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Database: UniProt
Entry: Q8TAF3
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Original site: Q8TAF3 
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   29-SEP-2021, entry version 173.
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   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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19] {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   [20] {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   [21] {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   [22]
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). {ECO:0000269|PubMed:18082604,
CC       ECO:0000269|PubMed:19075014, 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: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       Interacts with PHLPP1 (PubMed:24145035). Interacts with RAD51AP1; the
CC       interaction is direct and promotes formation of a trimeric complex with
CC       RAD51 via RAD51AP1 (PubMed:27463890, PubMed:27239033).
CC       {ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014,
CC       ECO:0000269|PubMed:24145035, ECO:0000269|PubMed:26388029,
CC       ECO:0000269|PubMed:27239033, ECO:0000269|PubMed:27373336,
CC       ECO:0000269|PubMed:27463890, ECO:0000269|PubMed:27650958}.
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   -!- 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   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   SMR; Q8TAF3; -.
DR   BioGRID; 121649; 107.
DR   CORUM; Q8TAF3; -.
DR   DIP; DIP-50841N; -.
DR   IntAct; Q8TAF3; 82.
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; Q8TAF3; -.
DR   PeptideAtlas; Q8TAF3; -.
DR   PRIDE; 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   Antibodypedia; 50460; 108 antibodies.
DR   DNASU; 57599; -.
DR   Ensembl; ENST00000302313; ENSP00000307491; ENSG00000114742. [Q8TAF3-1]
DR   GeneID; 57599; -.
DR   KEGG; hsa:57599; -.
DR   UCSC; uc003cit.4; human. [Q8TAF3-1]
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; NWFNVDL; -.
DR   OrthoDB; 261328at2759; -.
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; 250 hits in 1032 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 colon and 239 other tissues.
DR   ExpressionAtlas; Q8TAF3; baseline and differential.
DR   Genevisible; Q8TAF3; HS.
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: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:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
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:1903003; P:positive regulation of protein deubiquitination; IDA:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
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   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR021772; WDR48/Bun107.
DR   Pfam; PF11816; DUF3337; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 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                   unknown pathological 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:5CVL"
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
//
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