RAD9A
entrez
5883
canonical
uniprot
Q99638
canonical
ensembl
ENSG00000172613
resolver
ensp
ENSP00000311360
resolver
enst
ENST00000307980
resolver
genesymbol
RAD9A
resolver
hgnc
HGNC:9827
resolver
uniprot
B2RCZ8
resolver
uniprot
Q6FI29
resolver
uniprot
Q96C41
resolver
uniprot_entry
RAD9A_HUMAN
resolver
uniprot_sec
B2RCZ8
resolver
uniprot_sec
Q6FI29
resolver
uniprot_sec
Q96C41
resolver
amino_acid_sequence
MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQYQAATPGQDLLRCKILMKSFLSVFRSLAMLEKTVEKCCISLNGRSSRLVVQLHCKFGVRKTHNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRSYHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHFDAPGRPAIFTIKDSLLDGHFVLATLSDTDSHSQDLGSPERHQPVPQLQAHSTPHPDDFANDDIDSYMIAMETTIGNEGSRVLPSISLSPGPQPPKSPGPHSEEEDEAEPSTVPGTPPPKKFRSLFFGSILAPVRSPQGPSPVLAEDSEGEG
uniprot
proteins
ec_number
3.1.11.2
uniprot
proteins
function
FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10713044, PubMed:17575048, PubMed:20545769, PubMed:21659603, PubMed:31135337). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:21659603). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:21659603). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:21659603). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). RAD9A possesses 3'->5' double stranded DNA exonuclease activity (PubMed:10713044). {ECO:0000269|PubMed:10713044, ECO:0000269|PubMed:17575048, ECO:0000269|PubMed:20545769, ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:31135337}.
uniprot
proteins
mass_dalton
42547
uniprot
proteins
mutagenesis
MUTAGEN 28; /note="Y->F: Abolishes phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:11971963"; MUTAGEN 272; /note="S->A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-277; A-328; A-341; A-375; A-380 and A-387."; /evidence="ECO:0000269|PubMed:12709442"; MUTAGEN 277; /note="S->A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-328; A-341; A-375; A-380 and A-387."; /evidence="ECO:0000269|PubMed:12709442"; MUTAGEN 328; /note="S->A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-341; A-375; A-380 and A-387."; /evidence="ECO:0000269|PubMed:12709442"; MUTAGEN 341; /note="S->A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-375; A-380 and A-387. Abolished phosphorylation by CK2, preventing interaction with TOPBP1; when associated with A-387."; /evidence="ECO:0000269|PubMed:12709442, ECO:0000269|PubMed:20545769"; MUTAGEN 341; /note="S->E: Mimics phosphorylation, leading to weak but significant interaction with TOPBP1; when associated with E-387."; /evidence="ECO:0000269|PubMed:20545769"; MUTAGEN 375; /note="S->A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-380 and A-387."; /evidence="ECO:0000269|PubMed:12709442"; MUTAGEN 380; /note="S->A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-387."; /evidence="ECO:0000269|PubMed:12709442"; MUTAGEN 387; /note="S->A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-380. Abolished phosphorylation by CK2, preventing interaction with TOPBP1; when associated with A-341."; /evidence="ECO:0000269|PubMed:12709442, ECO:0000269|PubMed:20545769"; MUTAGEN 387; /note="S->E: Mimics phosphorylation, leading to weak but significant interaction with TOPBP1; when associated with E-341."; /evidence="ECO:0000269|PubMed:20545769
uniprot
proteins
post_translational_modification
PTM: Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage (PubMed:12628935). Hyperphosphorylated by PRKCD and ABL1 upon DNA damage (PubMed:11971963, PubMed:12709442). Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex (PubMed:12628935). Phosphorylated at Ser-341 and Ser-387 by CK2, promoting interaction with TOPBP1 (PubMed:17575048, PubMed:20545769). {ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12628935, ECO:0000269|PubMed:12709442, ECO:0000269|PubMed:17575048, ECO:0000269|PubMed:20545769}.
uniprot
proteins
protein_family
Rad9 family
uniprot
proteins
pubmed
10359610
uniprot
proteins
pubmed
10713044
uniprot
proteins
pubmed
10777662
uniprot
proteins
pubmed
10846170
uniprot
proteins
pubmed
10884395
uniprot
proteins
pubmed
11573955
uniprot
proteins
pubmed
11971963
uniprot
proteins
pubmed
12578958
uniprot
proteins
pubmed
12628935
uniprot
proteins
pubmed
12709442
uniprot
proteins
pubmed
14500360
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15314187
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15556996
uniprot
proteins
pubmed
15871698
uniprot
proteins
pubmed
15897895
uniprot
proteins
pubmed
16216273
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17575048
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20545769
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21659603
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
31135337
uniprot
proteins
pubmed
31776186
uniprot
proteins
pubmed
36841485
uniprot
proteins
pubmed
8943031
uniprot
proteins
sequence_length
391
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12628935}.
uniprot
proteins