Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P46935 (NEDD4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase NEDD4

EC=6.3.2.-
Alternative name(s):
Neural precursor cell expressed developmentally down-regulated protein 4
Short name=NEDD-4
Gene names
Name:Nedd4
Synonyms:Kiaa0093, Nedd-4, Nedd4-1, Nedd4a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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 (Ref.14). 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 (Ref.15). 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 By similarity. Ref.9 Ref.13 Ref.14 Ref.15 Ref.17

Enzyme regulation

Activated by NDFIP1- and NDFIP2-binding By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. 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. Interacts with murine leukemia virus Gag polyprotein (via PPXY motif). Interacts (via C2 domain) with GRB10 (via SH2 domain). Interacts with ERBB4. 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 By similarity. Interacts with ISG15 By similarity. Interacts (via WW domain) with RAPGEF2; this interaction leads to ubiquitination and degradation via the proteasome pathway By similarity. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18

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. Ref.3 Ref.13 Ref.15

Tissue specificity

Brain.

Domain

The WW domains mediate interaction with LITAF, RNF11, WBP1, WBP2, TMEPAI, NDFIP1 and PRRG2. Ref.7

Post-translational modification

Auto-ubiquitinated By similarity.

Disruption phenotype

Lethal during late gestation. Embryos show a retarded development and defects in vasculogenesis and angiogenesis. Ref.17

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Sequence similarities

Contains 1 C2 domain.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Contains 3 WW domains.

Sequence caution

The sequence AAB63360.1 differs from that shown. Reason: Frameshift at position 12.

Ontologies

Keywords
   Biological processNeurogenesis
Ubl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation

Inferred from mutant phenotype PubMed 18931680. Source: MGI

adaptive immune response

Inferred from mutant phenotype PubMed 18931680. Source: MGI

blood vessel morphogenesis

Inferred from mutant phenotype PubMed 20026598. Source: MGI

development involved in symbiotic interaction

Inferred from electronic annotation. Source: Ensembl

endocardial cushion development

Inferred from mutant phenotype PubMed 20026598. Source: MGI

glucocorticoid receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of sodium ion transport

Inferred from direct assay PubMed 10212229. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20026598. Source: MGI

negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage

Inferred from electronic annotation. Source: Ensembl

negative regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

neuromuscular junction development

Inferred from mutant phenotype PubMed 19345204. Source: MGI

neuron projection development

Inferred from electronic annotation. Source: Ensembl

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 20026598. Source: MGI

positive regulation of nucleocytoplasmic transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein catabolic process

Inferred from direct assay PubMed 11748237. Source: MGI

progesterone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein K63-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein monoubiquitination

Inferred from direct assay PubMed 21920314. Source: MGI

protein targeting to lysosome

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from direct assay Ref.3. Source: MGI

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 18931680. Source: MGI

receptor catabolic process

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from electronic annotation. Source: Ensembl

regulation of dendrite morphogenesis

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of potassium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

regulation of synapse organization

Inferred from mutant phenotype PubMed 19345204. Source: MGI

transmission of virus

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: Ensembl

chromatin

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 14973438. Source: MGI

cytosol

Inferred from direct assay PubMed 19794060Ref.3. Source: MGI

membrane

Inferred from direct assay PubMed 14973438. Source: MGI

nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ubiquitin ligase complex

Inferred from physical interaction Ref.7. Source: MGI

   Molecular_functionphosphoserine binding

Inferred from direct assay PubMed 10037602. Source: BHF-UCL

phosphothreonine binding

Inferred from direct assay PubMed 10037602. Source: BHF-UCL

proline-rich region binding

Inferred from physical interaction PubMed 11748237PubMed 9305852. Source: MGI

sodium channel inhibitor activity

Inferred from direct assay PubMed 10212229. Source: MGI

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 11717310Ref.3. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 887887E3 ubiquitin-protein ligase NEDD4
PRO_0000120320

Regions

Domain65 – 166102C2
Domain249 – 28234WW 1
Domain405 – 43834WW 2
Domain460 – 49334WW 3
Domain552 – 887336HECT
Region217 – 549333Mediates interaction with TNIK

Sites

Active site8541Glycyl thioester intermediate

Amino acid modifications

Modified residue2871Phosphothreonine Ref.16
Modified residue3091Phosphoserine; by host Ref.11 Ref.12 Ref.16
Modified residue3851Phosphoserine; by host By similarity

Experimental info

Mutagenesis8541C → S: Loss of ubiquitin-ligase activity. No effect on VEGFR-2/KDFR degradation. Ref.9

Secondary structure

................... 887
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46935 [UniParc].

Last modified June 20, 2003. Version 3.
Checksum: AE7DD3ED63986C50

FASTA887102,706
        10         20         30         40         50         60 
MSSDMAADES EAPVLSEDEV WEFCLDKTED GGGSPGSDVT DTCEPPCGCW ELNPNSLEEE 

        70         80         90        100        110        120 
HVLFTADPYL ELHNDDTRVV RVKVIAGIGL AKKDILGASD PYVRVTLYDP MSGILTSVQT 

       130        140        150        160        170        180 
KTIKKSLNPK WNEEILFRVL PQRHRILFEV FDENRLTRDD FLGQVDVPLY PLPTENPRME 

       190        200        210        220        230        240 
RPYTFKDFVL HPRSHKSRVK GYLRLKMTYL PKNGSEDENA DQAEELEPGW VVLDQPDAAT 

       250        260        270        280        290        300 
HLPHPPEPSP LPPGWEERQD VLGRTYYVNH ESRRTQWKRP SPDDDLTDED NDDMQLQAQR 

       310        320        330        340        350        360 
AFTTRRQISE DVDGPDNRES PENWEIVRED ENTEYSGQAV QSPPSGHIDV QTHLAEEFNT 

       370        380        390        400        410        420 
RLAVCGNPAT SQPVTSSNHS SRGGSLQTCI FEEQPTLPVL LPTSSGLPPG WEEKQDDRGR 

       430        440        450        460        470        480 
SYYVDHNSKT TTWSKPTMQD DPRSKIPAHL RGKTDSNDLG PLPPGWEERT HTDGRVFFIN 

       490        500        510        520        530        540 
HNIKKTQWED PRLQNVAITG PAVPYSRDYK RKYEFFRRKL KKQTDIPNKF EMKLRRANIL 

       550        560        570        580        590        600 
EDSYRRIMGV KRADLLKARL WIEFDGEKGL DYGGVAREWF FLISKEMFNP YYGLFEYSAT 

       610        620        630        640        650        660 
DNYTLQINPN SGLCNEDHLS YFKFIGRVAG MAVYHGKLLD GFFIRPFYKM MLQKLITLHD 

       670        680        690        700        710        720 
MESVDSEYYS SLRWILENDP TELDLRFIID EELFGQTHQH ELKTGGSEIV VTNKNKKEYI 

       730        740        750        760        770        780 
YLVIQWRFVN RIQKQMAAFK EGFFELIPQD LIKIFDENEL ELLMCGLGDV DVNDWREHTK 

       790        800        810        820        830        840 
YKNGYSMNHQ VIHWFWKAVW MMDSEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQSFTVE 

       850        860        870        880 
QWGTPDKLPR AHTCFNRLDL PPYESFDELW DKLQMAIENT QGFDGVD 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a set of genes with developmentally down-regulated expression in the mouse brain."
Kumar S., Tomooka Y., Noda M.
Biochem. Biophys. Res. Commun. 185:1155-1161(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[2]Kumar S.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases."
Hatakeyama S., Jensen J.P., Weissman A.M.
J. Biol. Chem. 272:15085-15092(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH UBE2D2.
Strain: C57BL/6 X CBA.
[4]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Thymus.
[5]"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."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled."
Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T., Sudol M.
J. Biol. Chem. 272:32869-32877(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ENAH.
[7]"Identification of multiple proteins expressed in murine embryos as binding partners for the WW domains of the ubiquitin-protein ligase Nedd4."
Jolliffe C.N., Harvey K.F., Haines B.P., Parasivam G., Kumar S.
Biochem. J. 351:557-565(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BEAN1; LITAF; RNF11; WBP1; WBP2; TMEPAI; NDFIP1 AND PRRG2, DOMAINS.
Tissue: Embryo.
[8]"The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor."
Vecchione A., Marchese A., Henry P., Rotin D., Morrione A.
Mol. Cell. Biol. 23:3363-3372(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB10.
[9]"Grb10 prevents Nedd4-mediated vascular endothelial growth factor receptor-2 degradation."
Murdaca J., Treins C., Monthouel-Kartmann M.N., Pontier-Bres R., Kumar S., Van Obberghen E., Giorgetti-Peraldi S.
J. Biol. Chem. 279:26754-26761(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GRB10, MUTAGENESIS OF CYS-854.
[10]"Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding."
Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., Basyuk E.
J. Biol. Chem. 280:27004-27012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MURINE LEUKEMIA VIRUS GAG POLYPROTEIN.
[11]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[12]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor receptor regulates receptor internalization."
Monami G., Emiliozzi V., Morrione A.
J. Cell. Physiol. 216:426-437(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GRB10, SUBCELLULAR LOCATION.
[14]"Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells."
Zeng F., Xu J., Harris R.C.
FASEB J. 23:1935-1945(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF ERBB4, INTERACTION WITH ERBB4.
[15]"The E3 ubiquitin ligase WWP1 selectively targets HER4 and its proteolytically derived signaling isoforms for degradation."
Feng S.M., Muraoka-Cook R.S., Hunter D., Sandahl M.A., Caskey L.S., Miyazawa K., Atfi A., Earp H.S. III
Mol. Cell. Biol. 29:892-906(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF ERBB4, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[16]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[17]"Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite development."
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.
Neuron 65:358-372(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RAP2A AND TNIK.
[18]"Structural basis for the interaction between the growth factor-binding protein GRB10 and the E3 ubiquitin ligase NEDD4."
Huang Q., Szebenyi D.M.
J. Biol. Chem. 285:42130-42139(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 71-246 IN COMPLEX WITH GRB10, INTERACTION WITH GRB10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85414 mRNA. Translation: BAA12803.1.
U96635 mRNA. Translation: AAB63360.1. Frameshift.
AK088620 mRNA. Translation: BAC40458.1.
AK088767 mRNA. Translation: BAC40558.1.
AK122203 mRNA. Translation: BAC65485.1.
AK133838 mRNA. Translation: BAE21875.1.
RefSeqNP_035020.2. NM_010890.3.
UniGeneMm.279923.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3M7FX-ray2.00B71-246[»]
ProteinModelPortalP46935.
SMRP46935. Positions 71-246, 250-281, 347-883.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201723. 43 interactions.
DIPDIP-32323N.
IntActP46935. 16 interactions.
MINTMINT-90132.

PTM databases

PhosphoSiteP46935.

Proteomic databases

PaxDbP46935.
PRIDEP46935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034740; ENSMUSP00000034740; ENSMUSG00000032216.
GeneID17999.
KEGGmmu:17999.
UCSCuc009qqe.1. mouse.

Organism-specific databases

CTD4734.
MGIMGI:97297. Nedd4.
RougeSearch...

Phylogenomic databases

eggNOGCOG5021.
GeneTreeENSGT00570000078756.
HOGENOMHOG000208451.
HOVERGENHBG004134.
InParanoidP46935.
KOK10591.
OMAYRRILSV.
OrthoDBEOG7RFTGT.
PhylomeDBP46935.
TreeFamTF323658.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressP46935.
BgeeP46935.
GenevestigatorP46935.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
PIRSFPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 3 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNEDD4. mouse.
NextBio292995.
PROP46935.
SOURCESearch...

Entry information

Entry nameNEDD4_MOUSE
AccessionPrimary (citable) accession number: P46935
Secondary accession number(s): O08758, Q3UZI2, Q8BGB3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 20, 2003
Last modified: April 16, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot