Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8CFI0

- NED4L_MOUSE

UniProt

Q8CFI0 - NED4L_MOUSE

Protein

E3 ubiquitin-protein ligase NEDD4-like

Gene

Nedd4l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK1 and TNK2.5 Publications

    Enzyme regulationi

    Activated by NDFIP1- and NDFIP2-binding. Interacts with SGK1.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei971 – 9711Glycyl thioester intermediate

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. sodium channel inhibitor activity Source: MGI
    4. ubiquitin-protein transferase activity Source: MGI

    GO - Biological processi

    1. negative regulation of sodium ion transport Source: MGI
    2. negative regulation of systemic arterial blood pressure Source: MGI
    3. positive regulation of cation channel activity Source: MGI
    4. positive regulation of sodium ion transport Source: MGI
    5. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
    6. regulation of tight junction assembly Source: MGI
    7. response to salt stress Source: MGI
    8. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Protein family/group databases

    TCDBi8.A.30.1.1. the nedd4-family interacting protein-2 (nedd4) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase NEDD4-like (EC:6.3.2.-)
    Alternative name(s):
    NEDD4.2
    Nedd4-2
    Gene namesi
    Name:Nedd4l
    Synonyms:Kiaa0439, Nedd4b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1933754. Nedd4l.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. nucleus Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi371 – 3711S → A: Weakly reduces phosphorylation by SGK1. 1 Publication
    Mutagenesisi477 – 4771S → A: Strongly reduces phosphorylation by SGK1. 1 Publication
    Mutagenesisi971 – 9711C → S: Abolishes catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10041004E3 ubiquitin-protein ligase NEDD4-likePRO_0000120324Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei347 – 3471PhosphothreonineBy similarity
    Modified residuei371 – 3711Phosphoserine; by WNK1 and WNK41 Publication
    Modified residuei396 – 3961Phosphothreonine; by SGK1By similarity
    Modified residuei475 – 4751PhosphoserineBy similarity
    Modified residuei477 – 4771Phosphoserine; by SGK12 Publications
    Modified residuei478 – 4781Phosphoserine; by WNK1 and WNK4By similarity
    Modified residuei493 – 4931PhosphoserineBy similarity
    Modified residuei508 – 5081Phosphoserine1 Publication
    Modified residuei512 – 5121PhosphoserineBy similarity
    Modified residuei516 – 5161PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated; which impairs interaction with SCNN. Interaction with YWHAH inhibits dephosphorylation By similarity. Aldosterone induces Ser-477 phosphorylation by SGK1.By similarity3 Publications
    Auto-ubiquitinated.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8CFI0.
    PaxDbiQ8CFI0.
    PRIDEiQ8CFI0.

    PTM databases

    PhosphoSiteiQ8CFI0.

    Expressioni

    Tissue specificityi

    Highly expressed in liver and kidney. Also expressed in heart, brain and lung. Isoform 1 is expressed in kidney, lung and gut. Isoform 3 is ubiquitously expressed.2 Publications

    Gene expression databases

    GenevestigatoriQ8CFI0.

    Interactioni

    Subunit structurei

    Interacts with SMAD2, SMAD3, SMAD6 and SMAD7. Interacts with CLCN5. The phosphorylated form interacts with 14-3-3 proteins. Interacts with NDIF1P in vitro By similarity. Interacts via its WW domains with SCNN1A, SCNN1B, SCNN1G, SCN1A, SCN2A, SCN3A, SCN5A, SCN8A, SCN9A and SCN10A. Interacts with UBE2E3. Interacts with NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-protein ligase. Interacts with TNK2 By similarity. Interacts (via C2 domain) with NPC2 By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-48843N.
    IntActiQ8CFI0. 2 interactions.
    MINTiMINT-5097552.

    Structurei

    Secondary structure

    1
    1004
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi227 – 2315
    Beta strandi233 – 2353
    Beta strandi237 – 2415
    Turni242 – 2443
    Beta strandi247 – 2504
    Beta strandi420 – 4245
    Beta strandi426 – 4283
    Beta strandi430 – 4345
    Turni435 – 4384
    Beta strandi439 – 4435
    Beta strandi532 – 5365
    Beta strandi542 – 5465
    Turni547 – 5504
    Beta strandi551 – 5555
    Helixi557 – 5593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WR3NMR-A221-254[»]
    1WR4NMR-A414-447[»]
    1WR7NMR-A525-560[»]
    ProteinModelPortaliQ8CFI0.
    SMRiQ8CFI0. Positions 40-182, 221-254, 415-449, 525-560, 569-617, 623-995.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8CFI0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 137103C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini221 – 25434WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini414 – 44734WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini526 – 55934WW 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini577 – 61034WW 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini669 – 1003335HECTPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi321 – 3244Poly-Pro

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 4 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5021.
    HOGENOMiHOG000208451.
    HOVERGENiHBG004134.
    InParanoidiQ8CFI0.
    PhylomeDBiQ8CFI0.

    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. 4 hits.
    [Graphical view]
    PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    PRINTSiPR00360. C2DOMAIN.
    SMARTiSM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 4 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 4 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 4 hits.
    PS50020. WW_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CFI0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSLCEAPVHV GDKELKYFQI PQMLSQLSLL ASHHSRGLEF SGGQGESRIL     50
    RVKVVSGIDL AKKDIFGASD PYVKLSLYVA DENRELALVQ TKTIKKTLNP 100
    KWNEEFYFRV NPSNHRLLFE VFDENRLTRD DFLGQVDVPL SHLPTEDPTM 150
    ERPYTFKDFL LRPRSHKSRV KGFLRLKMAY MPKNGGQDEE NSEQRDDMEH 200
    GWEVVDSNDS ASQHQEELPP PPLPPGWEEK VDNLGRTYYV NHNNRSTQWH 250
    RPSLMDVSSE SDNNIRQINQ EAAHRRFRSR RHISEDLEPE ASEGGGEGPE 300
    PWETISEEMN MAGDSLSLAL PPPPASPVSR TSPQELSEEV SRRLQITPDS 350
    NGEQFSSLIQ REPSSRLRSC SVTDTVAEQA HLPPPSTPTR RARSSTVTGG 400
    EEPTPSVAYV HTTPGLPSGW EERKDAKGRT YYVNHNNRTT TWTRPIMQLA 450
    EDGASGSATN SNNHLVEPQI RRPRSLSSPT VTLSAPLEGA KDSPIRRAVK 500
    DTLSNPQSPQ PSPYNSPKPQ HKVTQSFLPP GWEMRIAPNG RPFFIDHNTK 550
    TTTWEDPRLK FPVHMRSKAS LNPNDLGPLP PGWEERIHLD GRTFYIDHNS 600
    KITQWEDPRL QNPAITGPAV PYSREFKQKY DYFRKKLKKP ADIPNRFEMK 650
    LHRNNIFEES YRRIMSVKRP DVLKARLWIE FESEKGLDYG GVAREWFFLL 700
    SKEMFNPYYG LFEYSATDNY TLQINPNSGL CNEDHLSYFT FIGRVAGLAV 750
    FHGKLLDGFF IRPFYKMMLG KQITLNDMES VDSEYYNSLK WILENDPTEL 800
    DLMFCIDEEN FGQTYQVDLK PNGSEIMVTN ENKREYIDLV IQWRFVNRVQ 850
    KQMNAFLEGF TELLPIDLIK IFDENELELL MCGLGDVDVN DWRQHSIYKN 900
    GYCPNHPVIQ WFWKAVLLMD AEKRIRLLQF VTGTSRVPMN GFAELYGSNG 950
    PQLFTIEQWG SPEKLPRAHT CFNRLDLPPY ETFEDLREKL LMAVENAQGF 1000
    EGVD 1004
    Length:1,004
    Mass (Da):115,419
    Last modified:August 30, 2005 - v2
    Checksum:i50CBB3436052AA60
    GO
    Isoform 2 (identifier: Q8CFI0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-149: Missing.

    Show »
    Length:855
    Mass (Da):98,466
    Checksum:i96C452B442855895
    GO
    Isoform 3 (identifier: Q8CFI0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         385-404: Missing.

    Show »
    Length:984
    Mass (Da):113,350
    Checksum:iB6888DF5810B6362
    GO

    Sequence cautioni

    The sequence BAC31307.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti179 – 1791A → G in AAK00809. (PubMed:11149908)Curated
    Sequence conflicti390 – 3901R → G in AAK00809. (PubMed:11149908)Curated
    Sequence conflicti403 – 4031P → S in AAK00809. (PubMed:11149908)Curated
    Sequence conflicti585 – 5851E → G in AAK00809. (PubMed:11149908)Curated
    Sequence conflicti832 – 8321N → T in AAK00809. (PubMed:11149908)Curated
    Sequence conflicti847 – 8471N → D in AAK00809. (PubMed:11149908)Curated
    Sequence conflicti949 – 9491N → K in BAC31307. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 149149Missing in isoform 2. 2 PublicationsVSP_015450Add
    BLAST
    Alternative sequencei385 – 40420Missing in isoform 3. 2 PublicationsVSP_015453Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF277232 mRNA. Translation: AAK00809.1.
    BC039746 mRNA. Translation: AAH39746.1.
    BC071210 mRNA. Translation: AAH71210.1.
    AK042621 mRNA. Translation: BAC31307.1. Different initiation.
    CCDSiCCDS29305.1. [Q8CFI0-2]
    UniGeneiMm.98668.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF277232 mRNA. Translation: AAK00809.1 .
    BC039746 mRNA. Translation: AAH39746.1 .
    BC071210 mRNA. Translation: AAH71210.1 .
    AK042621 mRNA. Translation: BAC31307.1 . Different initiation.
    CCDSi CCDS29305.1. [Q8CFI0-2 ]
    UniGenei Mm.98668.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WR3 NMR - A 221-254 [» ]
    1WR4 NMR - A 414-447 [» ]
    1WR7 NMR - A 525-560 [» ]
    ProteinModelPortali Q8CFI0.
    SMRi Q8CFI0. Positions 40-182, 221-254, 415-449, 525-560, 569-617, 623-995.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48843N.
    IntActi Q8CFI0. 2 interactions.
    MINTi MINT-5097552.

    Protein family/group databases

    TCDBi 8.A.30.1.1. the nedd4-family interacting protein-2 (nedd4) family.

    PTM databases

    PhosphoSitei Q8CFI0.

    Proteomic databases

    MaxQBi Q8CFI0.
    PaxDbi Q8CFI0.
    PRIDEi Q8CFI0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:1933754. Nedd4l.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOGENOMi HOG000208451.
    HOVERGENi HBG004134.
    InParanoidi Q8CFI0.
    PhylomeDBi Q8CFI0.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi NEDD4L. mouse.
    EvolutionaryTracei Q8CFI0.
    PROi Q8CFI0.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q8CFI0.

    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. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    PRINTSi PR00360. C2DOMAIN.
    SMARTi SM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 4 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 4 hits.
    PS50020. WW_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel."
      Kamynina E., Debonneville C., Bens M., Vandewalle A., Staub O.
      FASEB J. 15:204-214(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF CYS-971.
      Strain: C57BL/6.
    2. "The role of individual Nedd4-2 (KIAA0439) WW domains in binding and regulating epithelial sodium channels."
      Fotia A.B., Dinudom A., Shearwin K.E., Koch J.-P., Korbmacher C., Cook D.I., Kumar S.
      FASEB J. 17:70-72(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G, FUNCTION.
      Tissue: Brain.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Kidney and Mammary gland.
    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] OF 44-1004 (ISOFORM 3).
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    5. "Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell surface expression."
      Debonneville C., Flores S.Y., Kamynina E., Plant P.J., Tauxe C., Thomas M.A., Muenster C., Chraiebi A., Pratt J.H., Horisberger J.-D., Pearce D., Loffing J., Staub O.
      EMBO J. 20:7052-7059(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G, PHOSPHORYLATION AT SER-371 AND SER-477, MUTAGENESIS OF SER-371 AND SER-477.
    6. "The Nedd4-like protein KIAA0439 is a potential regulator of the epithelial sodium channel."
      Harvey K.F., Dinudom A., Cook D.I., Kumar S.
      J. Biol. Chem. 276:8597-8601(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G, TISSUE SPECIFICITY.
    7. "Regulation of the epithelial sodium channel by N4WBP5A, a novel Nedd4/Nedd4-2-interacting protein."
      Konstas A.-A., Shearwin-Whyatt L.M., Fotia A.B., Degger B., Riccardi D., Cook D.I., Korbmacher C., Kumar S.
      J. Biol. Chem. 277:29406-29416(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDFIP2, SUBCELLULAR LOCATION.
    8. "Regulation of neuronal voltage-gated sodium channels by the ubiquitin-protein ligases Nedd4 and Nedd4-2."
      Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.
      J. Biol. Chem. 279:28930-28935(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SCN1A; SCN2A; SCN3A; SCN5A; SCN8A; SCN9A; SCN10A; SCNN1A; SCNN1B AND SCNN1G.
    9. "Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-dependent regulation of the epithelial Na+ channel."
      Debonneville C., Staub O.
      Mol. Cell. Biol. 24:2397-2409(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2E3.
    10. "Aldosterone-induced serum and glucocorticoid-induced kinase 1 expression is accompanied by nedd4-2 phosphorylation and increased na+ transport in cortical collecting duct cells."
      Flores S.Y., Loffing-Cueni D., Kamynina E., Daidie D., Gerbex C., Chabanel S., Dudler J., Loffing J., Staub O.
      J. Am. Soc. Nephrol. 16:2279-2287(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-477.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "Solution structures of WW domains of NEDD4-2."
      Kowalski K., Merkel A.L., Booker G.W.
      Submitted (OCT-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 221-254; 414-447 AND 525-560.

    Entry informationi

    Entry nameiNED4L_MOUSE
    AccessioniPrimary (citable) accession number: Q8CFI0
    Secondary accession number(s): Q8BRT9, Q8BS42, Q99PK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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