CPLM-004383

Genbank Nucleotide ID

Proliferating cell nuclear antigen

Protein Synonyms/Alias

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Position	Peptide	Type	References
13	FEEASLFKRIIDGFK	acetylation	[1]
77	MDLTSLSKILRCGNN	ubiquitination	[2]
127	DIDADFLKIEELQYD	sumoylation	[3, 4, 5, 6, 7]
164	SINIMITKETIKFVA	sumoylation	[3, 4, 7, 8]
164	SINIMITKETIKFVA	ubiquitination	[2, 9, 10]
217	KYLLDIIKGSSLSDR	acetylation	[1]

[1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
[2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
[3] RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO.
Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S.
Nature. 2002 Sep 12;419(6903):135-41. [PMID: 12226657]
[4] Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae.
Haracska L, Torres-Ramos CA, Johnson RE, Prakash S, Prakash L.
Mol Cell Biol. 2004 May;24(10):4267-74. [PMID: 15121847]
[5] SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis.
Colby T, Matthäi A, Boeckelmann A, Stuible HP.
Plant Physiol. 2006 Sep;142(1):318-32. [PMID: 16920872]
[6] Regulation of DNA repair throughout the cell cycle.
Branzei D, Foiani M.
Nat Rev Mol Cell Biol. 2008 Apr;9(4):297-308. [PMID: 18285803]
[7] SUMO modification of PCNA is controlled by DNA.
Parker JL, Bucceri A, Davies AA, Heidrich K, Windecker H, Ulrich HD.
EMBO J. 2008 Sep 17;27(18):2422-31. [PMID: 18701921]
[8] A proteomic strategy for gaining insights into protein sumoylation in yeast.
Denison C, Rudner AD, Gerber SA, Bakalarski CE, Moazed D, Gygi SP.
Mol Cell Proteomics. 2005 Mar;4(3):246-54. [PMID: 15542864]
[9] Identification, analysis, and prediction of protein ubiquitination sites.
Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
[10] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]

Functional Description

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. Involved in DNA repair.

DNA_BIND 61 80 Potential.
CROSSLNK 127 127 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; DNA-binding; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; IDA:SGD.
GO:0043626; C:PCNA complex; TAS:SGD.
GO:0005657; C:replication fork; TAS:SGD.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0030337; F:DNA polymerase processivity factor activity; IDA:SGD.
GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO:0006273; P:lagging strand elongation; IDA:SGD.
GO:0006272; P:leading strand elongation; IDA:SGD.
GO:0000710; P:meiotic mismatch repair; IMP:SGD.
GO:0007064; P:mitotic sister chromatid cohesion; IPI:SGD.
GO:0006289; P:nucleotide-excision repair; IMP:SGD.
GO:0006301; P:postreplication repair; IMP:SGD.
GO:0006275; P:regulation of DNA replication; IEA:InterPro.

IPR000730; Pr_cel_nuc_antig.
IPR022649; Pr_cel_nuc_antig_C.
IPR022659; Pr_cel_nuc_antig_CS.
IPR022648; Pr_cel_nuc_antig_N.

PF02747; PCNA_C
PF00705; PCNA_N

PS01251; PCNA_1
PS00293; PCNA_2

PR00339; PCNACYCLIN.