PAF15_HUMAN
ID PAF15_HUMAN Reviewed; 111 AA.
AC Q15004; A6NNU5; A8K3Y3; G9G694; G9G696;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=PCNA-associated factor {ECO:0000305};
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 9;
DE Short=HCV NS5A-transactivated protein 9;
DE AltName: Full=Overexpressed in anaplastic thyroid carcinoma 1;
DE Short=OEATC-1;
DE AltName: Full=PCNA-associated factor of 15 kDa;
DE Short=PAF15;
DE Short=p15PAF;
DE AltName: Full=PCNA-clamp-associated factor {ECO:0000312|HGNC:HGNC:28961};
GN Name=PCLAF {ECO:0000312|HGNC:HGNC:28961}; Synonyms=KIAA0101, NS5ATP9, PAF;
GN ORFNames=L5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 9 transactivated by hepatitis C
RT virus NS5A protein.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15334068; DOI=10.1038/sj.onc.1207921;
RA Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C.,
RA Cerveny C., Law C.-L., Wahl A., Carter P.;
RT "Suppression subtractive hybridization and expression profiling identifies
RT a unique set of genes overexpressed in non-small-cell lung cancer.";
RL Oncogene 23:7734-7745(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Adrenal gland;
RX PubMed=22096502; DOI=10.1371/journal.pone.0026866;
RA Jain M., Zhang L., Patterson E.E., Kebebew E.;
RT "KIAA0101 is overexpressed, and promotes growth and invasion in adrenal
RT cancer.";
RL PLoS ONE 6:E26866-E26866(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, Lymph, and Retinoblastoma;
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 [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PCNA, AND
RP MUTAGENESIS OF ILE-65 AND PHE-68.
RX PubMed=11313979; DOI=10.1038/sj.onc.1204113;
RA Yu P., Huang B., Shen M., Lau C., Chan E., Michel J., Xiong Y., Payan D.G.,
RA Luo Y.;
RT "p15(PAF), a novel PCNA associated factor with increased expression in
RT tumor tissues.";
RL Oncogene 20:484-489(2001).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=15789362; DOI=10.1002/cncr.20988;
RA Mizutani K., Onda M., Asaka S., Akaishi J., Miyamoto S., Yoshida A.,
RA Nagahama M., Ito K., Emi M.;
RT "Overexpressed in anaplastic thyroid carcinoma-1 (OEATC-1) as a novel gene
RT responsible for anaplastic thyroid carcinoma.";
RL Cancer 103:1785-1790(2005).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH ING1 AND PCNA, AND INDUCTION.
RX PubMed=16288740; DOI=10.1016/j.yexcr.2005.09.020;
RA Simpson F., Lammerts van Bueren K., Butterfield N., Bennetts J.S.,
RA Bowles J., Adolphe C., Simms L.A., Young J., Walsh M.D., Leggett B.,
RA Fowles L.F., Wicking C.;
RT "The PCNA-associated factor KIAA0101/p15(PAF) binds the potential tumor
RT suppressor product p33ING1b.";
RL Exp. Cell Res. 312:73-85(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP INTERACTION WITH PCNA, AND INDUCTION.
RX PubMed=19219066; DOI=10.1038/cdd.2009.2;
RA Turchi L., Fareh M., Aberdam E., Kitajima S., Simpson F., Wicking C.,
RA Aberdam D., Virolle T.;
RT "ATF3 and p15PAF are novel gatekeepers of genomic integrity upon UV
RT stress.";
RL Cell Death Differ. 16:728-737(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA1.
RX PubMed=21673012; DOI=10.1158/1541-7786.mcr-10-0503;
RA Kais Z., Barsky S.H., Mathsyaraja H., Zha A., Ransburgh D.J., He G.,
RA Pilarski R.T., Shapiro C.L., Huang K., Parvin J.D.;
RT "KIAA0101 interacts with BRCA1 and regulates centrosome number.";
RL Mol. Cancer Res. 9:1091-1099(2011).
RN [17]
RP UBIQUITINATION, INTERACTION WITH PCNA, AND MUTAGENESIS OF 93-LYS--LYS-97.
RX PubMed=21700221; DOI=10.1016/j.molcel.2011.04.022;
RA Williamson A., Banerjee S., Zhu X., Philipp I., Iavarone A.T., Rape M.;
RT "Regulation of ubiquitin chain initiation to control the timing of
RT substrate degradation.";
RL Mol. Cell 42:744-757(2011).
RN [18]
RP SUBCELLULAR LOCATION, INTERACTION WITH PCNA, UBIQUITINATION,
RP PHOSPHORYLATION AT SER-31 AND SER-72, AND MUTAGENESIS OF 68-PHE-PHE-69 AND
RP LYS-78.
RX PubMed=21628590; DOI=10.1073/pnas.1106136108;
RA Emanuele M.J., Ciccia A., Elia A.E., Elledge S.J.;
RT "Proliferating cell nuclear antigen (PCNA)-associated KIAA0101/PAF15
RT protein is a cell cycle-regulated anaphase-promoting complex/cyclosome
RT substrate.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9845-9850(2011).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA, UBIQUITINATION AT
RP LYS-15 AND LYS-24, AND MUTAGENESIS OF LYS-15 AND LYS-24.
RX PubMed=23000965; DOI=10.1038/ncb2579;
RA Povlsen L.K., Beli P., Wagner S.A., Poulsen S.L., Sylvestersen K.B.,
RA Poulsen J.W., Nielsen M.L., Bekker-Jensen S., Mailand N., Choudhary C.;
RT "Systems-wide analysis of ubiquitylation dynamics reveals a key role for
RT PAF15 ubiquitylation in DNA-damage bypass.";
RL Nat. Cell Biol. 14:1089-1098(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-28 AND SER-72, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(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.
CC {ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}.
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 {ECO:0000269|PubMed:11313979, ECO:0000269|PubMed:16288740,
CC ECO:0000269|PubMed:19219066, ECO:0000269|PubMed:21628590,
CC ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:21700221,
CC ECO:0000269|PubMed:23000965}.
CC -!- INTERACTION:
CC Q15004; P12004: PCNA; NbExp=5; IntAct=EBI-10971436, EBI-358311;
CC Q15004; P54274-2: TERF1; NbExp=3; IntAct=EBI-10971436, EBI-711018;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11313979,
CC ECO:0000269|PubMed:16288740, ECO:0000269|PubMed:21673012,
CC ECO:0000269|PubMed:23000965}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:21673012}. Note=Following DNA damage, localizes to
CC DNA damage sites (PubMed:21628590). Colocalizes with centrosomes in
CC perinuclear region (PubMed:21673012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15004-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15004-2; Sequence=VSP_045659;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver, pancreas and
CC placenta. Not detected in heart or brain. Highly expressed in a number
CC of tumors, especially esophageal tumors, in anaplastic thyroid
CC carcinomas, adrenocortical carcinomas, and in non-small-cell lung
CC cancer lines. {ECO:0000269|PubMed:11313979,
CC ECO:0000269|PubMed:15789362, ECO:0000269|PubMed:22096502}.
CC -!- DEVELOPMENTAL STAGE: Present only during S and G2 phases of the cell
CC cycle. Peaks at the G2/M phase of the cell cycle and drops rapidly at
CC mitotic exit in an APC/C-dependent manner (at protein level).
CC -!- INDUCTION: By UV irradiation. By ATF3 in response to UV-stress.
CC {ECO:0000269|PubMed:16288740, ECO:0000269|PubMed:19219066}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA
CC (PubMed:21628590, PubMed:23000965). {ECO:0000269|PubMed:21628590,
CC ECO:0000269|PubMed:23000965}.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C
CC complex. {ECO:0000269|PubMed:21628590}.
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 (PubMed:21700221).
CC {ECO:0000269|PubMed:21700221}.
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. {ECO:0000269|PubMed:21628590,
CC ECO:0000269|PubMed:21700221, ECO:0000269|PubMed:23000965}.
CC -!- MISCELLANEOUS: Overexpression in adrenocortical neoplasms (ACC), may
CC promote growth and invasion in adrenal cancer.
CC {ECO:0000305|PubMed:22096502}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03491.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KIAA0101ID41058ch15q22.html";
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DR EMBL; AF529370; AAQ09604.1; -; mRNA.
DR EMBL; AY598324; AAT06735.1; -; mRNA.
DR EMBL; JN245882; AEW89488.1; -; Genomic_DNA.
DR EMBL; JN245883; AEW89489.1; -; Genomic_DNA.
DR EMBL; JN245884; AEW89490.1; -; Genomic_DNA.
DR EMBL; JN245885; AEW89491.1; -; Genomic_DNA.
DR EMBL; JN245886; AEW89492.1; -; Genomic_DNA.
DR EMBL; JN245889; AEW89495.1; -; Genomic_DNA.
DR EMBL; JN245890; AEW89496.1; -; Genomic_DNA.
DR EMBL; JN245892; AEW89498.1; -; Genomic_DNA.
DR EMBL; JN245893; AEW89499.1; -; Genomic_DNA.
DR EMBL; JN245894; AEW89500.1; -; Genomic_DNA.
DR EMBL; JN245895; AEW89501.1; -; Genomic_DNA.
DR EMBL; JN245896; AEW89502.1; -; Genomic_DNA.
DR EMBL; JN245897; AEW89503.1; -; Genomic_DNA.
DR EMBL; JN245898; AEW89504.1; -; Genomic_DNA.
DR EMBL; JN245899; AEW89505.1; -; Genomic_DNA.
DR EMBL; JN245900; AEW89506.1; -; Genomic_DNA.
DR EMBL; JN245901; AEW89507.1; -; Genomic_DNA.
DR EMBL; JN245902; AEW89508.1; -; Genomic_DNA.
DR EMBL; JN245903; AEW89509.1; -; Genomic_DNA.
DR EMBL; JN245904; AEW89510.1; -; Genomic_DNA.
DR EMBL; JN245906; AEW89512.1; -; Genomic_DNA.
DR EMBL; JN245907; AEW89513.1; -; Genomic_DNA.
DR EMBL; JN245908; AEW89514.1; -; Genomic_DNA.
DR EMBL; JN245910; AEW89516.1; -; Genomic_DNA.
DR EMBL; JN245911; AEW89517.1; -; Genomic_DNA.
DR EMBL; JN245912; AEW89518.1; -; Genomic_DNA.
DR EMBL; JN245936; AEW89560.1; -; Genomic_DNA.
DR EMBL; JN245937; AEW89561.1; -; Genomic_DNA.
DR EMBL; JN245938; AEW89562.1; -; Genomic_DNA.
DR EMBL; JN245939; AEW89563.1; -; Genomic_DNA.
DR EMBL; JN245940; AEW89564.1; -; Genomic_DNA.
DR EMBL; JN245941; AEW89565.1; -; Genomic_DNA.
DR EMBL; JN245942; AEW89566.1; -; Genomic_DNA.
DR EMBL; JN245943; AEW89567.1; -; Genomic_DNA.
DR EMBL; JN245944; AEW89568.1; -; Genomic_DNA.
DR EMBL; JN245945; AEW89569.1; -; Genomic_DNA.
DR EMBL; JN245887; AEW89493.1; -; Genomic_DNA.
DR EMBL; JN245888; AEW89494.1; -; Genomic_DNA.
DR EMBL; JN245891; AEW89497.1; -; Genomic_DNA.
DR EMBL; JN245905; AEW89511.1; -; Genomic_DNA.
DR EMBL; JN245909; AEW89515.1; -; Genomic_DNA.
DR EMBL; JN245913; AEW89519.1; -; Genomic_DNA.
DR EMBL; JN245914; AEW89520.1; -; Genomic_DNA.
DR EMBL; JN245915; AEW89521.1; -; Genomic_DNA.
DR EMBL; JN245916; AEW89522.1; -; Genomic_DNA.
DR EMBL; JN245917; AEW89523.1; -; Genomic_DNA.
DR EMBL; D14657; BAA03491.2; ALT_INIT; mRNA.
DR EMBL; AK290748; BAF83437.1; -; mRNA.
DR EMBL; AC087632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77679.1; -; Genomic_DNA.
DR EMBL; BC005832; AAH05832.1; -; mRNA.
DR EMBL; BC007101; AAH07101.1; -; mRNA.
DR EMBL; BC016782; AAH16782.1; -; mRNA.
DR EMBL; BU170434; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS10193.1; -. [Q15004-1]
DR CCDS; CCDS32269.1; -. [Q15004-2]
DR RefSeq; NP_001025160.1; NM_001029989.2. [Q15004-2]
DR RefSeq; NP_055551.1; NM_014736.5. [Q15004-1]
DR PDB; 4D2G; X-ray; 2.65 A; D/E=52-69.
DR PDB; 6EHT; X-ray; 3.20 A; D/E=52-71.
DR PDB; 6GWS; X-ray; 2.90 A; D/E/F=41-72.
DR PDB; 6IIW; X-ray; 1.70 A; B=2-11.
DR PDBsum; 4D2G; -.
DR PDBsum; 6EHT; -.
DR PDBsum; 6GWS; -.
DR PDBsum; 6IIW; -.
DR AlphaFoldDB; Q15004; -.
DR BMRB; Q15004; -.
DR SMR; Q15004; -.
DR BioGRID; 115114; 70.
DR CORUM; Q15004; -.
DR IntAct; Q15004; 5.
DR STRING; 9606.ENSP00000300035; -.
DR ChEMBL; CHEMBL5574; -.
DR GlyGen; Q15004; 1 site.
DR iPTMnet; Q15004; -.
DR PhosphoSitePlus; Q15004; -.
DR BioMuta; PCLAF; -.
DR EPD; Q15004; -.
DR jPOST; Q15004; -.
DR MassIVE; Q15004; -.
DR MaxQB; Q15004; -.
DR PaxDb; Q15004; -.
DR PeptideAtlas; Q15004; -.
DR PRIDE; Q15004; -.
DR ProteomicsDB; 1637; -.
DR Antibodypedia; 25814; 232 antibodies from 26 providers.
DR DNASU; 9768; -.
DR Ensembl; ENST00000300035.9; ENSP00000300035.4; ENSG00000166803.14. [Q15004-1]
DR Ensembl; ENST00000380258.6; ENSP00000369608.2; ENSG00000166803.14. [Q15004-2]
DR GeneID; 9768; -.
DR KEGG; hsa:9768; -.
DR MANE-Select; ENST00000300035.9; ENSP00000300035.4; NM_014736.6; NP_055551.1.
DR UCSC; uc002ank.5; human. [Q15004-1]
DR CTD; 9768; -.
DR DisGeNET; 9768; -.
DR GeneCards; PCLAF; -.
DR HGNC; HGNC:28961; PCLAF.
DR HPA; ENSG00000166803; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 610696; gene.
DR neXtProt; NX_Q15004; -.
DR OpenTargets; ENSG00000166803; -.
DR OpenTargets; ENSG00000259316; -.
DR PharmGKB; PA134974023; -.
DR VEuPathDB; HostDB:ENSG00000166803; -.
DR eggNOG; ENOG502S3UM; Eukaryota.
DR GeneTree; ENSGT00510000048252; -.
DR HOGENOM; CLU_142343_0_0_1; -.
DR InParanoid; Q15004; -.
DR OMA; QPDHTDE; -.
DR OrthoDB; 1508906at2759; -.
DR PhylomeDB; Q15004; -.
DR TreeFam; TF333199; -.
DR PathwayCommons; Q15004; -.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR SignaLink; Q15004; -.
DR SIGNOR; Q15004; -.
DR BioGRID-ORCS; 9768; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; KIAA0101; human.
DR GeneWiki; KIAA0101; -.
DR GenomeRNAi; 9768; -.
DR Pharos; Q15004; Tbio.
DR PRO; PR:Q15004; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q15004; protein.
DR Bgee; ENSG00000166803; Expressed in endometrium epithelium and 191 other tissues.
DR ExpressionAtlas; Q15004; baseline and differential.
DR Genevisible; Q15004; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB.
DR DisProt; DP01425; -.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA damage;
KW DNA repair; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..111
FT /note="PCNA-associated factor"
FT /id="PRO_0000096684"
FT REGION 23..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..34
FT /note="D-box"
FT MOTIF 62..72
FT /note="PIP-box"
FT MOTIF 78..80
FT /note="KEN box"
FT MOTIF 85..97
FT /note="Initiation motif"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQX4"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21628590"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21628590,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23000965"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:23000965"
FT VAR_SEQ 43..111
FT /note="AENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKA
FT KRKACPLQPDHTNDEKE -> EHVLCNLITQMMKKNRTFSFIFE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045659"
FT VARIANT 79
FT /note="E -> K (in dbSNP:rs11554313)"
FT /id="VAR_051262"
FT MUTAGEN 15
FT /note="K->R: Loss of monoubiquitination; when associated
FT with R-24."
FT /evidence="ECO:0000269|PubMed:23000965"
FT MUTAGEN 24
FT /note="K->R: Loss of monoubiquitination; when associated
FT with R-15."
FT /evidence="ECO:0000269|PubMed:23000965"
FT MUTAGEN 65
FT /note="I->A: Loss of binding to PCNA."
FT /evidence="ECO:0000269|PubMed:11313979"
FT MUTAGEN 68..69
FT /note="FF->AA: Loss of binding to PCNA."
FT /evidence="ECO:0000269|PubMed:21628590"
FT MUTAGEN 68
FT /note="F->A: Loss of binding to PCNA."
FT /evidence="ECO:0000269|PubMed:11313979"
FT MUTAGEN 78
FT /note="K->A: Stabilizes the protein in G1 by preventing
FT association with the APC/C complex and degradation by the
FT proteasome."
FT /evidence="ECO:0000269|PubMed:21628590"
FT MUTAGEN 93..97
FT /note="KAKRK->AAAAA: Inhibits chain initiation by APC/C."
FT /evidence="ECO:0000269|PubMed:21700221"
FT MUTAGEN 93..97
FT /note="KAKRK->RARRR: No effect on chain initiation by
FT APC/C."
FT /evidence="ECO:0000269|PubMed:21700221"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4D2G"
SQ SEQUENCE 111 AA; 11986 MW; FEF2C4E398B70E40 CRC64;
MVRTKADSVP GTYRKVVAAR APRKVLGSST SATNSTSVSS RKAENKYAGG NPVCVRPTPK
WQKGIGEFFR LSPKDSEKEN QIPEEAGSSG LGKAKRKACP LQPDHTNDEK E
