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P46935

- NEDD4_MOUSE

UniProt

P46935 - NEDD4_MOUSE

Protein

E3 ubiquitin-protein ligase NEDD4

Gene

Nedd4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (20 Jun 2003)
      Previous versions | rss
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    Functioni

    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 (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 By similarity.By similarity2 Publications

    Enzyme regulationi

    Activated by NDFIP1- and NDFIP2-binding.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei854 – 8541Glycyl thioester intermediate

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. phosphoserine binding Source: BHF-UCL
    3. phosphothreonine binding Source: BHF-UCL
    4. proline-rich region binding Source: MGI
    5. protein binding Source: UniProtKB
    6. sodium channel inhibitor activity Source: MGI
    7. ubiquitin-protein transferase activity Source: MGI

    GO - Biological processi

    1. adaptive immune response Source: MGI
    2. blood vessel morphogenesis Source: MGI
    3. development involved in symbiotic interaction Source: Ensembl
    4. endocardial cushion development Source: MGI
    5. glucocorticoid receptor signaling pathway Source: Ensembl
    6. negative regulation of sodium ion transport Source: MGI
    7. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    8. negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage Source: Ensembl
    9. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    10. neuromuscular junction development Source: MGI
    11. neuron projection development Source: Ensembl
    12. outflow tract morphogenesis Source: MGI
    13. positive regulation of nucleocytoplasmic transport Source: Ensembl
    14. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    15. positive regulation of protein catabolic process Source: MGI
    16. progesterone receptor signaling pathway Source: Ensembl
    17. protein K63-linked ubiquitination Source: UniProtKB
    18. protein monoubiquitination Source: MGI
    19. protein targeting to lysosome Source: Ensembl
    20. protein ubiquitination Source: MGI
    21. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
    22. receptor catabolic process Source: Ensembl
    23. receptor internalization Source: Ensembl
    24. regulation of dendrite morphogenesis Source: UniProtKB
    25. regulation of membrane potential Source: Ensembl
    26. regulation of potassium ion transmembrane transporter activity Source: Ensembl
    27. regulation of synapse organization Source: MGI
    28. T cell activation Source: MGI
    29. transmission of virus Source: Ensembl
    30. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Neurogenesis, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_198533. ISG15 antiviral mechanism.
    REACT_199100. Downregulation of ERBB4 signaling.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Nedd4
    Synonyms:Kiaa0093, Nedd-4, Nedd4-1, Nedd4a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:97297. Nedd4.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cell cortex Source: Ensembl
    2. chromatin Source: Ensembl
    3. cytoplasm Source: MGI
    4. cytosol Source: MGI
    5. Golgi apparatus Source: Ensembl
    6. membrane Source: MGI
    7. nucleus Source: RefGenome
    8. perinuclear region of cytoplasm Source: Ensembl
    9. plasma membrane Source: UniProtKB-SubCell
    10. ubiquitin ligase complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Lethal during late gestation. Embryos show a retarded development and defects in vasculogenesis and angiogenesis.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi854 – 8541C → S: Loss of ubiquitin-ligase activity. No effect on VEGFR-2/KDFR degradation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 887887E3 ubiquitin-protein ligase NEDD4PRO_0000120320Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei287 – 2871Phosphothreonine1 Publication
    Modified residuei309 – 3091Phosphoserine; by host3 Publications
    Modified residuei385 – 3851Phosphoserine; by hostBy similarity

    Post-translational modificationi

    Auto-ubiquitinated.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP46935.
    PaxDbiP46935.
    PRIDEiP46935.

    PTM databases

    PhosphoSiteiP46935.

    Expressioni

    Tissue specificityi

    Brain.

    Gene expression databases

    ArrayExpressiP46935.
    BgeeiP46935.
    GenevestigatoriP46935.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bean1Q9EQG53EBI-773516,EBI-6304006
    Grb10Q607606EBI-773516,EBI-861810
    LitafQ9JLJ05EBI-773516,EBI-643664
    Ndfip1Q8R0W65EBI-773516,EBI-6304119
    Pmepa1Q9D7R25EBI-773516,EBI-6304097
    Prrg2Q8R1825EBI-773516,EBI-6304055
    Rnf11Q9QYK74EBI-773516,EBI-4405826
    Wbp1P977643EBI-773516,EBI-6304160
    Wbp2P977655EBI-773516,EBI-6304181

    Protein-protein interaction databases

    BioGridi201723. 45 interactions.
    DIPiDIP-32323N.
    IntActiP46935. 16 interactions.
    MINTiMINT-90132.

    Structurei

    Secondary structure

    1
    887
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi78 – 8912
    Beta strandi101 – 1099
    Turni110 – 1123
    Beta strandi113 – 1197
    Beta strandi130 – 13910
    Turni141 – 1433
    Beta strandi145 – 1528
    Beta strandi160 – 16910
    Beta strandi186 – 1894
    Beta strandi201 – 2099

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3M7FX-ray2.00B71-246[»]
    ProteinModelPortaliP46935.
    SMRiP46935. Positions 71-246, 250-281, 406-883.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 166102C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini249 – 28234WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 43834WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini460 – 49334WW 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini552 – 887336HECTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni217 – 549333Mediates interaction with TNIKAdd
    BLAST

    Domaini

    The WW domains mediate interaction with LITAF, RNF11, WBP1, WBP2, TMEPAI, NDFIP1 and PRRG2.1 Publication

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 3 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5021.
    GeneTreeiENSGT00570000078756.
    HOGENOMiHOG000208451.
    HOVERGENiHBG004134.
    InParanoidiP46935.
    KOiK10591.
    OMAiYRRILSV.
    OrthoDBiEOG7RFTGT.
    PhylomeDBiP46935.
    TreeFamiTF323658.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 3 hits.
    [Graphical view]
    PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTiSM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 3 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 3 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 3 hits.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P46935-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSDMAADES EAPVLSEDEV WEFCLDKTED GGGSPGSDVT DTCEPPCGCW    50
    ELNPNSLEEE HVLFTADPYL ELHNDDTRVV RVKVIAGIGL AKKDILGASD 100
    PYVRVTLYDP MSGILTSVQT KTIKKSLNPK WNEEILFRVL PQRHRILFEV 150
    FDENRLTRDD FLGQVDVPLY PLPTENPRME RPYTFKDFVL HPRSHKSRVK 200
    GYLRLKMTYL PKNGSEDENA DQAEELEPGW VVLDQPDAAT HLPHPPEPSP 250
    LPPGWEERQD VLGRTYYVNH ESRRTQWKRP SPDDDLTDED NDDMQLQAQR 300
    AFTTRRQISE DVDGPDNRES PENWEIVRED ENTEYSGQAV QSPPSGHIDV 350
    QTHLAEEFNT RLAVCGNPAT SQPVTSSNHS SRGGSLQTCI FEEQPTLPVL 400
    LPTSSGLPPG WEEKQDDRGR SYYVDHNSKT TTWSKPTMQD DPRSKIPAHL 450
    RGKTDSNDLG PLPPGWEERT HTDGRVFFIN HNIKKTQWED PRLQNVAITG 500
    PAVPYSRDYK RKYEFFRRKL KKQTDIPNKF EMKLRRANIL EDSYRRIMGV 550
    KRADLLKARL WIEFDGEKGL DYGGVAREWF FLISKEMFNP YYGLFEYSAT 600
    DNYTLQINPN SGLCNEDHLS YFKFIGRVAG MAVYHGKLLD GFFIRPFYKM 650
    MLQKLITLHD MESVDSEYYS SLRWILENDP TELDLRFIID EELFGQTHQH 700
    ELKTGGSEIV VTNKNKKEYI YLVIQWRFVN RIQKQMAAFK EGFFELIPQD 750
    LIKIFDENEL ELLMCGLGDV DVNDWREHTK YKNGYSMNHQ VIHWFWKAVW 800
    MMDSEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQSFTVE QWGTPDKLPR 850
    AHTCFNRLDL PPYESFDELW DKLQMAIENT QGFDGVD 887
    Length:887
    Mass (Da):102,706
    Last modified:June 20, 2003 - v3
    Checksum:iAE7DD3ED63986C50
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS72275.1.
    RefSeqiNP_035020.2. NM_010890.3.
    UniGeneiMm.279923.

    Genome annotation databases

    EnsembliENSMUST00000034740; ENSMUSP00000034740; ENSMUSG00000032216.
    GeneIDi17999.
    KEGGimmu:17999.
    UCSCiuc009qqe.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS72275.1.
    RefSeqi NP_035020.2. NM_010890.3.
    UniGenei Mm.279923.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3M7F X-ray 2.00 B 71-246 [» ]
    ProteinModelPortali P46935.
    SMRi P46935. Positions 71-246, 250-281, 406-883.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201723. 45 interactions.
    DIPi DIP-32323N.
    IntActi P46935. 16 interactions.
    MINTi MINT-90132.

    PTM databases

    PhosphoSitei P46935.

    Proteomic databases

    MaxQBi P46935.
    PaxDbi P46935.
    PRIDEi P46935.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034740 ; ENSMUSP00000034740 ; ENSMUSG00000032216 .
    GeneIDi 17999.
    KEGGi mmu:17999.
    UCSCi uc009qqe.1. mouse.

    Organism-specific databases

    CTDi 4734.
    MGIi MGI:97297. Nedd4.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5021.
    GeneTreei ENSGT00570000078756.
    HOGENOMi HOG000208451.
    HOVERGENi HBG004134.
    InParanoidi P46935.
    KOi K10591.
    OMAi YRRILSV.
    OrthoDBi EOG7RFTGT.
    PhylomeDBi P46935.
    TreeFami TF323658.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_198533. ISG15 antiviral mechanism.
    REACT_199100. Downregulation of ERBB4 signaling.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi NEDD4. mouse.
    NextBioi 292995.
    PROi P46935.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46935.
    Bgeei P46935.
    Genevestigatori P46935.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTi SM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 3 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 3 hits.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiNEDD4_MOUSE
    AccessioniPrimary (citable) accession number: P46935
    Secondary accession number(s): O08758, Q3UZI2, Q8BGB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 20, 2003
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    A cysteine residue is required for ubiquitin-thioester formation.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3