EXO1
entrez
9156
canonical
uniprot
Q9UQ84
canonical
ensembl
ENSG00000174371
resolver
ensp
ENSP00000311873
resolver
ensp
ENSP00000355506
resolver
ensp
ENSP00000430251
resolver
ensp
ENSP00000596807
resolver
ensp
ENSP00000596808
resolver
ensp
ENSP00000596809
resolver
ensp
ENSP00000596810
resolver
ensp
ENSP00000596811
resolver
genesymbol
EXO1
resolver
genesymbol_syn
EXOI
resolver
genesymbol_syn
HEX1
resolver
hgnc
HGNC:3511
resolver
uniprot
A8K5H6
resolver
uniprot
O60545
resolver
uniprot
O75214
resolver
uniprot
O75466
resolver
uniprot
Q5T396
resolver
uniprot
Q96IJ1
resolver
uniprot
Q9UG38
resolver
uniprot
Q9UNW0
resolver
uniprot_entry
A8K5H6_HUMAN
resolver
uniprot_entry
EXO1_HUMAN
resolver
uniprot_sec
O60545
resolver
uniprot_sec
O75214
resolver
uniprot_sec
O75466
resolver
uniprot_sec
Q5T396
resolver
uniprot_sec
Q96IJ1
resolver
uniprot_sec
Q9UG38
resolver
uniprot_sec
Q9UNW0
resolver
amino_acid_sequence
MGIQGLLQFIKEASEPIHVRKYKGQVVAVDTYCWLHKGAIACAEKLAKGEPTDRYVGFCMKFVNMLLSHGIKPILVFDGCTLPSKKEVERSRRERRQANLLKGKQLLREGKVSEARECFTRSINITHAMAHKVIKAARSQGVDCLVAPYEADAQLAYLNKAGIVQAIITEDSDLLAFGCKKVILKMDQFGNGLEIDQARLGMCRQLGDVFTEEKFRYMCILSGCDYLSSLRGIGLAKACKVLRLANNPDIVKVIKKIGHYLKMNITVPEDYINGFIRANNTFLYQLVFDPIKRKLIPLNAYEDDVDPETLSYAGQYVDDSIALQIALGNKDINTFEQIDDYNPDTAMPAHSRSHSWDDKTCQKSANVSSIWHRNYSPRPESGTVSDAPQLKENPSTVGVERVISTKGLNLPRKSSIVKRPRSAELSEDDLLSQYSLSFTKKTKKNSSEGNKSLSFSEVFVPDLVNGPTNKKSVSTPPRTRNKFATFLQRKNEESGAVVVPGTRSRFFCSSDSTDCVSNKVSIQPLDETAVTDKENNLHESEYGDQEGKRLVDTDVARNSSDDIPNNHIPGDHIPDKATVFTDEESYSFESSKFTRTISPPTLGTLRSCFSWSGGLGDFSRTPSPSPSTALQQFRRKSDSPTSLPENNMSDVSQLKSEESSDDESHPLREEACSSQSQESGEFSLQSSNASKLSQCSSKDSDSEESDCNIKLLDSQSDQTSKLRLSHFSKKDTPLRNKVPGLYKSSSADSLSTTKIKPLGPARASGLSKKPASIQKRKHHNAENKPGLQIKLNELWKNFGFKKDSEKLPPCKKPLSPVRDNIQLTPEAEEDIFNKPECGRVQRAIFQ
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis. {ECO:0000269|PubMed:10364235, ECO:0000269|PubMed:10608837, ECO:0000269|PubMed:11809771, ECO:0000269|PubMed:11842105, ECO:0000269|PubMed:12414623, ECO:0000269|PubMed:12704184, ECO:0000269|PubMed:14636568, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:15225546, ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:16143102, ECO:0000269|PubMed:9685493}.
uniprot
proteins
mass_dalton
94103
uniprot
proteins
mutagenesis
MUTAGEN 78; /note="D->A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also reduces DNA-binding to 5'-overhanging flap structures."; /evidence="ECO:0000269|PubMed:11842105"; MUTAGEN 173; /note="D->A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. No effect on DNA-binding to 5'-overhanging flap structures."; /evidence="ECO:0000269|PubMed:11842105, ECO:0000269|PubMed:15225546"; MUTAGEN 225; /note="D->A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also enhances DNA-binding to 5'-overhanging flap structures."; /evidence="ECO:0000269|PubMed:11842105"; MUTAGEN 418; /note="K->A,T: Complete loss of nuclear localization."; /evidence="ECO:0000269|PubMed:17426132"; MUTAGEN 419; /note="R->A: Complete loss of nuclear localization."; /evidence="ECO:0000269|PubMed:17426132"; MUTAGEN 454; /note="S->A: No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-621 and A-714."; /evidence="ECO:0000269|PubMed:18048416"; MUTAGEN 621; /note="T->A: No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-714."; /evidence="ECO:0000269|PubMed:18048416"; MUTAGEN 714; /note="S->A: No rescue of HU-induced degradation and loss of HU-induced increase of phosphorylation. No rescue of HU-induced degradation; when associated with A-621. No rescue of HU-induced degradation; when associated with A-454. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-621."; /evidence="ECO:0000269|PubMed:18048416
uniprot
proteins
post_translational_modification
PTM: Phosphorylated upon DNA damage and in response to agents stalling DNA replication, probably by ATM or ATR. Phosphorylation at Ser-454, Thr-621 and Ser-714 is induced upon DNA-damage caused by treatment with hydroxyurea (HU) but not upon IR treatment. The HU-induced EXO1 triple phosphorylation facilitates destabilization/degradation of the protein. {ECO:0000269|PubMed:18048416}.
uniprot
proteins
protein_family
EXO1 subfamily
uniprot
proteins
protein_family
XPG/RAD2 endonuclease family
uniprot
proteins
pubmed
10364235
uniprot
proteins
pubmed
10608837
uniprot
proteins
pubmed
10856833
uniprot
proteins
pubmed
11375940
uniprot
proteins
pubmed
11427529
uniprot
proteins
pubmed
11429708
uniprot
proteins
pubmed
11809771
uniprot
proteins
pubmed
11842105
uniprot
proteins
pubmed
12414623
uniprot
proteins
pubmed
12517792
uniprot
proteins
pubmed
12704184
uniprot
proteins
pubmed
14623461
uniprot
proteins
pubmed
14636568
uniprot
proteins
pubmed
14676842
uniprot
proteins
pubmed
14756672
uniprot
proteins
pubmed
15225546
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15550454
uniprot
proteins
pubmed
15886194
uniprot
proteins
pubmed
16143102
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17426132
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18048416
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25860647
uniprot
proteins
pubmed
34552057
uniprot
proteins
pubmed
36400755
uniprot
proteins
pubmed
9685493
uniprot
proteins
pubmed
9788596
uniprot
proteins
pubmed
9823303
uniprot
proteins
sequence_length
846
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. Note=Colocalizes with PCNA to discrete nuclear foci in S-phase.
uniprot
proteins