PCLAF
entrez
9768
canonical
uniprot
Q15004
canonical
ensembl
ENSG00000166803
resolver
ensembl
ENSG00000259316
resolver
ensp
ENSP00000300035
resolver
ensp
ENSP00000369608
resolver
genesymbol
PCLAF
resolver
genesymbol_syn
KIAA0101
resolver
genesymbol_syn
NS5ATP9
resolver
genesymbol_syn
PAF
resolver
hgnc
HGNC:28961
resolver
uniprot
A6NNU5
resolver
uniprot
A8K3Y3
resolver
uniprot
G9G694
resolver
uniprot
G9G696
resolver
uniprot_entry
PAF15_HUMAN
resolver
uniprot_sec
A6NNU5
resolver
uniprot_sec
A8K3Y3
resolver
uniprot_sec
G9G694
resolver
uniprot_sec
G9G696
resolver
amino_acid_sequence
MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKAKRKACPLQPDHTNDEKE
uniprot
proteins
function
FUNCTION: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number. {ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}.
uniprot
proteins
mass_dalton
11986
uniprot
proteins
mutagenesis
MUTAGEN 15; /note="K->R: Loss of monoubiquitination; when associated with R-24."; /evidence="ECO:0000269|PubMed:23000965"; MUTAGEN 24; /note="K->R: Loss of monoubiquitination; when associated with R-15."; /evidence="ECO:0000269|PubMed:23000965"; MUTAGEN 65; /note="I->A: Loss of binding to PCNA."; /evidence="ECO:0000269|PubMed:11313979"; MUTAGEN 68..69; /note="FF->AA: Loss of binding to PCNA."; /evidence="ECO:0000269|PubMed:21628590"; MUTAGEN 68; /note="F->A: Loss of binding to PCNA."; /evidence="ECO:0000269|PubMed:11313979"; MUTAGEN 78; /note="K->A: Stabilizes the protein in G1 by preventing association with the APC/C complex and degradation by the proteasome."; /evidence="ECO:0000269|PubMed:21628590"; MUTAGEN 93..97; /note="KAKRK->AAAAA: Inhibits chain initiation by APC/C."; /evidence="ECO:0000269|PubMed:21700221"; MUTAGEN 93..97; /note="KAKRK->RARRR: No effect on chain initiation by APC/C."; /evidence="ECO:0000269|PubMed:21700221
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated at Lys-15 and Lys-24 during normal S phase, promoting its association with PCNA. Also diubiquitinated at these 2 sites. Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24 are probably extended, leading to disrupt the interaction with PCNA. Polyubiquitinated by the APC/C complex at the mitotic exit, leading to its degradation by the proteasome. {ECO:0000269|PubMed:21628590, ECO:0000269|PubMed:21700221, ECO:0000269|PubMed:23000965}.
uniprot
proteins
pubmed
11313979
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15334068
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15789362
uniprot
proteins
pubmed
16288740
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19219066
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21628590
uniprot
proteins
pubmed
21673012
uniprot
proteins
pubmed
21700221
uniprot
proteins
pubmed
22096502
uniprot
proteins
pubmed
23000965
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
7788527
uniprot
proteins
sequence_length
111
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11313979, ECO:0000269|PubMed:16288740, ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21673012}. Note=Following DNA damage, localizes to DNA damage sites (PubMed:21628590). Colocalizes with centrosomes in perinuclear region (PubMed:21673012).
uniprot
proteins