RAD23A
entrez
5886
canonical
uniprot
P54725
canonical
ensembl
ENSG00000179262
resolver
ensp
ENSP00000321365
resolver
ensp
ENSP00000467024
resolver
ensp
ENSP00000468674
resolver
genesymbol
RAD23A
resolver
hgnc
HGNC:9812
resolver
uniprot
A8K1J3
resolver
uniprot
K7ESE3
resolver
uniprot
Q59EU8
resolver
uniprot
Q5M7Z1
resolver
uniprot_entry
A8K1J3_HUMAN
resolver
uniprot_entry
RD23A_HUMAN
resolver
uniprot_sec
K7ESE3
resolver
uniprot_sec
Q59EU8
resolver
uniprot_sec
Q5M7Z1
resolver
amino_acid_sequence
MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
uniprot
proteins
ec_number
1.14.11.-
uniprot
proteins
function
FUNCTION: Multifunctional protein that participates in histone H4K20 demethylation, DNA repair, ubiquitin-dependent protein degradation, transcriptional regulation, and viral replication (PubMed:12643283, PubMed:14621999, PubMed:15321727, PubMed:20614012, PubMed:32209475, PubMed:9372924). Specifically demethylates mono-, di- and trimethylated 'Lys-20' of histone H4 (H4K20me1, H4K20me2, H4K20me3, respectively) into unmethylated forms. Activates the transcription of coding genes by demethylating H4K20me1 and the transcription of repetitive elements by demethylating H4K20me3 (PubMed:32209475). Involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome (PubMed:12643283, PubMed:14621999, PubMed:15321727). Involved in nucleotide excision repair, is considered functionally equivalent to RAD23B in global genome nucleotide excision repair (GG-NER) through its association with XPC. In vitro, the XPC-RAD23A complex demonstrates NER activity (PubMed:9372924). Can stabilize XPC (By similarity). {ECO:0000250|UniProtKB:P54726, ECO:0000269|PubMed:12643283, ECO:0000269|PubMed:14621999, ECO:0000269|PubMed:15321727, ECO:0000269|PubMed:20614012, ECO:0000269|PubMed:32209475, ECO:0000269|PubMed:9372924}.; FUNCTION: (Microbial infection) Involved in -dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269|PubMed:20614012}.
uniprot
proteins
mass_dalton
39609
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="K->A: No effect on interaction with EEF1A1."; /evidence="ECO:0000269|PubMed:16712842"; MUTAGEN 9; /note="T->A: Abolishes interaction with PSMD4; when associated with T-49."; /evidence="ECO:0000269|PubMed:14557549"; MUTAGEN 10; /note="L->E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with E-47."; /evidence="ECO:0000269|PubMed:18234089"; MUTAGEN 47; /note="K->A: No effect on UBL-UBA domain interaction."; /evidence="ECO:0000269|PubMed:18234089"; MUTAGEN 47; /note="K->E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with E-10. Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with E-77."; /evidence="ECO:0000269|PubMed:18234089"; MUTAGEN 49; /note="I->A: Impairs interaction with PSMD4."; /evidence="ECO:0000269|PubMed:12970176, ECO:0000269|PubMed:14557549"; MUTAGEN 49; /note="I->T: Abolishes interaction with PSMD4; when associated with A-9."; /evidence="ECO:0000269|PubMed:12970176, ECO:0000269|PubMed:14557549"; MUTAGEN 54; /note="I->A: Impairs interaction with PSMD4."; /evidence="ECO:0000269|PubMed:12970176"; MUTAGEN 71; /note="F->A: Impairs interaction with PSMD4."; /evidence="ECO:0000269|PubMed:12970176"; MUTAGEN 77; /note="T->E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with E-47."; /evidence="ECO:0000269|PubMed:12970176, ECO:0000269|PubMed:18234089"; MUTAGEN 77; /note="T->S: No effect on interaction with PSMD4."; /evidence="ECO:0000269|PubMed:12970176, ECO:0000269|PubMed:18234089"; MUTAGEN 79; /note="T->P: Increases interaction with PSMD1 and PSMC1."; /evidence="ECO:0000269|PubMed:16712842"; MUTAGEN 192; /note="H->A: Decreases binding to Ni(2+). Abolishes binding to Ni(2+); when associated with A-196."; /evidence="ECO:0000269|PubMed:32209475"; MUTAGEN 196; /note="E->A: Decreases binding to Ni(2+). Abolishes binding to Ni(2+); when associated with A-192."; /evidence="ECO:0000269|PubMed:32209475"; MUTAGEN 333; /note="P->E: Abolishes interaction with HIV-1 vpr."; /evidence="ECO:0000269|PubMed:11087358
uniprot
proteins
protein_family
RAD23 family
uniprot
proteins
pubmed
10488153
uniprot
proteins
pubmed
10915768
uniprot
proteins
pubmed
11087358
uniprot
proteins
pubmed
12079361
uniprot
proteins
pubmed
12643283
uniprot
proteins
pubmed
12970176
uniprot
proteins
pubmed
14557549
uniprot
proteins
pubmed
14621999
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15321727
uniprot
proteins
pubmed
15322280
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15949443
uniprot
proteins
pubmed
16712842
uniprot
proteins
pubmed
17098253
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18234089
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20614012
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
30455355
uniprot
proteins
pubmed
32209475
uniprot
proteins
pubmed
8168482
uniprot
proteins
pubmed
9371639
uniprot
proteins
pubmed
9372924
uniprot
proteins
pubmed
9846873
uniprot
proteins
sequence_length
363
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32209475}.
uniprot
proteins