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P46935

- NEDD4_MOUSE

UniProt

P46935 - NEDD4_MOUSE

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Protein

E3 ubiquitin-protein ligase NEDD4

Gene
Nedd4, Kiaa0093, Nedd-4, Nedd4-1, Nedd4a
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 (1 Publication). 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 (1 Publication). 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.5 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
Complete GO annotation...

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 NDFIP1.3 Publications

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
Complete GO annotation...

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 host By 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.11 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 166102C2Add
BLAST
Domaini249 – 28234WW 1Add
BLAST
Domaini405 – 43834WW 2Add
BLAST
Domaini460 – 49334WW 3Add
BLAST
Domaini552 – 887336HECTAdd
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.
Contains 3 WW domains.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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