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PCNA (human)

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 Cellular Component: microtubule cytoskeleton; nucleoplasm; PCNA complex; nuclear replication fork; DNA replication factor C complex; cytoplasm; nucleolus; nucleus Molecular Function: identical protein binding; protein binding; DNA polymerase processivity factor activity; purine-specific mismatch base pair DNA N-glycosylase activity; MutLalpha complex binding; dinucleotide insertion or deletion binding; receptor tyrosine kinase binding Biological Process: mismatch repair; phosphoinositide-mediated signaling; heart development; positive regulation of deoxyribonuclease activity; DNA strand elongation during DNA replication; DNA repair; response to lipid; G1/S-specific transcription in mitotic cell cycle; telomere maintenance via semi-conservative replication; cell proliferation; bypass DNA synthesis; response to cadmium ion; base-excision repair; nucleotide-excision repair; transcription-coupled nucleotide-excision repair; telomere maintenance via recombination; mitotic cell cycle; nucleotide-excision repair, DNA gap filling; DNA replication; S phase of mitotic cell cycle; telomere maintenance; G1/S transition of mitotic cell cycle; regulation of DNA replication 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®

Select Structure to View Below PCNA 1AXC - A/C/E=1-261 (human) 1U76 - A/C/E=1-261 (human) 1U7B - A=1-261 (human) 1UL1 - A/B/C=1-261 (human) 1VYJ - A/C/E/G/I/K=1-261 (human) 1VYM - A/B/C=1-261 (human) 1W60 - A/B=1-261 (human) 2ZVK - A/C/B=1-261 (human) 2ZVL - F/A/D/C/E/B=1-261 (human) 2ZVM - A/C/B=1-261 (human) 3P87 - F/A/D/C/E/B=1-261 (human) 3TBL - A/C/B=1-261 (human) 3VKX - A=1-261 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1AXC 1U76 1U7B 1UL1 1VYJ 1VYM 1W60 2ZVK 2ZVL 2ZVM 3P87 3TBL 3VKX  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
cell growth, altered: 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

SS  SS: 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.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	4		K13-u	LVQGSILkkVLEALK
0	2		K14-u	VQGSILkkVLEALKD
0	1		K77-a	VNLTSMSkILkCAGN
0	14		K77-u	VNLTSMSkILkCAGN
0	3		K80-a	TSMSkILkCAGNEDI
0	33		K80-u	TSMSkILkCAGNEDI
0	11		K110-u	FEAPNQEkVSDYEMk
1	0		Y114	NQEkVSDYEMkLMDL
0	6		K117-u	kVSDYEMkLMDLDVE
9	141		K164-u	AVVISCAkDGVkFSA
1	0		K164-s	AVVISCAkDGVkFSA
0	19		K168-u	SCAkDGVkFSASGEL
0	1		K181-u	ELGNGNIkLSQTSNV
0	1		K190-a	SQTSNVDkEEEAVTI
2	1		Y211-p	QLTFALRyLNFFTkA
0	1		K217-a	RyLNFFTkATPLSST
0	2		K217	RyLNFFTKATPLSST
0	1		K248-a	IADMGHLkYYLAPkI
0	95		K248-u	IADMGHLkYYLAPkI
0	7		K254-u	LkYYLAPkIEDEEGs
0	1		S261-p	kIEDEEGs_______

	mouse
K13	LIQGSILKKVLEALK
K14	IQGSILKKVLEALKD
K77	VNLTSMSKILkCAGN
K77	VNLTSMSKILkCAGN
K80	TSMSKILKCAGNEDI
K80-u	TSMSKILkCAGNEDI
K110	FEAPNQEKVSDyEMk
Y114-p	NQEKVSDyEMkLMDL
K117-u	KVSDyEMkLMDLDVE
K164-u	AVVISCAkNGVkFSA
K164	AVVISCAKNGVkFSA
K168-u	SCAkNGVkFSASGEL
K181	ELGNGNIKLSQTSNV
K190	SQTSNVDKEEEAVTI
Y211	HLTFALRYLNFFTkA
K217	RYLNFFTKATPLSPT
K217-u	RYLNFFTkATPLSPT
K248	IADMGHLKYYLAPKI
K248-u	IADMGHLkYYLAPKI
K254	LkYYLAPKIEDEEAS
S261	KIEDEEAS_______

	rat
K13	LIQGSILKKVLEALK
K14	IQGSILKKVLEALKD
K77	VNLTSMSKILKCAGN
K77	VNLTSMSKILKCAGN
K80	TSMSKILKCAGNEDI
K80	TSMSKILKCAGNEDI
K110	FEAPNQEKVSDYEMK
Y114	NQEKVSDYEMKLMDL
K117	KVSDYEMKLMDLDVE
K164	AVVISCAKDGVKFSA
K164	AVVISCAKDGVKFSA
K168	SCAKDGVKFSASGEL
K181	ELGNGNIKLSQTSNV
K190	SQTSNVDKEEEAVSI
Y211	QLTFALRYLNFFTKA
K217	RYLNFFTKATPLSPT
K217	RYLNFFTKATPLSPT
K248	IADMGHLKYYLAPKI
K248	IADMGHLKYYLAPKI
K254	LKYYLAPKIEDEEGS
S261	KIEDEEGS_______

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