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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.
29-SEP-2021, entry version 191.
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; DOI=10.1046/j.1471-4159.2003.01937.x;
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]
INTERACTION WITH PRRG4.
PubMed=23873930; DOI=10.1074/jbc.m113.484683;
Yazicioglu M.N., Monaldini L., Chu K., Khazi F.R., Murphy S.L., Huang H.,
Margaritis P., High K.A.;
"Cellular localization and characterization of cytosolic binding partners
for Gla domain-containing proteins PRRG4 and PRRG2.";
J. Biol. Chem. 288:25908-25914(2013).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
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).
[49]
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:
Reaction=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.;
EC=2.3.2.26;
-!- ACTIVITY 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). Interacts with PRRG4 (via
cytoplasmic domain) (PubMed:23873930). {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:23873930,
ECO:0000269|PubMed:26363003, ECO:0000269|PubMed:27445338}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus LMP2A.
{ECO:0000269|PubMed:11046148}.
-!- INTERACTION:
Q96PU5; Q15038: DAZAP2; NbExp=3; IntAct=EBI-717962, EBI-724310;
Q96PU5; P49281: SLC11A2; NbExp=2; IntAct=EBI-717962, EBI-4319335;
Q96PU5-2; Q96B67: ARRDC3; NbExp=5; IntAct=EBI-6955201, EBI-2875665;
Q96PU5-2; Q15038: DAZAP2; NbExp=3; IntAct=EBI-6955201, EBI-724310;
Q96PU5-5; 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;
Name=3; Synonyms=NEDD4Le;
IsoId=Q96PU5-3; Sequence=VSP_015447;
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 variants
affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA23711.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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]
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; -.
BMRB; Q96PU5; -.
SMR; Q96PU5; -.
BioGRID; 116915; 241.
CORUM; Q96PU5; -.
DIP; DIP-41935N; -.
IntAct; Q96PU5; 48.
MINT; Q96PU5; -.
STRING; 9606.ENSP00000383199; -.
GlyGen; Q96PU5; 2 sites, 2 O-linked glycans (2 sites).
iPTMnet; Q96PU5; -.
PhosphoSitePlus; Q96PU5; -.
BioMuta; NEDD4L; -.
DMDM; 73921204; -.
EPD; Q96PU5; -.
jPOST; Q96PU5; -.
MassIVE; Q96PU5; -.
MaxQB; Q96PU5; -.
PaxDb; Q96PU5; -.
PeptideAtlas; Q96PU5; -.
PRIDE; Q96PU5; -.
ProteomicsDB; 77752; -. [Q96PU5-1]
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]
Antibodypedia; 5421; 258 antibodies.
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]
Ensembl; ENST00000674517; ENSP00000501665; ENSG00000049759. [Q96PU5-9]
Ensembl; ENST00000675502; ENSP00000502428; ENSG00000049759. [Q96PU5-9]
Ensembl; ENST00000675801; ENSP00000502688; ENSG00000049759. [Q96PU5-9]
Ensembl; ENST00000675865; ENSP00000502003; ENSG00000049759. [Q96PU5-9]
Ensembl; ENST00000676226; ENSP00000502325; ENSG00000049759. [Q96PU5-9]
GeneID; 23327; -.
KEGG; hsa:23327; -.
UCSC; uc002lgx.4; human. [Q96PU5-1]
CTD; 23327; -.
DisGeNET; 23327; -.
GeneCards; NEDD4L; -.
HGNC; HGNC:7728; NEDD4L.
HPA; ENSG00000049759; Low tissue specificity.
MalaCards; NEDD4L; -.
MIM; 606384; gene.
MIM; 617201; phenotype.
neXtProt; NX_Q96PU5; -.
OpenTargets; ENSG00000049759; -.
Orphanet; 98892; Periventricular nodular heterotopia.
PharmGKB; PA31534; -.
VEuPathDB; HostDB:ENSG00000049759; -.
eggNOG; KOG0940; Eukaryota.
GeneTree; ENSGT00940000156873; -.
InParanoid; Q96PU5; -.
OMA; VRDWREN; -.
OrthoDB; 271539at2759; -.
PhylomeDB; Q96PU5; -.
TreeFam; TF323658; -.
BioCyc; MetaCyc:ENSG00000049759-MONOMER; -.
BRENDA; 2.3.2.26; 2681.
BRENDA; 2.3.2.B8; 2681.
PathwayCommons; Q96PU5; -.
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; -.
BioGRID-ORCS; 23327; 10 hits in 1057 CRISPR screens.
ChiTaRS; NEDD4L; human.
EvolutionaryTrace; Q96PU5; -.
GeneWiki; NEDD4L; -.
GenomeRNAi; 23327; -.
Pharos; Q96PU5; Tbio.
PRO; PR:Q96PU5; -.
Proteomes; UP000005640; Chromosome 18.
RNAct; Q96PU5; protein.
Bgee; ENSG00000049759; Expressed in forebrain and 226 other tissues.
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:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
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; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
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:0030104; P:water homeostasis; NAS:UniProtKB.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 4.
DisProt; DP02292; -.
Gene3D; 2.60.40.150; -; 1.
IDEAL; IID00114; -.
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; SSF49562; SSF49562; 1.
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; Cytoplasm;
Differentiation; Direct protein sequencing; Endosome; Golgi apparatus;
Host-virus interaction; Phosphoprotein; Reference proteome; Repeat;
Transferase; Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1
/note="Removed"
/evidence="ECO:0007744|PubMed:22814378"
CHAIN 2..975
/note="E3 ubiquitin-protein ligase NEDD4-like"
/id="PRO_0000120323"
DOMAIN 4..126
/note="C2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
DOMAIN 193..226
/note="WW 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 385..418
/note="WW 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 497..530
/note="WW 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 548..581
/note="WW 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 640..974
/note="HECT"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
REGION 178..202
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 244..272
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 285..312
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 349..393
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 424..496
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 244..261
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 424..455
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 942
/note="Glycyl thioester intermediate"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0007744|PubMed:22814378"
MOD_RES 312
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 318
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163"
MOD_RES 342
/note="Phosphoserine; by WNK1 and WNK4"
/evidence="ECO:0000269|PubMed:15328345,
ECO:0000269|PubMed:20525693, ECO:0007744|PubMed:18669648"
MOD_RES 367
/note="Phosphothreonine; by SGK1"
/evidence="ECO:0000305|PubMed:15328345"
MOD_RES 446
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332"
MOD_RES 448
/note="Phosphoserine; by PKA and SGK1"
/evidence="ECO:0000269|PubMed:15328345,
ECO:0000269|PubMed:15677482, ECO:0007744|PubMed:23186163"
MOD_RES 449
/note="Phosphoserine; by WNK1 and WNK4"
/evidence="ECO:0000269|PubMed:20525693,
ECO:0007744|PubMed:18669648"
MOD_RES 464
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648"
MOD_RES 475
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 479
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 483
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 487
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:21406692"
VAR_SEQ 1..121
/note="Missing (in isoform 4 and isoform 8)"
/evidence="ECO:0000303|PubMed:11840194,
ECO:0000303|PubMed:14615060, ECO:0000303|PubMed:9455477,
ECO:0000303|Ref.5"
/id="VSP_015444"
VAR_SEQ 1..16
/note="MATGLGEPVYGLSEDE -> MRRLAFEQ (in isoform 6 and
isoform 7)"
/evidence="ECO:0000303|PubMed:14615060"
/id="VSP_015446"
VAR_SEQ 356..459
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_015447"
VAR_SEQ 356..419
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_015448"
VAR_SEQ 356..375
/note="Missing (in isoform 5, isoform 6 and isoform 8)"
/evidence="ECO:0000303|PubMed:14615060,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9455477,
ECO:0000303|Ref.4, ECO:0000303|Ref.5"
/id="VSP_043848"
VARIANT 355
/note="P -> L (impaired ability to inhibit SCNN;
dbSNP:rs767136811)"
/evidence="ECO:0000269|PubMed:15140763"
/id="VAR_023415"
VARIANT 497
/note="S -> R"
/evidence="ECO:0000269|PubMed:15140763"
/id="VAR_023416"
VARIANT 679
/note="Y -> C (in PVNH7; dbSNP:rs879255599)"
/evidence="ECO:0000269|PubMed:27694961"
/id="VAR_077880"
VARIANT 694
/note="Q -> H (in PVNH7; increased degradation; changed
function in regulation of TOR signaling;
dbSNP:rs879255598)"
/evidence="ECO:0000269|PubMed:27694961"
/id="VAR_077881"
VARIANT 893
/note="E -> K (in PVNH7; increased degradation; changed
function in regulation of TOR signaling;
dbSNP:rs879255597)"
/evidence="ECO:0000269|PubMed:27694961"
/id="VAR_077882"
VARIANT 897
/note="R -> Q (in PVNH7; increased degradation; changed
function in regulation of TOR signaling;
dbSNP:rs879255596)"
/evidence="ECO:0000269|PubMed:27694961"
/id="VAR_077883"
MUTAGEN 448
/note="S->A: Abolishes interaction with 1433F."
/evidence="ECO:0000269|PubMed:15677482"
MUTAGEN 942
/note="C->S: Abolishes activity. No effect on USP36 protein
levels."
/evidence="ECO:0000269|PubMed:15217910,
ECO:0000269|PubMed:27445338"
CONFLICT 52
/note="A -> P (in Ref. 3; AAM76729/AAM76730)"
/evidence="ECO:0000305"
CONFLICT 188
/note="E -> K (in Ref. 2; AAP75706)"
/evidence="ECO:0000305"
STRAND 9..11
/evidence="ECO:0007829|PDB:2NSQ"
TURN 16..18
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 20..31
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 43..51
/evidence="ECO:0007829|PDB:2NSQ"
TURN 52..55
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 56..62
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 73..82
/evidence="ECO:0007829|PDB:2NSQ"
TURN 84..86
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 87..95
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 98..100
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 103..111
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 129..132
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 145..152
/evidence="ECO:0007829|PDB:2NSQ"
STRAND 391..396
/evidence="ECO:0007829|PDB:2LB2"
TURN 397..399
/evidence="ECO:0007829|PDB:2LB2"
STRAND 400..405
/evidence="ECO:0007829|PDB:2LB2"
TURN 406..409
/evidence="ECO:0007829|PDB:2LB2"
STRAND 410..414
/evidence="ECO:0007829|PDB:2LB2"
HELIX 417..419
/evidence="ECO:0007829|PDB:2LB2"
STRAND 503..508
/evidence="ECO:0007829|PDB:2LAJ"
TURN 509..511
/evidence="ECO:0007829|PDB:2LAJ"
STRAND 512..517
/evidence="ECO:0007829|PDB:2LAJ"
TURN 518..521
/evidence="ECO:0007829|PDB:2LAJ"
STRAND 522..526
/evidence="ECO:0007829|PDB:2LAJ"
HELIX 528..534
/evidence="ECO:0007829|PDB:2LAJ"
HELIX 594..607
/evidence="ECO:0007829|PDB:2ONI"
STRAND 612..614
/evidence="ECO:0007829|PDB:2ONI"
STRAND 616..622
/evidence="ECO:0007829|PDB:2ONI"
HELIX 624..626
/evidence="ECO:0007829|PDB:2ONI"
HELIX 627..637
/evidence="ECO:0007829|PDB:2ONI"
HELIX 641..645
/evidence="ECO:0007829|PDB:2ONI"
STRAND 646..652
/evidence="ECO:0007829|PDB:2ONI"
STRAND 653..655
/evidence="ECO:0007829|PDB:3JVZ"
HELIX 660..675
/evidence="ECO:0007829|PDB:2ONI"
HELIX 678..680
/evidence="ECO:0007829|PDB:2ONI"
STRAND 681..687
/evidence="ECO:0007829|PDB:2ONI"
TURN 688..690
/evidence="ECO:0007829|PDB:3JW0"
STRAND 693..695
/evidence="ECO:0007829|PDB:2ONI"
HELIX 699..702
/evidence="ECO:0007829|PDB:2ONI"
HELIX 706..723
/evidence="ECO:0007829|PDB:2ONI"
STRAND 728..731
/evidence="ECO:0007829|PDB:3JW0"
HELIX 733..739
/evidence="ECO:0007829|PDB:2ONI"
HELIX 746..749
/evidence="ECO:0007829|PDB:2ONI"
TURN 750..752
/evidence="ECO:0007829|PDB:2ONI"
HELIX 754..765
/evidence="ECO:0007829|PDB:2ONI"
HELIX 769..771
/evidence="ECO:0007829|PDB:2ONI"
STRAND 774..781
/evidence="ECO:0007829|PDB:2ONI"
STRAND 784..791
/evidence="ECO:0007829|PDB:2ONI"
HELIX 794..796
/evidence="ECO:0007829|PDB:2ONI"
TURN 801..803
/evidence="ECO:0007829|PDB:2ONI"
HELIX 804..816
/evidence="ECO:0007829|PDB:2ONI"
TURN 817..819
/evidence="ECO:0007829|PDB:2ONI"
HELIX 821..834
/evidence="ECO:0007829|PDB:2ONI"
HELIX 837..840
/evidence="ECO:0007829|PDB:2ONI"
HELIX 845..853
/evidence="ECO:0007829|PDB:2ONI"
HELIX 860..865
/evidence="ECO:0007829|PDB:2ONI"
STRAND 868..870
/evidence="ECO:0007829|PDB:2ONI"
HELIX 878..889
/evidence="ECO:0007829|PDB:2ONI"
HELIX 892..903
/evidence="ECO:0007829|PDB:2ONI"
HELIX 913..915
/evidence="ECO:0007829|PDB:2ONI"
STRAND 919..922
/evidence="ECO:0007829|PDB:5HPK"
STRAND 926..929
/evidence="ECO:0007829|PDB:2ONI"
STRAND 933..935
/evidence="ECO:0007829|PDB:3JW0"
STRAND 938..940
/evidence="ECO:0007829|PDB:2ONI"
HELIX 941..943
/evidence="ECO:0007829|PDB:2ONI"
STRAND 945..948
/evidence="ECO:0007829|PDB:2ONI"
HELIX 954..965
/evidence="ECO:0007829|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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Pathways :
WP960: Proteasome Degradation
WP1079: Proteasome Degradation
WP2005: Muscle cell TarBase
WP2199: Seed Development
WP158: Proteasome Degradation
WP519: Proteasome Degradation
WP2004: Lymphocyte TarBase
WP281: Proteasome Degradation
WP1196: Proteasome Degradation
WP841: Proteasome Degradation
WP470: Proteasome Degradation
WP183: Proteasome Degradation
WP2292: Chemokine signaling pathway
WP2002: Epithelium TarBase
WP2006: Squamous cell TarBase
WP267: Proteasome Degradation
WP302: Proteasome Degradation
WP211: BMP signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1678: Nucleotide excision repair
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1625: Base excision repair
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP1714: Tyrosine metabolism

Related Genes :
[NEDD4L KIAA0439 NEDL3] E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase NED4L) (NEDD4.2) (Nedd4-2)
[Nedd4l Kiaa0439 Nedd4b] E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase NED4L) (NEDD4.2) (Nedd4-2)
[NEDD4L] E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase NED4L)
[NDFIP2 KIAA1165 N4WBP5A] NEDD4 family-interacting protein 2 (NEDD4 WW domain-binding protein 5A) (Putative MAPK-activating protein PM04/PM05/PM06/PM07) (Putative NF-kappa-B-activating protein 413)
[ITCH] E3 ubiquitin-protein ligase Itchy homolog (Itch) (EC 2.3.2.26) (Atrophin-1-interacting protein 4) (AIP4) (HECT-type E3 ubiquitin transferase Itchy homolog) (NFE2-associated polypeptide 1) (NAPP1)
[Itch] E3 ubiquitin-protein ligase Itchy (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase Itchy homolog)
[NDFIP1 N4WBP5 PSEC0192 PSEC0223] NEDD4 family-interacting protein 1 (Breast cancer-associated protein SGA-1M) (NEDD4 WW domain-binding protein 5) (Putative MAPK-activating protein PM13) (Putative NF-kappa-B-activating protein 164) (Putative NFKB and MAPK-activating protein)
[RSP5 MDP1 NPI1 YER125W SYGP-ORF41] E3 ubiquitin-protein ligase RSP5 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase RSP5) (Reverses SPT-phenotype protein 5)
[hulA AN1339] E3 ubiquitin-protein ligase RSP5 (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase RSP5)
[hulA An08g01060] Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA)
[hulA ATEG_08573] Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA)
[hulA NFIA_016110] Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase RSP5)
[hulA ACLA_026000] Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA)
[hulA AFLA_021670] Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA)
[hulA AO090012000923] Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA)
[RSP5 CTHT_0046110] E3 ubiquitin-protein ligase RSP5 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase RSP5)
[Rnf11 N4wbp2 Sid1669] RING finger protein 11 (NEDD4 WW domain-binding protein 2) (Sid 1669)
[N4bp1 Kiaa0615] NEDD4-binding protein 1 (N4BP1) (EC 3.1.-.-)
[Litaf N4wbp3 Tbx1] Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog (LPS-induced TNF-alpha factor homolog) (Estrogen-enhanced transcript protein) (mEET) (LITAF-like protein) (NEDD4 WW domain-binding protein 3)
[N4BP1 KIAA0615] NEDD4-binding protein 1 (N4BP1) (EC 3.1.-.-)
[UCRNP2_5757] E3 ubiquitin-protein ligase (EC 2.3.2.26)
[CC84DRAFT_1163391] E3 ubiquitin-protein ligase (EC 2.3.2.26)
[TRIREDRAFT_57334] HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (Fragment)
[N4BP2 B3BP KIAA1413] NEDD4-binding protein 2 (N4BP2) (EC 3.-.-.-) (BCL-3-binding protein)
[SETTUDRAFT_30757] E3 ubiquitin-protein ligase (EC 2.3.2.26)
[GLRG_10163] E3 ubiquitin-protein ligase (EC 2.3.2.26)
[UCDDS831_g08210] HECT-type E3 ubiquitin transferase (EC 2.3.2.26)
[MAJ_07043] HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (Fragment)
[UCDDA912_g02017] HECT-type E3 ubiquitin transferase (EC 2.3.2.26)
[UCRPA7_4162] HECT-type E3 ubiquitin transferase (EC 2.3.2.26)

Bibliography :