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E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase NED4L) (NEDD4.2) (Nedd4-2)

 NED4L_HUMAN             Reviewed;         975 AA.
Q96PU5; O43165; Q3LSM7; Q7Z5F1; Q7Z5F2; Q7Z5N3; Q8N5A7; Q8WUU9;
Q9BW58; Q9H2W4; Q9NT88;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 2.
20-JUN-2018, entry version 169.
RecName: Full=E3 ubiquitin-protein ligase NEDD4-like;
EC=2.3.2.26;
AltName: Full=HECT-type E3 ubiquitin transferase NED4L;
AltName: Full=NEDD4.2;
AltName: Full=Nedd4-2;
Name=NEDD4L; Synonyms=KIAA0439, NEDL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
PubMed=11840194; DOI=10.1038/sj.ejhg.5200747;
Chen H., Ross C.A., Wang N., Huo Y., MacKinnon D.F., Potash J.B.,
Simpson S.G., McMahon F.J., DePaulo J.R. Jr., McInnis M.G.;
"NEDD4L on human chromosome 18q21 has multiple forms of transcripts
and is a homologue of the mouse Nedd4-2 gene.";
Eur. J. Hum. Genet. 9:922-930(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH SCNN1A;
SCNN1B AND SCNN1G.
TISSUE=Kidney;
PubMed=14556380; DOI=10.1016/S1631-0691(03)00154-9;
Malbert-Colas L., Nicolas G., Galand C., Lecomte M.-C., Dhermy D.;
"Identification of new partners of the epithelial sodium channel alpha
subunit.";
C. R. Biol. 326:615-624(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 7), TISSUE SPECIFICITY,
AND INDUCTION.
TISSUE=Prostate;
PubMed=14615060; DOI=10.1016/j.mce.2003.08.009;
Qi H., Grenier J., Fournier A., Labrie C.;
"Androgens differentially regulate the expression of NEDD4L
transcripts in LNCaP human prostate cancer cells.";
Mol. Cell. Endocrinol. 210:51-62(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Okamoto Y., Miyazaki K., Sakamoto M., Kato C., Nakagawara A.;
"Homo sapiens NEDD4-like ubiquitin ligase 3.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
Qi H., Labrie C.;
"NEDD4L transcripts expressed in human prostate cells.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 101-975 (ISOFORM 5).
TISSUE=Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII.
78 new cDNA clones from brain which code for large proteins in
vitro.";
DNA Res. 4:307-313(1997).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 52-975 (ISOFORM 3).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
PROTEIN SEQUENCE OF 448-462, INTERACTION WITH YWHAB; YWHAG; YWHAE;
YWHAQ AND YWHAH, PHOSPHORYLATION AT SER-448, MUTAGENESIS OF SER-448,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15677482; DOI=10.1074/jbc.M412884200;
Ichimura T., Yamamura H., Sasamoto K., Tominaga Y., Taoka M.,
Kakiuchi K., Shinkawa T., Takahashi N., Shimada S., Isobe T.;
"14-3-3 proteins modulate the expression of epithelial Na+ channels by
phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase.";
J. Biol. Chem. 280:13187-13194(2005).
[12]
INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
PubMed=11046148; DOI=10.1128/MCB.20.22.8526-8535.2000;
Winberg G., Matskova L., Chen F., Plant P., Rotin D., Gish G.,
Ingham R., Ernberg I., Pawson T.;
"Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3
protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases.";
Mol. Cell. Biol. 20:8526-8535(2000).
[13]
INTERACTION WITH SGK1 AND SCNN1A, AND PHOSPHORYLATION.
PubMed=11696533; DOI=10.1074/jbc.C100623200;
Snyder P.M., Olson D.R., Thomas B.C.;
"Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated
inhibition of the epithelial Na+ channel.";
J. Biol. Chem. 277:5-8(2002).
[14]
INTERACTION WITH NDFIP1.
PubMed=11748237; DOI=10.1074/jbc.M110443200;
Harvey K.F., Shearwin-Whyatt L.M., Fotia A., Parton R.G., Kumar S.;
"N4WBP5, a potential target for ubiquitination by the Nedd4 family of
proteins, is a novel Golgi-associated protein.";
J. Biol. Chem. 277:9307-9317(2002).
[15]
FUNCTION.
PubMed=12911626;
Boehmer C., Henke G., Schniepp R., Palmada M., Rothstein J.D.,
Broeer S., Lang F.;
"Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase
Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms
SGK1/3 and protein kinase B.";
J. Neurochem. 86:1181-1188(2003).
[16]
FUNCTION, MUTAGENESIS OF CYS-942, AND INTERACTION WITH SCN5A.
PubMed=15217910; DOI=10.1161/01.RES.0000136816.05109.89;
van Bemmelen M.X., Rougier J.-S., Gavillet B., Apotheloz F.,
Daidie D., Tateyama M., Rivolta I., Thomas M.A., Kass R.S., Staub O.,
Abriel H.;
"Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2
mediated ubiquitination.";
Circ. Res. 95:284-291(2004).
[17]
FUNCTION, INTERACTION WITH CLCN5, AND INDUCTION.
PubMed=15489223; DOI=10.1074/jbc.M411491200;
Hryciw D.H., Ekberg J., Lee A., Lensink I.L., Kumar S., Guggino W.B.,
Cook D.I., Pollock C.A., Poronnik P.;
"Nedd4-2 functionally interacts with ClC-5: involvement in
constitutive albumin endocytosis in proximal tubule cells.";
J. Biol. Chem. 279:54996-55007(2004).
[18]
PHOSPHORYLATION AT SER-342; THR-367 AND SER-448.
PubMed=15328345; DOI=10.1074/jbc.M407858200;
Snyder P.M., Olson D.R., Kabra R., Zhou R., Steines J.C.;
"cAMP and serum and glucocorticoid-inducible kinase (SGK) regulate the
epithelial Na(+) channel through convergent phosphorylation of Nedd4-
2.";
J. Biol. Chem. 279:45753-45758(2004).
[19]
FUNCTION.
PubMed=15040001; DOI=10.1002/jcp.10430;
Henke G., Maier G., Wallisch S., Boehmer C., Lang F.;
"Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin
ligase Nedd4-2 and the serum and glucocorticoid inducible kinase
SGK1.";
J. Cell. Physiol. 199:194-199(2004).
[20]
INTERACTION WITH SCN2A; SCN3A AND SCN5A.
PubMed=15548568; DOI=10.1152/ajpcell.00460.2004;
Rougier J.-S., van Bemmelen M.X., Bruce M.C., Jespersen T.,
Gavillet B., Apotheloz F., Cordonier S., Staub O., Rotin D.,
Abriel H.;
"Molecular determinants of voltage-gated sodium channel regulation by
the Nedd4/Nedd4-like proteins.";
Am. J. Physiol. 288:C692-C701(2005).
[21]
FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD6 AND SMAD7, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=15496141; DOI=10.1042/BJ20040738;
Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K.,
Miyazono K., Imamura T.;
"NEDD4-2 (neural precursor cell expressed, developmentally down-
regulated 4-2) negatively regulates TGF-beta (transforming growth
factor-beta) signalling by inducing ubiquitin-mediated degradation of
Smad2 and TGF-beta type I receptor.";
Biochem. J. 386:461-470(2005).
[22]
FUNCTION.
PubMed=15576372; DOI=10.1074/jbc.M411053200;
Zhou R., Snyder P.M.;
"Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated
kinase (SGK) ubiquitination and degradation.";
J. Biol. Chem. 280:4518-4523(2005).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[24]
SUBCELLULAR LOCATION.
PubMed=18819914; DOI=10.1074/jbc.M804120200;
Putz U., Howitt J., Lackovic J., Foot N., Kumar S., Silke J.,
Tan S.S.;
"Nedd4 family-interacting protein 1 (Ndfip1) is required for the
exosomal secretion of Nedd4 family proteins.";
J. Biol. Chem. 283:32621-32627(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-342; SER-446;
SER-449; SER-464; SER-479 AND SER-487, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[28]
INTERACTION WITH NPC2, AND TISSUE SPECIFICITY.
PubMed=19664597; DOI=10.1016/j.bbrc.2009.07.158;
Araki N., Ishigami T., Ushio H., Minegishi S., Umemura M., Miyagi Y.,
Aoki I., Morinaga H., Tamura K., Toya Y., Uchino K., Umemura S.;
"Identification of NPC2 protein as interaction molecule with C2 domain
of human Nedd4L.";
Biochem. Biophys. Res. Commun. 388:290-296(2009).
[29]
ACTIVATION BY NDFIP1 AND NDFIP2, AND AUTOUBIQUITINATION.
PubMed=19343052; DOI=10.1038/embor.2009.30;
Mund T., Pelham H.R.;
"Control of the activity of WW-HECT domain E3 ubiquitin ligases by
NDFIP proteins.";
EMBO Rep. 10:501-507(2009).
[30]
FUNCTION AS A UBIQUITIN-PROTEIN LIGASE FOR TNK2, AND INTERACTION WITH
TNK2.
PubMed=19144635; DOI=10.1074/jbc.M806877200;
Chan W., Tian R., Lee Y.-F., Sit S.T., Lim L., Manser E.;
"Down-regulation of active ACK1 is mediated by association with the E3
ubiquitin ligase Nedd4-2.";
J. Biol. Chem. 284:8185-8194(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[32]
PHOSPHORYLATION AT SER-342 AND SER-449, AND INTERACTION WITH WNK1.
PubMed=20525693; DOI=10.1074/jbc.M110.103432;
Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S.,
Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L.,
Cobb M.H.;
"Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial
sodium channel are regulated by multiple with no lysine (WNK) family
members.";
J. Biol. Chem. 285:25161-25167(2010).
[33]
INTERACTION WITH TNK2.
PubMed=20086093; DOI=10.1128/MCB.00013-10;
Lin Q., Wang J., Childress C., Sudol M., Carey D.J., Yang W.;
"HECT E3 ubiquitin ligase Nedd4-1 ubiquitinates ACK and regulates
epidermal growth factor (EGF)-induced degradation of EGF receptor and
ACK.";
Mol. Cell. Biol. 30:1541-1554(2010).
[34]
PHOSPHORYLATION BY SGK1, AND INTERACTION WITH SGK1.
PubMed=20730100; DOI=10.1371/journal.pone.0012163;
Wiemuth D., Lott J.S., Ly K., Ke Y., Teesdale-Spittle P., Snyder P.M.,
McDonald F.J.;
"Interaction of serum- and glucocorticoid regulated kinase 1 (SGK1)
with the WW-domains of Nedd4-2 is required for epithelial sodium
channel regulation.";
PLoS ONE 5:E12163-E12163(2010).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 AND SER-483, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; SER-483 AND
SER-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[38]
INTERACTION WITH KCNQ1.
PubMed=22024150; DOI=10.1016/j.hrthm.2011.10.026;
Krzystanek K., Rasmussen H.B., Grunnet M., Staub O., Olesen S.P.,
Abriel H., Jespersen T.;
"Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated
downregulation of KCNQ1 potassium channels.";
Heart Rhythm 9:440-448(2012).
[39]
INTERACTION WITH ARRDC4.
PubMed=23236378; DOI=10.1371/journal.pone.0050557;
Shea F.F., Rowell J.L., Li Y., Chang T.H., Alvarez C.E.;
"Mammalian alpha arrestins link activated seven transmembrane
receptors to Nedd4 family e3 ubiquitin ligases and interact with beta
arrestins.";
PLoS ONE 7:E50557-E50557(2012).
[40]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[41]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G.,
Park J.Y., Yoon T.J.;
"SYT14L, especially its C2 domain, is involved in regulating
melanocyte differentiation.";
J. Dermatol. Sci. 72:246-251(2013).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; THR-318; SER-448;
SER-475; SER-479 AND SER-483, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
FUNCTION, INTERACTION WITH NDFIP1 AND NDFIP2, AND SUBCELLULAR
LOCATION.
PubMed=26363003; DOI=10.1042/BJ20141282;
Kang Y., Guo J., Yang T., Li W., Zhang S.;
"Regulation of the human ether-a-go-go-related gene (hERG) potassium
channel by Nedd4 family interacting proteins (Ndfips).";
Biochem. J. 472:71-82(2015).
[45]
FUNCTION IN UBIQUITINATION OF BRAT1.
PubMed=25631046; DOI=10.1074/jbc.M114.613687;
Low L.H., Chow Y.L., Li Y., Goh C.P., Putz U., Silke J., Ouchi T.,
Howitt J., Tan S.S.;
"Nedd4 family interacting protein 1 (Ndfip1) is required for
ubiquitination and nuclear trafficking of BRCA1-associated ATM
activator 1 (BRAT1) during the DNA damage response.";
J. Biol. Chem. 290:7141-7150(2015).
[46]
FUNCTION, INTERACTION WITH USP36, DEUBIQUITINATION BY USP36, AND
MUTAGENESIS OF CYS-942.
PubMed=27445338; DOI=10.1074/jbc.M116.722637;
Anta B., Martin-Rodriguez C., Gomis-Perez C., Calvo L.,
Lopez-Benito S., Calderon-Garcia A.A., Vicente-Garcia C.,
Villarroel A., Arevalo J.C.;
"Ubiquitin-specific Protease 36 (USP36) Controls Neuronal Precursor
Cell-expressed Developmentally Down-regulated 4-2 (Nedd4-2) Actions
over the Neurotrophin Receptor TrkA and Potassium Voltage-gated
Channels 7.2/3 (Kv7.2/3).";
J. Biol. Chem. 291:19132-19145(2016).
[47]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN PVNH7, VARIANTS PVNH7
CYS-679; HIS-694; LYS-893 AND GLN-897, AND CHARACTERIZATION OF
VARIANTS PVNH7 HIS-694; LYS-893 AND GLN-897.
PubMed=27694961; DOI=10.1038/ng.3676;
Deciphering Developmental Disorders study;
Broix L., Jagline H., Ivanova L.E., Schmucker S., Drouot N.,
Clayton-Smith J., Pagnamenta A.T., Metcalfe K.A., Isidor B.,
Louvier U.W., Poduri A., Taylor J.C., Tilly P., Poirier K.,
Saillour Y., Lebrun N., Stemmelen T., Rudolf G., Muraca G.,
Saintpierre B., Elmorjani A., Moise M., Weirauch N.B., Guerrini R.,
Boland A., Olaso R., Masson C., Tripathy R., Keays D., Beldjord C.,
Nguyen L., Godin J., Kini U., Nischke P., Deleuze J.F.,
Bahi-Buisson N., Sumara I., Hinckelmann M.V., Chelly J.;
"Mutations in the HECT domain of NEDD4L lead to AKT-mTOR pathway
deregulation and cause periventricular nodular heterotopia.";
Nat. Genet. 48:1349-1358(2016).
[48]
VARIANTS LEU-355 AND ARG-497.
PubMed=15140763; DOI=10.1152/ajprenal.00353.2003;
Fouladkou F., Alikhani-Koopaei R., Vogt B., Flores S.Y.,
Malbert-Colas L., Lecomte M.-C., Loffing J., Frey F.J., Frey B.M.,
Staub O.;
"A naturally occurring human Nedd4-2 variant displays impaired ENaC
regulation in Xenopus laevis oocytes.";
Am. J. Physiol. 287:F550-F561(2004).
-!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
an E2 ubiquitin-conjugating enzyme in the form of a thioester and
then directly transfers the ubiquitin to targeted substrates.
Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1
ubiquitination and proteasome-dependent degradation. Promotes
ubiquitination and internalization of various plasma membrane
channels such as ENaC, SCN2A/Nav1.2, SCN3A/Nav1.3, SCN5A/Nav1.5,
SCN9A/Nav1.7, SCN10A/Nav1.8, KCNA3/Kv1.3, KCNH2, EAAT1,
KCNQ2/Kv7.2, KCNQ3/Kv7.3 or CLC5 (PubMed:26363003,
PubMed:27445338). Promotes ubiquitination and degradation of SGK1
and TNK2. Ubiquitinates BRAT1 and this ubiquitination is enhanced
in the presence of NDFIP1 (PubMed:25631046). Plays a role in
dendrite formation by melanocytes (PubMed:23999003). Involved in
the regulation of TOR signaling (PubMed:27694961). Ubiquitinates
and regulates protein levels of NTRK1 once this one is activated
by NGF (PubMed:27445338). {ECO:0000250|UniProtKB:Q8CFI0,
ECO:0000269|PubMed:12911626, ECO:0000269|PubMed:15040001,
ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15489223,
ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:15576372,
ECO:0000269|PubMed:19144635, ECO:0000269|PubMed:23999003,
ECO:0000269|PubMed:25631046, ECO:0000269|PubMed:26363003,
ECO:0000269|PubMed:27445338, ECO:0000269|PubMed:27694961}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- ENZYME REGULATION: Activated by NDFIP1- and NDFIP2-binding.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with UBE2E3 (By similarity). Interacts with
NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-
protein ligase (PubMed:26363003, PubMed:11748237). Interacts via
its WW domains with SCNN1A, SCNN1B, SCNN1G, SCN1A, SCN2A, SCN3A,
SCN5A, SCN8A, SCN9A, SCN10A and CLCN5 (PubMed:11696533,
PubMed:14556380, PubMed:15217910, PubMed:15489223,
PubMed:15548568). Interacts with SMAD2, SMAD3, SMAD6 and SMAD7
(PubMed:15496141). The phosphorylated form interacts with 14-3-3
proteins (PubMed:15677482). Interacts with TNK2 (PubMed:19144635,
PubMed:20086093). Interacts with WNK1 (PubMed:20525693). Interacts
with SGK1 (PubMed:11696533, PubMed:20730100). Interacts (via C2
domain) with NPC2 (PubMed:19664597). Interacts with ARRDC4
(PubMed:23236378). Interacts with KCNQ1; promotes internalization
of KCNQ1 (PubMed:22024150). Interacts (via domains WW1, 3 and 4)
with USP36; the interaction inhibits ubiquitination of, at least,
NTRK1, KCNQ2 and KCNQ3 by NEDD4L (PubMed:27445338).
{ECO:0000250|UniProtKB:Q8CFI0, ECO:0000269|PubMed:11696533,
ECO:0000269|PubMed:11748237, ECO:0000269|PubMed:14556380,
ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15489223,
ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:15548568,
ECO:0000269|PubMed:15677482, ECO:0000269|PubMed:19144635,
ECO:0000269|PubMed:19664597, ECO:0000269|PubMed:20086093,
ECO:0000269|PubMed:20525693, ECO:0000269|PubMed:20730100,
ECO:0000269|PubMed:22024150, ECO:0000269|PubMed:23236378,
ECO:0000269|PubMed:26363003, ECO:0000269|PubMed:27445338}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
LMP2A. {ECO:0000269|PubMed:11046148}.
-!- INTERACTION:
Q15038:DAZAP2; NbExp=3; IntAct=EBI-717962, EBI-724310;
P49281:SLC11A2; NbExp=2; IntAct=EBI-717962, EBI-4319335;
O15105:SMAD7; NbExp=3; IntAct=EBI-7196393, EBI-3861591;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15496141,
ECO:0000269|PubMed:18819914, ECO:0000269|PubMed:27694961}. Golgi
apparatus {ECO:0000269|PubMed:26363003}. Endosome, multivesicular
body {ECO:0000269|PubMed:26363003}. Note=May be recruited to
exosomes by NDFIP1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=Nedd4-2c;
IsoId=Q96PU5-1; Sequence=Displayed;
Name=2;
IsoId=Q96PU5-2; Sequence=VSP_015448;
Note=No experimental confirmation available.;
Name=3; Synonyms=NEDD4Le;
IsoId=Q96PU5-3; Sequence=VSP_015447;
Note=No experimental confirmation available.;
Name=4; Synonyms=NEDD4La, NEDD4Lb, NEDD4Lf;
IsoId=Q96PU5-4; Sequence=VSP_015444;
Name=5; Synonyms=NEDD4Ld;
IsoId=Q96PU5-5; Sequence=VSP_043848;
Name=6; Synonyms=NEDD4Lh;
IsoId=Q96PU5-6; Sequence=VSP_015446, VSP_043848;
Name=7; Synonyms=NEDD4Lg;
IsoId=Q96PU5-7; Sequence=VSP_015446;
Name=8;
IsoId=Q96PU5-9; Sequence=VSP_015444, VSP_043848;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
prostate, pancreas and kidney (PubMed:14615060, PubMed:15496141,
PubMed:19664597). Expressed in melanocytes (PubMed:23999003).
{ECO:0000269|PubMed:14615060, ECO:0000269|PubMed:15496141,
ECO:0000269|PubMed:19664597, ECO:0000269|PubMed:23999003}.
-!- INDUCTION: By androgens in prostate, and by albumin in kidney.
{ECO:0000269|PubMed:14615060, ECO:0000269|PubMed:15489223}.
-!- PTM: Phosphorylated by SGK1 or PKA; which impairs interaction with
SCNN. Interaction with YWHAH inhibits dephosphorylation.
{ECO:0000269|PubMed:11696533, ECO:0000269|PubMed:15328345,
ECO:0000269|PubMed:15677482, ECO:0000269|PubMed:20525693,
ECO:0000269|PubMed:20730100}.
-!- PTM: Auto-ubiquitinated (PubMed:19343052). Deubiquitinated by
USP36, no effect on NEDD4L protein levels. Both proteins interact
and regulate each other's ubiquitination levels (PubMed:27445338).
{ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:27445338}.
-!- DISEASE: Periventricular nodular heterotopia 7 (PVNH7)
[MIM:617201]: A form of periventricular nodular heterotopia, a
disorder resulting from a defect in the pattern of neuronal
migration in which ectopic collections of neurons lie along the
lateral ventricles of the brain or just beneath, contiguously or
in isolated patches. PVNH7 is an autosomal dominant disease
characterized by delayed psychomotor development, intellectual
disability, and seizures in some patients. Additional features
include cleft palate and toe syndactyly.
{ECO:0000269|PubMed:27694961}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA23711.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA23711.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF210730; AAG43524.1; -; mRNA.
EMBL; AF385931; AAM46208.1; -; mRNA.
EMBL; AY312514; AAP75706.1; -; mRNA.
EMBL; AY112983; AAM76728.1; -; mRNA.
EMBL; AY112984; AAM76729.1; -; mRNA.
EMBL; AY112985; AAM76730.1; -; mRNA.
EMBL; AB071179; BAB69424.1; -; mRNA.
EMBL; DQ181796; ABA10330.1; -; mRNA.
EMBL; AC015988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471096; EAW63065.1; -; Genomic_DNA.
EMBL; BC000621; AAH00621.2; -; mRNA.
EMBL; BC019345; AAH19345.1; -; mRNA.
EMBL; BC032597; AAH32597.1; -; mRNA.
EMBL; AB007899; BAA23711.1; ALT_INIT; mRNA.
EMBL; AL137469; CAB70754.1; -; mRNA.
CCDS; CCDS45872.1; -. [Q96PU5-1]
CCDS; CCDS45873.1; -. [Q96PU5-5]
CCDS; CCDS45874.1; -. [Q96PU5-7]
CCDS; CCDS45875.1; -. [Q96PU5-4]
CCDS; CCDS45876.1; -. [Q96PU5-9]
CCDS; CCDS58632.1; -. [Q96PU5-2]
CCDS; CCDS59323.1; -. [Q96PU5-6]
PIR; T46412; T46412.
RefSeq; NP_001138436.1; NM_001144964.1. [Q96PU5-4]
RefSeq; NP_001138437.1; NM_001144965.1. [Q96PU5-4]
RefSeq; NP_001138438.1; NM_001144966.2. [Q96PU5-4]
RefSeq; NP_001138439.1; NM_001144967.2. [Q96PU5-1]
RefSeq; NP_001138440.1; NM_001144968.1. [Q96PU5-7]
RefSeq; NP_001138441.1; NM_001144969.1. [Q96PU5-6]
RefSeq; NP_001138442.1; NM_001144970.2. [Q96PU5-9]
RefSeq; NP_001138443.1; NM_001144971.1. [Q96PU5-9]
RefSeq; NP_001230889.1; NM_001243960.1. [Q96PU5-2]
RefSeq; NP_056092.2; NM_015277.5. [Q96PU5-5]
RefSeq; XP_016881168.1; XM_017025679.1. [Q96PU5-4]
UniGene; Hs.185677; -.
PDB; 2LAJ; NMR; -; A=496-535.
PDB; 2LB2; NMR; -; A=386-420.
PDB; 2LTY; NMR; -; A=385-417.
PDB; 2MPT; NMR; -; A=496-539, B=945-957.
PDB; 2NSQ; X-ray; 1.85 A; A=1-154.
PDB; 2ONI; X-ray; 2.20 A; A=594-967.
PDB; 3JVZ; X-ray; 3.30 A; C/D=596-975.
PDB; 3JW0; X-ray; 3.10 A; C/D=596-975.
PDB; 5HPK; X-ray; 2.43 A; A=594-975.
PDBsum; 2LAJ; -.
PDBsum; 2LB2; -.
PDBsum; 2LTY; -.
PDBsum; 2MPT; -.
PDBsum; 2NSQ; -.
PDBsum; 2ONI; -.
PDBsum; 3JVZ; -.
PDBsum; 3JW0; -.
PDBsum; 5HPK; -.
ProteinModelPortal; Q96PU5; -.
SMR; Q96PU5; -.
BioGrid; 116915; 207.
DIP; DIP-41935N; -.
IntAct; Q96PU5; 28.
MINT; Q96PU5; -.
STRING; 9606.ENSP00000383199; -.
iPTMnet; Q96PU5; -.
PhosphoSitePlus; Q96PU5; -.
BioMuta; NEDD4L; -.
DMDM; 73921204; -.
EPD; Q96PU5; -.
MaxQB; Q96PU5; -.
PaxDb; Q96PU5; -.
PeptideAtlas; Q96PU5; -.
PRIDE; Q96PU5; -.
ProteomicsDB; 77752; -.
ProteomicsDB; 77753; -. [Q96PU5-2]
ProteomicsDB; 77754; -. [Q96PU5-3]
ProteomicsDB; 77755; -. [Q96PU5-4]
ProteomicsDB; 77756; -. [Q96PU5-5]
ProteomicsDB; 77757; -. [Q96PU5-6]
ProteomicsDB; 77758; -. [Q96PU5-7]
ProteomicsDB; 77760; -. [Q96PU5-9]
DNASU; 23327; -.
Ensembl; ENST00000256830; ENSP00000256830; ENSG00000049759. [Q96PU5-3]
Ensembl; ENST00000356462; ENSP00000348847; ENSG00000049759. [Q96PU5-2]
Ensembl; ENST00000357895; ENSP00000350569; ENSG00000049759. [Q96PU5-7]
Ensembl; ENST00000382850; ENSP00000372301; ENSG00000049759. [Q96PU5-5]
Ensembl; ENST00000400345; ENSP00000383199; ENSG00000049759. [Q96PU5-1]
Ensembl; ENST00000431212; ENSP00000389406; ENSG00000049759. [Q96PU5-4]
Ensembl; ENST00000435432; ENSP00000393395; ENSG00000049759. [Q96PU5-9]
Ensembl; ENST00000456173; ENSP00000405440; ENSG00000049759. [Q96PU5-9]
Ensembl; ENST00000456986; ENSP00000411947; ENSG00000049759. [Q96PU5-4]
Ensembl; ENST00000586263; ENSP00000468546; ENSG00000049759. [Q96PU5-6]
GeneID; 23327; -.
KEGG; hsa:23327; -.
UCSC; uc002lgx.4; human. [Q96PU5-1]
CTD; 23327; -.
DisGeNET; 23327; -.
EuPathDB; HostDB:ENSG00000049759.16; -.
GeneCards; NEDD4L; -.
HGNC; HGNC:7728; NEDD4L.
HPA; HPA024618; -.
HPA; HPA064730; -.
MalaCards; NEDD4L; -.
MIM; 606384; gene.
MIM; 617201; phenotype.
neXtProt; NX_Q96PU5; -.
OpenTargets; ENSG00000049759; -.
PharmGKB; PA31534; -.
eggNOG; KOG0940; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00760000118966; -.
HOVERGEN; HBG004134; -.
InParanoid; Q96PU5; -.
KO; K13305; -.
OMA; SEQRDDM; -.
OrthoDB; EOG091G0SS8; -.
PhylomeDB; Q96PU5; -.
TreeFam; TF323658; -.
BioCyc; MetaCyc:ENSG00000049759-MONOMER; -.
BRENDA; 2.3.2.B8; 2681.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q96PU5; -.
SIGNOR; Q96PU5; -.
UniPathway; UPA00143; -.
ChiTaRS; NEDD4L; human.
EvolutionaryTrace; Q96PU5; -.
GeneWiki; NEDD4L; -.
GenomeRNAi; 23327; -.
PRO; PR:Q96PU5; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000049759; -.
ExpressionAtlas; Q96PU5; baseline and differential.
Genevisible; Q96PU5; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IC:UniProtKB.
GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0019870; F:potassium channel inhibitor activity; IDA:BHF-UCL.
GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL.
GO; GO:0019871; F:sodium channel inhibitor activity; IDA:BHF-UCL.
GO; GO:0017080; F:sodium channel regulator activity; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0006883; P:cellular sodium ion homeostasis; NAS:UniProtKB.
GO; GO:0007588; P:excretion; NAS:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:BHF-UCL.
GO; GO:1902306; P:negative regulation of sodium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; ISS:BHF-UCL.
GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; NAS:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:BHF-UCL.
GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0003254; P:regulation of membrane depolarization; IDA:BHF-UCL.
GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0042176; P:regulation of protein catabolic process; NAS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:0010038; P:response to metal ion; IDA:UniProtKB.
GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0030104; P:water homeostasis; NAS:UniProtKB.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 4.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR024928; E3_ub_ligase_SMURF1.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00168; C2; 1.
Pfam; PF00632; HECT; 1.
Pfam; PF00397; WW; 4.
PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
PRINTS; PR00360; C2DOMAIN.
SMART; SM00239; C2; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00456; WW; 4.
SUPFAM; SSF51045; SSF51045; 4.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS01159; WW_DOMAIN_1; 4.
PROSITE; PS50020; WW_DOMAIN_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Differentiation; Direct protein sequencing; Endosome;
Golgi apparatus; Host-virus interaction; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 975 E3 ubiquitin-protein ligase NEDD4-like.
/FTId=PRO_0000120323.
DOMAIN 7 109 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 193 226 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 385 418 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 497 530 WW 3. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 548 581 WW 4. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 640 974 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
ACT_SITE 942 942 Glycyl thioester intermediate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 318 318 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 342 342 Phosphoserine; by WNK1 and WNK4.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:15328345,
ECO:0000269|PubMed:20525693}.
MOD_RES 367 367 Phosphothreonine; by SGK1.
{ECO:0000305|PubMed:15328345}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 448 448 Phosphoserine; by PKA and SGK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15328345,
ECO:0000269|PubMed:15677482}.
MOD_RES 449 449 Phosphoserine; by WNK1 and WNK4.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:20525693}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 475 475 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 487 487 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
VAR_SEQ 1 121 Missing (in isoform 4 and isoform 8).
{ECO:0000303|PubMed:11840194,
ECO:0000303|PubMed:14615060,
ECO:0000303|PubMed:9455477,
ECO:0000303|Ref.5}.
/FTId=VSP_015444.
VAR_SEQ 1 16 MATGLGEPVYGLSEDE -> MRRLAFEQ (in isoform
6 and isoform 7).
{ECO:0000303|PubMed:14615060}.
/FTId=VSP_015446.
VAR_SEQ 356 459 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015447.
VAR_SEQ 356 419 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015448.
VAR_SEQ 356 375 Missing (in isoform 5, isoform 6 and
isoform 8). {ECO:0000303|PubMed:14615060,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9455477,
ECO:0000303|Ref.4, ECO:0000303|Ref.5}.
/FTId=VSP_043848.
VARIANT 355 355 P -> L (common polymorphism; impaired
ability to inhibit SCNN;
dbSNP:rs767136811).
{ECO:0000269|PubMed:15140763}.
/FTId=VAR_023415.
VARIANT 497 497 S -> R. {ECO:0000269|PubMed:15140763}.
/FTId=VAR_023416.
VARIANT 679 679 Y -> C (in PVNH7; dbSNP:rs879255599).
{ECO:0000269|PubMed:27694961}.
/FTId=VAR_077880.
VARIANT 694 694 Q -> H (in PVNH7; increased degradation;
changed function in regulation of TOR
signaling; dbSNP:rs879255598).
{ECO:0000269|PubMed:27694961}.
/FTId=VAR_077881.
VARIANT 893 893 E -> K (in PVNH7; increased degradation;
changed function in regulation of TOR
signaling; dbSNP:rs879255597).
{ECO:0000269|PubMed:27694961}.
/FTId=VAR_077882.
VARIANT 897 897 R -> Q (in PVNH7; increased degradation;
changed function in regulation of TOR
signaling; dbSNP:rs879255596).
{ECO:0000269|PubMed:27694961}.
/FTId=VAR_077883.
MUTAGEN 448 448 S->A: Abolishes interaction with 1433F.
{ECO:0000269|PubMed:15677482}.
MUTAGEN 942 942 C->S: Abolishes activity. No effect on
USP36 protein levels.
{ECO:0000269|PubMed:15217910,
ECO:0000269|PubMed:27445338}.
CONFLICT 52 52 A -> P (in Ref. 3; AAM76729/AAM76730).
{ECO:0000305}.
CONFLICT 188 188 E -> K (in Ref. 2; AAP75706).
{ECO:0000305}.
STRAND 9 11 {ECO:0000244|PDB:2NSQ}.
TURN 16 18 {ECO:0000244|PDB:2NSQ}.
STRAND 20 31 {ECO:0000244|PDB:2NSQ}.
STRAND 43 51 {ECO:0000244|PDB:2NSQ}.
TURN 52 55 {ECO:0000244|PDB:2NSQ}.
STRAND 56 62 {ECO:0000244|PDB:2NSQ}.
STRAND 73 82 {ECO:0000244|PDB:2NSQ}.
TURN 84 86 {ECO:0000244|PDB:2NSQ}.
STRAND 87 95 {ECO:0000244|PDB:2NSQ}.
STRAND 98 100 {ECO:0000244|PDB:2NSQ}.
STRAND 103 111 {ECO:0000244|PDB:2NSQ}.
STRAND 129 132 {ECO:0000244|PDB:2NSQ}.
STRAND 145 152 {ECO:0000244|PDB:2NSQ}.
STRAND 391 396 {ECO:0000244|PDB:2LB2}.
TURN 397 399 {ECO:0000244|PDB:2LB2}.
STRAND 400 405 {ECO:0000244|PDB:2LB2}.
TURN 406 409 {ECO:0000244|PDB:2LB2}.
STRAND 410 414 {ECO:0000244|PDB:2LB2}.
HELIX 417 419 {ECO:0000244|PDB:2LB2}.
STRAND 503 508 {ECO:0000244|PDB:2LAJ}.
TURN 509 511 {ECO:0000244|PDB:2LAJ}.
STRAND 512 517 {ECO:0000244|PDB:2LAJ}.
TURN 518 521 {ECO:0000244|PDB:2LAJ}.
STRAND 522 526 {ECO:0000244|PDB:2LAJ}.
HELIX 528 534 {ECO:0000244|PDB:2LAJ}.
HELIX 594 607 {ECO:0000244|PDB:2ONI}.
STRAND 612 614 {ECO:0000244|PDB:2ONI}.
STRAND 616 622 {ECO:0000244|PDB:2ONI}.
HELIX 624 626 {ECO:0000244|PDB:2ONI}.
HELIX 627 637 {ECO:0000244|PDB:2ONI}.
HELIX 641 645 {ECO:0000244|PDB:2ONI}.
STRAND 646 652 {ECO:0000244|PDB:2ONI}.
STRAND 653 655 {ECO:0000244|PDB:3JVZ}.
HELIX 660 675 {ECO:0000244|PDB:2ONI}.
HELIX 678 680 {ECO:0000244|PDB:2ONI}.
STRAND 681 687 {ECO:0000244|PDB:2ONI}.
TURN 688 690 {ECO:0000244|PDB:3JW0}.
STRAND 693 695 {ECO:0000244|PDB:2ONI}.
HELIX 699 702 {ECO:0000244|PDB:2ONI}.
HELIX 706 723 {ECO:0000244|PDB:2ONI}.
STRAND 728 731 {ECO:0000244|PDB:3JW0}.
HELIX 733 739 {ECO:0000244|PDB:2ONI}.
HELIX 746 749 {ECO:0000244|PDB:2ONI}.
TURN 750 752 {ECO:0000244|PDB:2ONI}.
HELIX 754 765 {ECO:0000244|PDB:2ONI}.
HELIX 769 771 {ECO:0000244|PDB:2ONI}.
STRAND 774 781 {ECO:0000244|PDB:2ONI}.
STRAND 784 791 {ECO:0000244|PDB:2ONI}.
HELIX 794 796 {ECO:0000244|PDB:2ONI}.
TURN 801 803 {ECO:0000244|PDB:2ONI}.
HELIX 804 816 {ECO:0000244|PDB:2ONI}.
TURN 817 819 {ECO:0000244|PDB:2ONI}.
HELIX 821 834 {ECO:0000244|PDB:2ONI}.
HELIX 837 840 {ECO:0000244|PDB:2ONI}.
HELIX 845 853 {ECO:0000244|PDB:2ONI}.
HELIX 860 865 {ECO:0000244|PDB:2ONI}.
STRAND 868 870 {ECO:0000244|PDB:2ONI}.
HELIX 878 889 {ECO:0000244|PDB:2ONI}.
HELIX 892 903 {ECO:0000244|PDB:2ONI}.
HELIX 913 915 {ECO:0000244|PDB:2ONI}.
STRAND 919 922 {ECO:0000244|PDB:5HPK}.
STRAND 926 929 {ECO:0000244|PDB:2ONI}.
STRAND 933 935 {ECO:0000244|PDB:3JW0}.
STRAND 938 940 {ECO:0000244|PDB:2ONI}.
HELIX 941 943 {ECO:0000244|PDB:2ONI}.
STRAND 945 948 {ECO:0000244|PDB:2ONI}.
HELIX 954 965 {ECO:0000244|PDB:2ONI}.
SEQUENCE 975 AA; 111932 MW; 2C958625B4A1AB3F CRC64;
MATGLGEPVY GLSEDEGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY VADENRELAL
VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT RDDFLGQVDV PLSHLPTEDP
TMERPYTFKD FLLRPRSHKS RVKGFLRLKM AYMPKNGGQD EENSDQRDDM EHGWEVVDSN
DSASQHQEEL PPPPLPPGWE EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS SESDNNIRQI
NQEAAHRRFR SRRHISEDLE PEPSEGGDVP EPWETISEEV NIAGDSLGLA LPPPPASPGS
RTSPQELSEE LSRRLQITPD SNGEQFSSLI QREPSSRLRS CSVTDAVAEQ GHLPPPSAPA
GRARSSTVTG GEEPTPSVAY VHTTPGLPSG WEERKDAKGR TYYVNHNNRT TTWTRPIMQL
AEDGASGSAT NSNNHLIEPQ IRRPRSLSSP TVTLSAPLEG AKDSPVRRAV KDTLSNPQSP
QPSPYNSPKP QHKVTQSFLP PGWEMRIAPN GRPFFIDHNT KTTTWEDPRL KFPVHMRSKT
SLNPNDLGPL PPGWEERIHL DGRTFYIDHN SKITQWEDPR LQNPAITGPA VPYSREFKQK
YDYFRKKLKK PADIPNRFEM KLHRNNIFEE SYRRIMSVKR PDVLKARLWI EFESEKGLDY
GGVAREWFFL LSKEMFNPYY GLFEYSATDN YTLQINPNSG LCNEDHLSYF TFIGRVAGLA
VFHGKLLDGF FIRPFYKMML GKQITLNDME SVDSEYYNSL KWILENDPTE LDLMFCIDEE
NFGQTYQVDL KPNGSEIMVT NENKREYIDL VIQWRFVNRV QKQMNAFLEG FTELLPIDLI
KIFDENELEL LMCGLGDVDV NDWRQHSIYK NGYCPNHPVI QWFWKAVLLM DAEKRIRLLQ
FVTGTSRVPM NGFAELYGSN GPQLFTIEQW GSPEKLPRAH TCFNRLDLPP YETFEDLREK
LLMAVENAQG FEGVD


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