ID WDR48_HUMAN Reviewed; 677 AA.
AC Q8TAF3; B4DM86; B4DQI2; B4DY84; Q63HJ2; Q658Y1; Q8N3Z1; Q9NSK8; Q9P279;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=WD repeat-containing protein 48 {ECO:0000303|PubMed:24145035};
DE AltName: Full=USP1-associated factor 1 {ECO:0000303|PubMed:18082604};
DE AltName: Full=WD repeat endosomal protein;
DE AltName: Full=p80 {ECO:0000303|PubMed:12196293};
GN Name=WDR48 {ECO:0000303|PubMed:24145035, ECO:0000312|HGNC:HGNC:30914};
GN Synonyms=KIAA1449 {ECO:0000303|PubMed:10819331},
GN UAF1 {ECO:0000303|PubMed:18082604};
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), FUNCTION (MICROBIAL INFECTION),
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH HERPESVIRUS
RP SAIMIRI TIP (MICROBIAL INFECTION).
RX PubMed=12196293; DOI=10.1016/s1074-7613(02)00368-0;
RA Park J., Lee B.-S., Choi J.-K., Means R.E., Choe J., Jung J.U.;
RT "Herpesviral protein targets a cellular WD repeat endosomal protein to
RT downregulate T lymphocyte receptor expression.";
RL Immunity 17:221-233(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC TISSUE=Brain, Teratocarcinoma, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3-677 (ISOFORM 1).
RC TISSUE=Melanoma, Retina, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 [7]
RP INTERACTION WITH HERPESVIRUS SAIMIRI TIP (MICROBIAL INFECTION).
RX PubMed=12885920; DOI=10.1128/jvi.77.16.9041-9051.2003;
RA Park J., Cho N.-H., Choi J.-K., Feng P., Choe J., Jung J.U.;
RT "Distinct roles of cellular Lck and p80 proteins in herpesvirus saimiri Tip
RT function on lipid rafts.";
RL J. Virol. 77:9041-9051(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH USP1.
RX PubMed=18082604; DOI=10.1016/j.molcel.2007.09.031;
RA Cohn M.A., Kowal P., Yang K., Haas W., Huang T.T., Gygi S.P.,
RA D'Andrea A.D.;
RT "A UAF1-containing multisubunit protein complex regulates the Fanconi
RT anemia pathway.";
RL Mol. Cell 28:786-797(2007).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH
RP HPV11 E1 (MICROBIAL INFECTION).
RX PubMed=18032488; DOI=10.1128/jvi.01405-07;
RA Cote-Martin A., Moody C., Fradet-Turcotte A., D'Abramo C.M., Lehoux M.,
RA Joubert S., Poirier G.G., Coulombe B., Laimins L.A., Archambault J.;
RT "Human papillomavirus E1 helicase interacts with the WD repeat protein p80
RT to promote maintenance of the viral genome in keratinocytes.";
RL J. Virol. 82:1271-1283(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH USP12 AND USP46.
RX PubMed=19075014; DOI=10.1074/jbc.m808430200;
RA Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D.;
RT "UAF1 is a subunit of multiple deubiquitinating enzyme complexes.";
RL J. Biol. Chem. 284:5343-5351(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP FUNCTION, AND INTERACTION WITH ATAD5.
RX PubMed=20147293; DOI=10.1074/jbc.m109.092544;
RA Lee K.Y., Yang K., Cohn M.A., Sikdar N., D'Andrea A.D., Myung K.;
RT "Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear
RT antigen (PCNA) through Its interactions with PCNA and USP1.";
RL J. Biol. Chem. 285:10362-10369(2010).
RN [13]
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 [14]
RP FUNCTION, MUTAGENESIS OF LEU-580, AND INTERACTION WITH PHLPP1.
RX PubMed=24145035; DOI=10.1074/jbc.m113.503383;
RA Gangula N.R., Maddika S.;
RT "WD repeat protein WDR48 in complex with deubiquitinase USP12 suppresses
RT Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich
RT repeat protein phosphatase 1 (PHLPP1).";
RL J. Biol. Chem. 288:34545-34554(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEINS EBNA3 (MICROBIAL INFECTION).
RX PubMed=25855980; DOI=10.1371/journal.ppat.1004822;
RA Ohashi M., Holthaus A.M., Calderwood M.A., Lai C.Y., Krastins B.,
RA Sarracino D., Johannsen E.;
RT "The EBNA3 family of Epstein-Barr virus nuclear proteins associates with
RT the USP46/USP12 deubiquitination complexes to regulate lymphoblastoid cell
RT line growth.";
RL PLoS Pathog. 11:e1004822-e1004822(2015).
RN [17]
RP FUNCTION, AND INTERACTION WITH RAD51AP1.
RX PubMed=27463890; DOI=10.1080/15384101.2016.1209613;
RA Cukras S., Lee E., Palumbo E., Benavidez P., Moldovan G.L., Kee Y.;
RT "The USP1-UAF1 complex interacts with RAD51AP1 to promote homologous
RT recombination repair.";
RL Cell Cycle 15:2636-2646(2016).
RN [18]
RP FUNCTION, DNA-BINDING, INTERACTION WITH RAD51AP1, AND MUTAGENESIS OF
RP LYS-459; 595-LYS--HIS-599; LYS-595 AND HIS-599.
RX PubMed=27239033; DOI=10.1016/j.celrep.2016.05.007;
RA Liang F., Longerich S., Miller A.S., Tang C., Buzovetsky O., Xiong Y.,
RA Maranon D.G., Wiese C., Kupfer G.M., Sung P.;
RT "Promotion of RAD51-mediated homologous DNA pairing by the RAD51AP1-UAF1
RT complex.";
RL Cell Rep. 15:2118-2126(2016).
RN [19]
RP FUNCTION, AND INTERACTION WITH RAD51 AND ATAD5.
RX PubMed=31844045; DOI=10.1038/s41467-019-13667-4;
RA Park S.H., Kang N., Song E., Wie M., Lee E.A., Hwang S., Lee D., Ra J.S.,
RA Park I.B., Park J., Kang S., Park J.H., Hohng S., Lee K.Y., Myung K.;
RT "ATAD5 promotes replication restart by regulating RAD51 and PCNA in
RT response to replication stress.";
RL Nat. Commun. 10:5718-5718(2019).
RN [20]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF ARG-30; ARG-50; LYS-117; THR-161;
RP LYS-168; SER-230; ARG-272; ARG-274; LYS-275; LYS-318 AND ILE-363.
RX PubMed=31253762; DOI=10.1038/s41467-019-10408-5;
RA Liang F., Miller A.S., Longerich S., Tang C., Maranon D., Williamson E.A.,
RA Hromas R., Wiese C., Kupfer G.M., Sung P.;
RT "DNA requirement in FANCD2 deubiquitination by USP1-UAF1-RAD51AP1 in the
RT Fanconi anemia DNA damage response.";
RL Nat. Commun. 10:2849-2849(2019).
RN [21]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF ARG-30; ARG-50; LYS-117; THR-161;
RP LYS-168; SER-230; ARG-272; ARG-274; LYS-275; LYS-318 AND ILE-363.
RX PubMed=32350107; DOI=10.1074/jbc.ra120.013714;
RA Liang F., Miller A.S., Tang C., Maranon D., Williamson E.A., Hromas R.,
RA Wiese C., Zhao W., Sung P., Kupfer G.M.;
RT "The DNA-binding activity of USP1-associated factor 1 is required for
RT efficient RAD51-mediated homologous DNA pairing and homology-directed DNA
RT repair.";
RL J. Biol. Chem. 295:8186-8194(2020).
RN [22]
RP SUBUNIT.
RX PubMed=33844468; DOI=10.1111/febs.15875;
RA Olazabal-Herrero A., Bilbao-Arribas M., Carlevaris O., Sendino M.,
RA Varela-Martinez E., Jugo B.M., Berra E., Rodriguez J.A.;
RT "The dystrophia myotonica WD repeat-containing protein DMWD and WDR20
RT differentially regulate USP12 deubiquitinase.";
RL FEBS J. 288:5943-5963(2021).
RN [23]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL138 (MICROBIAL INFECTION).
RX PubMed=37289831; DOI=10.1371/journal.ppat.1011185;
RA Zarrella K., Longmire P., Zeltzer S., Collins-McMillen D., Hancock M.,
RA Buehler J., Reitsma J.M., Terhune S.S., Nelson J.A., Goodrum F.;
RT "Human Cytomegalovirus UL138 interaction with USP1 activates STAT1 in
RT infection.";
RL PLoS Pathog. 19:e1011185-e1011185(2023).
RN [24] {ECO:0007744|PDB:5CVL, ECO:0007744|PDB:5CVN, ECO:0007744|PDB:5CVO}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-580 IN COMPLEX WITH USP46 AND
RP UBIQUITIN, INTERACTION WITH USP46 AND USP1, FUNCTION, AND MUTAGENESIS OF
RP SER-170; LYS-214; TRP-256 AND ARG-272.
RX PubMed=26388029; DOI=10.1016/j.str.2015.08.010;
RA Yin J., Schoeffler A.J., Wickliffe K., Newton K., Starovasnik M.A.,
RA Dueber E.C., Harris S.F.;
RT "Structural insights into WD-repeat 48 activation of ubiquitin-specific
RT protease 46.";
RL Structure 23:2043-2054(2015).
RN [25] {ECO:0007744|PDB:5L8E, ECO:0007744|PDB:5L8W}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 9-580, X-RAY CRYSTALLOGRAPHY
RP (2.79 ANGSTROMS) OF 9-580 IN COMPLEX WITH USP12 AND UBIQUITIN, INTERACTION
RP WITH USP12, FUNCTION, AND MUTAGENESIS OF LYS-214; TRP-256 AND ARG-272.
RX PubMed=27650958; DOI=10.1016/j.jsb.2016.09.011;
RA Dharadhar S., Clerici M., van Dijk W.J., Fish A., Sixma T.K.;
RT "A conserved two-step binding for the UAF1 regulator to the USP12
RT deubiquitinating enzyme.";
RL J. Struct. Biol. 196:437-447(2016).
RN [26] {ECO:0007744|PDB:5K1A, ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH USP12 AND WDR20,
RP INTERACTION WITH USP12, FUNCTION, AND MUTAGENESIS OF TRP-77; TYR-119;
RP TYR-172 AND TRP-256.
RX PubMed=27373336; DOI=10.1016/j.molcel.2016.05.031;
RA Li H., Lim K.S., Kim H., Hinds T.R., Jo U., Mao H., Weller C.E., Sun J.,
RA Chatterjee C., D'Andrea A.D., Zheng N.;
RT "Allosteric activation of ubiquitin-specific proteases by beta-propeller
RT proteins UAF1 and WDR20.";
RL Mol. Cell 63:249-260(2016).
RN [27]
RP VARIANT GLU-628 DEL.
RX PubMed=24482476; DOI=10.1126/science.1247363;
RA Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA Gleeson J.G.;
RT "Exome sequencing links corticospinal motor neuron disease to common
RT neurodegenerative disorders.";
RL Science 343:506-511(2014).
CC -!- FUNCTION: Regulator of deubiquitinating complexes, which acts as a
CC strong activator of USP1, USP12 and USP46 (PubMed:18082604,
CC PubMed:19075014, PubMed:31253762, PubMed:26388029). Enhances the USP1-
CC mediated deubiquitination of FANCD2; USP1 being almost inactive by
CC itself (PubMed:18082604, PubMed:31253762). Activates deubiquitination
CC by increasing the catalytic turnover without increasing the affinity of
CC deubiquitinating enzymes for the substrate (PubMed:19075014,
CC PubMed:27373336). Also activates deubiquitinating activity of complexes
CC containing USP12 (PubMed:19075014, PubMed:27650958, PubMed:27373336).
CC In complex with USP12, acts as a potential tumor suppressor by
CC positively regulating PHLPP1 stability (PubMed:24145035). Docks at the
CC distal end of the USP12 fingers domain and induces a cascade of
CC structural changes leading to the activation of the enzyme
CC (PubMed:27650958, PubMed:27373336). Together with RAD51AP1, promotes
CC DNA repair by stimulating RAD51-mediated homologous recombination
CC (PubMed:27463890, PubMed:27239033, PubMed:32350107). Binds single-
CC stranded DNA (ssDNA) and double-stranded DNA (dsDNA) (PubMed:27239033,
CC PubMed:31253762, PubMed:32350107). DNA-binding is required both for
CC USP1-mediated deubiquitination of FANCD2 and stimulation of RAD51-
CC mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have
CC coordinated role in DNA-binding during these processes
CC (PubMed:31253762, PubMed:32350107). Together with ATAD5 and by
CC regulating USP1 activity, has a role in PCNA-mediated translesion
CC synthesis (TLS) by deubiquitinating monoubiquitinated PCNA
CC (PubMed:20147293). Together with ATAD5, has a role in recruiting RAD51
CC to stalled forks during replication stress (PubMed:31844045).
CC {ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014,
CC ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:24145035,
CC ECO:0000269|PubMed:26388029, ECO:0000269|PubMed:27239033,
CC ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:27463890,
CC ECO:0000269|PubMed:27650958, ECO:0000269|PubMed:31253762,
CC ECO:0000269|PubMed:31844045, ECO:0000269|PubMed:32350107}.
CC -!- FUNCTION: (Microbial infection) In case of infection by Herpesvirus
CC saimiri, may play a role in vesicular transport or membrane fusion
CC events necessary for transport to lysosomes. Induces lysosomal vesicle
CC formation via interaction with Herpesvirus saimiri tyrosine kinase-
CC interacting protein (TIP). Subsequently, TIP recruits tyrosine-protein
CC kinase LCK, resulting in down-regulation of T-cell antigen receptor
CC TCR. May play a role in generation of enlarged endosomal vesicles via
CC interaction with TIP (PubMed:12196293). In case of infection by
CC papillomavirus HPV11, promotes the maintenance of the viral genome via
CC its interaction with HPV11 helicase E1 (PubMed:18032488).
CC {ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18032488}.
CC -!- SUBUNIT: Interacts with USP46 (PubMed:19075014, PubMed:26388029).
CC Interacts with USP1 (PubMed:18082604, PubMed:26388029). Interacts with
CC USP12 (PubMed:19075014, PubMed:27650958, PubMed:27373336). Component of
CC the USP12-WDR20-WDR48 deubiquitinating complex (PubMed:27373336).
CC Component of the USP12/DMWD/WDR48 deubiquitinating complex
CC (PubMed:33844468). Interacts with PHLPP1 (PubMed:24145035). Interacts
CC with RAD51AP1; the interaction is direct and promotes formation of a
CC trimeric complex with RAD51 via RAD51AP1 (PubMed:27463890,
CC PubMed:27239033). Interacts with ATAD5; the interaction regulates USP1-
CC mediated PCNA deubiquitination (PubMed:20147293). Interacts with RAD51;
CC the interaction is enhanced under replication stress (PubMed:31844045).
CC {ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014,
CC ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:24145035,
CC ECO:0000269|PubMed:26388029, ECO:0000269|PubMed:27239033,
CC ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:27463890,
CC ECO:0000269|PubMed:27650958, ECO:0000269|PubMed:31844045,
CC ECO:0000269|PubMed:33844468}.
CC -!- SUBUNIT: (Microbial infection) Interacts with papillomavirus HPV11 E1
CC protein. {ECO:0000269|PubMed:18032488}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Saimiriine herpesvirus
CC TIP protein. {ECO:0000269|PubMed:12196293,
CC ECO:0000269|PubMed:12885920}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL138. {ECO:0000269|PubMed:37289831}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC protein EBNA3. {ECO:0000269|PubMed:18032488}.
CC -!- INTERACTION:
CC Q8TAF3-1; O94782: USP1; NbExp=2; IntAct=EBI-16178048, EBI-2513396;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18032488}. Cytoplasm
CC {ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18032488}. Lysosome
CC {ECO:0000269|PubMed:12196293}. Late endosome
CC {ECO:0000269|PubMed:12196293}. Note=Mainly in cytoplasmic compartments
CC (PubMed:12196293, PubMed:18032488). In case of infection by
CC papillomavirus HPV11, translocates to the nucleus via its interaction
CC with papillomavirus HPV11 (PubMed:18032488).
CC {ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18032488}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8TAF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAF3-2; Sequence=VSP_016776, VSP_016777;
CC Name=3;
CC IsoId=Q8TAF3-3; Sequence=VSP_037625;
CC Name=4;
CC IsoId=Q8TAF3-4; Sequence=VSP_037623;
CC Name=5;
CC IsoId=Q8TAF3-5; Sequence=VSP_037624, VSP_037626;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12196293}.
CC -!- DOMAIN: N-terminal WD region interacts with TIP and C-terminal region
CC mediates lysosomal localization (Probable). The WD repeats are required
CC for the interaction with deubiquitinating enzymes USP1, USP12 and
CC USP46. {ECO:0000269|PubMed:26388029, ECO:0000305}.
CC -!- MISCELLANEOUS: Knockdown of WDR48 increases Akt activation.
CC {ECO:0000269|PubMed:24145035}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA95973.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH56182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH56300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF468833; AAL78650.1; -; mRNA.
DR EMBL; AB040882; BAA95973.2; ALT_INIT; mRNA.
DR EMBL; AK297349; BAG59798.1; -; mRNA.
DR EMBL; AK298810; BAG60944.1; -; mRNA.
DR EMBL; AK302307; BAG63646.1; -; mRNA.
DR EMBL; AL162064; CAB82402.1; -; mRNA.
DR EMBL; AL832926; CAH56300.1; ALT_INIT; mRNA.
DR EMBL; BX649170; CAH56182.1; ALT_INIT; mRNA.
DR EMBL; BC026353; AAH26353.1; -; mRNA.
DR EMBL; BC037168; AAH37168.1; ALT_INIT; mRNA.
DR CCDS; CCDS33738.1; -. [Q8TAF3-1]
DR PIR; T47168; T47168.
DR RefSeq; NP_001290331.1; NM_001303402.1. [Q8TAF3-4]
DR RefSeq; NP_001290332.1; NM_001303403.1. [Q8TAF3-3]
DR RefSeq; NP_001333156.1; NM_001346227.1.
DR RefSeq; NP_001333157.1; NM_001346228.1.
DR RefSeq; NP_065890.1; NM_020839.3. [Q8TAF3-1]
DR PDB; 5CVL; X-ray; 3.00 A; A=2-580.
DR PDB; 5CVN; X-ray; 3.36 A; A=2-580.
DR PDB; 5CVO; X-ray; 3.88 A; A/D=1-677.
DR PDB; 5K1A; X-ray; 2.30 A; B/D/F/H=1-677.
DR PDB; 5K1B; X-ray; 3.30 A; B=1-677.
DR PDB; 5K1C; X-ray; 3.00 A; B=1-563.
DR PDB; 5L8E; X-ray; 2.30 A; A/B=9-580.
DR PDB; 5L8W; X-ray; 2.79 A; B=9-580.
DR PDB; 6JLQ; X-ray; 3.10 A; B=1-580.
DR PDB; 7AY0; X-ray; 3.60 A; A/C=1-563.
DR PDB; 7AY1; EM; 3.70 A; E=1-677.
DR PDB; 7AY2; X-ray; 3.20 A; A/D=1-563.
DR PDB; 8A9J; EM; 2.80 A; E=1-677.
DR PDB; 8A9K; EM; 2.85 A; E=1-677.
DR PDBsum; 5CVL; -.
DR PDBsum; 5CVN; -.
DR PDBsum; 5CVO; -.
DR PDBsum; 5K1A; -.
DR PDBsum; 5K1B; -.
DR PDBsum; 5K1C; -.
DR PDBsum; 5L8E; -.
DR PDBsum; 5L8W; -.
DR PDBsum; 6JLQ; -.
DR PDBsum; 7AY0; -.
DR PDBsum; 7AY1; -.
DR PDBsum; 7AY2; -.
DR PDBsum; 8A9J; -.
DR PDBsum; 8A9K; -.
DR AlphaFoldDB; Q8TAF3; -.
DR EMDB; EMD-11934; -.
DR EMDB; EMD-15284; -.
DR SMR; Q8TAF3; -.
DR BioGRID; 121649; 158.
DR CORUM; Q8TAF3; -.
DR DIP; DIP-50841N; -.
DR IntAct; Q8TAF3; 85.
DR MINT; Q8TAF3; -.
DR STRING; 9606.ENSP00000307491; -.
DR BindingDB; Q8TAF3; -.
DR ChEMBL; CHEMBL3430885; -.
DR GlyGen; Q8TAF3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TAF3; -.
DR PhosphoSitePlus; Q8TAF3; -.
DR BioMuta; WDR48; -.
DR DMDM; 74760390; -.
DR EPD; Q8TAF3; -.
DR jPOST; Q8TAF3; -.
DR MassIVE; Q8TAF3; -.
DR MaxQB; Q8TAF3; -.
DR PaxDb; 9606-ENSP00000307491; -.
DR PeptideAtlas; Q8TAF3; -.
DR ProteomicsDB; 73870; -. [Q8TAF3-1]
DR ProteomicsDB; 73871; -. [Q8TAF3-2]
DR ProteomicsDB; 73872; -. [Q8TAF3-3]
DR ProteomicsDB; 73873; -. [Q8TAF3-4]
DR ProteomicsDB; 73874; -. [Q8TAF3-5]
DR Pumba; Q8TAF3; -.
DR Antibodypedia; 50460; 132 antibodies from 25 providers.
DR DNASU; 57599; -.
DR Ensembl; ENST00000302313.10; ENSP00000307491.5; ENSG00000114742.14. [Q8TAF3-1]
DR GeneID; 57599; -.
DR KEGG; hsa:57599; -.
DR MANE-Select; ENST00000302313.10; ENSP00000307491.5; NM_020839.4; NP_065890.1.
DR UCSC; uc003cit.4; human. [Q8TAF3-1]
DR AGR; HGNC:30914; -.
DR CTD; 57599; -.
DR DisGeNET; 57599; -.
DR GeneCards; WDR48; -.
DR HGNC; HGNC:30914; WDR48.
DR HPA; ENSG00000114742; Low tissue specificity.
DR MalaCards; WDR48; -.
DR MIM; 612167; gene.
DR neXtProt; NX_Q8TAF3; -.
DR OpenTargets; ENSG00000114742; -.
DR Orphanet; 401800; Autosomal recessive spastic paraplegia type 60.
DR PharmGKB; PA134956949; -.
DR VEuPathDB; HostDB:ENSG00000114742; -.
DR eggNOG; KOG0308; Eukaryota.
DR GeneTree; ENSGT00920000149157; -.
DR HOGENOM; CLU_014960_0_1_1; -.
DR InParanoid; Q8TAF3; -.
DR OMA; ENDCFSA; -.
DR OrthoDB; 2786585at2759; -.
DR PhylomeDB; Q8TAF3; -.
DR TreeFam; TF315205; -.
DR PathwayCommons; Q8TAF3; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-HSA-9673766; Signaling by cytosolic PDGFRA and PDGFRB fusion proteins.
DR SignaLink; Q8TAF3; -.
DR SIGNOR; Q8TAF3; -.
DR BioGRID-ORCS; 57599; 261 hits in 1171 CRISPR screens.
DR ChiTaRS; WDR48; human.
DR GenomeRNAi; 57599; -.
DR Pharos; Q8TAF3; Tbio.
DR PRO; PR:Q8TAF3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8TAF3; Protein.
DR Bgee; ENSG00000114742; Expressed in ventricular zone and 212 other cell types or tissues.
DR ExpressionAtlas; Q8TAF3; baseline and differential.
DR Genevisible; Q8TAF3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProt.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035800; F:deubiquitinase activator activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProt.
DR GO; GO:1902525; P:regulation of protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd17041; Ubl_WDR48; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR021772; WDR48/Bun107.
DR PANTHER; PTHR19862; WD REPEAT-CONTAINING PROTEIN 48; 1.
DR PANTHER; PTHR19862:SF14; WD REPEAT-CONTAINING PROTEIN 48; 1.
DR Pfam; PF11816; DUF3337; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA damage;
KW DNA repair; DNA-binding; Endosome; Host-virus interaction; Lysosome;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..677
FT /note="WD repeat-containing protein 48"
FT /id="PRO_0000051399"
FT REPEAT 28..67
FT /note="WD 1"
FT REPEAT 73..112
FT /note="WD 2"
FT REPEAT 115..154
FT /note="WD 3"
FT REPEAT 166..205
FT /note="WD 4"
FT REPEAT 208..247
FT /note="WD 5"
FT REPEAT 250..289
FT /note="WD 6"
FT REPEAT 292..334
FT /note="WD 7"
FT REPEAT 358..397
FT /note="WD 8"
FT REGION 607..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH57"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 578
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH57"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..558
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016776"
FT VAR_SEQ 1..90
FT /note="MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDS
FT IIRIWSVNQHKQDPYIASMEHHTDWVNDIVLCCNGKTL -> MECQSAQV (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037623"
FT VAR_SEQ 16..223
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037624"
FT VAR_SEQ 91..99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037625"
FT VAR_SEQ 325..391
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037626"
FT VAR_SEQ 645
FT /note="D -> DQV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016777"
FT VARIANT 628
FT /note="Missing (found in a patient with spastic paraplegia;
FT uncertain significance)"
FT /evidence="ECO:0000269|PubMed:24482476"
FT /id="VAR_077846"
FT MUTAGEN 30
FT /note="R->A: In UAF1(3A); impaired DNA-binding; when
FT associated with A-50 and A-168. In UAF1(3A); does not
FT affect ability to promote USP1-mediated deubiquitination of
FT FANCD2 and stimulate RAD51-mediated homologous
FT recombination, because of DNA-binding mediated by RAD51AP1;
FT when associated with A-50 and A-168. In UAF1(11A); impaired
FT DNA-binding; when associated with A-50, A-117, A-161, A-
FT 168, A-230, A-272, A-274, A-275, A-318 and A-363. In
FT UAF1(11A); does not affect ability to promote USP1-mediated
FT deubiquitination of FANCD2 and stimulate RAD51-mediated
FT homologous recombination, because of DNA-binding mediated
FT by RAD51AP1; when associated with A-50, A-117, A-161, A-
FT 168, A-230, A-272, A-274, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 50
FT /note="R->A: In UAF1(3A); impaired DNA-binding; when
FT associated with A-30 and A-168. In UAF1(3A); does not
FT affect ability to promote USP1-mediated deubiquitination of
FT FANCD2 and stimulate RAD51-mediated homologous
FT recombination, because of DNA-binding mediated by RAD51AP1;
FT when associated with A-30 and A-168. In UAF1(11A); impaired
FT DNA-binding; when associated with A-30, A-117, A-161, A-
FT 168, A-230, A-272, A-274, A-275, A-318 and A-363. In
FT UAF1(11A); does not affect ability to promote USP1-mediated
FT deubiquitination of FANCD2 and stimulate RAD51-mediated
FT homologous recombination, because of DNA-binding mediated
FT by RAD51AP1; when associated with A-30, A-117, A-161, A-
FT 168, A-230, A-272, A-274, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 77
FT /note="W->A: Impaired binding to USP12; when associated
FT with Ala-256."
FT /evidence="ECO:0000269|PubMed:27373336"
FT MUTAGEN 117
FT /note="K->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-161, A-168, A-230, A-272, A-
FT 274, A-275, A-318 and A-363. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-161, A-168, A-230, A-272, A-
FT 274, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 119
FT /note="Y->A: Impaired binding to USP12; when associated
FT with Ala-172."
FT /evidence="ECO:0000269|PubMed:27373336"
FT MUTAGEN 161
FT /note="T->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-117, A-168, A-230, A-272, A-
FT 274, A-275, A-318 and A-363. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-117, A-168, A-230, A-272, A-
FT 274, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 168
FT /note="K->A: In UAF1(3A); impaired DNA-binding; when
FT associated with A-30 and A-50. In UAF1(3A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30 and A-50. In UAF1(11A); impaired DNA-
FT binding; when associated with A-30, A-50, A-117, A-161, A-
FT 230, A-272, A-274, A-275, A-318 and A-363. In UAF1(11A);
FT does not affect ability to promote USP1-mediated
FT deubiquitination of FANCD2 and stimulate RAD51-mediated
FT homologous recombination, because of DNA-binding mediated
FT by RAD51AP1; when associated with A-30, A-50, A-117, A-161,
FT A-230, A-272, A-274, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 170
FT /note="S->Y: Strongly reduces interaction with USP46 and
FT abolishes stimulation of USP46 enzyme activity."
FT /evidence="ECO:0000269|PubMed:26388029"
FT MUTAGEN 172
FT /note="Y->A: Impaired binding to USP12; when associated
FT with Ala-119."
FT /evidence="ECO:0000269|PubMed:27373336"
FT MUTAGEN 214
FT /note="K->E: Strongly reduces interaction with USP12 or
FT USP46 and abolishes stimulation of their enzyme activity;
FT when associated with A-256 and D-272."
FT /evidence="ECO:0000269|PubMed:26388029,
FT ECO:0000269|PubMed:27650958"
FT MUTAGEN 230
FT /note="S->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-272, A-
FT 274, A-275, A-318 and A-363. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-272, A-
FT 274, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 256
FT /note="W->A: Strongly reduces interaction with USP12 or
FT USP46 and abolishes stimulation of their enzyme activity;
FT when associated with E-214 and D-272. Impaired binding to
FT USP12; when associated with Ala-77."
FT /evidence="ECO:0000269|PubMed:26388029,
FT ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:27650958"
FT MUTAGEN 272
FT /note="R->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 274, A-275, A-318 and A-363. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 274, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 272
FT /note="R->D: Strongly reduces interaction with USP12 or
FT USP46 and abolishes stimulation of their enzyme activity;
FT when associated with E-214 and A-256."
FT /evidence="ECO:0000269|PubMed:26388029,
FT ECO:0000269|PubMed:27650958"
FT MUTAGEN 274
FT /note="R->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-275, A-318 and A-363. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-275, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 275
FT /note="K->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-274, A-318 and A-363. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-274, A-318 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 318
FT /note="K->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-274, A-275 and A-363. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-274, A-275 and A-363."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 363
FT /note="I->A: In UAF1(11A); impaired DNA-binding; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-274, A-275 and A-318. In UAF1(11A); does not affect
FT ability to promote USP1-mediated deubiquitination of FANCD2
FT and stimulate RAD51-mediated homologous recombination,
FT because of DNA-binding mediated by RAD51AP1; when
FT associated with A-30, A-50, A-117, A-161, A-168, A-230, A-
FT 272, A-274, A-275 and A-318."
FT /evidence="ECO:0000269|PubMed:31253762"
FT MUTAGEN 459
FT /note="K->E: Decreased interaction with RAD51AP1."
FT /evidence="ECO:0000269|PubMed:27239033"
FT MUTAGEN 580
FT /note="L->F: Impaired binding to PHLPP1. Defective in
FT stabilizing PHLPP1."
FT /evidence="ECO:0000269|PubMed:24145035"
FT MUTAGEN 595..599
FT /note="KVMEH->EVMEA: Decreased interaction with RAD51AP1."
FT /evidence="ECO:0000269|PubMed:27239033"
FT MUTAGEN 595
FT /note="K->E: Does not affect interaction with RAD51AP1."
FT /evidence="ECO:0000269|PubMed:27239033"
FT MUTAGEN 599
FT /note="H->A: Does not affect interaction with RAD51AP1."
FT /evidence="ECO:0000269|PubMed:27239033"
FT CONFLICT 161
FT /note="T -> A (in Ref. 6; AAH37168)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="I -> V (in Ref. 4; BAG63646)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> F (in Ref. 4; BAG63646)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="G -> E (in Ref. 4; BAG63646)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="L -> P (in Ref. 4; BAG63646)"
FT /evidence="ECO:0000305"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:8A9K"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5L8E"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6JLQ"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:5CVL"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 435..439
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 445..449
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:5L8E"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:5K1A"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 530..534
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 536..545
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 548..554
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 631..638
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:5K1A"
FT HELIX 654..660
FT /evidence="ECO:0007829|PDB:5K1A"
FT STRAND 664..674
FT /evidence="ECO:0007829|PDB:5K1A"
SQ SEQUENCE 677 AA; 76210 MW; 20FDA620E02696E0 CRC64;
MAAHHRQNTA GRRKVQVSYV IRDEVEKYNR NGVNALQLDP ALNRLFTAGR DSIIRIWSVN
QHKQDPYIAS MEHHTDWVND IVLCCNGKTL ISASSDTTVK VWNAHKGFCM STLRTHKDYV
KALAYAKDKE LVASAGLDRQ IFLWDVNTLT ALTASNNTVT TSSLSGNKDS IYSLAMNQLG
TIIVSGSTEK VLRVWDPRTC AKLMKLKGHT DNVKALLLNR DGTQCLSGSS DGTIRLWSLG
QQRCIATYRV HDEGVWALQV NDAFTHVYSG GRDRKIYCTD LRNPDIRVLI CEEKAPVLKM
ELDRSADPPP AIWVATTKST VNKWTLKGIH NFRASGDYDN DCTNPITPLC TQPDQVIKGG
ASIIQCHILN DKRHILTKDT NNNVAYWDVL KACKVEDLGK VDFEDEIKKR FKMVYVPNWF
SVDLKTGMLT ITLDESDCFA AWVSAKDAGF SSPDGSDPKL NLGGLLLQAL LEYWPRTHVN
PMDEEENEVN HVNGEQENRV QKGNGYFQVP PHTPVIFGEA GGRTLFRLLC RDSGGETESM
LLNETVPQWV IDITVDKNMP KFNKIPFYLQ PHASSGAKTL KKDRLSASDM LQVRKVMEHV
YEKIINLDNE SQTTSSSNNE KPGEQEKEED IAVLAEEKIE LLCQDQVLDP NMDLRTVKHF
IWKSGGDLTL HYRQKST
//
