAVFSVFVMIQRGYLESQLRSQHASLVFTKRLLEDTVSNVFLRTLVEYLASTDECDEDAITETFNPIFGILRSGIICQRFEDNKDEIVRQILRVMNLLLSIRLPSNGPRPLSNLLVNREDFLPTPSEKIQGREFGLMSFLGPFFSYGLESSARRPNHRVFVDCEEDARKYDGSVNTEQKLYFQRMDPIRTMLHQLMLPLASDQGSRNKTLRWIATIISTNDIRTRSHYDPSDVLCDHYMTNFLSVMYMFSEKIDLSKIIVDYPFLPSSLINISKETRLKMDESGAVAFASQFADRPDEYHFSTVCFFLTIAAQRLVIPPLMNQISEYSRHLKELKHKINALKEKLNTVSGFERAEVEKKLNYETEHWKLMSRHLLCVKTQAQDPALMASSMDFVDKQMKFILNLLCDNLDLLGDDSQLPTEVSQMFCALPEYFLEDALDFYIFAISNGMKLLMERNADWISRLTVLFTQYHYIKSPFLVSKLVRVLSSIQPPLWFNVVRLRMAQENLLMCMIKFYSDFEDNGDFYEKFNVRGNIQYMLEKMEEDMFYKGKFMDMARECGAEFIRFVNMVINDATWCIDESLSGLKSIHDVEKKMANKVEWDNTDQEIRNQDLGVYEEAKRKVKGWLGTAKSNLKLLLSITVNSPEPFRTPVLGERLAAMLNHNLSQLIGSKASELKVKDPRSYGWEPREFVSLLISIYLKLNMPAFVKYIAYDERTYSPEFFHNAIECMRKNSIVGFSQLESFEHLAEDVKKEYEAKAELEEEYDDVPEEFKDPIMDAIMVDPVKLPSGHVMDRAVIERHLLSTPNNPFNRAPLSHNELSPDSELKAKIQEWICQKRNSKK
What is the function of this protein?
Acts as an E4 ubiquitin ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (PubMed:27669035).  The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues (PubMed:27669035).  Also functions as an E3 ligase in conjunction with specific E1 and E2 ligases (PubMed:15294159, PubMed:27669035, PubMed:29396393).  Probably by regulating protein ubiquitination at DNA damage repair sites, coordinates DNA double-strand-break repair and apoptosis in the germline (PubMed:27669035).  Required for germline apoptosis in response to DNA damage downstream of cep-1 (PubMed:27669035).  Involved in the resolution of DNA-repair sites by promoting the release of rad-51 from DNA damage foci (PubMed:27669035).  In association with protein-ligase chn-1, acts as an E3/E4 ligase to poly-ubiquitinate lysine residues in the UCS domain of myosin chaperone unc-45 (PubMed:15294159, PubMed:29396393).  By targeting myosin chaperone unc-45 for proteasomal degradation, regulates myosin assembly in body wall muscles in association with cdc-48. 1 and chn-1 (PubMed:15294159, PubMed:17369820).  However, in a contrasting study, acts as an E3 ligase, independently of chn-1, to poly-ubiquitinate unc-45 without promoting unc-45 proteasomal degradation (PubMed:29396393).  Instead, uses unc-45 as an adapter protein to recruit and poly-ubiquitinate unfolded myosin heavy chain B unc-54 (PubMed:29396393).
What are the official names of this protein?
Ubiquitin conjugation factor E4 ufd-2, E4 ubiquitin-protein ligase ufd-2, RING-type E3 ubiquitin transferase E4, Ubiquitin fusion degradation protein 2.
What is the protein family that this protein belongs to?
Belongs to the ubiquitin conjugation factor E4 family.
What are the subcellular locations of this protein?
Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nucleolus. Note=Localizes to germline syncytium. In the late pachytene, accumulates at the nuclear periphery forming a ring. Following ionizing radiation-mediated DNA damage, localizes to foci within nucleoli where it colocalizes with cdc-48.1 and/or cdc- 48.2, atx-3, proteasome alpha subunit and ubiquitinated proteins. Localization to foci is ubiquitin-dependent and regulated by E3 ligase hecd-1 and deubiquitinating enzyme atx-3. ufd-2 foci are formed following the initiation of homologous recombination (HR) and persist until HR is completed. ufd-2 foci are also formed upon cep-1 activation.