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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_MOUSE             Reviewed;        1004 AA.
Q8CFI0; Q8BRT9; Q8BS42; Q99PK2;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 2.
29-SEP-2021, entry version 173.
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, Nedd4b;
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] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION, AND
MUTAGENESIS OF CYS-971.
STRAIN=C57BL/6J;
PubMed=11149908; DOI=10.1096/fj.00-0191com;
Kamynina E., Debonneville C., Bens M., Vandewalle A., Staub O.;
"A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+
channel.";
FASEB J. 15:204-214(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH SCNN1A;
SCNN1B AND SCNN1G, AND FUNCTION.
TISSUE=Brain;
PubMed=12424229; DOI=10.1096/fj.02-0497fje;
Fotia A.B., Dinudom A., Shearwin K.E., Koch J.-P., Korbmacher C.,
Cook D.I., Kumar S.;
"The role of individual Nedd4-2 (KIAA0439) WW domains in binding and
regulating epithelial sodium channels.";
FASEB J. 17:70-72(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-1004 (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
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]
FUNCTION, INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G, PHOSPHORYLATION AT
SER-371 AND SER-477, AND MUTAGENESIS OF SER-371 AND SER-477.
PubMed=11742982; DOI=10.1093/emboj/20.24.7052;
Debonneville C., Flores S.Y., Kamynina E., Plant P.J., Tauxe C.,
Thomas M.A., Muenster C., Chraiebi A., Pratt J.H., Horisberger J.-D.,
Pearce D., Loffing J., Staub O.;
"Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell
surface expression.";
EMBO J. 20:7052-7059(2001).
[6]
FUNCTION, INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G, AND TISSUE
SPECIFICITY.
PubMed=11244092; DOI=10.1074/jbc.c000906200;
Harvey K.F., Dinudom A., Cook D.I., Kumar S.;
"The Nedd4-like protein KIAA0439 is a potential regulator of the epithelial
sodium channel.";
J. Biol. Chem. 276:8597-8601(2001).
[7]
INTERACTION WITH NDFIP2, AND SUBCELLULAR LOCATION.
PubMed=12050153; DOI=10.1074/jbc.m203018200;
Konstas A.-A., Shearwin-Whyatt L.M., Fotia A.B., Degger B., Riccardi D.,
Cook D.I., Korbmacher C., Kumar S.;
"Regulation of the epithelial sodium channel by N4WBP5A, a novel
Nedd4/Nedd4-2-interacting protein.";
J. Biol. Chem. 277:29406-29416(2002).
[8]
FUNCTION, AND INTERACTION WITH SCN1A; SCN2A; SCN3A; SCN5A; SCN8A; SCN9A;
SCN10A; SCNN1A; SCNN1B AND SCNN1G.
PubMed=15123669; DOI=10.1074/jbc.m402820200;
Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
"Regulation of neuronal voltage-gated sodium channels by the ubiquitin-
protein ligases Nedd4 and Nedd4-2.";
J. Biol. Chem. 279:28930-28935(2004).
[9]
INTERACTION WITH UBE2E3.
PubMed=14993279; DOI=10.1128/mcb.24.6.2397-2409.2004;
Debonneville C., Staub O.;
"Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-
dependent regulation of the epithelial Na+ channel.";
Mol. Cell. Biol. 24:2397-2409(2004).
[10]
PHOSPHORYLATION AT SER-477.
PubMed=15958725; DOI=10.1681/asn.2004100828;
Flores S.Y., Loffing-Cueni D., Kamynina E., Daidie D., Gerbex C.,
Chabanel S., Dudler J., Loffing J., Staub O.;
"Aldosterone-induced serum and glucocorticoid-induced kinase 1 expression
is accompanied by nedd4-2 phosphorylation and increased na+ transport in
cortical collecting duct cells.";
J. Am. Soc. Nephrol. 16:2279-2287(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-493; SER-508;
SER-512 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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).
[13]
DEVELOPMENTAL STAGE.
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).
[14]
STRUCTURE BY NMR OF 221-254; 414-447 AND 525-560.
Kowalski K., Merkel A.L., Booker G.W.;
"Solution structures of WW domains of NEDD4-2.";
Submitted (OCT-2005) to the PDB data bank.
-!- 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. Promotes
ubiquitination and degradation of SGK1 and TNK2. Ubiquitinates BRAT1
and this ubiquitination is enhanced in the presence of NDFIP1. Plays a
role in dendrite formation by melanocytes (By similarity). Involved in
the regulation of TOR signaling (By similarity). Ubiquitinates and
regulates protein levels of NTRK1 once this one is activated by NGF (By
similarity). {ECO:0000250|UniProtKB:Q96PU5,
ECO:0000269|PubMed:11149908, ECO:0000269|PubMed:11244092,
ECO:0000269|PubMed:11742982, ECO:0000269|PubMed:12424229,
ECO:0000269|PubMed:15123669}.
-!- 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. Interacts
with SGK1. {ECO:0000250}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with SMAD2, SMAD3, SMAD6 and SMAD7 (By similarity).
Interacts with CLCN5 (By similarity). The phosphorylated form interacts
with 14-3-3 proteins (By similarity). Interacts via its WW domains with
SCNN1A, SCNN1B, SCNN1G, SCN1A, SCN2A, SCN3A, SCN5A, SCN8A, SCN9A and
SCN10A (PubMed:11244092., PubMed:11742982, PubMed:12424229,
PubMed:15123669). Interacts with NDFIP1 and NDFIP2; this interaction
activates the E3 ubiquitin-protein ligase (PubMed:12050153). Interacts
with TNK2 (By similarity). Interacts (via C2 domain) with NPC2 (By
similarity). Interacts with ARRDC4 (By similarity). Interacts with
KCNQ1; promotes internalization of KCNQ1 (By similarity). Interacts
(via domains WW1, 3 and 4) with USP36; the interaction inhibits
ubiquitination of, at least, NTRK1, KCNQ2 and KCNQ3 by NEDD4L (By
similarity). Interacts with PRRG4 (via cytoplasmic domain) (By
similarity). {ECO:0000250|UniProtKB:Q96PU5,
ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:11742982,
ECO:0000269|PubMed:12050153, ECO:0000269|PubMed:12424229,
ECO:0000269|PubMed:14993279, ECO:0000269|PubMed:15123669}.
-!- INTERACTION:
Q8CFI0; Q99N57: Raf1; NbExp=2; IntAct=EBI-8046183, EBI-397757;
Q8CFI0; Q9Z2S7-3: Tsc22d3; NbExp=2; IntAct=EBI-8046183, EBI-15771036;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12050153}. Golgi
apparatus {ECO:0000250|UniProtKB:Q96PU5}. Endosome, multivesicular body
{ECO:0000250|UniProtKB:Q96PU5}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8CFI0-1; Sequence=Displayed;
Name=2;
IsoId=Q8CFI0-2; Sequence=VSP_015450;
Name=3;
IsoId=Q8CFI0-3; Sequence=VSP_015453;
-!- TISSUE SPECIFICITY: Highly expressed in liver and kidney. Also
expressed in heart, brain and lung. Isoform 1 is expressed in kidney,
lung and gut. Isoform 3 is ubiquitously expressed.
{ECO:0000269|PubMed:11149908, ECO:0000269|PubMed:11244092}.
-!- DEVELOPMENTAL STAGE: In the developing brain, it is homogenously
distributed in the cortical plate, ventricular zone and ganglionic
eminences at 15 dpc. A peak of expression in the cortex is observed at
16.5 dpc. {ECO:0000269|PubMed:27694961}.
-!- PTM: Phosphorylated; which impairs interaction with SCNN. Interaction
with YWHAH inhibits dephosphorylation (By similarity). Aldosterone
induces Ser-477 phosphorylation by SGK1. {ECO:0000250,
ECO:0000269|PubMed:11742982, ECO:0000269|PubMed:15958725}.
-!- PTM: Auto-ubiquitinated. Deubiquitinated by USP36, no effect on NEDD4L
protein levels. Both proteins interact and regulate each other's
ubiquitination levels. {ECO:0000250|UniProtKB:Q96PU5}.
-!- SEQUENCE CAUTION:
Sequence=BAC31307.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; AF277232; AAK00809.1; -; mRNA.
EMBL; BC039746; AAH39746.1; -; mRNA.
EMBL; BC071210; AAH71210.1; -; mRNA.
EMBL; AK042621; BAC31307.1; ALT_INIT; mRNA.
CCDS; CCDS29305.1; -. [Q8CFI0-2]
PDB; 1WR3; NMR; -; A=221-254.
PDB; 1WR4; NMR; -; A=414-447.
PDB; 1WR7; NMR; -; A=525-560.
PDBsum; 1WR3; -.
PDBsum; 1WR4; -.
PDBsum; 1WR7; -.
BMRB; Q8CFI0; -.
SMR; Q8CFI0; -.
DIP; DIP-48843N; -.
IntAct; Q8CFI0; 10.
STRING; 10090.ENSMUSP00000132838; -.
TCDB; 8.A.30.1.1; the nedd4-family interacting protein-2 (nedd4) family.
iPTMnet; Q8CFI0; -.
PhosphoSitePlus; Q8CFI0; -.
jPOST; Q8CFI0; -.
PaxDb; Q8CFI0; -.
PeptideAtlas; Q8CFI0; -.
PRIDE; Q8CFI0; -.
ProteomicsDB; 253057; -. [Q8CFI0-1]
ProteomicsDB; 253058; -. [Q8CFI0-2]
ProteomicsDB; 253059; -. [Q8CFI0-3]
Antibodypedia; 5421; 258 antibodies.
Ensembl; ENSMUST00000237410; ENSMUSP00000158044; ENSMUSG00000024589. [Q8CFI0-3]
UCSC; uc008fen.2; mouse. [Q8CFI0-3]
MGI; MGI:1933754; Nedd4l.
VEuPathDB; HostDB:ENSMUSG00000024589; -.
eggNOG; KOG0940; Eukaryota.
GeneTree; ENSGT00940000156873; -.
InParanoid; Q8CFI0; -.
PhylomeDB; Q8CFI0; -.
Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Nedd4l; mouse.
EvolutionaryTrace; Q8CFI0; -.
PRO; PR:Q8CFI0; -.
Proteomes; UP000000589; Chromosome 18.
RNAct; Q8CFI0; protein.
ExpressionAtlas; Q8CFI0; baseline and differential.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0019870; F:potassium channel inhibitor activity; ISO:MGI.
GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
GO; GO:0019871; F:sodium channel inhibitor activity; IDA:MGI.
GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:MGI.
GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; ISO:MGI.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISO:MGI.
GO; GO:1902306; P:negative regulation of sodium ion transmembrane transport; ISO:MGI.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0010766; P:negative regulation of sodium ion transport; IDA:MGI.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:2001259; P:positive regulation of cation channel activity; IGI:MGI.
GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; ISO:MGI.
GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:0010765; P:positive regulation of sodium ion transport; IGI:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IDA:MGI.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
GO; GO:0034765; P:regulation of ion transmembrane transport; ISO:MGI.
GO; GO:0003254; P:regulation of membrane depolarization; ISO:MGI.
GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
GO; GO:0010038; P:response to metal ion; ISO:MGI.
GO; GO:0009651; P:response to salt stress; IMP:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 4.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR024928; E3_ub_ligase_SMURF1.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00168; C2; 1.
Pfam; PF00632; HECT; 1.
Pfam; PF00397; WW; 4.
PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
PRINTS; PR00360; C2DOMAIN.
SMART; SM00239; C2; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00456; WW; 4.
SUPFAM; 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; Alternative splicing; Cytoplasm; Differentiation; Endosome;
Golgi apparatus; Phosphoprotein; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1..1004
/note="E3 ubiquitin-protein ligase NEDD4-like"
/id="PRO_0000120324"
DOMAIN 30..154
/note="C2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
DOMAIN 221..254
/note="WW 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 414..447
/note="WW 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 526..559
/note="WW 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 577..610
/note="WW 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
DOMAIN 669..1003
/note="HECT"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
REGION 207..230
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 272..407
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 453..523
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 272..289
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 330..402
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 453..484
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 971
/note="Glycyl thioester intermediate"
MOD_RES 341
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q96PU5"
MOD_RES 347
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q96PU5"
MOD_RES 371
/note="Phosphoserine; by WNK1 and WNK4"
/evidence="ECO:0000269|PubMed:11742982"
MOD_RES 396
/note="Phosphothreonine; by SGK1"
/evidence="ECO:0000250|UniProtKB:Q96PU5"
MOD_RES 475
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q96PU5"
MOD_RES 477
/note="Phosphoserine; by SGK1"
/evidence="ECO:0000269|PubMed:11742982,
ECO:0000269|PubMed:15958725"
MOD_RES 478
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 493
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 504
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q96PU5"
MOD_RES 508
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17242355,
ECO:0007744|PubMed:21183079"
MOD_RES 512
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 516
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
VAR_SEQ 1..149
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:11149908,
ECO:0000303|PubMed:15489334"
/id="VSP_015450"
VAR_SEQ 385..404
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:12424229,
ECO:0000303|PubMed:16141072"
/id="VSP_015453"
MUTAGEN 371
/note="S->A: Weakly reduces phosphorylation by SGK1."
/evidence="ECO:0000269|PubMed:11742982"
MUTAGEN 477
/note="S->A: Strongly reduces phosphorylation by SGK1."
/evidence="ECO:0000269|PubMed:11742982"
MUTAGEN 971
/note="C->S: Abolishes catalytic activity."
/evidence="ECO:0000269|PubMed:11149908"
CONFLICT 179
/note="A -> G (in Ref. 1; AAK00809)"
/evidence="ECO:0000305"
CONFLICT 390
/note="R -> G (in Ref. 1; AAK00809)"
/evidence="ECO:0000305"
CONFLICT 403
/note="P -> S (in Ref. 1; AAK00809)"
/evidence="ECO:0000305"
CONFLICT 585
/note="E -> G (in Ref. 1; AAK00809)"
/evidence="ECO:0000305"
CONFLICT 832
/note="N -> T (in Ref. 1; AAK00809)"
/evidence="ECO:0000305"
CONFLICT 847
/note="N -> D (in Ref. 1; AAK00809)"
/evidence="ECO:0000305"
CONFLICT 949
/note="N -> K (in Ref. 4; BAC31307)"
/evidence="ECO:0000305"
STRAND 227..231
/evidence="ECO:0007829|PDB:1WR3"
STRAND 233..235
/evidence="ECO:0007829|PDB:1WR3"
STRAND 237..241
/evidence="ECO:0007829|PDB:1WR3"
TURN 242..244
/evidence="ECO:0007829|PDB:1WR3"
STRAND 247..250
/evidence="ECO:0007829|PDB:1WR3"
STRAND 420..424
/evidence="ECO:0007829|PDB:1WR4"
STRAND 426..428
/evidence="ECO:0007829|PDB:1WR4"
STRAND 430..434
/evidence="ECO:0007829|PDB:1WR4"
TURN 435..438
/evidence="ECO:0007829|PDB:1WR4"
STRAND 439..443
/evidence="ECO:0007829|PDB:1WR4"
STRAND 532..536
/evidence="ECO:0007829|PDB:1WR7"
STRAND 542..546
/evidence="ECO:0007829|PDB:1WR7"
TURN 547..550
/evidence="ECO:0007829|PDB:1WR7"
STRAND 551..555
/evidence="ECO:0007829|PDB:1WR7"
HELIX 557..559
/evidence="ECO:0007829|PDB:1WR7"
SEQUENCE 1004 AA; 115419 MW; 50CBB3436052AA60 CRC64;
MSLCEAPVHV GDKELKYFQI PQMLSQLSLL ASHHSRGLEF SGGQGESRIL RVKVVSGIDL
AKKDIFGASD PYVKLSLYVA DENRELALVQ TKTIKKTLNP KWNEEFYFRV NPSNHRLLFE
VFDENRLTRD DFLGQVDVPL SHLPTEDPTM ERPYTFKDFL LRPRSHKSRV KGFLRLKMAY
MPKNGGQDEE NSEQRDDMEH GWEVVDSNDS ASQHQEELPP PPLPPGWEEK VDNLGRTYYV
NHNNRSTQWH RPSLMDVSSE SDNNIRQINQ EAAHRRFRSR RHISEDLEPE ASEGGGEGPE
PWETISEEMN MAGDSLSLAL PPPPASPVSR TSPQELSEEV SRRLQITPDS NGEQFSSLIQ
REPSSRLRSC SVTDTVAEQA HLPPPSTPTR RARSSTVTGG EEPTPSVAYV HTTPGLPSGW
EERKDAKGRT YYVNHNNRTT TWTRPIMQLA EDGASGSATN SNNHLVEPQI RRPRSLSSPT
VTLSAPLEGA KDSPIRRAVK DTLSNPQSPQ PSPYNSPKPQ HKVTQSFLPP GWEMRIAPNG
RPFFIDHNTK TTTWEDPRLK FPVHMRSKAS LNPNDLGPLP PGWEERIHLD GRTFYIDHNS
KITQWEDPRL QNPAITGPAV PYSREFKQKY DYFRKKLKKP ADIPNRFEMK LHRNNIFEES
YRRIMSVKRP DVLKARLWIE FESEKGLDYG GVAREWFFLL SKEMFNPYYG LFEYSATDNY
TLQINPNSGL CNEDHLSYFT FIGRVAGLAV FHGKLLDGFF IRPFYKMMLG KQITLNDMES
VDSEYYNSLK WILENDPTEL DLMFCIDEEN FGQTYQVDLK PNGSEIMVTN ENKREYIDLV
IQWRFVNRVQ KQMNAFLEGF TELLPIDLIK IFDENELELL MCGLGDVDVN DWRQHSIYKN
GYCPNHPVIQ WFWKAVLLMD AEKRIRLLQF VTGTSRVPMN GFAELYGSNG PQLFTIEQWG
SPEKLPRAHT CFNRLDLPPY ETFEDLREKL LMAVENAQGF EGVD


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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 :