{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P12004","secondaryAccessions":["B2R897","D3DW02"],"uniProtkbId":"PCNA_HUMAN","entryAudit":{"firstPublicDate":"1989-10-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1989-10-01","entryVersion":260,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DNA sliding clamp PCNA"}},"alternativeNames":[{"fullName":{"value":"Cyclin"}},{"fullName":{"value":"Proliferating cell nuclear antigen"},"shortNames":[{"value":"PCNA"}]}]},"genes":[{"geneName":{"value":"PCNA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18719106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19443450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24695737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24939902"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35585232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38459011"}],"value":"Confers DNA tethering and processivity to DNA polymerases and other proteins (PubMed:24695737, PubMed:24939902, PubMed:35585232). 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 (PubMed:35585232). 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 (PubMed:24939902). 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 (PubMed:24695737)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P04961"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P17918"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11376153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11595739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11784855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12522211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12786946"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15149598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15225546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15543136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15616578"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16510448"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16949367"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17115032"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17130289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18316726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18499658"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18703516"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18719106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18794347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19336415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19419956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19443450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19995904"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20147293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20457750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20733054"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21549307"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21628590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22148433"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22153967"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22521144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22634751"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22681887"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22704558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22705370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22759634"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23000965"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23677613"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23711367"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24115439"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24561620"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24695737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24911150"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24939902"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26408825"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26760506"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27084448"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27462463"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27906959"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28191891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28621305"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29290612"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35849344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37014751"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37218877"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38459011"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9302295"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9305916"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9566895"}],"value":"Homotrimer (PubMed:24939902). Interacts with p300/EP300; the interaction occurs on chromatin in UV-irradiated damaged cells (PubMed:24939902). Interacts with CREBBP (via transactivation domain and C-terminus); the interaction occurs on chromatin in UV-irradiated damaged cells (PubMed:24939902). Directly interacts with POLD1, POLD3 and POLD4 subunits of the DNA polymerase delta complex, POLD3 being the major interacting partner; the interaction with POLD3 is inhibited by CDKN1A/p21(CIP1) (PubMed:11595739, PubMed:16510448, PubMed:22148433, PubMed:24939902). Forms a complex with the replication factor C complex in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, FEN1, CDC6 and POLDIP2 (PubMed:11784855, PubMed:12522211, PubMed:15149598, PubMed:15225546, PubMed:15616578, PubMed:24911150, PubMed:26760506, PubMed:9302295, PubMed:9305916, PubMed:9566895). Interacts with POLB (PubMed:19336415, PubMed:26760506). Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA (PubMed:11376153, PubMed:19443450). Forms a ternary complex with DNTTIP2 and core histone (PubMed:12786946). Interacts with KCTD10 and PPP1R15A (By similarity). Interacts with SMARCA5/SNF2H (PubMed:15543136). Interacts with BAZ1B/WSTF; the interaction is direct and is required for BAZ1B/WSTF binding to replication foci during S phase (PubMed:15543136). Interacts with HLTF and SHPRH (PubMed:17130289, PubMed:18316726, PubMed:18719106). Interacts with NUDT15; this interaction is disrupted in response to UV irradiation and acetylation (PubMed:19419956). Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex. The interaction with CDKN1A inhibits POLD3 binding (PubMed:11595739, PubMed:16949367, PubMed:18703516, PubMed:18794347). Interacts with DDX11 (PubMed:18499658). Interacts with EGFR; positively regulates PCNA (PubMed:17115032). Interacts with PARPBP (PubMed:22153967). Interacts (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA ubiquitination (PubMed:22681887, PubMed:27084448). Interacts (when polyubiquitinated) with ZRANB3; the interaction stimulates ZRANB3 endonuclease activity and is required for ZRANB3 recruitment to DNA replication sites (PubMed:22704558, PubMed:22705370, PubMed:22759634, PubMed:28621305). Interacts with SMARCAD1 (PubMed:21549307). Interacts with CDKN1C (PubMed:22634751). Interacts with PCLAF (via PIP-box) (PubMed:21628590, PubMed:23000965). Interacts with RTEL1 (via PIP-box); the interaction is direct and essential for the suppression of telomere fragility (PubMed:24115439). Interacts with FAM111A (via PIP-box); the interaction is direct and required for PCNA loading on chromatin binding (PubMed:24561620). Interacts with LIG1 (PubMed:24911150). Interacts with SETMAR (PubMed:20457750). Interacts with ANKRD17 (PubMed:23711367). Interacts with FBXO18/FBH1 (via PIP-box); the interaction recruits the DCX(DTL) complex and promotes ubiquitination and degradation of FBXO18/FBH1 (PubMed:23677613). Interacts with POLN (PubMed:19995904). Interacts with SDE2 (via PIP-box); the interaction is direct and prevents ultraviolet light induced monoubiquitination (PubMed:27906959). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR; interaction at least with PCNA occurs during DNA replication (PubMed:28191891). Interacts with MAPK15; the interaction is chromatin binding dependent and prevents MDM2-mediated PCNA destruction by inhibiting the association of PCNA with MDM2 (PubMed:20733054). Interacts with PARP10 (via PIP-box) (PubMed:24695737). Interacts with DDI2 (PubMed:29290612). Interacts with HMCES (via PIP-box) (PubMed:30554877). Interacts with TRAIP (via PIP-box) (PubMed:26711499, PubMed:27462463). Interacts with UHRF2 (PubMed:28951215). Interacts with ALKBH2; this interaction is enhanced during the S-phase of the cell cycle. Interacts with ATAD5; the interaction promotes USP1-mediated PCNA deubiquitination (PubMed:20147293). Interacts with DNA damage up-regulated protein DDUP (PubMed:35849344). Interacts (when phosphorylated) with GRB2 (PubMed:38459011). Interacts with ANG (PubMed:37218877). Interacts with nuclear UNG (isoform 2); this interaction mediates UNG recruitment to S-phase replication foci. Interacts with ERCC6L2 (via an atypical PIP-box); this interaction facilitates cenrtomeric localization of ERCC6L2 (PubMed:37014751). Interacts with REV1 (via BRCT domain); this interaction is enhanced with a monoubiquitinated form of PCNA and mediates REV1 recruitment to stalled DNA replication (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26223641"}],"value":"(Microbial infection) Interacts with herpes virus 8 protein LANA1"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P04075","geneName":"ALDOA","intActId":"EBI-709613"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P03950","geneName":"ANG","intActId":"EBI-525291"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P07355","geneName":"ANXA2","intActId":"EBI-352622"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P61769","geneName":"B2M","intActId":"EBI-714718"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P38936","geneName":"CDKN1A","intActId":"EBI-375077"},"numberOfExperiments":39,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P42771","geneName":"CDKN2A","intActId":"EBI-375053"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q9H211","geneName":"CDT1","intActId":"EBI-456953"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q13111","geneName":"CHAF1A","intActId":"EBI-1020839"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q96DZ9-2","geneName":"CMTM5","intActId":"EBI-11522780"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P68104","geneName":"EEF1A1","intActId":"EBI-352162"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P06733","geneName":"ENO1","intActId":"EBI-353877"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P39748","geneName":"FEN1","intActId":"EBI-707816"},"numberOfExperiments":22,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P24522","geneName":"GADD45A","intActId":"EBI-448167"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P04406","geneName":"GAPDH","intActId":"EBI-354056"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q14527","geneName":"HLTF","intActId":"EBI-1045161"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q9H160","geneName":"ING2","intActId":"EBI-389787"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q9H063","geneName":"MAF1","intActId":"EBI-720354"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P20585","geneName":"MSH3","intActId":"EBI-1164205"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"O95944","geneName":"NCR2","intActId":"EBI-14058375"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P61970","geneName":"NUTF2","intActId":"EBI-591778"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q15004","geneName":"PCLAF","intActId":"EBI-10971436"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P12004","geneName":"PCNA","intActId":"EBI-358311"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P18669","geneName":"PGAM1","intActId":"EBI-717905"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P00558","geneName":"PGK1","intActId":"EBI-709599"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P28340","geneName":"POLD1","intActId":"EBI-716569"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P49005","geneName":"POLD2","intActId":"EBI-372354"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q15054","geneName":"POLD3","intActId":"EBI-864956"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q9HCU8","geneName":"POLD4","intActId":"EBI-864968"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P30041","geneName":"PRDX6","intActId":"EBI-2255129"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q9UBF6","geneName":"RNF7","intActId":"EBI-398632"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q86TU7","geneName":"SETD3","intActId":"EBI-2908049"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q8IWU4","geneName":"SLC30A8","intActId":"EBI-10262251"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q9NZD8","geneName":"SPG21","intActId":"EBI-742688"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"A2RU14","geneName":"TMEM218","intActId":"EBI-10173151"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"P60174","geneName":"TPI1","intActId":"EBI-717475"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q5FWF4","geneName":"ZRANB3","intActId":"EBI-13954615"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q8TE30","intActId":"EBI-8874509"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q9Z111","geneName":"Gadd45g","intActId":"EBI-1173616"},"numberOfExperiments":9,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"Q1K9H5","geneName":"PB1","intActId":"EBI-6050669"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P12004","intActId":"EBI-358311"},"interactantTwo":{"uniProtKBAccession":"B4URF7","geneName":"PB2","intActId":"EBI-6050648"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15543136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24939902"}],"value":"Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (PubMed:24939902). Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase (PubMed:15543136). Co-localizes with SMARCA5/SNF2H and BAZ1B/WSTF at replication foci during S phase (PubMed:15543136). Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15543136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24115439"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24939902"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38459011"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17115032"}],"value":"Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24939902"}],"value":"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 (PubMed:19419956, PubMed:24939902). 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 (PubMed:24939902). Acetylation disrupts interaction with NUDT15 and promotes degradation (PubMed:19419956)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15149598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17108083"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17130289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18316726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18719106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18948756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20129063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20227374"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22153967"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24939902"}],"value":"Ubiquitinated (PubMed:20227374, PubMed:24939902). 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"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25732820"}],"value":"Methylated on glutamate residues by DCPH1/C6orf211"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Ataxia-telangiectasia-like disorder 2","diseaseAccession":"DI-04180","acronym":"ATLD2","description":"A neurodegenerative disorder due to defects in DNA excision repair. 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