PAXX
entrez
286257
canonical
uniprot
Q9BUH6
canonical
ensembl
ENSG00000310560
resolver
ensp
ENSP00000360682
resolver
ensp
ENSP00000770315
resolver
genesymbol
PAXX
resolver
genesymbol_syn
C9orf142
resolver
genesymbol_syn
XLS
resolver
hgnc
HGNC:27849
resolver
uniprot
Q8IY19
resolver
uniprot_entry
PAXX_HUMAN
resolver
uniprot_sec
Q8IY19
resolver
amino_acid_sequence
MDPLSPPLCTLPPGPEPPRFVCYCEGEESGEGDRGGFNLYVTDAAELWSTCFTPDSLAALKARFGLSAAEDITPRFRAACEQQAVALTLQEDRASLTLSGGPSALAFDLSKVPGPEAAPRLRALTLGLAKRVWSLERRLAAAEETAVSPRKSPRPAGPQLFLPDPDPQRGGPGPGVRRRCPGESLINPGFKSKKPAGGVDFDET
uniprot
proteins
function
FUNCTION: Non-essential DNA repair protein involved in DNA non-homologous end joining (NHEJ); participates in double-strand break (DSB) repair and V(D)J recombination (PubMed:25574025, PubMed:25670504, PubMed:25941166, PubMed:27705800). May act as a scaffold required for accumulation of the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites and promote the assembly and/or stability of the NHEJ machinery (PubMed:25574025, PubMed:25670504, PubMed:25941166). Involved in NHEJ by promoting the ligation of blunt-ended DNA ends (PubMed:27703001). Together with NHEJ1/XLF, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends (PubMed:25670504, PubMed:30250067). Constitutes a non-essential component of classical NHEJ: has a complementary but distinct function with NHEJ1/XLF in DNA repair (PubMed:27705800). Able to restrict infection by herpesvirus 1 (HSV-1) via an unknown mechanism (PubMed:29144403). {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:25941166, ECO:0000269|PubMed:27703001, ECO:0000269|PubMed:27705800, ECO:0000269|PubMed:29144403, ECO:0000269|PubMed:30250067}.
uniprot
proteins
mass_dalton
21640
uniprot
proteins
mutagenesis
MUTAGEN 96..109; /note="LTLSGGPSALAFDL->DTDSGGPSADAFDD: Loss of function in DNA non-homologous end joining (NHEJ)."; /evidence="ECO:0000269|PubMed:25670504"; MUTAGEN 134; /note="S->A: Does not affect interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with 145-D--152."; /evidence="ECO:0000269|PubMed:27705800"; MUTAGEN 134; /note="S->D: Phospho-mimetic mutant; abolished interaction with DNA-bound the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with 145-D--152."; /evidence="ECO:0000269|PubMed:27705800"; MUTAGEN 145..152; /note="TAVSPRKS->AAVAPRKA: Does not affect interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with A-134."; /evidence="ECO:0000269|PubMed:27705800"; MUTAGEN 145..152; /note="TAVSPRKS->DAVDPRKD: Phospho-mimetic mutant; abolished interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with D-134."; /evidence="ECO:0000269|PubMed:27705800"; MUTAGEN 177..179; /note="RRR->AAA: Abolishes the association with the non-homologous end joining complex. Abolished interaction with XRCC6/Ku70."; /evidence="ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:27705800"; MUTAGEN 184; /note="S->E: Abolished interaction with XRCC5/Ku80 and XRCC6/Ku70."; /evidence="ECO:0000269|PubMed:27601299"; MUTAGEN 186..187; /note="IN->AA: Abolishes the association with the non-homologous end joining complex."; /evidence="ECO:0000269|PubMed:25670504"; MUTAGEN 199..201; /note="VDF->ADA: Abolished interaction with XRCC5/Ku80 and XRCC6/Ku70."; /evidence="ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:27601299"; MUTAGEN 201; /note="F->A: Abolishes the association with the non-homologous end joining complex and localization to double-strand break sites. Abolished interaction with XRCC6/Ku70."; /evidence="ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:27705800
uniprot
proteins
post_translational_modification
PTM: Phosphorylation may inhibit interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer (Ku complex). {ECO:0000269|PubMed:27705800}.
uniprot
proteins
protein_family
PAXX subfamily
uniprot
proteins
protein_family
XRCC4-XLF family
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25574025
uniprot
proteins
pubmed
25670504
uniprot
proteins
pubmed
25941166
uniprot
proteins
pubmed
27063109
uniprot
proteins
pubmed
27601299
uniprot
proteins
pubmed
27703001
uniprot
proteins
pubmed
27705800
uniprot
proteins
pubmed
29144403
uniprot
proteins
pubmed
30250067
uniprot
proteins
sequence_length
204
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:29144403}. Chromosome {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504}. Note=Predominantly localizes to the nucleus. Accumulates at sites of DNA damage generated by laser microirradiation. {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29144403}. Note=(Microbial infection) Upon infection by herpesvirus 1 (HSV-1), it is partially translocated into the cytoplasm in an HSV-1-dependent manner. {ECO:0000269|PubMed:29144403}.
uniprot
proteins