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Protein Page:
PCNA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PCNA This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility 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. Homotrimer. Forms a complex with activator 1 heteropentamer in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, FEN1, CDC6 and POLDIP2. Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA. Forms a ternary complex with DNTTIP2 and core histone. Interacts with KCTD10 and PPP1R15A. Interacts with POLD1, POLD3 and POLD4. Interacts with BAZ1B; the interaction is direct. Interacts with HLTF and SHPRH. Interacts with NUDT15. Interaction is disrupted in response to UV irradiation and acetylation. Interacts with p21Cip1/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex. Interacts with DDX11. Interacts with EGFR; positively regulates PCNA. Interacts with C12orf48/PARI. Interacts with SMARCAD1. Belongs to the PCNA family. Note: This description may include information from UniProtKB.
Protein type: Cell cycle regulation; DNA replication
Chromosomal Location of Human Ortholog: 20pter-p12
Cellular Component: centrosome; cytoplasm; DNA replication factor C complex; nuclear chromosome, telomeric region; nuclear replication fork; nucleoplasm; nucleus; PCNA complex
Molecular Function: chromatin binding; damaged DNA binding; dinucleotide insertion or deletion binding; DNA polymerase processivity factor activity; enzyme binding; histone acetyltransferase binding; identical protein binding; MutLalpha complex binding; protein binding; purine-specific mismatch base pair DNA N-glycosylase activity; receptor tyrosine kinase binding
Biological Process: bypass DNA synthesis; cell proliferation; DNA damage response, detection of DNA damage; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; DNA strand elongation during DNA replication; epithelial cell differentiation; error-prone postreplication DNA repair; G1/S transition of mitotic cell cycle; G1/S-specific transcription in mitotic cell cycle; leading strand elongation; mismatch repair; nucleotide-excision repair, DNA gap filling; nucleotide-excision repair, DNA incision; nucleotide-excision repair, DNA incision, 5'-to lesion; positive regulation of deoxyribonuclease activity; positive regulation of DNA repair; positive regulation of DNA replication; protein sumoylation; replication fork processing; telomere maintenance; telomere maintenance via recombination; transcription-coupled nucleotide-excision repair
Disease: Ataxia-telangiectasia-like Disorder 2
Reference #:  P12004 (UniProtKB)
Alt. Names/Synonyms: Cyclin; DNA polymerase delta auxiliary protein; MGC8367; PCNA; Proliferating cell nuclear antigen
Gene Symbols: PCNA
Molecular weight: 28,769 Da
Basal Isoelectric point: 4.57  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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PCNA

Protein Structure Not Found.
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Sites Implicated In
cell growth, altered: Y211‑p
DNA repair, inhibited: Y211‑p
phosphorylation: Y211‑p
protein degradation: Y211‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K13‑ac LVQGSILkkVLEALK
0 4 K13‑ub LVQGSILkkVLEALK
0 1 K13‑sc LVQGSILkkVLEALK
0 3 K14‑ub VQGSILkkVLEALKD
0 2 K77‑ac VNLTSMSkILkCAGN
0 14 K77‑ub VNLTSMSkILkCAGN
0 6 K80‑ac TSMSkILkCAGNEDI
0 34 K80‑ub TSMSkILkCAGNEDI
0 12 K110‑ub FEAPNQEkVSDYEMk
1 0 Y114 NQEkVSDYEMkLMDL
0 7 K117‑ub kVSDYEMkLMDLDVE
0 1 S134‑p GIPEQEYsCVVkMPS
0 1 K138‑ub QEYsCVVkMPSGEFA
0 1 S152‑p ARICRDLsHIGDAVV
0 1 S161‑p IGDAVVIsCAkDGVk
0 2 K164‑ac AVVIsCAkDGVkFSA
12 142 K164‑ub AVVIsCAkDGVkFSA
1 1 K164‑sm AVVIsCAkDGVkFSA
0 1 K164‑sc AVVIsCAkDGVkFSA
0 20 K168‑ub sCAkDGVkFSASGEL
0 1 K181‑ub ELGNGNIkLSQTSNV
0 1 K190‑ac SQTSNVDkEEEAVTI
3 2 Y211‑p QLTFALRyLNFFtkA
0 1 T216‑p LRyLNFFtkATPLSS
0 1 K217‑ac RyLNFFtkATPLSST
0 2 K217 RyLNFFtKATPLSST
0 2 K248‑ac IADMGHLkYYLAPkI
0 96 K248‑ub IADMGHLkYYLAPkI
0 8 K254‑ub LkYYLAPkIEDEEGs
0 1 K254‑sm LkYYLAPkIEDEEGs
0 5 S261‑p kIEDEEGs_______
13439 : Ubiquityl-PCNA (Lys164) (D5C7P) Rabbit mAb
  mouse

 
K13 LIQGSILKKVLEALK
K13 LIQGSILKKVLEALK
K13 LIQGSILKKVLEALK
K14 IQGSILKKVLEALKD
K77 VNLTSMSKILkCAGN
K77 VNLTSMSKILkCAGN
K80 TSMSKILKCAGNEDI
K80‑ub TSMSKILkCAGNEDI
K110 FEAPNQEKVSDyEMk
Y114‑p NQEKVSDyEMkLMDL
K117‑ub KVSDyEMkLMDLDVE
S134 GIPEQEYSCVIKMPS
K138 QEYSCVIKMPSGEFA
S152 ARICRDLSHIGDAVV
S161 IGDAVVISCAkNGVk
K164 AVVISCAKNGVkFSA
K164‑ub AVVISCAkNGVkFSA
K164 AVVISCAKNGVkFSA
K164 AVVISCAKNGVkFSA
K168‑ub SCAkNGVkFSASGEL
K181 ELGNGNIKLSQTSNV
K190 SQTSNVDKEEEAVTI
Y211 HLTFALRYLNFFTkA
T216 LRYLNFFTkATPLSP
K217 RYLNFFTKATPLSPT
K217‑ub RYLNFFTkATPLSPT
K248 IADMGHLKYYLAPKI
K248‑ub IADMGHLkYYLAPKI
K254 LkYYLAPKIEDEEAS
K254 LkYYLAPKIEDEEAS
S261 KIEDEEAS_______
  rat

 
K13 LIQGSILKKVLEALK
K13 LIQGSILKKVLEALK
K13 LIQGSILKKVLEALK
K14 IQGSILKKVLEALKD
K77 VNLTSMSKILKCAGN
K77 VNLTSMSKILKCAGN
K80 TSMSKILKCAGNEDI
K80 TSMSKILKCAGNEDI
K110 FEAPNQEKVSDYEMK
Y114 NQEKVSDYEMKLMDL
K117 KVSDYEMKLMDLDVE
S134 GIPEQEYSCVVKMPS
K138 QEYSCVVKMPSGEFA
S152 ARICRDLSHIGDAVV
S161 IGDAVVISCAKDGVK
K164 AVVISCAKDGVKFSA
K164 AVVISCAKDGVKFSA
K164 AVVISCAKDGVKFSA
K164 AVVISCAKDGVKFSA
K168 SCAKDGVKFSASGEL
K181 ELGNGNIKLSQTSNV
K190 SQTSNVDKEEEAVSI
Y211 QLTFALRYLNFFTKA
T216 LRYLNFFTKATPLSP
K217 RYLNFFTKATPLSPT
K217 RYLNFFTKATPLSPT
K248 IADMGHLKYYLAPKI
K248 IADMGHLKYYLAPKI
K254 LKYYLAPKIEDEEGS
K254 LKYYLAPKIEDEEGS
S261 KIEDEEGS_______
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