A0A1L8GLK3 · RFW3L_XENLA
- ProteinE3 ubiquitin-protein ligase rfwd3.L
- Generfwd3.L
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids751 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage (By similarity).
Plays a key role in RPA-mediated DNA damage signaling and repair (By similarity).
Required to translesion DNA synthesis across DNA-protein cross-link adducts by catalyzing ubiquitination of proteins on single-stranded DNA (ssDNA) (PubMed:33321094).
Mediates ubiquitination of the hmces DNA-protein cross-link, possibly promoting its degradation (PubMed:33321094).
Plays a key role in RPA-mediated DNA damage signaling and repair (By similarity).
Required to translesion DNA synthesis across DNA-protein cross-link adducts by catalyzing ubiquitination of proteins on single-stranded DNA (ssDNA) (PubMed:33321094).
Mediates ubiquitination of the hmces DNA-protein cross-link, possibly promoting its degradation (PubMed:33321094).
Catalytic activity
Cofactor
Note: Binds 1 [4Fe-4S] cluster.
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | PML body | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | interstrand cross-link repair | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase rfwd3.L
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionA0A1L8GLK3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies. In response to replication block, such as that caused by hydroxyurea treatment, or to DNA damage caused by ionizing radiations or doxorubicin, recruited to the nucleus, to stalled replication forks or to sites of DNA repair.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000459743 | 1-751 | E3 ubiquitin-protein ligase rfwd3.L | |||
Sequence: MAQEEMEVDLPNLLGPMDSNRVSTSHQPLGSRQVLFLPPPITYSDDSEELFLGPTEPHDVIVLDSGEEAPAQVVAPTNPLQMLHGALEQLRQAAELRSSVRRTRVQRRSTRRQQRGGSQRTAGTSSRAALSSFFQINRTQGLAPTLEREERNTVLRTESLRTLPGDSSDETVELSEEEEGEGSSTDVDEVEINAGAAPPAEPAPEELQINVVEVQAEASAVSDSLPIPERVTLPLQIQTKQKTPVKLLSPVKPLPPEEDEGDTCAICFEPWTNAGQHRLSALRCGHLFGFTCIERWLKGGASKCPQCNKKAKRADIVVLYARSLKALDTSEQERMKSSLEMEQSMRRKAQLESAQCRLQVQVLTDECGKLRNQIQELKMLIAQHGTGTSVQASSSRSTISGSLSSSQGQHKYSFEKAILISQTGSCRVMSYCESMSCLVVSQPSPQTTLIPGCGIKKLSAANLKSSQYVPIHSKQIRGLAFSNRSEGLLLSAALDNTVKLTSLLTNTVVQTYNTGRPVWSCCWCSDNSNYVYAGLINGSVLVYDLRDTSNCVQELVPLGSRCPVVSLSYVPRAASEVFPCGGVLVGTLEGACFWEMKDDQYRPHVLPLEPGGCTDIQIESNTRHCLVTYRPGKNYNFVRGVMMELTSNRLNDSEDEYSCSCYPVQTFNAGSTCKLLTKNAIFQSPERDGTVLVCAGDEASNSAMLWHSGNGTLLQKLQADQPVLDICPMEVNQSSMLATLTEKMVKIYKWE |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: MAQEEMEVDLPNLLGPMDSNRVSTSHQPLGSRQ | ||||||
Compositional bias | 17-31 | Polar residues | ||||
Sequence: MDSNRVSTSHQPLGS | ||||||
Region | 97-188 | Disordered | ||||
Sequence: RSSVRRTRVQRRSTRRQQRGGSQRTAGTSSRAALSSFFQINRTQGLAPTLEREERNTVLRTESLRTLPGDSSDETVELSEEEEGEGSSTDVD | ||||||
Compositional bias | 115-142 | Polar residues | ||||
Sequence: RGGSQRTAGTSSRAALSSFFQINRTQGL | ||||||
Compositional bias | 170-186 | Acidic residues | ||||
Sequence: ETVELSEEEEGEGSSTD | ||||||
Zinc finger | 264-308 | RING-type; degenerate | ||||
Sequence: CAICFEPWTNAGQHRLSALRCGHLFGFTCIERWLKGGASKCPQCN | ||||||
Repeat | 471-511 | WD 1 | ||||
Sequence: IHSKQIRGLAFSNRSEGLLLSAALDNTVKLTSLLTNTVVQT | ||||||
Repeat | 513-553 | WD 2 | ||||
Sequence: NTGRPVWSCCWCSDNSNYVYAGLINGSVLVYDLRDTSNCVQ | ||||||
Repeat | 559-604 | WD 3 | ||||
Sequence: GSRCPVVSLSYVPRAASEVFPCGGVLVGTLEGACFWEMKDDQYRPH |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length751
- Mass (Da)82,410
- Last updated2017-03-15 v1
- Checksum934CFDA861504586
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 17-31 | Polar residues | ||||
Sequence: MDSNRVSTSHQPLGS | ||||||
Compositional bias | 115-142 | Polar residues | ||||
Sequence: RGGSQRTAGTSSRAALSSFFQINRTQGL | ||||||
Compositional bias | 170-186 | Acidic residues | ||||
Sequence: ETVELSEEEEGEGSSTD |
Keywords
- Technical term