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Protein

PCNA-associated factor

Gene

Paf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-MMU-5656169. Termination of translesion DNA synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
PCNA-associated factor
Alternative name(s):
HCV NS5A-transactivated protein 9 homolog
PCNA-associated factor of 15 kDa
Short name:
PAF15
Short name:
p15PAF
Gene namesi
Name:Paf
Synonyms:Ns5atp9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1915276. 2810417H13Rik.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmperinuclear region By similarity

  • Note: Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 110110PCNA-associated factorPRO_0000096685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei24 – 241N6-acetyllysine; alternateCombined sources
Cross-linki24 – 24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei71 – 711PhosphoserineBy similarity

Post-translational modificationi

Monoubiquitinated at Lys-15 and Lys-24 during normal S phase, promoting its association with PCNA. Also diubiquitinated at these 2 sites. Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24 are probably extended, leading to disrupt the interaction with PCNA. Polyubiquitinated by the APC/C complex at the mitotic exit, leading to its degradation by the proteasome (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9CQX4.
MaxQBiQ9CQX4.
PaxDbiQ9CQX4.
PRIDEiQ9CQX4.

PTM databases

iPTMnetiQ9CQX4.
PhosphoSiteiQ9CQX4.

Expressioni

Gene expression databases

BgeeiQ9CQX4.
CleanExiMM_2810417H13RIK.
GenevisibleiQ9CQX4. MM.

Interactioni

Subunit structurei

Interacts (when monoubiquitinated at Lys-15 and Lys-24) with PCNA. Interacts with isoform 2/p33ING1b of ING1. Interacts with BRCA1 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9CQX4. 1 interaction.
MINTiMINT-8178480.
STRINGi10090.ENSMUSP00000038877.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi23 – 3412D-boxAdd
BLAST
Motifi61 – 7111PIP-boxAdd
BLAST
Motifi77 – 793KEN box
Motifi84 – 9613Initiation motifAdd
BLAST

Domaini

The PIP-box mediates the interaction with PCNA.By similarity
The KEN box is required for the association with the APC/C complex.By similarity
The D-box (destruction box) mediates the interaction with APC/C proteins, and acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.By similarity
The initiation motif is required for efficient chain initiation by the APC/C complex E2 ligase UBE2C. It determines the rate of substrate's degradation without affecting its affinity for the APC/C, a mechanism used by the APC/C to control the timing of substrate proteolysis during the cell cycle (By similarity).By similarity

Phylogenomic databases

eggNOGiENOG410J101. Eukaryota.
ENOG410Y3KP. LUCA.
GeneTreeiENSGT00510000048252.
HOGENOMiHOG000013069.
HOVERGENiHBG052567.
InParanoidiQ9CQX4.
OMAiVENKYAG.
OrthoDBiEOG7DZ8P3.
PhylomeDBiQ9CQX4.
TreeFamiTF333199.

Family and domain databases

InterProiIPR031444. PCNA-AF.
[Graphical view]
PfamiPF15715. PAF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRTKANYVP GAYRKAVASQ APRKVLGSST FVTNSSSSSR KAENKYAGGN
60 70 80 90 100
PVCVRPTPKW QKGIGEFFRL SPKESKKENQ APEEAGTSGL GKAKRKACPL
110
QPDHRDDENE
Length:110
Mass (Da):11,993
Last modified:June 1, 2001 - v1
Checksum:i47054C3F288B5BE3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401R → G in BAB28650 (PubMed:16141072).Curated
Sequence conflicti51 – 511P → Q in AK011645 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY496943 mRNA. Translation: AAR90858.1.
AK011090 mRNA. Translation: BAB27391.1.
AK011645 mRNA. No translation available.
AK011835 mRNA. Translation: BAB27868.1.
AK013105 mRNA. Translation: BAB28650.1.
AK017673 mRNA. Translation: BAB30866.1.
BC021413 mRNA. Translation: AAH21413.1.
BC096393 mRNA. Translation: AAH96393.1.
CCDSiCCDS23299.1.
RefSeqiNP_080791.2. NM_026515.2.
UniGeneiMm.351273.
Mm.460895.

Genome annotation databases

EnsembliENSMUST00000045802; ENSMUSP00000038877; ENSMUSG00000040204.
GeneIDi68026.
KEGGimmu:68026.
UCSCiuc009qeb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY496943 mRNA. Translation: AAR90858.1.
AK011090 mRNA. Translation: BAB27391.1.
AK011645 mRNA. No translation available.
AK011835 mRNA. Translation: BAB27868.1.
AK013105 mRNA. Translation: BAB28650.1.
AK017673 mRNA. Translation: BAB30866.1.
BC021413 mRNA. Translation: AAH21413.1.
BC096393 mRNA. Translation: AAH96393.1.
CCDSiCCDS23299.1.
RefSeqiNP_080791.2. NM_026515.2.
UniGeneiMm.351273.
Mm.460895.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CQX4. 1 interaction.
MINTiMINT-8178480.
STRINGi10090.ENSMUSP00000038877.

PTM databases

iPTMnetiQ9CQX4.
PhosphoSiteiQ9CQX4.

Proteomic databases

EPDiQ9CQX4.
MaxQBiQ9CQX4.
PaxDbiQ9CQX4.
PRIDEiQ9CQX4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045802; ENSMUSP00000038877; ENSMUSG00000040204.
GeneIDi68026.
KEGGimmu:68026.
UCSCiuc009qeb.1. mouse.

Organism-specific databases

MGIiMGI:1915276. 2810417H13Rik.

Phylogenomic databases

eggNOGiENOG410J101. Eukaryota.
ENOG410Y3KP. LUCA.
GeneTreeiENSGT00510000048252.
HOGENOMiHOG000013069.
HOVERGENiHBG052567.
InParanoidiQ9CQX4.
OMAiVENKYAG.
OrthoDBiEOG7DZ8P3.
PhylomeDBiQ9CQX4.
TreeFamiTF333199.

Enzyme and pathway databases

ReactomeiR-MMU-5656169. Termination of translesion DNA synthesis.

Miscellaneous databases

NextBioi326234.
PROiQ9CQX4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQX4.
CleanExiMM_2810417H13RIK.
GenevisibleiQ9CQX4. MM.

Family and domain databases

InterProiIPR031444. PCNA-AF.
[Graphical view]
PfamiPF15715. PAF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mus musculus homologous cDNA to Homo sapiens NS5ATP9 gene."
    Cheng J., Liu Y., Li Q.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Mammary tumor.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPAF15_MOUSE
AccessioniPrimary (citable) accession number: Q9CQX4
Secondary accession number(s): Q4VAG2, Q9CZ17, Q9D0A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.