Proliferating cell nuclear antigen - Mus musculus (Mouse)

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P17918 (PCNA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 123. History...

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

Documents (2) |

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

Alternative name(s):
Cyclin

Gene names

Name:

Pcna

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	261 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. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities By similarity. Has to be loaded onto DNA in order to be able to stimulate APEX2 By similarity.
Subunit structure	Homotrimer By similarity. Forms a complex with activator 1 heteropentamer in the presence of ATP. Interacts with POLH, POLK, DNMT1, ERCC5, FEN1, CDC6, POLD1, POLD3, POLD4 and POLDIP2. Interacts with EXO1, KCTD10 and SHPRH. Forms a ternary complex with DNTTIP2 and core histone. Interacts with BAZ1B; the interaction is direct. Interacts with HLTF and SHPRH By similarity. Interacts with PPP1R15A. Interacts with HHV-1 ICP34.5. Interacts with NUDT15 By similarity. Interaction is disrupted in response to UV irradiation and acetylation. Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex. Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA. Interacts with DDX11. Interacts with EGFR; positively regulates PCNA By similarity. Ref.5 Ref.6
Subcellular location	Nucleus By similarity. Note: Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents By similarity.
Induction	Induced in IL2-stimulated proliferating T-lymphocytes.
Post-translational modification	Upon methyl methanesulfonate-induced DNA damage, mono-ubiquitinated by the UBE2B-RAD18 complex on Lys-164. This induces non-canonical poly-ubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH, which is required for DNA repair. 'Lys-63' polyubiquitination prevents genomic instability on DNA damage. 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 By similarity. Acetylated in response to UV irradiation. Acetylation disrupts interaction with NUDT15 and promotes degradation By similarity. Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA By similarity. Ref.7
Sequence similarities	Belongs to the PCNA family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW base-excision repair, gap-filling Inferred from direct assay. Source: MGI intracellular protein transport Inferred from mutant phenotype. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: MGI positive regulation of deoxyribonuclease activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of DNA replication Inferred from electronic annotation. Source: InterPro translesion synthesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	PCNA complex Inferred from electronic annotation. Source: InterPro PCNA-p21 complex Inferred from sequence or structural similarity. Source: UniProtKB cyclin-dependent protein kinase holoenzyme complex Inferred from physical interaction. Source: MGI nuclear lamina Inferred from direct assay. Source: MGI
Molecular function	DNA polymerase processivity factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Gadd45g	Q9Z111	2	EBI-1173716,EBI-1173616
Ppp1ca	P62137	2	EBI-1173716,EBI-357187

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Proliferating cell nuclear antigen

PRO_0000149160

Regions

DNA binding

61 – 80

Potential

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

211

Phosphotyrosine; by EGFR Ref.7

Modified residue

248

N6-acetyllysine By similarity

Cross-link

164

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict

3 – 5

EAR → LES Ref.4

Sequence conflict

A → T in CAA37243. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P17918 [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: F705CCBDD3205986
Show »

FASTA

261

28,785

        10         20         30         40         50         60 
MFEARLIQGS ILKKVLEALK DLINEACWDV SSGGVNLQSM DSSHVSLVQL TLRSEGFDTY 

        70         80         90        100        110        120 
RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD 

       130        140        150        160        170        180 
LDVEQLGIPE QEYSCVIKMP SGEFARICRD LSHIGDAVVI SCAKNGVKFS ASGELGNGNI 

       190        200        210        220        230        240 
KLSQTSNVDK EEEAVTIEMN EPVHLTFALR YLNFFTKATP LSPTVTLSMS ADVPLVVEYK 

       250        260 
IADMGHLKYY LAPKIEDEEA S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of murine PCNA: interspecies comparison of the cDNA and the 5' flanking region of the gene." Shipman-Appasamy P.M., Cohen K.S., Prystowsky M.B. DNA Seq. 2:181-191(1991) [PubMed: 1726365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Lymphoid tissue.
[2]	"Molecular cloning and structural analysis of mouse gene and pseudogenes for proliferating cell nuclear antigen." Yamaguchi M., Hayashi Y., Hirose F., Matsuoka S., Moriuchi T., Shiroishi T., Moriwaki K., Matsukage A. Nucleic Acids Res. 19:2403-2410(1991) [PubMed: 1674997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6. Tissue: Spleen.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[4]	"Cyclin mRNA and protein expression in recombinant interleukin 2-stimulated cloned murine T lymphocytes." Shipman P.M., Sabath D.E., Fischer A.H., Comber P.G., Sullivan K., Tan E.M., Prystowsky M.B. J. Cell. Biochem. 38:189-198(1988) [PubMed: 2906640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-42. Tissue: T-cell.
[5]	"The herpes simplex virus virulence factor ICP34.5 and the cellular protein MyD116 complex with proliferating cell nuclear antigen through the 63-amino-acid domain conserved in ICP34.5, MyD116, and GADD34." Brown S.M., MacLean A.R., McKie E.A., Harland J. J. Virol. 71:9442-9449(1997) [PubMed: 9371605] [Abstract] Cited for: INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5.
[6]	"Characterization of the genomic structure and expression of the mouse Apex2 gene." Ide Y., Tsuchimoto D., Tominaga Y., Iwamoto Y., Nakabeppu Y. Genomics 81:47-57(2003) [PubMed: 12573260] [Abstract] Cited for: INTERACTION WITH APEX2.
[7]	"Tyrosine phosphorylation controls PCNA function through protein stability." Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C., McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C. Nat. Cell Biol. 8:1359-1368(2006) [PubMed: 17115032] [Abstract] Cited for: PHOSPHORYLATION AT TYR-211.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53068 mRNA. Translation: CAA37243.1. X57800 Genomic DNA. Translation: CAA40938.1. BC005778 mRNA. Translation: AAH05778.1. BC010343 mRNA. Translation: AAH10343.1.
IPI	IPI00113870.
PIR	WMMS. S15703.
RefSeq	NP_035175.1. NM_011045.2.
UniGene	Mm.7141.
3D structure databases
ProteinModelPortal	P17918.
SMR	P17918. Positions 1-257.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39409N.
IntAct	P17918. 6 interactions.
MINT	MINT-1510748.
STRING	P17918.
PTM databases
PhosphoSite	P17918.
2D gel databases
REPRODUCTION-2DPAGE	P17918.
Proteomic databases
PRIDE	P17918.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028817; ENSMUSP00000028817; ENSMUSG00000027342.
GeneID	18538.
KEGG	mmu:18538.
Organism-specific databases
CTD	5111.
MGI	MGI:97503. Pcna.
Phylogenomic databases
eggNOG	roNOG14028.
HOVERGEN	HBG000947.
InParanoid	P17918.
OMA	KAQDNAD.
OrthoDB	EOG4933JJ.
PhylomeDB	P17918.
Gene expression databases
ArrayExpress	P17918.
Bgee	P17918.
CleanEx	MM_PCNA.
Genevestigator	P17918.
GermOnline	ENSMUSG00000027342. Mus musculus.
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]
KO	K04802.
PANTHER	PTHR11352. Pr_cel_nuc_antig. 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
NextBio	294312.
SOURCE	Search...

Entry information

Entry name

PCNA_MOUSE

Accession

Primary (citable) accession number: P17918

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	March 1, 1992
Last modified:	December 14, 2011
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel 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