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

 NEDD4_MOUSE             Reviewed;         887 AA.
P46935; O08758; Q3UZI2; Q8BGB3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
20-JUN-2003, sequence version 3.
22-NOV-2017, entry version 179.
RecName: Full=E3 ubiquitin-protein ligase NEDD4;
EC=2.3.2.26 {ECO:0000250|UniProtKB:P46934};
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, Nedd-4, Nedd4-1, Nedd4a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=1378265; DOI=10.1016/0006-291X(92)91747-E;
Kumar S., Tomooka Y., Noda M.;
"Identification of a set of genes with developmentally down-regulated
expression in the mouse brain.";
Biochem. Biophys. Res. Commun. 185:1155-1161(1992).
[2]
SEQUENCE REVISION.
Kumar S.;
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
UBE2D2.
STRAIN=C57BL/6 X CBA;
PubMed=9182527; DOI=10.1074/jbc.272.24.15085;
Hatakeyama S., Jensen J.P., Weissman A.M.;
"Subcellular localization and ubiquitin-conjugating enzyme (E2)
interactions of mammalian HECT family ubiquitin protein ligases.";
J. Biol. Chem. 272:15085-15092(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[6]
INTERACTION WITH ENAH.
PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F.,
Russo T., Sudol M.;
"The WW domain of neural protein FE65 interacts with proline-rich
motifs in Mena, the mammalian homolog of Drosophila enabled.";
J. Biol. Chem. 272:32869-32877(1997).
[7]
INTERACTION WITH BEAN1; LITAF; RNF11; WBP1; WBP2; PMEPAI; NDFIP1 AND
PRRG2, AND DOMAINS.
TISSUE=Embryo;
PubMed=11042109; DOI=10.1042/bj3510557;
Jolliffe C.N., Harvey K.F., Haines B.P., Parasivam G., Kumar S.;
"Identification of multiple proteins expressed in murine embryos as
binding partners for the WW domains of the ubiquitin-protein ligase
Nedd4.";
Biochem. J. 351:557-565(2000).
[8]
INTERACTION WITH GRB10.
PubMed=12697834; DOI=10.1128/MCB.23.9.3363-3372.2003;
Vecchione A., Marchese A., Henry P., Rotin D., Morrione A.;
"The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and
stability of the insulin-like growth factor I receptor.";
Mol. Cell. Biol. 23:3363-3372(2003).
[9]
FUNCTION, INTERACTION WITH GRB10, AND MUTAGENESIS OF CYS-854.
PubMed=15060076; DOI=10.1074/jbc.M311802200;
Murdaca J., Treins C., Monthouel-Kartmann M.N., Pontier-Bres R.,
Kumar S., Van Obberghen E., Giorgetti-Peraldi S.;
"Grb10 prevents Nedd4-mediated vascular endothelial growth factor
receptor-2 degradation.";
J. Biol. Chem. 279:26754-26761(2004).
[10]
INTERACTION WITH MURINE LEUKEMIA VIRUS GAG POLYPROTEIN.
PubMed=15908698; DOI=10.1074/jbc.M413735200;
Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R.,
Bertrand E., Basyuk E.;
"Tsg101 and Alix interact with murine leukemia virus Gag and cooperate
with Nedd4 ubiquitin ligases during budding.";
J. Biol. Chem. 280:27004-27012(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
FUNCTION, INTERACTION WITH GRB10, AND SUBCELLULAR LOCATION.
PubMed=18286479; DOI=10.1002/jcp.21405;
Monami G., Emiliozzi V., Morrione A.;
"Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth
factor receptor regulates receptor internalization.";
J. Cell. Physiol. 216:426-437(2008).
[14]
FUNCTION IN UBIQUITINATION OF ERBB4, AND INTERACTION WITH ERBB4.
PubMed=19193720; DOI=10.1096/fj.08-121947;
Zeng F., Xu J., Harris R.C.;
"Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in
MDCK II cells.";
FASEB J. 23:1935-1945(2009).
[15]
FUNCTION IN UBIQUITINATION OF ERBB4, INTERACTION WITH ERBB4, AND
SUBCELLULAR LOCATION.
PubMed=19047365; DOI=10.1128/MCB.00595-08;
Feng S.M., Muraoka-Cook R.S., Hunter D., Sandahl M.A., Caskey L.S.,
Miyazawa K., Atfi A., Earp H.S. III;
"The E3 ubiquitin ligase WWP1 selectively targets HER4 and its
proteolytically derived signaling isoforms for degradation.";
Mol. Cell. Biol. 29:892-906(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
FUNCTION, DISRUPTION PHENOTYPE, AND 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]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 71-246 IN COMPLEX WITH GRB10,
AND INTERACTION WITH GRB10.
PubMed=20980250; DOI=10.1074/jbc.M110.143412;
Huang Q., Szebenyi D.M.;
"Structural basis for the interaction between the growth factor-
binding protein GRB10 and the E3 ubiquitin ligase NEDD4.";
J. Biol. Chem. 285:42130-42139(2010).
-!- 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 (By
similarity). Monoubiquitinates IGF1R at multiple sites, thus
leading to receptor internalization and degradation in lysosomes.
Ubiquitinates FGFR1, leading to receptor internalization and
degradation in lysosomes. Involved in ubiquitination of ERBB4
intracellular domain E4ICD1 (PubMed:19193720). Predominantly
involved in ubiquitination of membrane bound forms of ERBB4 rather
than processed precursors and intermediate membrane-anchored 80
kDa fragments (m80HER4), with a lesser role in ubiquitination of
ERBB4 intracellular domain E4ICD1 (PubMed:19047365). Promotes
ubiquitination of RAPGEF2. Involved in the pathway leading to the
degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase
activity. 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 (By similarity). 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 (By
similarity). {ECO:0000250|UniProtKB:P46934,
ECO:0000269|PubMed:19047365, ECO:0000269|PubMed:19193720}.
-!- 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:0000250|UniProtKB:P46934}.
-!- ENZYME REGULATION: Activated by NDFIP1- and NDFIP2-binding.
{ECO:0000250}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Binds SCNN1A, SCNN1B and SCNN1G. Interacts with NDFIP1
and NDFIP2; this interaction activates the E3 ubiquitin-protein
ligase and may induce its recruitment to exosomes. Interacts with
UBE2D2 (PubMed:9182527). Binds, in vitro, through the WW2 and WW3
domains, to neural isoforms of ENAH that contain the PPSY motif
(PubMed:9407065). Interacts with BEAN1, LITAF, RNF11, WBP1, WBP2,
PMEPAI and PRRG2 (PubMed:11042109). Interacts with murine leukemia
virus Gag polyprotein (via PPXY motif) (PubMed:15908698).
Interacts (via C2 domain) with GRB10 (via SH2 domain)
(PubMed:12697834, PubMed:15060076, PubMed:18286479,
PubMed:20980250). Interacts with ERBB4 (PubMed:19193720,
PubMed:19047365). Interacts with TNIK; the interaction is direct,
allows the TNIK-dependent recruitment of RAP2A and its
ubiquitination by NEDD4 (PubMed:20159449). Interacts (via WW3
domain) with TNK2; EGF promotes this interaction. Interacts (via
WW3 domain) with FGFR1 (via C-terminus). Interacts with OTUD7B (By
similarity). Interacts with ISG15 (By similarity). 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) (By similarity). Interacts
with LAPTM4B; may play a role in the lysosomal sorting of LAPTM4B
(By similarity). {ECO:0000250|UniProtKB:P46934,
ECO:0000269|PubMed:11042109, ECO:0000269|PubMed:12697834,
ECO:0000269|PubMed:15060076, ECO:0000269|PubMed:15908698,
ECO:0000269|PubMed:18286479, ECO:0000269|PubMed:19047365,
ECO:0000269|PubMed:19193720, ECO:0000269|PubMed:20159449,
ECO:0000269|PubMed:20980250, ECO:0000269|PubMed:9182527,
ECO:0000269|PubMed:9407065}.
-!- INTERACTION:
Q9EQG5:Bean1; NbExp=3; IntAct=EBI-773516, EBI-6304006;
Q60760:Grb10; NbExp=6; IntAct=EBI-773516, EBI-861810;
Q9JLJ0:Litaf; NbExp=5; IntAct=EBI-773516, EBI-643664;
Q8R0W6:Ndfip1; NbExp=5; IntAct=EBI-773516, EBI-6304119;
Q9D7R2:Pmepa1; NbExp=5; IntAct=EBI-773516, EBI-6304097;
Q8R182:Prrg2; NbExp=5; IntAct=EBI-773516, EBI-6304055;
Q9QYK7:Rnf11; NbExp=4; IntAct=EBI-773516, EBI-4405826;
P97764:Wbp1; NbExp=3; IntAct=EBI-773516, EBI-6304160;
P97765:Wbp2; NbExp=5; IntAct=EBI-773516, EBI-6304181;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein. 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}.
-!- TISSUE SPECIFICITY: Brain.
-!- DOMAIN: The WW domains mediate interaction with PPxY motif-
containing proteins (By similarity). The WW domains mediate
interaction with LITAF, RNF11, WBP1, WBP2, PMEPAI, NDFIP1 and
PRRG2 (PubMed:11042109). {ECO:0000250|UniProtKB:P46934,
ECO:0000269|PubMed:11042109}.
-!- PTM: Auto-ubiquitinated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Lethal during late gestation. Embryos show a
retarded development and defects in vasculogenesis and
angiogenesis. {ECO:0000269|PubMed:20159449}.
-!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
thioester formation.
-!- SEQUENCE CAUTION:
Sequence=AAB63360.1; Type=Frameshift; Positions=12; Evidence={ECO:0000305};
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EMBL; D85414; BAA12803.1; -; mRNA.
EMBL; U96635; AAB63360.1; ALT_FRAME; mRNA.
EMBL; AK088620; BAC40458.1; -; mRNA.
EMBL; AK088767; BAC40558.1; -; mRNA.
EMBL; AK122203; BAC65485.1; -; mRNA.
EMBL; AK133838; BAE21875.1; -; mRNA.
CCDS; CCDS72275.1; -.
RefSeq; NP_035020.2; NM_010890.3.
UniGene; Mm.279923; -.
PDB; 3M7F; X-ray; 2.00 A; B=71-246.
PDBsum; 3M7F; -.
ProteinModelPortal; P46935; -.
SMR; P46935; -.
BioGrid; 201723; 52.
DIP; DIP-32323N; -.
ELM; P46935; -.
IntAct; P46935; 17.
MINT; MINT-90132; -.
STRING; 10090.ENSMUSP00000034740; -.
iPTMnet; P46935; -.
PhosphoSitePlus; P46935; -.
SwissPalm; P46935; -.
EPD; P46935; -.
MaxQB; P46935; -.
PaxDb; P46935; -.
PRIDE; P46935; -.
Ensembl; ENSMUST00000034740; ENSMUSP00000034740; ENSMUSG00000032216.
GeneID; 17999; -.
KEGG; mmu:17999; -.
UCSC; uc009qqe.1; mouse.
CTD; 4734; -.
MGI; MGI:97297; Nedd4.
eggNOG; KOG0940; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00760000118966; -.
HOGENOM; HOG000208451; -.
HOVERGEN; HBG004134; -.
InParanoid; P46935; -.
KO; K10591; -.
OMA; FNSLKWI; -.
OrthoDB; EOG091G0SS8; -.
PhylomeDB; P46935; -.
TreeFam; TF323658; -.
Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
Reactome; R-MMU-1253288; Downregulation of ERBB4 signaling.
Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
UniPathway; UPA00143; -.
ChiTaRS; Nedd4; mouse.
PRO; PR:P46935; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032216; -.
ExpressionAtlas; P46935; baseline and differential.
Genevisible; P46935; MM.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000151; C:ubiquitin ligase complex; IPI:MGI.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IEA:Ensembl.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IDA:ParkinsonsUK-UCL.
GO; GO:0050815; F:phosphoserine residue binding; IDA:BHF-UCL.
GO; GO:0050816; F:phosphothreonine residue binding; IDA:BHF-UCL.
GO; GO:0070064; F:proline-rich region binding; IPI:MGI.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0070063; F:RNA polymerase binding; IEA:Ensembl.
GO; GO:0019871; F:sodium channel inhibitor activity; IDA:MGI.
GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0002250; P:adaptive immune response; IMP:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0044111; P:development involved in symbiotic interaction; IEA:Ensembl.
GO; GO:0003197; P:endocardial cushion development; IMP:MGI.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IEA:Ensembl.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0010766; P:negative regulation of sodium ion transport; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0010768; P:negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; IEA:Ensembl.
GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
GO; GO:0046824; P:positive regulation of nucleocytoplasmic transport; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IDA:MGI.
GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:MGI.
GO; GO:0032801; P:receptor catabolic process; IEA:Ensembl.
GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0050807; P:regulation of synapse organization; IMP:MGI.
GO; GO:0042110; P:T cell activation; IMP:MGI.
GO; GO:0019089; P:transmission of virus; IEA:Ensembl.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 3.
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; 3.
PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
SMART; SM00239; C2; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00456; WW; 3.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF51045; SSF51045; 3.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS01159; WW_DOMAIN_1; 3.
PROSITE; PS50020; WW_DOMAIN_2; 3.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasm; Membrane;
Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 887 E3 ubiquitin-protein ligase NEDD4.
/FTId=PRO_0000120320.
DOMAIN 65 166 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 249 282 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 405 438 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 460 493 WW 3. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 552 887 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
REGION 217 549 Mediates interaction with TNIK.
{ECO:0000269|PubMed:20159449}.
ACT_SITE 854 854 Glycyl thioester intermediate.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:Q62940}.
MOD_RES 287 287 Phosphothreonine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000250|UniProtKB:P46934}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000250|UniProtKB:P46934}.
MUTAGEN 854 854 C->S: Loss of ubiquitin-ligase activity.
No effect on VEGFR-2/KDFR degradation.
{ECO:0000269|PubMed:15060076}.
STRAND 78 89 {ECO:0000244|PDB:3M7F}.
STRAND 101 109 {ECO:0000244|PDB:3M7F}.
TURN 110 112 {ECO:0000244|PDB:3M7F}.
STRAND 113 119 {ECO:0000244|PDB:3M7F}.
STRAND 130 139 {ECO:0000244|PDB:3M7F}.
TURN 141 143 {ECO:0000244|PDB:3M7F}.
STRAND 145 152 {ECO:0000244|PDB:3M7F}.
STRAND 160 169 {ECO:0000244|PDB:3M7F}.
STRAND 186 189 {ECO:0000244|PDB:3M7F}.
STRAND 201 209 {ECO:0000244|PDB:3M7F}.
SEQUENCE 887 AA; 102706 MW; AE7DD3ED63986C50 CRC64;
MSSDMAADES EAPVLSEDEV WEFCLDKTED GGGSPGSDVT DTCEPPCGCW ELNPNSLEEE
HVLFTADPYL ELHNDDTRVV RVKVIAGIGL AKKDILGASD PYVRVTLYDP MSGILTSVQT
KTIKKSLNPK WNEEILFRVL PQRHRILFEV FDENRLTRDD FLGQVDVPLY PLPTENPRME
RPYTFKDFVL HPRSHKSRVK GYLRLKMTYL PKNGSEDENA DQAEELEPGW VVLDQPDAAT
HLPHPPEPSP LPPGWEERQD VLGRTYYVNH ESRRTQWKRP SPDDDLTDED NDDMQLQAQR
AFTTRRQISE DVDGPDNRES PENWEIVRED ENTEYSGQAV QSPPSGHIDV QTHLAEEFNT
RLAVCGNPAT SQPVTSSNHS SRGGSLQTCI FEEQPTLPVL LPTSSGLPPG WEEKQDDRGR
SYYVDHNSKT TTWSKPTMQD DPRSKIPAHL RGKTDSNDLG PLPPGWEERT HTDGRVFFIN
HNIKKTQWED PRLQNVAITG PAVPYSRDYK RKYEFFRRKL KKQTDIPNKF EMKLRRANIL
EDSYRRIMGV KRADLLKARL WIEFDGEKGL DYGGVAREWF FLISKEMFNP YYGLFEYSAT
DNYTLQINPN SGLCNEDHLS YFKFIGRVAG MAVYHGKLLD GFFIRPFYKM MLQKLITLHD
MESVDSEYYS SLRWILENDP TELDLRFIID EELFGQTHQH ELKTGGSEIV VTNKNKKEYI
YLVIQWRFVN RIQKQMAAFK EGFFELIPQD LIKIFDENEL ELLMCGLGDV DVNDWREHTK
YKNGYSMNHQ VIHWFWKAVW MMDSEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQSFTVE
QWGTPDKLPR AHTCFNRLDL PPYESFDELW DKLQMAIENT QGFDGVD


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