P46935 (NEDD4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Nedd4
Synonyms:	Kiaa0093, Nedd-4, Nedd4-1, Nedd4a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15). 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.16). 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. Ref.9 Ref.13 Ref.15 Ref.16 Ref.18
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. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19
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.16
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.18
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 process	Neurogenesis Ubl conjugation pathway
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T 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: Compara endocardial cushion development Inferred from mutant phenotype PubMed 20026598. Source: MGI glucocorticoid receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara outflow tract morphogenesis Inferred from mutant phenotype PubMed 20026598. Source: MGI positive regulation of nucleocytoplasmic transport Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase cascade Inferred from electronic annotation. Source: Compara positive regulation of protein catabolic process Inferred from direct assay PubMed 11748237. Source: MGI progesterone receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara receptor internalization Inferred from electronic annotation. Source: Compara regulation of dendrite morphogenesis Inferred from mutant phenotype Ref.18. Source: UniProtKB regulation of membrane potential Inferred from electronic annotation. Source: Compara regulation of potassium ion transmembrane transporter activity Inferred from electronic annotation. Source: Compara regulation of synapse organization Inferred from mutant phenotype PubMed 19345204. Source: MGI transmission of virus Inferred from electronic annotation. Source: Compara ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cell cortex Inferred from electronic annotation. Source: Compara chromatin Inferred from electronic annotation. Source: Compara 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: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Inferred from physical interaction Ref.7. Source: MGI
Molecular_function	phosphoserine binding Inferred from direct assay PubMed 10037602. Source: BHF-UCL phosphothreonine binding Inferred from direct assay PubMed 10037602. Source: BHF-UCL 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bean1	Q9EQG5	3	EBI-773516,EBI-6304006
Grb10	Q60760	6	EBI-773516,EBI-861810
Litaf	Q9JLJ0	5	EBI-773516,EBI-643664
Ndfip1	Q8R0W6	5	EBI-773516,EBI-6304119
Pmepa1	Q9D7R2	5	EBI-773516,EBI-6304097
Prrg2	Q8R182	5	EBI-773516,EBI-6304055
Rnf11	Q9QYK7	4	EBI-773516,EBI-4405826
Wbp1	P97764	3	EBI-773516,EBI-6304160
Wbp2	P97765	5	EBI-773516,EBI-6304181

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 887

887

E3 ubiquitin-protein ligase NEDD4

PRO_0000120320

Regions

Domain

65 – 166

102

C2

Domain

249 – 282

34

WW 1

Domain

405 – 438

34

WW 2

Domain

460 – 493

34

WW 3

Domain

552 – 887

336

HECT

Region

217 – 549

333

Mediates interaction with TNIK

Sites

Active site

854

1

Glycyl thioester intermediate

Amino acid modifications

Modified residue

287

1

Phosphothreonine Ref.12 Ref.14 Ref.17

Modified residue

309

1

Phosphoserine; by host Ref.11 Ref.14 Ref.17

Modified residue

385

1

Phosphoserine; by host By similarity

Experimental info

Mutagenesis

854

1

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

887

Helix Strand Turn

Details...

Beta strand

78 – 89

12

Beta strand

101 – 109

9

Turn

110 – 112

3

Beta strand

113 – 119

7

Beta strand

130 – 139

10

Turn

141 – 143

3

Beta strand

145 – 152

8

Beta strand

160 – 169

10

Beta strand

186 – 189

4

Beta strand

201 – 209

9

Sequences

	Sequence		Length	Mass (Da)
	P46935 [UniParc]. Last modified June 20, 2003. Version 3. Checksum: AE7DD3ED63986C50	FASTA	887	102,706
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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 THR-287, MASS SPECTROMETRY. 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, MASS SPECTROMETRY. Tissue: Melanoma.
[15]	"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.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[18]	"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.
[19]	"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.

IPI

IPI00462445.

RefSeq

NP_035020.2. NM_010890.3.

UniGene

Mm.279923.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M7F	X-ray	2.00	B	71-246	[»]

ProteinModelPortal

P46935.

SMR

P46935. Positions 71-246, 250-281, 406-880.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32323N.

IntAct

P46935. 11 interactions.

MINT

MINT-90132.

PTM databases

PhosphoSite

P46935.

Proteomic databases

PaxDb

P46935.

PRIDE

P46935.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034740; ENSMUSP00000034740; ENSMUSG00000032216.

GeneID

17999.

KEGG

mmu:17999.

Organism-specific databases

CTD

4734.

MGI

MGI:97297. Nedd4.

Rouge

Search...

Phylogenomic databases

eggNOG

COG5021.

GeneTree

ENSGT00570000078756.

HOGENOM

HOG000208451.

HOVERGEN

HBG004134.

InParanoid

P46935.

KO

K10591.

OMA

YRRILSV.

OrthoDB

EOG4P5K8F.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P46935.

Bgee

P46935.

Genevestigator

P46935.

GermOnline

ENSMUSG00000032216. Mus musculus.

Family and domain databases

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]

PIRSF

PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.

SMART

SM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56204. HECT. 1 hit.
SSF51045. WW_Rsp5_WWP. 3 hits.

PROSITE

PS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 3 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NEDD4. mouse.

NextBio

292995.

SOURCE

Search...

Entry information

Entry name

NEDD4_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program