PAF15_MOUSE
ID PAF15_MOUSE Reviewed; 110 AA.
AC Q9CQX4; Q4VAG2; Q9CZ17; Q9D0A5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=PCNA-associated factor {ECO:0000305};
DE AltName: Full=HCV NS5A-transactivated protein 9 homolog;
DE AltName: Full=PCNA-associated factor of 15 kDa;
DE Short=PAF15;
DE Short=p15PAF;
DE AltName: Full=PCNA-clamp-associated factor {ECO:0000250|UniProtKB:Q15004};
GN Name=Pclaf {ECO:0000250|UniProtKB:Q15004}; Synonyms=Ns5atp9, Paf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng J., Liu Y., Li Q.;
RT "Mus musculus homologous cDNA to Homo sapiens NS5ATP9 gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: PCNA-binding protein that acts as a regulator of DNA repair
CC during DNA replication. Following DNA damage, the interaction with PCNA
CC is disrupted, facilitating the interaction between monoubiquitinated
CC PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at
CC stalled replisomes, facilitating the bypass of replication-fork-
CC blocking lesions. Also acts as a regulator of centrosome number (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (when monoubiquitinated at Lys-15 and Lys-24) with
CC PCNA. Interacts with isoform 2/p33ING1b of ING1. Interacts with BRCA1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15004}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}.
CC Note=Following DNA damage, localizes to DNA damage sites. Colocalizes
CC with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA. {ECO:0000250}.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C
CC complex. {ECO:0000250}.
CC -!- DOMAIN: The D-box (destruction box) mediates the interaction with APC/C
CC proteins, and acts as a recognition signal for degradation via the
CC ubiquitin-proteasome pathway. {ECO:0000250}.
CC -!- DOMAIN: The initiation motif is required for efficient chain initiation
CC by the APC/C complex E2 ligase UBE2C. It determines the rate of
CC substrate's degradation without affecting its affinity for the APC/C, a
CC mechanism used by the APC/C to control the timing of substrate
CC proteolysis during the cell cycle (By similarity). {ECO:0000250}.
CC -!- PTM: Monoubiquitinated at Lys-15 and Lys-24 during normal S phase,
CC promoting its association with PCNA. Also diubiquitinated at these 2
CC sites. Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24
CC are probably extended, leading to disrupt the interaction with PCNA.
CC Polyubiquitinated by the APC/C complex at the mitotic exit, leading to
CC its degradation by the proteasome (By similarity). {ECO:0000250}.
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DR EMBL; AY496943; AAR90858.1; -; mRNA.
DR EMBL; AK011090; BAB27391.1; -; mRNA.
DR EMBL; AK011645; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK011835; BAB27868.1; -; mRNA.
DR EMBL; AK013105; BAB28650.1; -; mRNA.
DR EMBL; AK017673; BAB30866.1; -; mRNA.
DR EMBL; BC021413; AAH21413.1; -; mRNA.
DR EMBL; BC096393; AAH96393.1; -; mRNA.
DR CCDS; CCDS23299.1; -.
DR RefSeq; NP_080791.2; NM_026515.2.
DR AlphaFoldDB; Q9CQX4; -.
DR SMR; Q9CQX4; -.
DR BioGRID; 212606; 1.
DR IntAct; Q9CQX4; 1.
DR MINT; Q9CQX4; -.
DR STRING; 10090.ENSMUSP00000038877; -.
DR iPTMnet; Q9CQX4; -.
DR PhosphoSitePlus; Q9CQX4; -.
DR EPD; Q9CQX4; -.
DR jPOST; Q9CQX4; -.
DR MaxQB; Q9CQX4; -.
DR PaxDb; Q9CQX4; -.
DR PeptideAtlas; Q9CQX4; -.
DR PRIDE; Q9CQX4; -.
DR ProteomicsDB; 287937; -.
DR DNASU; 68026; -.
DR Ensembl; ENSMUST00000045802; ENSMUSP00000038877; ENSMUSG00000040204.
DR GeneID; 68026; -.
DR KEGG; mmu:68026; -.
DR UCSC; uc009qeb.1; mouse.
DR CTD; 9768; -.
DR MGI; MGI:1915276; Pclaf.
DR VEuPathDB; HostDB:ENSMUSG00000040204; -.
DR eggNOG; ENOG502S3UM; Eukaryota.
DR GeneTree; ENSGT00510000048252; -.
DR HOGENOM; CLU_142343_0_0_1; -.
DR InParanoid; Q9CQX4; -.
DR OMA; QPDHTDE; -.
DR OrthoDB; 1508906at2759; -.
DR PhylomeDB; Q9CQX4; -.
DR TreeFam; TF333199; -.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR BioGRID-ORCS; 68026; 5 hits in 108 CRISPR screens.
DR ChiTaRS; Pclaf; mouse.
DR PRO; PR:Q9CQX4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CQX4; protein.
DR Bgee; ENSMUSG00000040204; Expressed in yolk sac and 163 other tissues.
DR Genevisible; Q9CQX4; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR InterPro; IPR040444; PCNA-AF.
DR InterPro; IPR031444; PCNA-AF_dom.
DR PANTHER; PTHR15679; PTHR15679; 1.
DR Pfam; PF15715; PAF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA damage; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..110
FT /note="PCNA-associated factor"
FT /id="PRO_0000096685"
FT REGION 28..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..34
FT /note="D-box"
FT MOTIF 61..71
FT /note="PIP-box"
FT MOTIF 77..79
FT /note="KEN box"
FT MOTIF 84..96
FT /note="Initiation motif"
FT COMPBIAS 28..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT CONFLICT 40
FT /note="R -> G (in Ref. 2; BAB28650)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="P -> Q (in Ref. 2; AK011645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 11993 MW; 47054C3F288B5BE3 CRC64;
MVRTKANYVP GAYRKAVASQ APRKVLGSST FVTNSSSSSR KAENKYAGGN PVCVRPTPKW
QKGIGEFFRL SPKESKKENQ APEEAGTSGL GKAKRKACPL QPDHRDDENE
