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Q8CFI0

- NED4L_MOUSE

UniProt

Q8CFI0 - NED4L_MOUSE

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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

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. sodium channel inhibitor activity Source: MGI
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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

        10         20         30         40         50
MSLCEAPVHV GDKELKYFQI PQMLSQLSLL ASHHSRGLEF SGGQGESRIL
60 70 80 90 100
RVKVVSGIDL AKKDIFGASD PYVKLSLYVA DENRELALVQ TKTIKKTLNP
110 120 130 140 150
KWNEEFYFRV NPSNHRLLFE VFDENRLTRD DFLGQVDVPL SHLPTEDPTM
160 170 180 190 200
ERPYTFKDFL LRPRSHKSRV KGFLRLKMAY MPKNGGQDEE NSEQRDDMEH
210 220 230 240 250
GWEVVDSNDS ASQHQEELPP PPLPPGWEEK VDNLGRTYYV NHNNRSTQWH
260 270 280 290 300
RPSLMDVSSE SDNNIRQINQ EAAHRRFRSR RHISEDLEPE ASEGGGEGPE
310 320 330 340 350
PWETISEEMN MAGDSLSLAL PPPPASPVSR TSPQELSEEV SRRLQITPDS
360 370 380 390 400
NGEQFSSLIQ REPSSRLRSC SVTDTVAEQA HLPPPSTPTR RARSSTVTGG
410 420 430 440 450
EEPTPSVAYV HTTPGLPSGW EERKDAKGRT YYVNHNNRTT TWTRPIMQLA
460 470 480 490 500
EDGASGSATN SNNHLVEPQI RRPRSLSSPT VTLSAPLEGA KDSPIRRAVK
510 520 530 540 550
DTLSNPQSPQ PSPYNSPKPQ HKVTQSFLPP GWEMRIAPNG RPFFIDHNTK
560 570 580 590 600
TTTWEDPRLK FPVHMRSKAS LNPNDLGPLP PGWEERIHLD GRTFYIDHNS
610 620 630 640 650
KITQWEDPRL QNPAITGPAV PYSREFKQKY DYFRKKLKKP ADIPNRFEMK
660 670 680 690 700
LHRNNIFEES YRRIMSVKRP DVLKARLWIE FESEKGLDYG GVAREWFFLL
710 720 730 740 750
SKEMFNPYYG LFEYSATDNY TLQINPNSGL CNEDHLSYFT FIGRVAGLAV
760 770 780 790 800
FHGKLLDGFF IRPFYKMMLG KQITLNDMES VDSEYYNSLK WILENDPTEL
810 820 830 840 850
DLMFCIDEEN FGQTYQVDLK PNGSEIMVTN ENKREYIDLV IQWRFVNRVQ
860 870 880 890 900
KQMNAFLEGF TELLPIDLIK IFDENELELL MCGLGDVDVN DWRQHSIYKN
910 920 930 940 950
GYCPNHPVIQ WFWKAVLLMD AEKRIRLLQF VTGTSRVPMN GFAELYGSNG
960 970 980 990 1000
PQLFTIEQWG SPEKLPRAHT CFNRLDLPPY ETFEDLREKL LMAVENAQGF

EGVD
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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

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