ATAD5
entrez
79915
canonical
uniprot
Q96QE3
canonical
ensembl
ENSG00000176208
resolver
ensp
ENSP00000313171
resolver
ensp
ENSP00000463102
resolver
ensp
ENSP00000603330
resolver
genesymbol
ATAD5
resolver
genesymbol_syn
C17orf41
resolver
genesymbol_syn
Elg1
resolver
genesymbol_syn
FRAG1
resolver
hgnc
HGNC:25752
resolver
uniprot
Q05DH0
resolver
uniprot
Q69YR6
resolver
uniprot
Q9H9I1
resolver
uniprot_entry
ATAD5_HUMAN
resolver
uniprot_sec
Q05DH0
resolver
uniprot_sec
Q69YR6
resolver
uniprot_sec
Q9H9I1
resolver
amino_acid_sequence
MVGVLAMAAAAAPPPVKDCEIEPCKKRKKDDDTSTCKTITKYLSPLGKTRDRVFAPPKPSNILDYFRKTSPTNEKTQLGKECKIKSPESVPVDSNKDCTTPLEMFSNVEFKKKRKRVNLSHQLNNIKTENEAPIEISSDDSKEDYSLNNDFVESSTSVLRYKKQVEVLAENIQDTKSQPNTMTSLQNSKKVNPKQGTTKNDFKKLRKRKCRDVVDLSESLPLAEELNLLKKDGKDTKQMENTTSHANSRDNVTEAAQLNDSIITVSYEEFLKSHKENKVEEIPDSTMSICVPSETVDEIVKSGYISESENSEISQQVRFKTVTVLAQVHPIPPKKTGKIPRIFLKQKQFEMENSLSDPENEQTVQKRKSNVVIQEEELELAVLEAGSSEAVKPKCTLEERQQFMKAFRQPASDALKNGVKKSSDKQKDLNEKCLYEVGRDDNSKKIMENSGIQMVSKNGNLQLHTDKGSFLKEKNKKLKKKNKKTLDTGAIPGKNREGNTQKKETTFFLKEKQYQNRMSLRQRKTEFFKSSTLFNNESLVYEDIANDDLLKVSSLCNNNKLSRKTSIPVKDIKLTQSKAESEASLLNVSTPKSTRRSGRISSTPTTETIRGIDSDDVQDNSQLKASTQKAANLSEKHSLYTAELITVPFDSESPIRMKFTRISTPKKSKKKSNKRSEKSEATDGGFTSQIRKASNTSKNISKAKQLIEKAKALHISRSKVTEEIAIPLRRSSRHQTLPERKKLSETEDSVIIIDSSPTALKHPEKNQKKLQCLNDVLGKKLNTSTKNVPGKMKVAPLFLVRKAQKAADPVPSFDESSQDTSEKSQDCDVQCKAKRDFLMSGLPDLLKRQIAKKAAALDVYNAVSTSFQRVVHVQQKDDGCCLWHLKPPSCPLLTKFKELNTKVIDLSKCGIALGEFSTLNSKLKSGNSAAVFMRTRKEFTEEVRNLLLEEIRWSNPEFSLKKYFPLLLKKQIEHQVLSSECHSKQELEADVSHKETKRKLVEAENSKSKRKKPNEYSKNLEKTNRKSEELSKRNNSSGIKLDSSKDSGTEDMLWTEKYQPQTASELIGNELAIKKLHSWLKDWKRRAELEERQNLKGKRDEKHEDFSGGIDFKGSSDDEEESRLCNTVLITGPTGVGKTAAVYACAQELGFKIFEVNASSQRSGRQILSQLKEATQSHQVDKQGVNSQKPCFFNSYYIGKSPKKISSPKKVVTSPRKVPPPSPKSSGPKRALPPKTLANYFKVSPKPKNNEEIGMLLENNKGIKNSFEQKQITQTKSTNATNSNVKDVGAEEPSRKNATSLILFEEVDVIFDEDAGFLNAIKTFMATTKRPVILTTSDPTFSLMFDGCFEEIKFSTPSLLNVASYLQMICLTENFRTDVKDFVTLLTANTCDIRKSILYLQFWIRSGGGVLEERPLTLYRGNSRNVQLVCSEHGLDNKIYPKNTKKKRVDLPKCDSGCAETLFGLKNIFSPSEDLFSFLKHKITMKEEWHKFIQLLTEFQMRNVDFLYSNLEFILPLPVDTIPETKNFCGPSVTVDASAATKSMNCLARKHSEREQPLKKSQKKKQKKTLVILDDSDLFDTDLDFPDQSISLSSVSSSSNAEESKTGDEESKARDKGNNPETKKSIPCPPKTTAGKKCSALVSHCLNSLSEFMDNMSFLDALLTDVREQNKYGRNDFSWTNGKVTSGLCDEFSLESNDGWTSQSSGELKAAAEALSFTKCSSAISKALETLNSCKKLGRDPTNDLTFYVSQKRNNVYFSQSAANLDNAWKRISVIKSVFSSRSLLYVGNRQASIIEYLPTLRNICKTEKLKEQGKSKRRFLHYFEGIHLDIPKETVNTLAADFP
uniprot
proteins
function
FUNCTION: Has an important role in DNA replication and in maintaining genome integrity during replication stress (PubMed:15983387, PubMed:19755857). Involved in a RAD9A-related damage checkpoint, a pathway that is important in determining whether DNA damage is compatible with cell survival or whether it requires cell elimination by apoptosis (PubMed:15983387). Modulates the RAD9A interaction with BCL2 and thereby induces DNA damage-induced apoptosis (PubMed:15983387). Promotes PCNA deubiquitination by recruiting the ubiquitin-specific protease 1 (USP1) and WDR48 thereby down-regulating the error-prone damage bypass pathway (PubMed:20147293). As component of the ATAD5 RFC-like complex, regulates the function of the DNA polymerase processivity factor PCNA by unloading the ring-shaped PCNA homotrimer from DNA after replication during the S phase of the cell cycle (PubMed:23277426, PubMed:23937667). This seems to be dependent on its ATPase activity (PubMed:23277426). Plays important roles in restarting stalled replication forks under replication stress, by unloading the PCNA homotrimer from DNA and recruiting RAD51 possibly through an ATR-dependent manner (PubMed:31844045). Ultimately this enables replication fork regression, breakage, and eventual fork restart (PubMed:31844045). Both the PCNA unloading activity and the interaction with WDR48 are required to efficiently recruit RAD51 to stalled replication forks (PubMed:31844045). Promotes the generation of MUS81-mediated single-stranded DNA-associated breaks in response to replication stress, which is an alternative pathway to restart stalled/regressed replication forks (PubMed:31844045). {ECO:0000269|PubMed:15983387, ECO:0000269|PubMed:19755857, ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:23277426, ECO:0000269|PubMed:23937667, ECO:0000269|PubMed:31844045}.
uniprot
proteins
mass_dalton
207570
uniprot
proteins
mutagenesis
MUTAGEN 368..384; /note="Missing: Abolishes interaction with WDR48 and recruitment of RAD51 at site of stalled replication forks under replication stress. Reduces down-regulation of PCNA monoubiquitination but retains the ability to unload PCNA from chromatin."; /evidence="ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:23277426, ECO:0000269|PubMed:31844045"; MUTAGEN 642..645; /note="Missing: Loss of interaction with RAD51 and loading of RAD51 to stalled replication forks during replication stress. Loss of processing of stalled replication forks. Retains PCNA-unloading ability."; /evidence="ECO:0000269|PubMed:31844045"; MUTAGEN 1138; /note="K->E: Results in defective PCNA removal from chromatin and recruitment of RAD51 at site of stalled replication forks under replication stress. Loss of processing of stalled replication forks. Retains interaction with PCNA and RFC4."; /evidence="ECO:0000269|PubMed:23277426, ECO:0000269|PubMed:31844045"; MUTAGEN 1169; /note="S->A: No effect on the RAD9A interaction after MMS exposure. Resists to DNA damage after MMS exposure."; /evidence="ECO:0000269|PubMed:15983387"; MUTAGEN 1187; /note="S->A: Weakly affects the RAD9A interaction after MMS exposure."; /evidence="ECO:0000269|PubMed:15983387"; MUTAGEN 1430; /note="C->G: Abolishes RB1 binding. Abolishes RB1 binding; when associated with K-1432. Weakly detected after methyl methane-sulfonate (MMS) treatment. Expression detected after MMS treatment; when associated with K-1432. Weakly affects the RAD9A interaction after MMS exposure. No effect on the RAD9A interaction after MMS exposure; when associated with K-1432. Resists to DNA damage after MMS exposure; when associated with K-1432."; /evidence="ECO:0000269|PubMed:15983387"; MUTAGEN 1432; /note="E->K: Abolishes RB1 binding; when associated with G-1430. Expression detected after methyl methane-sulfonate (MMS) treatment; when associated with G-1430. No effect on the RAD9A interaction after MMS exposure; when associated with G-1430. Resists to DNA damage after MMS exposure; when associated with G-1430."; /evidence="ECO:0000269|PubMed:15983387
uniprot
proteins
post_translational_modification
PTM: ATR may stimulate the RAD9A dissociation.
uniprot
proteins
protein_family
AAA ATPase family
uniprot
proteins
pubmed
11468690
uniprot
proteins
pubmed
13678589
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15983387
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19755857
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20147293
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21555454
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23277426
uniprot
proteins
pubmed
23937667
uniprot
proteins
pubmed
26282398
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
31844045
uniprot
proteins
pubmed
39106866
uniprot
proteins
sequence_length
1844
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19755857, ECO:0000269|PubMed:20147293}. Note=Accumulates in nuclear foci at sites of stalled DNA replication forks in response to DNA damage. {ECO:0000269|PubMed:19755857}.
uniprot
proteins