Pcna
entrez
25737
canonical
uniprot
P04961
canonical
ensembl
ENSRNOG00000021264
resolver
ensembl
ENSRNOG00055005861
resolver
ensembl
ENSRNOG00060002045
resolver
ensembl
ENSRNOG00065013827
resolver
ensp
ENSRNOP00000028887
resolver
ensp
ENSRNOP00055007288
resolver
ensp
ENSRNOP00060002184
resolver
ensp
ENSRNOP00065017648
resolver
enst
ENSRNOT00000028887
resolver
enst
ENSRNOT00055009473
resolver
enst
ENSRNOT00060003205
resolver
enst
ENSRNOT00065022752
resolver
genesymbol
Pcna
resolver
uniprot_entry
PCNA_RAT
resolver
amino_acid_sequence
MFEARLIQGSILKKVLEALKDLINEACWDISSGGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVSIEMNEPVQLTFALRYLNFFTKATPLSPTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS
uniprot
proteins
function
FUNCTION: Confers DNA tethering and processivity to DNA polymerases and other proteins. Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of DNA replication by increasing the polymerases' processivity during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion. {ECO:0000250|UniProtKB:P12004}.
uniprot
proteins
mass_dalton
28749
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation. Lysine acetylation disrupts association with chromatin, hence promoting PCNA ubiquitination and proteasomal degradation in response to UV damage in a CREBBP- and EP300-dependent manner. Acetylation disrupts interaction with NUDT15 and promotes degradation (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Ubiquitinated. Following DNA damage, can be either monoubiquitinated to stimulate direct bypass of DNA lesions by specialized DNA polymerases or polyubiquitinated to promote recombination-dependent DNA synthesis across DNA lesions by template switching mechanisms. Following induction of replication stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, leading to recruit translesion (TLS) polymerases, which are able to synthesize across DNA lesions in a potentially error-prone manner. An error-free pathway also exists and requires non-canonical polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This error-free pathway, also known as template switching, employs recombination mechanisms to synthesize across the lesion, using as a template the undamaged, newly synthesized strand of the sister chromatid. Monoubiquitination at Lys-164 also takes place in undamaged proliferating cells, and is mediated by the DCX(DTL) complex, leading to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during S phase (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Methylated on glutamate residues by DCPH1. {ECO:0000250|UniProtKB:P12004}.
uniprot
proteins
protein_family
PCNA family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15982757
uniprot
proteins
pubmed
2884104
uniprot
proteins
sequence_length
261
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12004}. Note=Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:P12004}.
uniprot
proteins