Proliferating cell nuclear antigen - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P15873 (PCNA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proliferating cell nuclear antigen
Short name=PCNA

Gene names

Name:	POL30
Ordered Locus Names:	YBR088C
ORF Names:	YBR0811

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.7
Subunit structure	Homotrimer. Interacts with RAD30 and MCM10. Ref.6 Ref.10
Subcellular location	Nucleus.
Post-translational modification	Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and function in DNA repair. Ref.7 Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA damage, and then polyubiquitinated through 'Lys-63'-linkage by UBC13/MMS2. Ubiquitination is required for UBC2-mediated DNA repair.
Sequence similarities	Belongs to the PCNA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Cellular component	Nucleus
Ligand	DNA-binding
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Traceable author statement PubMed 9745046. Source: SGD chromatin silencing at silent mating-type cassette Inferred from mutant phenotype PubMed 16157874. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype PubMed 16157874. Source: SGD lagging strand elongation Inferred from direct assay PubMed 7673186. Source: SGD leading strand elongation Inferred from direct assay PubMed 1682321. Source: SGD meiotic mismatch repair Inferred from mutant phenotype PubMed 18245822. Source: SGD mitotic sister chromatid cohesion Inferred from genetic interaction PubMed 16934511. Source: SGD nucleotide-excision repair Inferred from mutant phenotype PubMed 9806417. Source: SGD postreplication repair Inferred from mutant phenotype PubMed 8790390. Source: SGD regulation of DNA replication Inferred from electronic annotation. Source: InterPro
Cellular_component	PCNA complex Traceable author statement PubMed 9745046. Source: SGD nucleus Inferred from direct assay PubMed 15282802. Source: SGD replication fork Traceable author statement PubMed 9759502. Source: SGD
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA polymerase processivity factor activity Inferred from direct assay PubMed 18635534 PubMed 2902631. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
itself		2	EBI-12993,EBI-12993
MCM10	P32354	4	EBI-12993,EBI-5965
RAD27	P26793	4	EBI-12993,EBI-14693
RAD30	Q04049	3	EBI-12993,EBI-36214

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 258

258

Proliferating cell nuclear antigen

PRO_0000149176

Regions

DNA binding

61 – 80

Potential

Amino acid modifications

Cross-link

127

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7 Ref.8

Cross-link

164

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.7 Ref.8 Ref.9

Cross-link

164

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Secondary structure

258

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P15873 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 9B56C5851621DDDC
Show »

FASTA

258

28,916

        10         20         30         40         50         60 
MLEAKFEEAS LFKRIIDGFK DCVQLVNFQC KEDGIIAQAV DDSRVLLVSL EIGVEAFQEY 

        70         80         90        100        110        120 
RCDHPVTLGM DLTSLSKILR CGNNTDTLTL IADNTPDSII LLFEDTKKDR IAEYSLKLMD 

       130        140        150        160        170        180 
IDADFLKIEE LQYDSTLSLP SSEFSKIVRD LSQLSDSINI MITKETIKFV ADGDIGSGSV 

       190        200        210        220        230        240 
IIKPFVDMEH PETSIKLEMD QPVDLTFGAK YLLDIIKGSS LSDRVGIRLS SEAPALFQFD 

       250 
LKSGFLQFFL APKFNDEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, structure and expression of the yeast proliferating cell nuclear antigen gene." Bauer G.A., Burgess P.M.J. Nucleic Acids Res. 18:261-265(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-41 AND 231-240.
[2]	"Analysis of a 70 kb region on the right arm of yeast chromosome II." Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H. Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Interaction with PCNA is essential for yeast DNA polymerase eta function." Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L. Mol. Cell 8:407-415(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAD30.
[7]	"RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO." Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S. Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUMOYLATION AT LYS-127 AND LYS-164, UBIQUITINATION AT LYS-164, MASS SPECTROMETRY.
[8]	"Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses." Zhou W., Ryan J.J., Zhou H. J. Biol. Chem. 279:32262-32268(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-164, MASS SPECTROMETRY.
[9]	"A proteomic strategy for gaining insights into protein sumoylation in yeast." Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., Gygi S.P. Mol. Cell. Proteomics 4:246-254(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, MASS SPECTROMETRY. Strain: EJY251-11b.
[10]	"Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast." Das-Bradoo S., Ricke R.M., Bielinsky A.-K. Mol. Cell. Biol. 26:4806-4817(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MCM10.
[11]	"Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA." Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J. Cell 79:1233-1243(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[12]	"Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex." Bowman G.D., O'Donnell M., Kuriyan J. Nature 429:724-730(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH RFC1; RCF2; RCF3; RCF4 AND RCF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16676 Genomic DNA. Translation: CAA34664.1.
X78993 Genomic DNA. Translation: CAA55594.1.
Z35957 Genomic DNA. Translation: CAA85038.1.
AY557715 Genomic DNA. Translation: AAS56041.1.
BK006936 Genomic DNA. Translation: DAA07209.1.

PIR

WMBYET. S22851.

RefSeq

NP_009645.1. NM_001178436.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PLQ	X-ray	2.30	A	1-258	[»]
1PLR	X-ray	3.00	A	1-258	[»]
1SXJ	X-ray	2.85	F/G/H	1-258	[»]
2OD8	X-ray	2.80	A	1-258	[»]
3F1W	X-ray	2.90	A	1-258	[»]
3GPM	X-ray	3.80	A	1-258	[»]
3GPN	X-ray	2.50	A	1-258	[»]
3L0W	X-ray	2.80	A	1-163	[»]
3L0X	X-ray	3.00	A	1-163	[»]
			B	165-258	[»]
3L10	X-ray	2.80	A	1-163	[»]
3PGE	X-ray	2.80	A	165-258	[»]
			B	1-163	[»]
3V60	X-ray	2.60	B	1-258	[»]
3V61	X-ray	2.80	B	1-258	[»]
3V62	X-ray	2.90	B/E	1-258	[»]

ProteinModelPortal

P15873.

SMR

P15873. Positions 1-258.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2417N.

IntAct

P15873. 18 interactions.

MINT

MINT-675752.

STRING

4932.YBR088C.

Proteomic databases

PaxDb

P15873.

PeptideAtlas

P15873.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBR088C; YBR088C; YBR088C.

GeneID

852385.

KEGG

sce:YBR088C.

Organism-specific databases

CYGD

YBR088c.

SGD

S000000292. POL30.

Phylogenomic databases

eggNOG

COG0592.

GeneTree

ENSGT00390000004965.

HOGENOM

HOG000211098.

K04802.

OMA

YEMKLMN.

OrthoDB

EOG46MFTZ.

Gene expression databases

Genevestigator

P15873.

GermOnline

YBR088C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000730. Pr_cel_nuc_antig.
IPR022649. Pr_cel_nuc_antig_C.
IPR022659. Pr_cel_nuc_antig_CS.
IPR022648. Pr_cel_nuc_antig_N.
[Graphical view]

PANTHER

PTHR11352. PTHR11352. 1 hit.

Pfam

PF02747. PCNA_C. 1 hit.
PF00705. PCNA_N. 1 hit.
[Graphical view]

PRINTS

PR00339. PCNACYCLIN.

TIGRFAMs

TIGR00590. pcna. 1 hit.

PROSITE

PS01251. PCNA_1. 1 hit.
PS00293. PCNA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P15873.

NextBio

971192.

Entry information

Entry name

PCNA_YEAST

Accession

Primary (citable) accession number: P15873
Secondary accession number(s): D6VQ89

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents