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E3 ubiquitin-protein ligase NEDD4 (EC 2.3.2.26) (Cell proliferation-inducing gene 53 protein) (HECT-type E3 ubiquitin transferase NEDD4) (Neural precursor cell expressed developmentally down-regulated protein 4) (NEDD-4)

 NEDD4_HUMAN             Reviewed;        1319 AA.
P46934; A1KY35; A6ND72; A7MD29; B4E2R7; B7ZM59; B7ZM60; B9EGN5;
D6RF89;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
30-AUG-2017, entry version 183.
RecName: Full=E3 ubiquitin-protein ligase NEDD4;
EC=2.3.2.26 {ECO:0000269|PubMed:17218260, ECO:0000269|PubMed:21399620};
AltName: Full=Cell proliferation-inducing gene 53 protein;
AltName: Full=HECT-type E3 ubiquitin transferase NEDD4;
AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 4;
Short=NEDD-4;
Name=NEDD4; Synonyms=KIAA0093, NEDD4-1; ORFNames=PIG53;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS
SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PTEN.
PubMed=17218260; DOI=10.1016/j.cell.2006.11.039;
Wang X., Trotman L.C., Koppie T., Alimonti A., Chen Z., Gao Z.,
Wang J., Erdjument-Bromage H., Tempst P., Cordon-Cardo C.,
Pandolfi P.P., Jiang X.;
"NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN.";
Cell 128:129-139(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
GLN-679 AND SER-698.
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
GLN-679 AND SER-698.
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
GLN-679 AND SER-698.
Kim J.W.;
"Identification of a human cell proliferation inducing gene.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Adipose tissue;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLN-679
AND SER-698.
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[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] (ISOFORMS 1; 2 AND 4), AND
VARIANTS GLN-679 AND SER-698.
TISSUE=Brain, and Testis;
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]
FUNCTION, AND INTERACTION WITH RAPGEF2.
PubMed=11598133; DOI=10.1074/jbc.M108373200;
Pham N., Rotin D.;
"Nedd4 regulates ubiquitination and stability of the guanine-
nucleotide exchange factor CNrasGEF.";
J. Biol. Chem. 276:46995-47003(2001).
[10]
INTERACTION WITH HTLV-1 MATRIX PROTEIN P19.
PubMed=14581525; DOI=10.1128/JVI.77.22.11882-11895.2003;
Bouamr F., Melillo J.A., Wang M.Q., Nagashima K., de Los Santos M.,
Rein A., Goff S.P.;
"PPPYVEPTAP motif is the late domain of human T-cell leukemia virus
type 1 Gag and mediates its functional interaction with cellular
proteins Nedd4 and Tsg101.";
J. Virol. 77:11882-11895(2003).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, 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).
[13]
FUNCTION, AND INTERACTION WITH ISG15.
PubMed=18305167; DOI=10.1073/pnas.0710629105;
Okumura A., Pitha P.M., Harty R.N.;
"ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner
by blocking Nedd4 ligase activity.";
Proc. Natl. Acad. Sci. U.S.A. 105:3974-3979(2008).
[14]
FUNCTION, AND INTERACTION WITH PTEN.
PubMed=18562292; DOI=10.1073/pnas.0803233105;
Fouladkou F., Landry T., Kawabe H., Neeb A., Lu C., Brose N.,
Stambolic V., Rotin D.;
"The ubiquitin ligase Nedd4-1 is dispensable for the regulation of
PTEN stability and localization.";
Proc. Natl. Acad. Sci. U.S.A. 105:8585-8590(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, 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).
[16]
INTERACTION WITH ARRDC3.
PubMed=20559325; DOI=10.1038/embor.2010.80;
Nabhan J.F., Pan H., Lu Q.;
"Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to
mediate ubiquitination of the beta2-adrenergic receptor.";
EMBO Rep. 11:605-611(2010).
[17]
FUNCTION, AND 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).
[18]
INTERACTION WITH RAP2A AND TNIK.
PubMed=20159449; DOI=10.1016/j.neuron.2010.01.007;
Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M.,
Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E.,
Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O.,
Rhee J., Brose N.;
"Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite
development.";
Neuron 65:358-372(2010).
[19]
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).
[20]
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).
[21]
INTERACTION WITH FGFR1, AND FUNCTION IN UBIQUITINATION OF FGFR1.
PubMed=21765395; DOI=10.1038/emboj.2011.234;
Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F.,
Dirks P., Ciruna B., Rotin D.;
"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its
endocytosis and function.";
EMBO J. 30:3259-3273(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 4), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 4), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
INTERACTION WITH OTUD7B.
PubMed=22179831; DOI=10.1038/onc.2011.587;
Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F.,
Aulmann S., Ben-Chetrit N., Pines G., Navon R., Crosetto N.,
Kostler W., Carvalho S., Lavi S., Schmitt F., Dikic I., Yakhini Z.,
Sinn P., Mills G.B., Yarden Y.;
"Deubiquitination of EGFR by Cezanne-1 contributes to cancer
progression.";
Oncogene 31:4599-4608(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742, 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).
[25]
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).
[26]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-152 (ISOFORM 4).
Structural genomics consortium (SGC);
"Crystal structure of the C2 domain of the E3 ubiquitin-protein ligase
Nedd4.";
Submitted (OCT-2007) to the PDB data bank.
[27]
STRUCTURE BY NMR OF 834-878.
Iglesias-Bexiga M.;
"Human NEDD4 3rd WW domain complex with ebola Zaire virus matrix
protein VP40 derived peptide.";
Submitted (OCT-2009) to the PDB data bank.
[28]
STRUCTURE BY NMR OF 834-878.
Iglesias-Bexiga M., Luque I., Macias M.;
"Human NEDD4 3rd WW domain complex with human T-cell leukemia virus
GAP-Pro polyprotein derived peptide.";
Submitted (OCT-2009) to the PDB data bank.
[29]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 938-1319 IN COMPLEX WITH
UBIQUITIN, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21399620; DOI=10.1038/embor.2011.21;
Maspero E., Mari S., Valentini E., Musacchio A., Fish A.,
Pasqualato S., Polo S.;
"Structure of the HECT:ubiquitin complex and its role in ubiquitin
chain elongation.";
EMBO Rep. 12:342-349(2011).
[30]
STRUCTURE BY NMR OF 838-877 IN COMPLEX WITH SCNN1A PEPTIDE, AND
INTERACTION WITH SCNN1A.
PubMed=23665454; DOI=10.1016/j.bbapap.2013.04.031;
Bobby R., Medini K., Neudecker P., Lee T.V., Brimble M.A.,
McDonald F.J., Lott J.S., Dingley A.J.;
"Structure and dynamics of human Nedd4-1 WW3 in complex with the
alphaENaC PY motif.";
Biochim. Biophys. Acta 1834:1632-1641(2013).
[31]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 938-1319 IN COMPLEX WITH
UBIQUITIN, FUNCTION, AND PATHWAY.
PubMed=23644597; DOI=10.1038/nsmb.2566;
Maspero E., Valentini E., Mari S., Cecatiello V., Soffientini P.,
Pasqualato S., Polo S.;
"Structure of a ubiquitin-loaded HECT ligase reveals the molecular
basis for catalytic priming.";
Nat. Struct. Mol. Biol. 20:696-701(2013).
[32]
X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 841-874 IN COMPLEX WITH WITH
ARRDC3 PEPTIDE, INTERACTION WITH ARRDC3, AND MUTAGENESIS OF TRP-795;
TRP-868 AND TRP-920.
PubMed=24379409; DOI=10.1074/jbc.M113.527473;
Qi S., O'Hayre M., Gutkind J.S., Hurley J.H.;
"Structural and biochemical basis for ubiquitin ligase recruitment by
arrestin-related domain-containing protein-3 (ARRDC3).";
J. Biol. Chem. 289:4743-4752(2014).
[33]
VARIANT [LARGE SCALE ANALYSIS] HIS-627.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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.
Specifically ubiquitinates 'Lys-63' in target proteins
(PubMed:23644597). Involved in the pathway leading to the
degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase
activity. Monoubiquitinates IGF1R at multiple sites, thus leading
to receptor internalization and degradation in lysosomes.
Ubiquitinates FGFR1, leading to receptor internalization and
degradation in lysosomes. Promotes ubiquitination of RAPGEF2.
According to PubMed:18562292 the direct link between NEDD4 and
PTEN regulation through polyubiquitination described in
PubMed:17218260 is questionable. Involved in ubiquitination of
ERBB4 intracellular domain E4ICD. Involved in the budding of many
viruses. Part of a signaling complex composed of NEDD4, RAP2A and
TNIK which regulates neuronal dendrite extension and arborization
during development. Ubiquitinates TNK2 and regulates EGF-induced
degradation of EGFR and TNF2. Involved in the ubiquitination of
ebola virus VP40 protein and this ubiquitination plays a role in
facilitating viral budding. Ubiquitinates BRAT1 and this
ubiquitination is enhanced in the presence of NDFIP1
(PubMed:25631046). {ECO:0000269|PubMed:11598133,
ECO:0000269|PubMed:17218260, ECO:0000269|PubMed:18305167,
ECO:0000269|PubMed:18562292, ECO:0000269|PubMed:20086093,
ECO:0000269|PubMed:21399620, ECO:0000269|PubMed:21765395,
ECO:0000269|PubMed:23644597, ECO:0000269|PubMed:25631046}.
-!- 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. {ECO:0000269|PubMed:17218260,
ECO:0000269|PubMed:21399620}.
-!- ENZYME REGULATION: Activated by NDFIP1- and NDFIP2-binding.
{ECO:0000250}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:23644597}.
-!- SUBUNIT: Interacts with UBE2D2. Binds SCNN1A, SCNN1B and SCNN1G.
Binds, in vitro, through the WW2 and WW3 domains, to neural
isoforms of ENAH that contain the PPSY motif. Interacts with
BEAN1, LITAF, RNF11, WBP1, WBP2, TMEPAI and PRRG2 (By similarity).
Interacts with NDFIP1 and NDFIP2; this interaction activates the
E3 ubiquitin-protein ligase and may induce its recruitment to
exosomes (By similarity). Interaction with PTEN is questionable
according to PubMed:18562292. Interacts with viral proteins that
contain a late- budding motif P-P-P-Y. This interaction is
essential for viral particle budding of a lot of retroviruses,
like HTLV-1 Gag and MLV Gag. Interacts (via C2 domain) with GRB10
(via SH2 domain). Interacts with ERBB4 (By similarity). Interacts
with TNIK; the interaction is direct, allows the TNIK-dependent
recruitment of RAP2A and its ubiquitination by NEDD4. Interacts
(via WW3 domain) with TNK2; EGF promotes this interaction.
Interacts (via WW3 domain) with FGFR1 (via C-terminus). Interacts
with OTUD7B. Interacts with ISG15. Interacts (via WW domain) with
RAPGEF2; this interaction leads to ubiquitination and degradation
via the proteasome pathway. Interacts (via WW domains) with ARRDC3
(via PPXY motifs) (PubMed:20559325, PubMed:24379409).
{ECO:0000250, ECO:0000269|PubMed:11598133,
ECO:0000269|PubMed:14581525, ECO:0000269|PubMed:17218260,
ECO:0000269|PubMed:18305167, ECO:0000269|PubMed:18562292,
ECO:0000269|PubMed:20086093, ECO:0000269|PubMed:20159449,
ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:21399620,
ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:22179831,
ECO:0000269|PubMed:23665454, ECO:0000269|PubMed:24379409}.
-!- INTERACTION:
P11362:FGFR1; NbExp=26; IntAct=EBI-726944, EBI-1028277;
O95166:GABARAP; NbExp=6; IntAct=EBI-726944, EBI-712001;
Q9H0R8:GABARAPL1; NbExp=6; IntAct=EBI-726944, EBI-746969;
P60520:GABARAPL2; NbExp=6; IntAct=EBI-726944, EBI-720116;
Q99732:LITAF; NbExp=4; IntAct=EBI-726944, EBI-725647;
P60484:PTEN; NbExp=4; IntAct=EBI-726944, EBI-696162;
Q9Y3C5:RNF11; NbExp=2; IntAct=EBI-726944, EBI-396669;
P51168:SCNN1B; NbExp=4; IntAct=EBI-726944, EBI-2547187;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Note=Recruited to the plasma membrane by GRB10. Once complexed
with GRB10 and IGF1R, follows IGF1R internalization, remaining
associated with early endosomes. Uncouples from IGF1R-containing
endosomes before the sorting of the receptor to the lysosomal
compartment (By similarity). May be recruited to exosomes by
NDFIP1. {ECO:0000250, ECO:0000269|PubMed:18819914}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P46934-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=P46934-2; Sequence=VSP_038259;
Note=No experimental confirmation available.;
Name=3;
IsoId=P46934-3; Sequence=VSP_038258;
Note=No experimental confirmation available.;
Name=4;
IsoId=P46934-4; Sequence=VSP_038256, VSP_038257;
Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
position 2. {ECO:0000244|PubMed:22223895};
-!- DOMAIN: The WW domains mediate interaction with LITAF, RNF11,
WBP1, WBP2, TMEPAI, NDFIP1 and PRRG2. {ECO:0000250}.
-!- PTM: Auto-ubiquitinated. {ECO:0000250}.
-!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
thioester formation.
-!- SEQUENCE CAUTION:
Sequence=BAA07655.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D42055; BAA07655.1; ALT_INIT; mRNA.
EMBL; AK304394; BAG65229.1; -; mRNA.
EMBL; AY550969; AAT52215.1; -; mRNA.
EMBL; AL832063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC009997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC039057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77495.1; -; Genomic_DNA.
EMBL; BC136605; AAI36606.1; -; mRNA.
EMBL; BC144284; AAI44285.1; -; mRNA.
EMBL; BC144285; AAI44286.1; -; mRNA.
EMBL; BC152452; AAI52453.1; -; mRNA.
EMBL; BC152562; AAI52563.1; -; mRNA.
CCDS; CCDS10156.1; -. [P46934-3]
CCDS; CCDS45265.1; -. [P46934-4]
CCDS; CCDS61643.1; -. [P46934-2]
CCDS; CCDS61644.1; -. [P46934-1]
RefSeq; NP_001271267.1; NM_001284338.1. [P46934-1]
RefSeq; NP_001271268.1; NM_001284339.1. [P46934-2]
RefSeq; NP_001271269.1; NM_001284340.1.
RefSeq; NP_001316141.1; NM_001329212.1.
RefSeq; NP_006145.2; NM_006154.3. [P46934-4]
RefSeq; NP_940682.2; NM_198400.3. [P46934-3]
UniGene; Hs.1565; -.
PDB; 2KPZ; NMR; -; A=834-878.
PDB; 2KQ0; NMR; -; A=834-878.
PDB; 2M3O; NMR; -; W=838-877.
PDB; 2XBB; X-ray; 2.68 A; A/B=938-1319.
PDB; 2XBF; X-ray; 2.50 A; A=938-1319.
PDB; 3B7Y; X-ray; 1.80 A; A/B=517-571.
PDB; 4BBN; X-ray; 2.51 A; A=938-1319.
PDB; 4BE8; X-ray; 3.00 A; A=938-1319.
PDB; 4N7F; X-ray; 1.10 A; A/B=841-874.
PDB; 4N7H; X-ray; 1.70 A; A=840-872.
PDB; 5AHT; NMR; -; A=838-877.
PDB; 5C7J; X-ray; 3.00 A; A/B=939-1319.
PDB; 5C91; X-ray; 2.44 A; A=938-1312.
PDBsum; 2KPZ; -.
PDBsum; 2KQ0; -.
PDBsum; 2M3O; -.
PDBsum; 2XBB; -.
PDBsum; 2XBF; -.
PDBsum; 3B7Y; -.
PDBsum; 4BBN; -.
PDBsum; 4BE8; -.
PDBsum; 4N7F; -.
PDBsum; 4N7H; -.
PDBsum; 5AHT; -.
PDBsum; 5C7J; -.
PDBsum; 5C91; -.
ProteinModelPortal; P46934; -.
SMR; P46934; -.
BioGrid; 110811; 312.
DIP; DIP-29815N; -.
ELM; P46934; -.
IntAct; P46934; 34.
MINT; MINT-86457; -.
STRING; 9606.ENSP00000345530; -.
ChEMBL; CHEMBL3621023; -.
TCDB; 8.A.30.1.2; the nedd4-family interacting protein-2 (nedd4) family.
iPTMnet; P46934; -.
PhosphoSitePlus; P46934; -.
BioMuta; NEDD4; -.
DMDM; 313104311; -.
EPD; P46934; -.
MaxQB; P46934; -.
PaxDb; P46934; -.
PeptideAtlas; P46934; -.
PRIDE; P46934; -.
DNASU; 4734; -.
Ensembl; ENST00000338963; ENSP00000345530; ENSG00000069869. [P46934-3]
Ensembl; ENST00000435532; ENSP00000410613; ENSG00000069869. [P46934-4]
Ensembl; ENST00000506154; ENSP00000422705; ENSG00000069869. [P46934-2]
Ensembl; ENST00000508342; ENSP00000424827; ENSG00000069869. [P46934-1]
GeneID; 4734; -.
KEGG; hsa:4734; -.
UCSC; uc002adi.5; human. [P46934-1]
CTD; 4734; -.
DisGeNET; 4734; -.
GeneCards; NEDD4; -.
HGNC; HGNC:7727; NEDD4.
HPA; CAB001991; -.
HPA; CAB072833; -.
HPA; HPA039883; -.
MIM; 602278; gene.
neXtProt; NX_P46934; -.
OpenTargets; ENSG00000069869; -.
PharmGKB; PA31533; -.
eggNOG; KOG0940; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00760000118966; -.
HOVERGEN; HBG004134; -.
InParanoid; P46934; -.
KO; K10591; -.
OMA; FNSLKWI; -.
OrthoDB; EOG091G0SS8; -.
PhylomeDB; P46934; -.
TreeFam; TF323658; -.
BRENDA; 2.3.2.B9; 2681.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-1253288; Downregulation of ERBB4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P46934; -.
UniPathway; UPA00143; -.
ChiTaRS; NEDD4; human.
EvolutionaryTrace; P46934; -.
GeneWiki; NEDD4; -.
GenomeRNAi; 4734; -.
PRO; PR:P46934; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000069869; -.
CleanEx; HS_NEDD4; -.
ExpressionAtlas; P46934; baseline and differential.
Genevisible; P46934; HS.
GO; GO:0016327; C:apicolateral plasma membrane; TAS:BHF-UCL.
GO; GO:0005938; C:cell cortex; IDA:BHF-UCL.
GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; ISS:BHF-UCL.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IDA:UniProtKB.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0050815; F:phosphoserine residue binding; ISS:BHF-UCL.
GO; GO:0050816; F:phosphothreonine residue binding; ISS:BHF-UCL.
GO; GO:0070064; F:proline-rich region binding; IMP:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0070063; F:RNA polymerase binding; IPI:BHF-UCL.
GO; GO:0019871; F:sodium channel inhibitor activity; IDA:BHF-UCL.
GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
GO; GO:0002250; P:adaptive immune response; IEA:Ensembl.
GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IMP:BHF-UCL.
GO; GO:0044111; P:development involved in symbiotic interaction; IMP:UniProtKB.
GO; GO:0003197; P:endocardial cushion development; IEA:Ensembl.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007041; P:lysosomal transport; IDA:UniProtKB.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0010766; P:negative regulation of sodium ion transport; IDA:UniProtKB.
GO; GO:0010768; P:negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; IMP:BHF-UCL.
GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IEP:BHF-UCL.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0046824; P:positive regulation of nucleocytoplasmic transport; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
GO; GO:0006622; P:protein targeting to lysosome; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0032801; P:receptor catabolic process; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; TAS:BHF-UCL.
GO; GO:0042110; P:T cell activation; IEA:Ensembl.
GO; GO:0019089; P:transmission of virus; IMP:BHF-UCL.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:BHF-UCL.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 4.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR000569; HECT_dom.
InterPro; IPR001202; WW_dom.
Pfam; PF00632; HECT; 1.
Pfam; PF00397; WW; 4.
SMART; SM00119; HECTc; 1.
SMART; SM00456; WW; 4.
SUPFAM; SSF51045; SSF51045; 4.
SUPFAM; SSF56204; SSF56204; 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; Cell membrane;
Complete proteome; Cytoplasm; Host-virus interaction; Membrane;
Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 1319 E3 ubiquitin-protein ligase NEDD4.
/FTId=PRO_0000120319.
DOMAIN 610 643 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 767 800 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 840 873 WW 3. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 892 925 WW 4. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 984 1318 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
REGION 578 981 Mediates interaction with TNIK.
{ECO:0000250}.
COMPBIAS 68 215 Ser-rich.
ACT_SITE 1286 1286 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000250|UniProtKB:Q62940}.
MOD_RES 648 648 Phosphothreonine.
{ECO:0000250|UniProtKB:P46935}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000250|UniProtKB:P46935}.
MOD_RES 742 742 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
VAR_SEQ 1 419 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7788527,
ECO:0000303|Ref.4}.
/FTId=VSP_038256.
VAR_SEQ 420 516 SACLPSSQNVDCQININGELERPHSQMNKNHGILRRSISLG
GAYPNISCLSSLKHNCSKGGPSQLLIKFASGNEGKVDNLSR
DSNRDCTNELSNSCK -> MATCAVEVFGLLEDEENSRIVR
VRVIAGIGLAKKDILGASDPYVRVTLYDPMNGVLTSVQTKT
IKKSLNPKWNEEILFRVHPQQHRLLFEVFDENRL (in
isoform 4). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7788527,
ECO:0000303|Ref.4}.
/FTId=VSP_038257.
VAR_SEQ 517 588 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_038258.
VAR_SEQ 589 604 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038259.
VARIANT 33 33 M -> V (in dbSNP:rs1912403).
/FTId=VAR_061985.
VARIANT 627 627 Y -> H (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036472.
VARIANT 679 679 R -> Q (in dbSNP:rs2303580).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16572171,
ECO:0000269|PubMed:7788527,
ECO:0000269|Ref.4}.
/FTId=VAR_047909.
VARIANT 698 698 N -> S (in dbSNP:rs2303579).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16572171,
ECO:0000269|PubMed:7788527,
ECO:0000269|Ref.4}.
/FTId=VAR_047910.
MUTAGEN 795 795 W->A: Abolishes interaction with ARRDC3;
when associated with A-868 and A-920.
{ECO:0000269|PubMed:24379409}.
MUTAGEN 868 868 W->A: Abolishes interaction with ARRDC3;
when associated with A-795 and A-920.
{ECO:0000269|PubMed:24379409}.
MUTAGEN 920 920 W->A: Abolishes interaction with ARRDC3;
when associated with A-795 and A-868.
{ECO:0000269|PubMed:24379409}.
CONFLICT 59 59 A -> T (in Ref. 5; AL832063).
{ECO:0000305}.
CONFLICT 407 407 N -> H (in Ref. 5; AL832063).
{ECO:0000305}.
CONFLICT 620 620 Q -> R (in Ref. 4; AAT52215 and 8;
AAI44285). {ECO:0000305}.
CONFLICT 863 863 T -> I (in Ref. 8; AAI36606/AAI44285).
{ECO:0000305}.
CONFLICT 1199 1199 L -> P (in Ref. 3; BAG65229).
{ECO:0000305}.
CONFLICT 1268 1268 S -> L (in Ref. 5; AL832063).
{ECO:0000305}.
STRAND 520 528 {ECO:0000244|PDB:3B7Y}.
STRAND 546 549 {ECO:0000244|PDB:3B7Y}.
STRAND 561 569 {ECO:0000244|PDB:3B7Y}.
STRAND 841 843 {ECO:0000244|PDB:5AHT}.
STRAND 846 850 {ECO:0000244|PDB:4N7F}.
TURN 852 854 {ECO:0000244|PDB:2KQ0}.
STRAND 856 860 {ECO:0000244|PDB:4N7F}.
TURN 861 864 {ECO:0000244|PDB:4N7F}.
STRAND 865 869 {ECO:0000244|PDB:4N7F}.
TURN 871 873 {ECO:0000244|PDB:2KQ0}.
HELIX 941 951 {ECO:0000244|PDB:5C91}.
STRAND 956 958 {ECO:0000244|PDB:5C91}.
STRAND 960 966 {ECO:0000244|PDB:5C91}.
HELIX 968 970 {ECO:0000244|PDB:5C91}.
HELIX 971 979 {ECO:0000244|PDB:5C91}.
HELIX 985 989 {ECO:0000244|PDB:5C91}.
STRAND 990 996 {ECO:0000244|PDB:5C91}.
HELIX 1004 1019 {ECO:0000244|PDB:5C91}.
HELIX 1022 1024 {ECO:0000244|PDB:5C91}.
STRAND 1025 1031 {ECO:0000244|PDB:5C91}.
STRAND 1037 1039 {ECO:0000244|PDB:5C91}.
HELIX 1043 1046 {ECO:0000244|PDB:5C91}.
HELIX 1050 1067 {ECO:0000244|PDB:5C91}.
STRAND 1071 1073 {ECO:0000244|PDB:2XBB}.
HELIX 1077 1083 {ECO:0000244|PDB:5C91}.
HELIX 1091 1096 {ECO:0000244|PDB:5C91}.
HELIX 1098 1109 {ECO:0000244|PDB:5C91}.
HELIX 1113 1115 {ECO:0000244|PDB:5C91}.
STRAND 1118 1125 {ECO:0000244|PDB:5C91}.
STRAND 1128 1135 {ECO:0000244|PDB:5C91}.
HELIX 1138 1140 {ECO:0000244|PDB:5C91}.
TURN 1145 1147 {ECO:0000244|PDB:5C91}.
HELIX 1148 1160 {ECO:0000244|PDB:5C91}.
HELIX 1162 1164 {ECO:0000244|PDB:5C91}.
HELIX 1165 1178 {ECO:0000244|PDB:5C91}.
HELIX 1181 1184 {ECO:0000244|PDB:5C91}.
HELIX 1189 1196 {ECO:0000244|PDB:5C91}.
HELIX 1204 1209 {ECO:0000244|PDB:5C91}.
STRAND 1212 1214 {ECO:0000244|PDB:5C91}.
STRAND 1219 1221 {ECO:0000244|PDB:2XBF}.
HELIX 1222 1233 {ECO:0000244|PDB:5C91}.
HELIX 1236 1247 {ECO:0000244|PDB:5C91}.
STRAND 1248 1250 {ECO:0000244|PDB:5C91}.
HELIX 1257 1259 {ECO:0000244|PDB:5C91}.
STRAND 1263 1266 {ECO:0000244|PDB:5C91}.
STRAND 1270 1272 {ECO:0000244|PDB:5C91}.
STRAND 1282 1284 {ECO:0000244|PDB:5C91}.
HELIX 1285 1287 {ECO:0000244|PDB:5C91}.
STRAND 1289 1291 {ECO:0000244|PDB:5C91}.
HELIX 1298 1309 {ECO:0000244|PDB:5C91}.
SEQUENCE 1319 AA; 149114 MW; D56EBBC50A34F13B CRC64;
MAQSLRLHFA ARRSNTYPLS ETSGDDLDSH VHMCFKRPTR ISTSNVVQMK LTPRQTALAP
LIKENVQSQE RSSVPSSENV NKKSSCLQIS LQPTRYSGYL QSSNVLADSD DASFTCILKD
GIYSSAVVDN ELNAVNDGHL VSSPAICSGS LSNFSTSDNG SYSSNGSDFG SCASITSGGS
YTNSVISDSS SYTFPPSDDT FLGGNLPSDS TSNRSVPNRN TTPCEIFSRS TSTDPFVQDD
LEHGLEIMKL PVSRNTKIPL KRYSSLVIFP RSPSTTRPTS PTSLCTLLSK GSYQTSHQFI
ISPSEIAHNE DGTSAKGFLS TAVNGLRLSK TICTPGEVRD IRPLHRKGSL QKKIVLSNNT
PRQTVCEKSS EGYSCVSVHF TQRKAATLDC ETTNGDCKPE MSEIKLNSDS EYIKLMHRTS
ACLPSSQNVD CQININGELE RPHSQMNKNH GILRRSISLG GAYPNISCLS SLKHNCSKGG
PSQLLIKFAS GNEGKVDNLS RDSNRDCTNE LSNSCKTRDD FLGQVDVPLY PLPTENPRLE
RPYTFKDFVL HPRSHKSRVK GYLRLKMTYL PKTSGSEDDN AEQAEELEPG WVVLDQPDAA
CHLQQQQEPS PLPPGWEERQ DILGRTYYVN HESRRTQWKR PTPQDNLTDA ENGNIQLQAQ
RAFTTRRQIS EETESVDNRE SSENWEIIRE DEATMYSNQA FPSPPPSSNL DVPTHLAEEL
NARLTIFGNS AVSQPASSSN HSSRRGSLQA YTFEEQPTLP VLLPTSSGLP PGWEEKQDER
GRSYYVDHNS RTTTWTKPTV QATVETSQLT SSQSSAGPQS QASTSDSGQQ VTQPSEIEQG
FLPKGWEVRH APNGRPFFID HNTKTTTWED PRLKIPAHLR GKTSLDTSND LGPLPPGWEE
RTHTDGRIFY INHNIKRTQW EDPRLENVAI TGPAVPYSRD YKRKYEFFRR KLKKQNDIPN
KFEMKLRRAT VLEDSYRRIM GVKRADFLKA RLWIEFDGEK GLDYGGVARE WFFLISKEMF
NPYYGLFEYS ATDNYTLQIN PNSGLCNEDH LSYFKFIGRV AGMAVYHGKL LDGFFIRPFY
KMMLHKPITL HDMESVDSEY YNSLRWILEN DPTELDLRFI IDEELFGQTH QHELKNGGSE
IVVTNKNKKE YIYLVIQWRF VNRIQKQMAA FKEGFFELIP QDLIKIFDEN ELELLMCGLG
DVDVNDWREH TKYKNGYSAN HQVIQWFWKA VLMMDSEKRI RLLQFVTGTS RVPMNGFAEL
YGSNGPQSFT VEQWGTPEKL PRAHTCFNRL DLPPYESFEE LWDKLQMAIE NTQGFDGVD


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EIAAB11921 Developmentally-regulated GTP-binding protein 1,DRG1,DRG-1,Homo sapiens,Human,NEDD3,NEDD-3,Neural precursor cell expressed developmentally down-regulated protein 3
EIAAB05382 Casp2,CASP-2,Caspase-2,Ich1,Mouse,Mus musculus,Nedd2,NEDD-2,Nedd-2,Neural precursor cell expressed developmentally down-regulated protein 2,Protease ICH-1
201-20-3716 NEDD4{neural precursor cell expressed, developmentally down-regulated 4}rabbit.pAb 0.2ml
EIAAB26860 Mouse,Mus musculus,Nedd1,NEDD-1,Nedd-1,Neural precursor cell expressed developmentally down-regulated protein 1,Protein NEDD1
CSB-EL015681RA Rat neural precursor cell expressed, developmentally down-regulated 4 (NEDD4) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB34913 60S ribosomal protein L10a,CSA-19,Homo sapiens,Human,NEDD6,NEDD-6,Neural precursor cell expressed developmentally down-regulated protein 6,RPL10A
ER-14-0476 Goat Anti-Neural Precursor Cell-expressed Developmentally Down-regulated protein4 (NEDD4), with HRP-conjugated secondary antibody 100
EIAAB05377 Casl,CAS-L,CRK-associated substrate-related protein,Enhancer of filamentation 1,mEF1,Mouse,Mus musculus,Nedd9,NEDD-9,Neural precursor cell expressed developmentally down-regulated protein 9,p105
CSB-EL015681HU Human neural precursor cell expressed, developmentally down-regulated 4 (NEDD4) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL015681MO Mouse neural precursor cell expressed, developmentally down-regulated 4 (NEDD4) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB26861 Bos taurus,Bovine,NEDD1,NEDD-1,Neural precursor cell expressed developmentally down-regulated protein 1,Protein NEDD1
EIAAB26862 Homo sapiens,Human,NEDD1,NEDD-1,Neural precursor cell expressed developmentally down-regulated protein 1,Protein NEDD1
EIAAB44908 Cell proliferation-inducing gene 50 protein,Homo sapiens,HSPC150,Human,PIG50,UBE2T,Ubiquitin carrier protein T,Ubiquitin-conjugating enzyme E2 T,Ubiquitin-protein ligase T
EIAAB05383 CASP2,CASP-2,Caspase-2,Homo sapiens,Human,ICH1,NEDD2,NEDD-2,Neural precursor cell expressed developmentally down-regulated protein 2,Protease ICH-1
20-272-190961 Caspase 2 - Mouse monoclonal [18E809] to Caspase 2; EC 3.4.22.55; CASP-2; ICH-1 protease; NEDD2 protein; Neural precursor cell expressed developmentally down-regulated protein 2; NEDD-2 Monoclonal 0.2 ml
20-272-191628 Caspase 2 - Mouse monoclonal [3G63] to Caspase 2; EC 3.4.22.55; CASP-2; ICH-1 protease; NEDD2 protein; Neural precursor cell expressed developmentally down-regulated protein 2; NEDD-2 Monoclonal 0.1 mg
20-272-191595 Caspase 2 - Mouse monoclonal [4i13] to Caspase 2; EC 3.4.22.55; CASP-2; ICH-1 protease; NEDD2 protein; Neural precursor cell expressed developmentally down-regulated protein 2; NEDD-2 Monoclonal 0.05 ml
EIAAB26859 E3 ubiquitin-protein ligase NEDD4-like,Kiaa0439,Mouse,Mus musculus,NEDD4.2,Nedd4-2,Nedd4b,Nedd4l


 

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