Q96PU5 (NED4L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase NEDD4-like
EC=6.3.2.-

Alternative name(s):
NEDD4.2
Nedd4-2

Gene names

Name:	NEDD4L
Synonyms:	KIAA0439, NEDL3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	975 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. 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. Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.29
Enzyme regulation	Activated by NDFIP1- and NDFIP2-binding.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with UBE2E3 By similarity. Interacts with NDFIP1 and NDFIP2 By similarity; this interaction activates the E3 ubiquitin-protein ligase. Interacts via its WW domains with SCNN1A, SCNN1B, SCNN1G, SCN1A, SCN2A, SCN3A, SCN5A, SCN8A, SCN9A, SCN10A and CLCN5. Interacts with SMAD2, SMAD3, SMAD6 and SMAD7. The phosphorylated form interacts with 14-3-3 proteins. Interacts with Epstein-Barr virus LMP2A. Interacts with TNK2. Interacts with WNK1. Interacts with SGK1. Interacts (via C2 domain) with NPC2. Ref.2 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.33
Subcellular location	Cytoplasm. Note: May be recruited to exosomes by NDFIP1. Ref.21 Ref.24
Tissue specificity	Ubiquitously expressed, with highest levels in prostate, pancreas and kidney. Ref.3 Ref.21 Ref.27
Induction	By androgens in prostate, and by albumin in kidney. Ref.3 Ref.17
Post-translational modification	Phosphorylated by SGK1 or PKA; which impairs interaction with SCNN. Interaction with YWHAH inhibits dephosphorylation. Ref.11 Ref.13 Ref.18 Ref.31 Ref.33 Auto-ubiquitinated.
Sequence similarities	Contains 1 C2 domain. Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 4 WW domains.
Sequence caution	The sequence BAA23711.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA23711.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
Biological process	Host-virus interaction Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular sodium ion homeostasis Non-traceable author statement PubMed 11244092. Source: UniProtKB excretion Non-traceable author statement PubMed 11244092. Source: UniProtKB ion transmembrane transport Traceable author statement. Source: Reactome negative regulation of sodium ion transport Inferred from electronic annotation. Source: Compara negative regulation of systemic arterial blood pressure Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome negative regulation of transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of cation channel activity Inferred from electronic annotation. Source: Compara positive regulation of endocytosis Non-traceable author statement PubMed 11244092. Source: UniProtKB positive regulation of sodium ion transport Inferred from electronic annotation. Source: Compara protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of membrane potential Inferred from direct assay PubMed 17289006. Source: BHF-UCL regulation of potassium ion transmembrane transporter activity Inferred from direct assay PubMed 17289006. Source: BHF-UCL regulation of protein catabolic process Non-traceable author statement PubMed 11244092. Source: UniProtKB regulation of tight junction assembly Inferred from electronic annotation. Source: Compara response to metal ion Inferred from direct assay PubMed 11244092. Source: UniProtKB response to salt stress Inferred from electronic annotation. Source: Compara sodium ion transport Non-traceable author statement PubMed 11244092. Source: UniProtKB transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW water homeostasis Non-traceable author statement PubMed 11244092. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	sodium channel inhibitor activity Inferred from electronic annotation. Source: Compara sodium channel regulator activity Inferred from direct assay PubMed 11244092. Source: UniProtKB ubiquitin-protein ligase activity Non-traceable author statement PubMed 11244092. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96PU5-1)

Also known as: Nedd4-2c;

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.

Isoform 2 (identifier: Q96PU5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     356-419: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q96PU5-3)

Also known as: NEDD4Le;

The sequence of this isoform differs from the canonical sequence as follows:
     356-459: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q96PU5-4)

Also known as: NEDD4La; NEDD4Lb; NEDD4Lf;

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.

Isoform 5 (identifier: Q96PU5-5)

Also known as: NEDD4Ld;

The sequence of this isoform differs from the canonical sequence as follows:
     356-375: Missing.

Isoform 6 (identifier: Q96PU5-6)

Also known as: NEDD4Lh;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MATGLGEPVYGLSEDE → MRRLAFEQ
     356-375: Missing.

Isoform 7 (identifier: Q96PU5-7)

Also known as: NEDD4Lg;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MATGLGEPVYGLSEDE → MRRLAFEQ

Isoform 8 (identifier: Q96PU5-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.
     356-375: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 975

975

E3 ubiquitin-protein ligase NEDD4-like

PRO_0000120323

Regions

Domain

7 – 109

103

C2

Domain

193 – 226

34

WW 1

Domain

385 – 418

34

WW 2

Domain

497 – 530

34

WW 3

Domain

548 – 581

34

WW 4

Domain

640 – 974

335

HECT

Sites

Active site

942

1

Glycyl thioester intermediate

Amino acid modifications

Modified residue

302

1

Phosphothreonine By similarity

Modified residue

318

1

Phosphothreonine Ref.26

Modified residue

342

1

Phosphoserine; by WNK1 and WNK4 Ref.18 Ref.26 Ref.31

Modified residue

367

1

Phosphothreonine; by SGK1 Probable

Modified residue

446

1

Phosphoserine Ref.26 Ref.30

Modified residue

448

1

Phosphoserine; by PKA and SGK1 Ref.11 Ref.18

Modified residue

449

1

Phosphoserine; by WNK1 and WNK4 Ref.26 Ref.31

Modified residue

464

1

Phosphoserine Ref.26

Modified residue

479

1

Phosphoserine Ref.23 Ref.26 Ref.34 Ref.36

Modified residue

483

1

Phosphoserine Ref.34 Ref.36

Modified residue

487

1

Phosphoserine Ref.26 Ref.36

Natural variations

Alternative sequence

1 – 121

121

Missing in isoform 4 and isoform 8.

VSP_015444

Alternative sequence

1 – 16

16

MATGL…LSEDE → MRRLAFEQ in isoform 6 and isoform 7.

VSP_015446

Alternative sequence

356 – 459

104

Missing in isoform 3.

VSP_015447

Alternative sequence

356 – 419

64

Missing in isoform 2.

VSP_015448

Alternative sequence

356 – 375

20

Missing in isoform 5, isoform 6 and isoform 8.

VSP_043848

Natural variant

355

1

P → L Common polymorphism; impaired ability to inhibit SCNN. Ref.37

VAR_023415

Natural variant

497

1

S → R. Ref.37

VAR_023416

Experimental info

Mutagenesis

448

1

S → A: Abolishes interaction with 1433F. Ref.11

Mutagenesis

942

1

C → S: Abolishes activity. Ref.16

Sequence conflict

52

1

A → P in AAM76729. Ref.3

Sequence conflict

52

1

A → P in AAM76730. Ref.3

Sequence conflict

188

1

E → K in AAP75706. Ref.2

Secondary structure

1

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975

Helix Strand Turn

Details...

Beta strand

9 – 11

3

Turn

16 – 18

3

Beta strand

20 – 31

12

Beta strand

43 – 51

9

Turn

52 – 55

4

Beta strand

56 – 62

7

Beta strand

73 – 82

10

Turn

84 – 86

3

Beta strand

87 – 95

9

Beta strand

98 – 100

3

Beta strand

103 – 111

9

Beta strand

129 – 132

4

Beta strand

145 – 152

8

Beta strand

391 – 396

6

Turn

397 – 399

3

Beta strand

400 – 405

6

Turn

406 – 409

4

Beta strand

410 – 414

5

Helix

417 – 419

3

Beta strand

503 – 508

6

Turn

509 – 511

3

Beta strand

512 – 517

6

Turn

518 – 521

4

Beta strand

522 – 526

5

Helix

528 – 534

7

Helix

594 – 607

14

Beta strand

612 – 614

3

Beta strand

616 – 622

7

Helix

624 – 626

3

Helix

627 – 637

11

Helix

641 – 645

5

Beta strand

646 – 652

7

Beta strand

653 – 655

3

Helix

660 – 675

16

Helix

678 – 680

3

Beta strand

681 – 687

7

Turn

688 – 690

3

Beta strand

693 – 695

3

Helix

699 – 702

4

Helix

706 – 723

18

Beta strand

728 – 731

4

Helix

733 – 739

7

Helix

746 – 749

4

Turn

750 – 752

3

Helix

754 – 765

12

Helix

769 – 771

3

Beta strand

774 – 781

8

Beta strand

784 – 791

8

Helix

794 – 796

3

Turn

801 – 803

3

Helix

804 – 816

13

Turn

817 – 819

3

Helix

821 – 834

14

Helix

837 – 840

4

Helix

845 – 853

9

Helix

860 – 865

6

Beta strand

868 – 870

3

Helix

878 – 889

12

Helix

892 – 903

12

Helix

913 – 915

3

Beta strand

926 – 929

4

Beta strand

933 – 935

3

Beta strand

938 – 940

3

Helix

941 – 943

3

Beta strand

945 – 948

4

Helix

954 – 965

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Nedd4-2c) [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 2C958625B4A1AB3F	FASTA	975	111,932
	10 20 30 40 50 60 MATGLGEPVY GLSEDEGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY VADENRELAL 70 80 90 100 110 120 VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT RDDFLGQVDV PLSHLPTEDP 130 140 150 160 170 180 TMERPYTFKD FLLRPRSHKS RVKGFLRLKM AYMPKNGGQD EENSDQRDDM EHGWEVVDSN 190 200 210 220 230 240 DSASQHQEEL PPPPLPPGWE EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS SESDNNIRQI 250 260 270 280 290 300 NQEAAHRRFR SRRHISEDLE PEPSEGGDVP EPWETISEEV NIAGDSLGLA LPPPPASPGS 310 320 330 340 350 360 RTSPQELSEE LSRRLQITPD SNGEQFSSLI QREPSSRLRS CSVTDAVAEQ GHLPPPSAPA 370 380 390 400 410 420 GRARSSTVTG GEEPTPSVAY VHTTPGLPSG WEERKDAKGR TYYVNHNNRT TTWTRPIMQL 430 440 450 460 470 480 AEDGASGSAT NSNNHLIEPQ IRRPRSLSSP TVTLSAPLEG AKDSPVRRAV KDTLSNPQSP 490 500 510 520 530 540 QPSPYNSPKP QHKVTQSFLP PGWEMRIAPN GRPFFIDHNT KTTTWEDPRL KFPVHMRSKT 550 560 570 580 590 600 SLNPNDLGPL PPGWEERIHL DGRTFYIDHN SKITQWEDPR LQNPAITGPA VPYSREFKQK 610 620 630 640 650 660 YDYFRKKLKK PADIPNRFEM KLHRNNIFEE SYRRIMSVKR PDVLKARLWI EFESEKGLDY 670 680 690 700 710 720 GGVAREWFFL LSKEMFNPYY GLFEYSATDN YTLQINPNSG LCNEDHLSYF TFIGRVAGLA 730 740 750 760 770 780 VFHGKLLDGF FIRPFYKMML GKQITLNDME SVDSEYYNSL KWILENDPTE LDLMFCIDEE 790 800 810 820 830 840 NFGQTYQVDL KPNGSEIMVT NENKREYIDL VIQWRFVNRV QKQMNAFLEG FTELLPIDLI 850 860 870 880 890 900 KIFDENELEL LMCGLGDVDV NDWRQHSIYK NGYCPNHPVI QWFWKAVLLM DAEKRIRLLQ 910 920 930 940 950 960 FVTGTSRVPM NGFAELYGSN GPQLFTIEQW GSPEKLPRAH TCFNRLDLPP YETFEDLREK 970 LLMAVENAQG FEGVD
	Isoform 2 [UniParc]. Checksum: CE04AAED677AA506	FASTA	911	104,922
	10 20 30 40 50 60 MATGLGEPVY GLSEDEGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY VADENRELAL 70 80 90 100 110 120 VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT RDDFLGQVDV PLSHLPTEDP 130 140 150 160 170 180 TMERPYTFKD FLLRPRSHKS RVKGFLRLKM AYMPKNGGQD EENSDQRDDM EHGWEVVDSN 190 200 210 220 230 240 DSASQHQEEL PPPPLPPGWE EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS SESDNNIRQI 250 260 270 280 290 300 NQEAAHRRFR SRRHISEDLE PEPSEGGDVP EPWETISEEV NIAGDSLGLA LPPPPASPGS 310 320 330 340 350 360 RTSPQELSEE LSRRLQITPD SNGEQFSSLI QREPSSRLRS CSVTDAVAEQ GHLPPLAEDG 370 380 390 400 410 420 ASGSATNSNN HLIEPQIRRP RSLSSPTVTL SAPLEGAKDS PVRRAVKDTL SNPQSPQPSP 430 440 450 460 470 480 YNSPKPQHKV TQSFLPPGWE MRIAPNGRPF FIDHNTKTTT WEDPRLKFPV HMRSKTSLNP 490 500 510 520 530 540 NDLGPLPPGW EERIHLDGRT FYIDHNSKIT QWEDPRLQNP AITGPAVPYS REFKQKYDYF 550 560 570 580 590 600 RKKLKKPADI PNRFEMKLHR NNIFEESYRR IMSVKRPDVL KARLWIEFES EKGLDYGGVA 610 620 630 640 650 660 REWFFLLSKE MFNPYYGLFE YSATDNYTLQ INPNSGLCNE DHLSYFTFIG RVAGLAVFHG 670 680 690 700 710 720 KLLDGFFIRP FYKMMLGKQI TLNDMESVDS EYYNSLKWIL ENDPTELDLM FCIDEENFGQ 730 740 750 760 770 780 TYQVDLKPNG SEIMVTNENK REYIDLVIQW RFVNRVQKQM NAFLEGFTEL LPIDLIKIFD 790 800 810 820 830 840 ENELELLMCG LGDVDVNDWR QHSIYKNGYC PNHPVIQWFW KAVLLMDAEK RIRLLQFVTG 850 860 870 880 890 900 TSRVPMNGFA ELYGSNGPQL FTIEQWGSPE KLPRAHTCFN RLDLPPYETF EDLREKLLMA 910 VENAQGFEGV D
	Isoform 3 (NEDD4Le) [UniParc]. Checksum: 5E2AB9B510060D4A	FASTA	871	100,752
	10 20 30 40 50 60 MATGLGEPVY GLSEDEGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY VADENRELAL 70 80 90 100 110 120 VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT RDDFLGQVDV PLSHLPTEDP 130 140 150 160 170 180 TMERPYTFKD FLLRPRSHKS RVKGFLRLKM AYMPKNGGQD EENSDQRDDM EHGWEVVDSN 190 200 210 220 230 240 DSASQHQEEL PPPPLPPGWE EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS SESDNNIRQI 250 260 270 280 290 300 NQEAAHRRFR SRRHISEDLE PEPSEGGDVP EPWETISEEV NIAGDSLGLA LPPPPASPGS 310 320 330 340 350 360 RTSPQELSEE LSRRLQITPD SNGEQFSSLI QREPSSRLRS CSVTDAVAEQ GHLPPGAKDS 370 380 390 400 410 420 PVRRAVKDTL SNPQSPQPSP YNSPKPQHKV TQSFLPPGWE MRIAPNGRPF FIDHNTKTTT 430 440 450 460 470 480 WEDPRLKFPV HMRSKTSLNP NDLGPLPPGW EERIHLDGRT FYIDHNSKIT QWEDPRLQNP 490 500 510 520 530 540 AITGPAVPYS REFKQKYDYF RKKLKKPADI PNRFEMKLHR NNIFEESYRR IMSVKRPDVL 550 560 570 580 590 600 KARLWIEFES EKGLDYGGVA REWFFLLSKE MFNPYYGLFE YSATDNYTLQ INPNSGLCNE 610 620 630 640 650 660 DHLSYFTFIG RVAGLAVFHG KLLDGFFIRP FYKMMLGKQI TLNDMESVDS EYYNSLKWIL 670 680 690 700 710 720 ENDPTELDLM FCIDEENFGQ TYQVDLKPNG SEIMVTNENK REYIDLVIQW RFVNRVQKQM 730 740 750 760 770 780 NAFLEGFTEL LPIDLIKIFD ENELELLMCG LGDVDVNDWR QHSIYKNGYC PNHPVIQWFW 790 800 810 820 830 840 KAVLLMDAEK RIRLLQFVTG TSRVPMNGFA ELYGSNGPQL FTIEQWGSPE KLPRAHTCFN 850 860 870 RLDLPPYETF EDLREKLLMA VENAQGFEGV D
	Isoform 4 (NEDD4La) (NEDD4Lb) (NEDD4Lf) [UniParc]. Checksum: 00C74E1661F52E7F	FASTA	854	98,181
	10 20 30 40 50 60 MERPYTFKDF LLRPRSHKSR VKGFLRLKMA YMPKNGGQDE ENSDQRDDME HGWEVVDSND 70 80 90 100 110 120 SASQHQEELP PPPLPPGWEE KVDNLGRTYY VNHNNRTTQW HRPSLMDVSS ESDNNIRQIN 130 140 150 160 170 180 QEAAHRRFRS RRHISEDLEP EPSEGGDVPE PWETISEEVN IAGDSLGLAL PPPPASPGSR 190 200 210 220 230 240 TSPQELSEEL SRRLQITPDS NGEQFSSLIQ REPSSRLRSC SVTDAVAEQG HLPPPSAPAG 250 260 270 280 290 300 RARSSTVTGG EEPTPSVAYV HTTPGLPSGW EERKDAKGRT YYVNHNNRTT TWTRPIMQLA 310 320 330 340 350 360 EDGASGSATN SNNHLIEPQI RRPRSLSSPT VTLSAPLEGA KDSPVRRAVK DTLSNPQSPQ 370 380 390 400 410 420 PSPYNSPKPQ HKVTQSFLPP GWEMRIAPNG RPFFIDHNTK TTTWEDPRLK FPVHMRSKTS 430 440 450 460 470 480 LNPNDLGPLP PGWEERIHLD GRTFYIDHNS KITQWEDPRL QNPAITGPAV PYSREFKQKY 490 500 510 520 530 540 DYFRKKLKKP ADIPNRFEMK LHRNNIFEES YRRIMSVKRP DVLKARLWIE FESEKGLDYG 550 560 570 580 590 600 GVAREWFFLL SKEMFNPYYG LFEYSATDNY TLQINPNSGL CNEDHLSYFT FIGRVAGLAV 610 620 630 640 650 660 FHGKLLDGFF IRPFYKMMLG KQITLNDMES VDSEYYNSLK WILENDPTEL DLMFCIDEEN 670 680 690 700 710 720 FGQTYQVDLK PNGSEIMVTN ENKREYIDLV IQWRFVNRVQ KQMNAFLEGF TELLPIDLIK 730 740 750 760 770 780 IFDENELELL MCGLGDVDVN DWRQHSIYKN GYCPNHPVIQ WFWKAVLLMD AEKRIRLLQF 790 800 810 820 830 840 VTGTSRVPMN GFAELYGSNG PQLFTIEQWG SPEKLPRAHT CFNRLDLPPY ETFEDLREKL 850 LMAVENAQGF EGVD
	Isoform 5 (NEDD4Ld) [UniParc]. Checksum: A8BB278A37F6A6B5	FASTA	955	110,022
	10 20 30 40 50 60 MATGLGEPVY GLSEDEGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY VADENRELAL 70 80 90 100 110 120 VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT RDDFLGQVDV PLSHLPTEDP 130 140 150 160 170 180 TMERPYTFKD FLLRPRSHKS RVKGFLRLKM AYMPKNGGQD EENSDQRDDM EHGWEVVDSN 190 200 210 220 230 240 DSASQHQEEL PPPPLPPGWE EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS SESDNNIRQI 250 260 270 280 290 300 NQEAAHRRFR SRRHISEDLE PEPSEGGDVP EPWETISEEV NIAGDSLGLA LPPPPASPGS 310 320 330 340 350 360 RTSPQELSEE LSRRLQITPD SNGEQFSSLI QREPSSRLRS CSVTDAVAEQ GHLPPPSVAY 370 380 390 400 410 420 VHTTPGLPSG WEERKDAKGR TYYVNHNNRT TTWTRPIMQL AEDGASGSAT NSNNHLIEPQ 430 440 450 460 470 480 IRRPRSLSSP TVTLSAPLEG AKDSPVRRAV KDTLSNPQSP QPSPYNSPKP QHKVTQSFLP 490 500 510 520 530 540 PGWEMRIAPN GRPFFIDHNT KTTTWEDPRL KFPVHMRSKT SLNPNDLGPL PPGWEERIHL 550 560 570 580 590 600 DGRTFYIDHN SKITQWEDPR LQNPAITGPA VPYSREFKQK YDYFRKKLKK PADIPNRFEM 610 620 630 640 650 660 KLHRNNIFEE SYRRIMSVKR PDVLKARLWI EFESEKGLDY GGVAREWFFL LSKEMFNPYY 670 680 690 700 710 720 GLFEYSATDN YTLQINPNSG LCNEDHLSYF TFIGRVAGLA VFHGKLLDGF FIRPFYKMML 730 740 750 760 770 780 GKQITLNDME SVDSEYYNSL KWILENDPTE LDLMFCIDEE NFGQTYQVDL KPNGSEIMVT 790 800 810 820 830 840 NENKREYIDL VIQWRFVNRV QKQMNAFLEG FTELLPIDLI KIFDENELEL LMCGLGDVDV 850 860 870 880 890 900 NDWRQHSIYK NGYCPNHPVI QWFWKAVLLM DAEKRIRLLQ FVTGTSRVPM NGFAELYGSN 910 920 930 940 950 GPQLFTIEQW GSPEKLPRAH TCFNRLDLPP YETFEDLREK LLMAVENAQG FEGVD
	Isoform 6 (NEDD4Lh) [UniParc]. Checksum: F107E5A8E0C3BB8D	FASTA	947	109,404
	10 20 30 40 50 60 MRRLAFEQGE SRILRVKVVS GIDLAKKDIF GASDPYVKLS LYVADENREL ALVQTKTIKK 70 80 90 100 110 120 TLNPKWNEEF YFRVNPSNHR LLFEVFDENR LTRDDFLGQV DVPLSHLPTE DPTMERPYTF 130 140 150 160 170 180 KDFLLRPRSH KSRVKGFLRL KMAYMPKNGG QDEENSDQRD DMEHGWEVVD SNDSASQHQE 190 200 210 220 230 240 ELPPPPLPPG WEEKVDNLGR TYYVNHNNRT TQWHRPSLMD VSSESDNNIR QINQEAAHRR 250 260 270 280 290 300 FRSRRHISED LEPEPSEGGD VPEPWETISE EVNIAGDSLG LALPPPPASP GSRTSPQELS 310 320 330 340 350 360 EELSRRLQIT PDSNGEQFSS LIQREPSSRL RSCSVTDAVA EQGHLPPPSV AYVHTTPGLP 370 380 390 400 410 420 SGWEERKDAK GRTYYVNHNN RTTTWTRPIM QLAEDGASGS ATNSNNHLIE PQIRRPRSLS 430 440 450 460 470 480 SPTVTLSAPL EGAKDSPVRR AVKDTLSNPQ SPQPSPYNSP KPQHKVTQSF LPPGWEMRIA 490 500 510 520 530 540 PNGRPFFIDH NTKTTTWEDP RLKFPVHMRS KTSLNPNDLG PLPPGWEERI HLDGRTFYID 550 560 570 580 590 600 HNSKITQWED PRLQNPAITG PAVPYSREFK QKYDYFRKKL KKPADIPNRF EMKLHRNNIF 610 620 630 640 650 660 EESYRRIMSV KRPDVLKARL WIEFESEKGL DYGGVAREWF FLLSKEMFNP YYGLFEYSAT 670 680 690 700 710 720 DNYTLQINPN SGLCNEDHLS YFTFIGRVAG LAVFHGKLLD GFFIRPFYKM MLGKQITLND 730 740 750 760 770 780 MESVDSEYYN SLKWILENDP TELDLMFCID EENFGQTYQV DLKPNGSEIM VTNENKREYI 790 800 810 820 830 840 DLVIQWRFVN RVQKQMNAFL EGFTELLPID LIKIFDENEL ELLMCGLGDV DVNDWRQHSI 850 860 870 880 890 900 YKNGYCPNHP VIQWFWKAVL LMDAEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQLFTIE 910 920 930 940 QWGSPEKLPR AHTCFNRLDL PPYETFEDLR EKLLMAVENA QGFEGVD
	Isoform 7 (NEDD4Lg) [UniParc]. Checksum: 9786AC67C8CD165F	FASTA	967	111,314
	10 20 30 40 50 60 MRRLAFEQGE SRILRVKVVS GIDLAKKDIF GASDPYVKLS LYVADENREL ALVQTKTIKK 70 80 90 100 110 120 TLNPKWNEEF YFRVNPSNHR LLFEVFDENR LTRDDFLGQV DVPLSHLPTE DPTMERPYTF 130 140 150 160 170 180 KDFLLRPRSH KSRVKGFLRL KMAYMPKNGG QDEENSDQRD DMEHGWEVVD SNDSASQHQE 190 200 210 220 230 240 ELPPPPLPPG WEEKVDNLGR TYYVNHNNRT TQWHRPSLMD VSSESDNNIR QINQEAAHRR 250 260 270 280 290 300 FRSRRHISED LEPEPSEGGD VPEPWETISE EVNIAGDSLG LALPPPPASP GSRTSPQELS 310 320 330 340 350 360 EELSRRLQIT PDSNGEQFSS LIQREPSSRL RSCSVTDAVA EQGHLPPPSA PAGRARSSTV 370 380 390 400 410 420 TGGEEPTPSV AYVHTTPGLP SGWEERKDAK GRTYYVNHNN RTTTWTRPIM QLAEDGASGS 430 440 450 460 470 480 ATNSNNHLIE PQIRRPRSLS SPTVTLSAPL EGAKDSPVRR AVKDTLSNPQ SPQPSPYNSP 490 500 510 520 530 540 KPQHKVTQSF LPPGWEMRIA PNGRPFFIDH NTKTTTWEDP RLKFPVHMRS KTSLNPNDLG 550 560 570 580 590 600 PLPPGWEERI HLDGRTFYID HNSKITQWED PRLQNPAITG PAVPYSREFK QKYDYFRKKL 610 620 630 640 650 660 KKPADIPNRF EMKLHRNNIF EESYRRIMSV KRPDVLKARL WIEFESEKGL DYGGVAREWF 670 680 690 700 710 720 FLLSKEMFNP YYGLFEYSAT DNYTLQINPN SGLCNEDHLS YFTFIGRVAG LAVFHGKLLD 730 740 750 760 770 780 GFFIRPFYKM MLGKQITLND MESVDSEYYN SLKWILENDP TELDLMFCID EENFGQTYQV 790 800 810 820 830 840 DLKPNGSEIM VTNENKREYI DLVIQWRFVN RVQKQMNAFL EGFTELLPID LIKIFDENEL 850 860 870 880 890 900 ELLMCGLGDV DVNDWRQHSI YKNGYCPNHP VIQWFWKAVL LMDAEKRIRL LQFVTGTSRV 910 920 930 940 950 960 PMNGFAELYG SNGPQLFTIE QWGSPEKLPR AHTCFNRLDL PPYETFEDLR EKLLMAVENA QGFEGVD
	Isoform 8 [UniParc]. Checksum: 47C33C4FB577C3DB	FASTA	834	96,271
	10 20 30 40 50 60 MERPYTFKDF LLRPRSHKSR VKGFLRLKMA YMPKNGGQDE ENSDQRDDME HGWEVVDSND 70 80 90 100 110 120 SASQHQEELP PPPLPPGWEE KVDNLGRTYY VNHNNRTTQW HRPSLMDVSS ESDNNIRQIN 130 140 150 160 170 180 QEAAHRRFRS RRHISEDLEP EPSEGGDVPE PWETISEEVN IAGDSLGLAL PPPPASPGSR 190 200 210 220 230 240 TSPQELSEEL SRRLQITPDS NGEQFSSLIQ REPSSRLRSC SVTDAVAEQG HLPPPSVAYV 250 260 270 280 290 300 HTTPGLPSGW EERKDAKGRT YYVNHNNRTT TWTRPIMQLA EDGASGSATN SNNHLIEPQI 310 320 330 340 350 360 RRPRSLSSPT VTLSAPLEGA KDSPVRRAVK DTLSNPQSPQ PSPYNSPKPQ HKVTQSFLPP 370 380 390 400 410 420 GWEMRIAPNG RPFFIDHNTK TTTWEDPRLK FPVHMRSKTS LNPNDLGPLP PGWEERIHLD 430 440 450 460 470 480 GRTFYIDHNS KITQWEDPRL QNPAITGPAV PYSREFKQKY DYFRKKLKKP ADIPNRFEMK 490 500 510 520 530 540 LHRNNIFEES YRRIMSVKRP DVLKARLWIE FESEKGLDYG GVAREWFFLL SKEMFNPYYG 550 560 570 580 590 600 LFEYSATDNY TLQINPNSGL CNEDHLSYFT FIGRVAGLAV FHGKLLDGFF IRPFYKMMLG 610 620 630 640 650 660 KQITLNDMES VDSEYYNSLK WILENDPTEL DLMFCIDEEN FGQTYQVDLK PNGSEIMVTN 670 680 690 700 710 720 ENKREYIDLV IQWRFVNRVQ KQMNAFLEGF TELLPIDLIK IFDENELELL MCGLGDVDVN 730 740 750 760 770 780 DWRQHSIYKN GYCPNHPVIQ WFWKAVLLMD AEKRIRLLQF VTGTSRVPMN GFAELYGSNG 790 800 810 820 830 PQLFTIEQWG SPEKLPRAHT CFNRLDLPPY ETFEDLREKL LMAVENAQGF EGVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"NEDD4L on human chromosome 18q21 has multiple forms of transcripts and is a homologue of the mouse Nedd4-2 gene." Chen H., Ross C.A., Wang N., Huo Y., MacKinnon D.F., Potash J.B., Simpson S.G., McMahon F.J., DePaulo J.R. Jr., McInnis M.G. Eur. J. Hum. Genet. 9:922-930(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING.
[2]	"Identification of new partners of the epithelial sodium channel alpha subunit." Malbert-Colas L., Nicolas G., Galand C., Lecomte M.-C., Dhermy D. C. R. Biol. 326:615-624(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G. Tissue: Kidney.
[3]	"Androgens differentially regulate the expression of NEDD4L transcripts in LNCaP human prostate cancer cells." Qi H., Grenier J., Fournier A., Labrie C. Mol. Cell. Endocrinol. 210:51-62(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 7), TISSUE SPECIFICITY, INDUCTION. Tissue: Prostate.
[4]	"Homo sapiens NEDD4-like ubiquitin ligase 3." Okamoto Y., Miyazaki K., Sakamoto M., Kato C., Nakagawara A. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[5]	"NEDD4L transcripts expressed in human prostate cells." Qi H., Labrie C. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
[6]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-975 (ISOFORM 5). Tissue: Skin and Uterus.
[9]	"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro." Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8). Tissue: Brain.
[10]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-975 (ISOFORM 3). Tissue: Testis.
[11]	"14-3-3 proteins modulate the expression of epithelial Na+ channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase." Ichimura T., Yamamura H., Sasamoto K., Tominaga Y., Taoka M., Kakiuchi K., Shinkawa T., Takahashi N., Shimada S., Isobe T. J. Biol. Chem. 280:13187-13194(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 448-462, INTERACTION WITH YWHAB; YWHAG; YWHAE; YWHAQ AND YWHAH, PHOSPHORYLATION AT SER-448, MUTAGENESIS OF SER-448, MASS SPECTROMETRY.
[12]	"Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases." Winberg G., Matskova L., Chen F., Plant P., Rotin D., Gish G., Ingham R., Ernberg I., Pawson T. Mol. Cell. Biol. 20:8526-8535(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
[13]	"Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel." Snyder P.M., Olson D.R., Thomas B.C. J. Biol. Chem. 277:5-8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SGK1 AND SCNN1A, PHOSPHORYLATION.
[14]	"N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein." Harvey K.F., Shearwin-Whyatt L.M., Fotia A., Parton R.G., Kumar S. J. Biol. Chem. 277:9307-9317(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDFIP1.
[15]	"Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B." Boehmer C., Henke G., Schniepp R., Palmada M., Rothstein J.D., Broeer S., Lang F. J. Neurochem. 86:1181-1188(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination." van Bemmelen M.X., Rougier J.-S., Gavillet B., Apotheloz F., Daidie D., Tateyama M., Rivolta I., Thomas M.A., Kass R.S., Staub O., Abriel H. Circ. Res. 95:284-291(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-942, INTERACTION WITH SCN5A.
[17]	"Nedd4-2 functionally interacts with ClC-5: involvement in constitutive albumin endocytosis in proximal tubule cells." Hryciw D.H., Ekberg J., Lee A., Lensink I.L., Kumar S., Guggino W.B., Cook D.I., Pollock C.A., Poronnik P. J. Biol. Chem. 279:54996-55007(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CLCN5, INDUCTION.
[18]	"cAMP and serum and glucocorticoid-inducible kinase (SGK) regulate the epithelial Na(+) channel through convergent phosphorylation of Nedd4-2." Snyder P.M., Olson D.R., Kabra R., Zhou R., Steines J.C. J. Biol. Chem. 279:45753-45758(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-342; THR-367 AND SER-448.
[19]	"Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1." Henke G., Maier G., Wallisch S., Boehmer C., Lang F. J. Cell. Physiol. 199:194-199(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Molecular determinants of voltage-gated sodium channel regulation by the Nedd4/Nedd4-like proteins." Rougier J.-S., van Bemmelen M.X., Bruce M.C., Jespersen T., Gavillet B., Apotheloz F., Cordonier S., Staub O., Rotin D., Abriel H. Am. J. Physiol. 288:C692-C701(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCN2A; SCN3A AND SCN5A.
[21]	"NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor." Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., Imamura T. Biochem. J. 386:461-470(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD6 AND SMAD7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[22]	"Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation." Zhou R., Snyder P.M. J. Biol. Chem. 280:4518-4523(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Nedd4 family-interacting protein 1 (Ndfip1) is required for the exosomal secretion of Nedd4 family proteins." Putz U., Howitt J., Lackovic J., Foot N., Kumar S., Silke J., Tan S.S. J. Biol. Chem. 283:32621-32627(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[25]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[26]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-342; SER-446; SER-449; SER-464; SER-479 AND SER-487, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Identification of NPC2 protein as interaction molecule with C2 domain of human Nedd4L." Araki N., Ishigami T., Ushio H., Minegishi S., Umemura M., Miyagi Y., Aoki I., Morinaga H., Tamura K., Toya Y., Uchino K., Umemura S. Biochem. Biophys. Res. Commun. 388:290-296(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NPC2, TISSUE SPECIFICITY.
[28]	"Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins." Mund T., Pelham H.R. EMBO Rep. 10:501-507(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVATION BY NDFIP1 AND NDFIP2, AUTOUBIQUITINATION.
[29]	"Down-regulation of active ACK1 is mediated by association with the E3 ubiquitin ligase Nedd4-2." Chan W., Tian R., Lee Y.-F., Sit S.T., Lim L., Manser E. J. Biol. Chem. 284:8185-8194(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A UBIQUITIN-PROTEIN LIGASE FOR TNK2, INTERACTION WITH TNK2.
[30]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[31]	"Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium channel are regulated by multiple with no lysine (WNK) family members." Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S., Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L., Cobb M.H. J. Biol. Chem. 285:25161-25167(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-342 AND SER-449, INTERACTION WITH WNK1.
[32]	"HECT E3 ubiquitin ligase Nedd4-1 ubiquitinates ACK and regulates epidermal growth factor (EGF)-induced degradation of EGF receptor and ACK." Lin Q., Wang J., Childress C., Sudol M., Carey D.J., Yang W. Mol. Cell. Biol. 30:1541-1554(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNK2.
[33]	"Interaction of serum- and glucocorticoid regulated kinase 1 (SGK1) with the WW-domains of Nedd4-2 is required for epithelial sodium channel regulation." Wiemuth D., Lott J.S., Ly K., Ke Y., Teesdale-Spittle P., Snyder P.M., McDonald F.J. PLoS ONE 5:E12163-E12163(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY SGK1, INTERACTION WITH SGK1.
[34]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 AND SER-483, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; SER-483 AND SER-487, MASS SPECTROMETRY.
[37]	"A naturally occurring human Nedd4-2 variant displays impaired ENaC regulation in Xenopus laevis oocytes." Fouladkou F., Alikhani-Koopaei R., Vogt B., Flores S.Y., Malbert-Colas L., Lecomte M.-C., Loffing J., Frey F.J., Frey B.M., Staub O. Am. J. Physiol. 287:F550-F561(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LEU-355 AND ARG-497.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF210730 mRNA. Translation: AAG43524.1.
AF385931 mRNA. Translation: AAM46208.1.
AY312514 mRNA. Translation: AAP75706.1.
AY112983 mRNA. Translation: AAM76728.1.
AY112984 mRNA. Translation: AAM76729.1.
AY112985 mRNA. Translation: AAM76730.1.
AB071179 mRNA. Translation: BAB69424.1.
DQ181796 mRNA. Translation: ABA10330.1.
AC015988 Genomic DNA. No translation available.
AC090236 Genomic DNA. No translation available.
AC107896 Genomic DNA. No translation available.
CH471096 Genomic DNA. Translation: EAW63065.1.
BC000621 mRNA. Translation: AAH00621.2.
BC019345 mRNA. Translation: AAH19345.1.
BC032597 mRNA. Translation: AAH32597.1.
AB007899 mRNA. Translation: BAA23711.1. Different initiation.
AL137469 mRNA. Translation: CAB70754.1.

IPI

IPI00023287.
IPI00163321.
IPI00166830.
IPI00640924.
IPI00643856.
IPI00644256.
IPI00645053.
IPI00941170.

PIR

T46412.

RefSeq

NP_001138436.1. NM_001144964.1.
NP_001138437.1. NM_001144965.1.
NP_001138438.1. NM_001144966.2.
NP_001138439.1. NM_001144967.2.
NP_001138440.1. NM_001144968.1.
NP_001138441.1. NM_001144969.1.
NP_001138442.1. NM_001144970.2.
NP_001138443.1. NM_001144971.1.
NP_001230889.1. NM_001243960.1.
NP_056092.2. NM_015277.5.

UniGene

Hs.185677.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LAJ	NMR	-	A	496-535	[»]
2LB2	NMR	-	A	386-420	[»]
2LTY	NMR	-	A	385-417	[»]
2NSQ	X-ray	1.85	A	1-154	[»]
2ONI	X-ray	2.20	A	594-967	[»]
3JVZ	X-ray	3.30	C/D	596-975	[»]
3JW0	X-ray	3.10	C/D	596-975	[»]

ProteinModelPortal

Q96PU5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41935N.

IntAct

Q96PU5. 8 interactions.

MINT

MINT-148327.

PTM databases

PhosphoSite

Q96PU5.

Polymorphism databases

DMDM

73921204.

Proteomic databases

PaxDb

Q96PU5.

PRIDE

Q96PU5.

Protocols and materials databases

DNASU

23327.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256830; ENSP00000256830; ENSG00000049759.
ENST00000356462; ENSP00000348847; ENSG00000049759.
ENST00000357895; ENSP00000350569; ENSG00000049759.
ENST00000382850; ENSP00000372301; ENSG00000049759.
ENST00000400345; ENSP00000383199; ENSG00000049759.
ENST00000431212; ENSP00000389406; ENSG00000049759.
ENST00000435432; ENSP00000393395; ENSG00000049759.
ENST00000456173; ENSP00000405440; ENSG00000049759.
ENST00000456986; ENSP00000411947; ENSG00000049759.
ENST00000586263; ENSP00000468546; ENSG00000049759.

GeneID

23327.

KEGG

hsa:23327.

UCSC

uc002lgx.3. human.
uc002lgy.3. human.
uc002lgz.3. human.
uc002lhb.2. human.
uc002lhc.2. human.
uc002lhe.2. human.
uc002lhh.2. human.

Organism-specific databases

CTD

23327.

GeneCards

GC18P055711.

HGNC

HGNC:7728. NEDD4L.

HPA

HPA024618.

MIM

606384. gene.

neXtProt

NX_Q96PU5.

PharmGKB

PA31534.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5021.

HOVERGEN

HBG004134.

KO

K13305.

OMA

PPSVAYV.

Enzyme and pathway databases

Pathway_Interaction_DB

trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.
REACT_71. Gene Expression.

SignaLink

Q96PU5.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q96PU5.

Bgee

Q96PU5.

Genevestigator

Q96PU5.

GermOnline

ENSG00000049759. Homo sapiens.

Family and domain databases

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020477. C2_dom.
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. 4 hits.
[Graphical view]

PIRSF

PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.

PRINTS

PR00360. C2DOMAIN.

SMART

SM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56204. HECT. 1 hit.
SSF51045. WW_Rsp5_WWP. 4 hits.

PROSITE

PS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NEDD4L. human.

EvolutionaryTrace

Q96PU5.

GenomeRNAi

23327.

NextBio

45240.

SOURCE

Search...

Entry information

Entry name

NED4L_HUMAN

Accession

Primary (citable) accession number: Q96PU5
Secondary accession number(s): O43165 , Q3LSM7, Q7Z5F1, Q7Z5F2, Q7Z5N3, Q8N5A7, Q8WUU9, Q9BW58, Q9H2W4, Q9NT88

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	May 29, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.