RFWD3
entrez
55159
canonical
uniprot
Q6PCD5
canonical
ensembl
ENSG00000168411
resolver
ensp
ENSP00000354361
resolver
ensp
ENSP00000460049
resolver
ensp
ENSP00000558082
resolver
ensp
ENSP00000608495
resolver
ensp
ENSP00000608496
resolver
ensp
ENSP00000608497
resolver
ensp
ENSP00000608498
resolver
ensp
ENSP00000608499
resolver
ensp
ENSP00000608500
resolver
ensp
ENSP00000608501
resolver
ensp
ENSP00000608502
resolver
enst
ENST00000361070
resolver
enst
ENST00000571750
resolver
enst
ENST00000938436
resolver
enst
ENST00000938438
resolver
enst
ENST00000938439
resolver
enst
ENST00000938440
resolver
enst
ENST00000938441
resolver
enst
ENST00000938442
resolver
enst
ENST00000938443
resolver
genesymbol
RFWD3
resolver
genesymbol_syn
RNF201
resolver
hgnc
HGNC:25539
resolver
uniprot
A8K585
resolver
uniprot
B2RE35
resolver
uniprot
D3DUJ8
resolver
uniprot
Q5XKR3
resolver
uniprot
Q9H9Q3
resolver
uniprot
Q9NVT4
resolver
uniprot_entry
RFWD3_HUMAN
resolver
uniprot_sec
A8K585
resolver
uniprot_sec
B2RE35
resolver
uniprot_sec
D3DUJ8
resolver
uniprot_sec
Q5XKR3
resolver
uniprot_sec
Q9H9Q3
resolver
uniprot_sec
Q9NVT4
resolver
amino_acid_sequence
MAHEAMEYDVQVQLNHAEQQPAPAGMASSQGGPALLQPVPADVVSSQGVPSILQPAPAEVISSQATPPLLQPAPQLSVDLTEVEVLGEDTVENINPRTSEQHRQGSDGNHTIPASSLHSMTNFISGLQRLHGMLEFLRPSSSNHSVGPMRTRRRVSASRRARAGGSQRTDSARLRAPLDAYFQVSRTQPDLPATTYDSETRNPVSEELQVSSSSDSDSDSSAEYGGVVDQAEESGAVILEEQLAGVSAEQEVTCIDGGKTLPKQPSPQKSEPLLPSASMDEEEGDTCTICLEQWTNAGDHRLSALRCGHLFGYRCISTWLKGQVRKCPQCNKKARHSDIVVLYARTLRALDTSEQERMKSSLLKEQMLRKQAELESAQCRLQLQVLTDKCTRLQRRVQDLQKLTSHQSQNLQQPRGSQAWVLSCSPSSQGQHKHKYHFQKTFTVSQAGNCRIMAYCDALSCLVISQPSPQASFLPGFGVKMLSTANMKSSQYIPMHGKQIRGLAFSSYLRGLLLSASLDNTIKLTSLETNTVVQTYNAGRPVWSCCWCLDEANYIYAGLANGSILVYDVRNTSSHVQELVAQKARCPLVSLSYMPRAASAAFPYGGVLAGTLEDASFWEQKMDFSHWPHVLPLEPGGCIDFQTENSSRHCLVTYRPDKNHTTIRSVLMEMSYRLDDTGNPICSCQPVHTFFGGPTCKLLTKNAIFQSPENDGNILVCTGDEAANSALLWDAASGSLLQDLQTDQPVLDICPFEVNRNSYLATLTEKMVHIYKWE
uniprot
proteins
disease_involvement
DISEASE: Fanconi anemia, complementation group W (FANCW) [MIM:617784]: A form of Fanconi anemia, a disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28691929}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage (PubMed:21504906, PubMed:21558276, PubMed:26474068, PubMed:28575657, PubMed:28575658, PubMed:33321094). Plays a key role in RPA-mediated DNA damage signaling and repair (PubMed:21504906, PubMed:21558276, PubMed:26474068, PubMed:28575657, PubMed:28575658, PubMed:28691929). Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leading to remove them from DNA damage sites and promote homologous recombination (PubMed:26474068, PubMed:28575657, PubMed:28575658). Also mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint (PubMed:20173098). May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome (PubMed:20173098). In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53 (PubMed:20173098). Required to translesion DNA synthesis across DNA-protein cross-link adducts by catalyzing ubiquitination of proteins on single-stranded DNA (ssDNA) (PubMed:33321094). {ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:26474068, ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658, ECO:0000269|PubMed:28691929, ECO:0000269|PubMed:33321094}.
uniprot
proteins
mass_dalton
85094
uniprot
proteins
mutagenesis
MUTAGEN 36..38; /note="LQP->AAA: Decreased interaction with RAD51; when associated with 53-A--A-55 and 70-A--A-72."; /evidence="ECO:0000269|PubMed:28575658"; MUTAGEN 46; /note="S->A: Markedly decreases phosphorylation following ionizing radiation and abolishes ability to stimulate p53/TP53 ubiquitination; when associated with A-63."; /evidence="ECO:0000269|PubMed:20173098"; MUTAGEN 53..55; /note="LQP->AAA: Decreased interaction with RAD51; when associated with 36-A--A-38 and 70-A--A-72."; /evidence="ECO:0000269|PubMed:28575658"; MUTAGEN 63; /note="S->A: Markedly decreases phosphorylation following ionizing radiation and abolishes ability to stimulate p53/TP53 ubiquitination; when associated with A-46."; /evidence="ECO:0000269|PubMed:20173098"; MUTAGEN 70..72; /note="LQP->AAA: Decreased interaction with RAD51; when associated with 36-A--A-38 and 53-A--A-55."; /evidence="ECO:0000269|PubMed:28575658"; MUTAGEN 315; /note="C->A: Abolishes ability to stimulate p53/TP53 ubiquitination. No effect on nuclear localization in response to DNA damage."; /evidence="ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658"; MUTAGEN 499; /note="Q->A: Does not affect interaction with the RPA complex and subsequent recruitment at DNA damage sites."; /evidence="ECO:0000269|PubMed:28575657"; MUTAGEN 518; /note="L->A: Does not affect interaction with the RPA complex and subsequent recruitment at DNA damage sites."; /evidence="ECO:0000269|PubMed:28575657"; MUTAGEN 543; /note="W->A: Abolishes interaction with the RPA complex and subsequent recruitment at DNA damage sites."; /evidence="ECO:0000269|PubMed:28575657
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:26474068, ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or ATR. ATM phosphorylation occurs at early times upon DNA damage, while ATR is the major kinase at later times. Phosphorylation by ATM and ATR is required to stabilize p53/TP53. Part of the phosphorylation depends upon RPA2 presence. {ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20173098
uniprot
proteins
pubmed
21504906
uniprot
proteins
pubmed
21558276
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26474068
uniprot
proteins
pubmed
28575657
uniprot
proteins
pubmed
28575658
uniprot
proteins
pubmed
28691929
uniprot
proteins
pubmed
33321094
uniprot
proteins
sequence_length
774
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28691929}. Nucleus, PML body {ECO:0000269|PubMed:21558276}. Cytoplasm {ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:28691929}. Note=In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies (PubMed:21558276). 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 (PubMed:21504906, PubMed:28575657). This recruitment depends upon RPA2 (PubMed:21504906). {ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:28575657}.
uniprot
proteins