P46934 (NEDD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Cell proliferation-inducing gene 53 protein
Neural precursor cell expressed developmentally down-regulated protein 4
Short name=NEDD-4

Gene names

Name:	NEDD4
Synonyms:	KIAA0093, NEDD4-1
ORF Names:	PIG53

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	1319 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. Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. According to Ref.12 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in Ref.1 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. 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. Ref.1 Ref.12 Ref.14 Ref.18 Ref.23
Enzyme regulation	Activated by NDFIP1- and NDFIP2-binding By similarity.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with UBE2D2. Binds SCNN1A, SCNN1B and SCNN1G. 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 By similarity. Interacts with NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-protein ligase and may induce its recruitment to exosomes By similarity. Interaction with PTEN is questionable according to Ref.12. Interacts with viral proteins that contain a late- budding motif P-P-P-Y. This interaction is essential for viral particle budding of a lot of retroviruses, like HTLV-1 Gag and MLV Gag. Interacts (via C2 domain) with GRB10 (via SH2 domain). Interacts with ERBB4 By similarity. 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. Ref.1 Ref.9 Ref.12 Ref.14 Ref.15 Ref.18 Ref.19
Subcellular location	Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. 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.10
Domain	The WW domains mediate interaction with LITAF, RNF11, WBP1, WBP2, TMEPAI, NDFIP1 and PRRG2 By similarity.
Post-translational modification	Auto-ubiquitinated By similarity.
Miscellaneous	A cysteine residue is required for ubiquitin-thioester formation.
Sequence similarities	Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 4 WW domains.
Sequence caution	The sequence BAA07655.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Host-virus interaction Neurogenesis Ubl conjugation pathway
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
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 electronic annotation. Source: Compara adaptive immune response Inferred from electronic annotation. Source: Compara blood vessel morphogenesis Inferred from electronic annotation. Source: Compara cytokine-mediated signaling pathway Traceable author statement. Source: Reactome development involved in symbiotic interaction Inferred from mutant phenotype PubMed 15126635. Source: UniProtKB endocardial cushion development Inferred from electronic annotation. Source: Compara glucocorticoid receptor signaling pathway Inferred from direct assay PubMed 8649367. Source: BHF-UCL negative regulation of sodium ion transport Inferred from direct assay PubMed 10642508. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage Inferred from mutant phenotype PubMed 17996703. Source: BHF-UCL negative regulation of vascular endothelial growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB neuromuscular junction development Inferred from electronic annotation. Source: Compara neuron projection development Inferred from expression pattern PubMed 9990509. Source: BHF-UCL outflow tract morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of nucleocytoplasmic transport Inferred from direct assay PubMed 17218261. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase cascade Inferred from mutant phenotype Ref.1. Source: BHF-UCL positive regulation of protein catabolic process Inferred from direct assay PubMed 14973438. Source: MGI progesterone receptor signaling pathway Inferred from direct assay PubMed 8649367. Source: BHF-UCL protein K63-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein monoubiquitination Inferred from electronic annotation. Source: Compara protein targeting to lysosome Inferred from direct assay PubMed 17116753. Source: UniProtKB protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.14. Source: BHF-UCL receptor catabolic process Inferred from direct assay PubMed 18544533. Source: UniProtKB receptor internalization Inferred from direct assay PubMed 18544533. Source: UniProtKB regulation of dendrite morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB 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 synapse organization Inferred from electronic annotation. Source: Compara response to calcium ion Traceable author statement PubMed 9405440. Source: BHF-UCL transmission of virus Inferred from mutant phenotype PubMed 15126635. Source: BHF-UCL ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred from mutant phenotype Ref.14. Source: BHF-UCL virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 16118794. Source: UniProtKB apicolateral plasma membrane Traceable author statement PubMed 9405440. Source: BHF-UCL cell cortex Inferred from direct assay PubMed 9990509. Source: BHF-UCL chromatin Inferred from direct assay PubMed 17996703. Source: BHF-UCL cytosol Inferred from sequence or structural similarity. Source: BHF-UCL nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome perinuclear region of cytoplasm Inferred from direct assay PubMed 9990509. Source: BHF-UCL ubiquitin ligase complex Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	beta-2 adrenergic receptor binding Inferred from direct assay PubMed 18544533. Source: UniProtKB phosphoserine binding Inferred from sequence or structural similarity. Source: BHF-UCL phosphothreonine binding Inferred from sequence or structural similarity. Source: BHF-UCL proline-rich region binding Inferred from mutant phenotype PubMed 15126635. Source: BHF-UCL sodium channel inhibitor activity Inferred from direct assay PubMed 10642508. Source: BHF-UCL ubiquitin binding Inferred from direct assay PubMed 9990509. Source: BHF-UCL ubiquitin-protein ligase activity Inferred from direct assay PubMed 17996703Ref.14. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAP	O95166	6	EBI-726944,EBI-712001
GABARAPL1	Q9H0R8	6	EBI-726944,EBI-746969
GABARAPL2	P60520	6	EBI-726944,EBI-720116
LITAF	Q99732	4	EBI-726944,EBI-725647
PTEN	P60484	4	EBI-726944,EBI-696162

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P46934-1)

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.

Note: No experimental confirmation available.

Isoform 2 (identifier: P46934-2)

The sequence of this isoform differs from the canonical sequence as follows:
     589-604: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P46934-3)

The sequence of this isoform differs from the canonical sequence as follows:
     517-588: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: P46934-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-419: Missing.
     420-516: SACLPSSQNV...CTNELSNSCK → MATCAVEVFG...LFEVFDENRL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1319

1319

E3 ubiquitin-protein ligase NEDD4

PRO_0000120319

Regions

Domain

610 – 643

34

WW 1

Domain

767 – 800

34

WW 2

Domain

840 – 873

34

WW 3

Domain

892 – 925

34

WW 4

Domain

984 – 1318

335

HECT

Region

578 – 981

404

Mediates interaction with TNIK By similarity

Compositional bias

68 – 215

148

Ser-rich

Sites

Active site

1286

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

648

1

Phosphothreonine By similarity

Modified residue

670

1

Phosphoserine By similarity

Modified residue

747

1

Phosphoserine Ref.11 Ref.13

Natural variations

Alternative sequence

1 – 419

419

Missing in isoform 4.

VSP_038256

Alternative sequence

420 – 516

97

SACLP…SNSCK → MATCAVEVFGLLEDEENSRI VRVRVIAGIGLAKKDILGAS DPYVRVTLYDPMNGVLTSVQ TKTIKKSLNPKWNEEILFRV HPQQHRLLFEVFDENRL in isoform 4.

VSP_038257

Alternative sequence

517 – 588

72

Missing in isoform 3.

VSP_038258

Alternative sequence

589 – 604

16

Missing in isoform 2.

VSP_038259

Natural variant

33

1

M → V.
Corresponds to variant rs1912403 [ dbSNP | Ensembl ].

VAR_061985

Natural variant

627

1

Y → H in a breast cancer sample; somatic mutation. Ref.24

VAR_036472

Natural variant

679

1

R → Q. Ref.2 Ref.3 Ref.4 Ref.6 Ref.8
Corresponds to variant rs2303580 [ dbSNP | Ensembl ].

VAR_047909

Natural variant

698

1

N → S. Ref.2 Ref.3 Ref.4 Ref.6 Ref.8
Corresponds to variant rs2303579 [ dbSNP | Ensembl ].

VAR_047910

Experimental info

Sequence conflict

59

1

A → T in AL832063. Ref.5

Sequence conflict

407

1

N → H in AL832063. Ref.5

Sequence conflict

620

1

Q → R in AAT52215. Ref.4

Sequence conflict

620

1

Q → R in AAI44285. Ref.8

Sequence conflict

863

1

T → I in AAI36606. Ref.8

Sequence conflict

863

1

T → I in AAI44285. Ref.8

Sequence conflict

1199

1

L → P in BAG65229. Ref.3

Sequence conflict

1268

1

S → L in AL832063. Ref.5

Secondary structure

1

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1319

Helix Strand Turn

Details...

Beta strand

520 – 528

9

Beta strand

546 – 549

4

Beta strand

561 – 569

9

Beta strand

846 – 850

5

Turn

852 – 854

3

Beta strand

856 – 860

5

Turn

861 – 864

4

Beta strand

865 – 869

5

Turn

871 – 873

3

Helix

941 – 951

11

Beta strand

956 – 958

3

Beta strand

960 – 966

7

Helix

968 – 970

3

Helix

971 – 979

9

Helix

985 – 989

5

Beta strand

990 – 996

7

Helix

1004 – 1019

16

Helix

1022 – 1024

3

Beta strand

1025 – 1031

7

Beta strand

1037 – 1039

3

Helix

1043 – 1046

4

Helix

1050 – 1066

17

Beta strand

1071 – 1073

3

Helix

1077 – 1083

7

Helix

1090 – 1094

5

Helix

1098 – 1109

12

Helix

1113 – 1115

3

Beta strand

1118 – 1125

8

Beta strand

1128 – 1135

8

Helix

1138 – 1140

3

Turn

1145 – 1147

3

Helix

1148 – 1160

13

Helix

1162 – 1164

3

Helix

1165 – 1175

11

Turn

1176 – 1178

3

Helix

1181 – 1184

4

Helix

1189 – 1197

9

Helix

1204 – 1209

6

Beta strand

1211 – 1214

4

Beta strand

1219 – 1221

3

Helix

1222 – 1233

12

Helix

1236 – 1247

12

Beta strand

1248 – 1250

3

Helix

1257 – 1259

3

Beta strand

1263 – 1266

4

Beta strand

1269 – 1273

5

Beta strand

1282 – 1284

3

Helix

1285 – 1287

3

Beta strand

1289 – 1292

4

Helix

1298 – 1310

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 30, 2010. Version 4. Checksum: D56EBBC50A34F13B	FASTA	1,319	149,114
	10 20 30 40 50 60 MAQSLRLHFA ARRSNTYPLS ETSGDDLDSH VHMCFKRPTR ISTSNVVQMK LTPRQTALAP 70 80 90 100 110 120 LIKENVQSQE RSSVPSSENV NKKSSCLQIS LQPTRYSGYL QSSNVLADSD DASFTCILKD 130 140 150 160 170 180 GIYSSAVVDN ELNAVNDGHL VSSPAICSGS LSNFSTSDNG SYSSNGSDFG SCASITSGGS 190 200 210 220 230 240 YTNSVISDSS SYTFPPSDDT FLGGNLPSDS TSNRSVPNRN TTPCEIFSRS TSTDPFVQDD 250 260 270 280 290 300 LEHGLEIMKL PVSRNTKIPL KRYSSLVIFP RSPSTTRPTS PTSLCTLLSK GSYQTSHQFI 310 320 330 340 350 360 ISPSEIAHNE DGTSAKGFLS TAVNGLRLSK TICTPGEVRD IRPLHRKGSL QKKIVLSNNT 370 380 390 400 410 420 PRQTVCEKSS EGYSCVSVHF TQRKAATLDC ETTNGDCKPE MSEIKLNSDS EYIKLMHRTS 430 440 450 460 470 480 ACLPSSQNVD CQININGELE RPHSQMNKNH GILRRSISLG GAYPNISCLS SLKHNCSKGG 490 500 510 520 530 540 PSQLLIKFAS GNEGKVDNLS RDSNRDCTNE LSNSCKTRDD FLGQVDVPLY PLPTENPRLE 550 560 570 580 590 600 RPYTFKDFVL HPRSHKSRVK GYLRLKMTYL PKTSGSEDDN AEQAEELEPG WVVLDQPDAA 610 620 630 640 650 660 CHLQQQQEPS PLPPGWEERQ DILGRTYYVN HESRRTQWKR PTPQDNLTDA ENGNIQLQAQ 670 680 690 700 710 720 RAFTTRRQIS EETESVDNRE SSENWEIIRE DEATMYSNQA FPSPPPSSNL DVPTHLAEEL 730 740 750 760 770 780 NARLTIFGNS AVSQPASSSN HSSRRGSLQA YTFEEQPTLP VLLPTSSGLP PGWEEKQDER 790 800 810 820 830 840 GRSYYVDHNS RTTTWTKPTV QATVETSQLT SSQSSAGPQS QASTSDSGQQ VTQPSEIEQG 850 860 870 880 890 900 FLPKGWEVRH APNGRPFFID HNTKTTTWED PRLKIPAHLR GKTSLDTSND LGPLPPGWEE 910 920 930 940 950 960 RTHTDGRIFY INHNIKRTQW EDPRLENVAI TGPAVPYSRD YKRKYEFFRR KLKKQNDIPN 970 980 990 1000 1010 1020 KFEMKLRRAT VLEDSYRRIM GVKRADFLKA RLWIEFDGEK GLDYGGVARE WFFLISKEMF 1030 1040 1050 1060 1070 1080 NPYYGLFEYS ATDNYTLQIN PNSGLCNEDH LSYFKFIGRV AGMAVYHGKL LDGFFIRPFY 1090 1100 1110 1120 1130 1140 KMMLHKPITL HDMESVDSEY YNSLRWILEN DPTELDLRFI IDEELFGQTH QHELKNGGSE 1150 1160 1170 1180 1190 1200 IVVTNKNKKE YIYLVIQWRF VNRIQKQMAA FKEGFFELIP QDLIKIFDEN ELELLMCGLG 1210 1220 1230 1240 1250 1260 DVDVNDWREH TKYKNGYSAN HQVIQWFWKA VLMMDSEKRI RLLQFVTGTS RVPMNGFAEL 1270 1280 1290 1300 1310 YGSNGPQSFT VEQWGTPEKL PRAHTCFNRL DLPPYESFEE LWDKLQMAIE NTQGFDGVD
	Isoform 2 [UniParc]. Checksum: C40112E4C9BC8416	FASTA	1,303	147,384
	10 20 30 40 50 60 MAQSLRLHFA ARRSNTYPLS ETSGDDLDSH VHMCFKRPTR ISTSNVVQMK LTPRQTALAP 70 80 90 100 110 120 LIKENVQSQE RSSVPSSENV NKKSSCLQIS LQPTRYSGYL QSSNVLADSD DASFTCILKD 130 140 150 160 170 180 GIYSSAVVDN ELNAVNDGHL VSSPAICSGS LSNFSTSDNG SYSSNGSDFG SCASITSGGS 190 200 210 220 230 240 YTNSVISDSS SYTFPPSDDT FLGGNLPSDS TSNRSVPNRN TTPCEIFSRS TSTDPFVQDD 250 260 270 280 290 300 LEHGLEIMKL PVSRNTKIPL KRYSSLVIFP RSPSTTRPTS PTSLCTLLSK GSYQTSHQFI 310 320 330 340 350 360 ISPSEIAHNE DGTSAKGFLS TAVNGLRLSK TICTPGEVRD IRPLHRKGSL QKKIVLSNNT 370 380 390 400 410 420 PRQTVCEKSS EGYSCVSVHF TQRKAATLDC ETTNGDCKPE MSEIKLNSDS EYIKLMHRTS 430 440 450 460 470 480 ACLPSSQNVD CQININGELE RPHSQMNKNH GILRRSISLG GAYPNISCLS SLKHNCSKGG 490 500 510 520 530 540 PSQLLIKFAS GNEGKVDNLS RDSNRDCTNE LSNSCKTRDD FLGQVDVPLY PLPTENPRLE 550 560 570 580 590 600 RPYTFKDFVL HPRSHKSRVK GYLRLKMTYL PKTSGSEDDN AEQAEELEQQ QEPSPLPPGW 610 620 630 640 650 660 EERQDILGRT YYVNHESRRT QWKRPTPQDN LTDAENGNIQ LQAQRAFTTR RQISEETESV 670 680 690 700 710 720 DNRESSENWE IIREDEATMY SNQAFPSPPP SSNLDVPTHL AEELNARLTI FGNSAVSQPA 730 740 750 760 770 780 SSSNHSSRRG SLQAYTFEEQ PTLPVLLPTS SGLPPGWEEK QDERGRSYYV DHNSRTTTWT 790 800 810 820 830 840 KPTVQATVET SQLTSSQSSA GPQSQASTSD SGQQVTQPSE IEQGFLPKGW EVRHAPNGRP 850 860 870 880 890 900 FFIDHNTKTT TWEDPRLKIP AHLRGKTSLD TSNDLGPLPP GWEERTHTDG RIFYINHNIK 910 920 930 940 950 960 RTQWEDPRLE NVAITGPAVP YSRDYKRKYE FFRRKLKKQN DIPNKFEMKL RRATVLEDSY 970 980 990 1000 1010 1020 RRIMGVKRAD FLKARLWIEF DGEKGLDYGG VAREWFFLIS KEMFNPYYGL FEYSATDNYT 1030 1040 1050 1060 1070 1080 LQINPNSGLC NEDHLSYFKF IGRVAGMAVY HGKLLDGFFI RPFYKMMLHK PITLHDMESV 1090 1100 1110 1120 1130 1140 DSEYYNSLRW ILENDPTELD LRFIIDEELF GQTHQHELKN GGSEIVVTNK NKKEYIYLVI 1150 1160 1170 1180 1190 1200 QWRFVNRIQK QMAAFKEGFF ELIPQDLIKI FDENELELLM CGLGDVDVND WREHTKYKNG 1210 1220 1230 1240 1250 1260 YSANHQVIQW FWKAVLMMDS EKRIRLLQFV TGTSRVPMNG FAELYGSNGP QSFTVEQWGT 1270 1280 1290 1300 PEKLPRAHTC FNRLDLPPYE SFEELWDKLQ MAIENTQGFD GVD
	Isoform 3 [UniParc]. Checksum: 827AC55FB4AFB6A3	FASTA	1,247	140,696
	10 20 30 40 50 60 MAQSLRLHFA ARRSNTYPLS ETSGDDLDSH VHMCFKRPTR ISTSNVVQMK LTPRQTALAP 70 80 90 100 110 120 LIKENVQSQE RSSVPSSENV NKKSSCLQIS LQPTRYSGYL QSSNVLADSD DASFTCILKD 130 140 150 160 170 180 GIYSSAVVDN ELNAVNDGHL VSSPAICSGS LSNFSTSDNG SYSSNGSDFG SCASITSGGS 190 200 210 220 230 240 YTNSVISDSS SYTFPPSDDT FLGGNLPSDS TSNRSVPNRN TTPCEIFSRS TSTDPFVQDD 250 260 270 280 290 300 LEHGLEIMKL PVSRNTKIPL KRYSSLVIFP RSPSTTRPTS PTSLCTLLSK GSYQTSHQFI 310 320 330 340 350 360 ISPSEIAHNE DGTSAKGFLS TAVNGLRLSK TICTPGEVRD IRPLHRKGSL QKKIVLSNNT 370 380 390 400 410 420 PRQTVCEKSS EGYSCVSVHF TQRKAATLDC ETTNGDCKPE MSEIKLNSDS EYIKLMHRTS 430 440 450 460 470 480 ACLPSSQNVD CQININGELE RPHSQMNKNH GILRRSISLG GAYPNISCLS SLKHNCSKGG 490 500 510 520 530 540 PSQLLIKFAS GNEGKVDNLS RDSNRDCTNE LSNSCKPGWV VLDQPDAACH LQQQQEPSPL 550 560 570 580 590 600 PPGWEERQDI LGRTYYVNHE SRRTQWKRPT PQDNLTDAEN GNIQLQAQRA FTTRRQISEE 610 620 630 640 650 660 TESVDNRESS ENWEIIREDE ATMYSNQAFP SPPPSSNLDV PTHLAEELNA RLTIFGNSAV 670 680 690 700 710 720 SQPASSSNHS SRRGSLQAYT FEEQPTLPVL LPTSSGLPPG WEEKQDERGR SYYVDHNSRT 730 740 750 760 770 780 TTWTKPTVQA TVETSQLTSS QSSAGPQSQA STSDSGQQVT QPSEIEQGFL PKGWEVRHAP 790 800 810 820 830 840 NGRPFFIDHN TKTTTWEDPR LKIPAHLRGK TSLDTSNDLG PLPPGWEERT HTDGRIFYIN 850 860 870 880 890 900 HNIKRTQWED PRLENVAITG PAVPYSRDYK RKYEFFRRKL KKQNDIPNKF EMKLRRATVL 910 920 930 940 950 960 EDSYRRIMGV KRADFLKARL WIEFDGEKGL DYGGVAREWF FLISKEMFNP YYGLFEYSAT 970 980 990 1000 1010 1020 DNYTLQINPN SGLCNEDHLS YFKFIGRVAG MAVYHGKLLD GFFIRPFYKM MLHKPITLHD 1030 1040 1050 1060 1070 1080 MESVDSEYYN SLRWILENDP TELDLRFIID EELFGQTHQH ELKNGGSEIV VTNKNKKEYI 1090 1100 1110 1120 1130 1140 YLVIQWRFVN RIQKQMAAFK EGFFELIPQD LIKIFDENEL ELLMCGLGDV DVNDWREHTK 1150 1160 1170 1180 1190 1200 YKNGYSANHQ VIQWFWKAVL MMDSEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQSFTVE 1210 1220 1230 1240 QWGTPEKLPR AHTCFNRLDL PPYESFEELW DKLQMAIENT QGFDGVD
	Isoform 4 [UniParc]. Checksum: 4303287D3133B1C7	FASTA	900	104,217
	10 20 30 40 50 60 MATCAVEVFG LLEDEENSRI VRVRVIAGIG LAKKDILGAS DPYVRVTLYD PMNGVLTSVQ 70 80 90 100 110 120 TKTIKKSLNP KWNEEILFRV HPQQHRLLFE VFDENRLTRD DFLGQVDVPL YPLPTENPRL 130 140 150 160 170 180 ERPYTFKDFV LHPRSHKSRV KGYLRLKMTY LPKTSGSEDD NAEQAEELEP GWVVLDQPDA 190 200 210 220 230 240 ACHLQQQQEP SPLPPGWEER QDILGRTYYV NHESRRTQWK RPTPQDNLTD AENGNIQLQA 250 260 270 280 290 300 QRAFTTRRQI SEETESVDNR ESSENWEIIR EDEATMYSNQ AFPSPPPSSN LDVPTHLAEE 310 320 330 340 350 360 LNARLTIFGN SAVSQPASSS NHSSRRGSLQ AYTFEEQPTL PVLLPTSSGL PPGWEEKQDE 370 380 390 400 410 420 RGRSYYVDHN SRTTTWTKPT VQATVETSQL TSSQSSAGPQ SQASTSDSGQ QVTQPSEIEQ 430 440 450 460 470 480 GFLPKGWEVR HAPNGRPFFI DHNTKTTTWE DPRLKIPAHL RGKTSLDTSN DLGPLPPGWE 490 500 510 520 530 540 ERTHTDGRIF YINHNIKRTQ WEDPRLENVA ITGPAVPYSR DYKRKYEFFR RKLKKQNDIP 550 560 570 580 590 600 NKFEMKLRRA TVLEDSYRRI MGVKRADFLK ARLWIEFDGE KGLDYGGVAR EWFFLISKEM 610 620 630 640 650 660 FNPYYGLFEY SATDNYTLQI NPNSGLCNED HLSYFKFIGR VAGMAVYHGK LLDGFFIRPF 670 680 690 700 710 720 YKMMLHKPIT LHDMESVDSE YYNSLRWILE NDPTELDLRF IIDEELFGQT HQHELKNGGS 730 740 750 760 770 780 EIVVTNKNKK EYIYLVIQWR FVNRIQKQMA AFKEGFFELI PQDLIKIFDE NELELLMCGL 790 800 810 820 830 840 GDVDVNDWRE HTKYKNGYSA NHQVIQWFWK AVLMMDSEKR IRLLQFVTGT SRVPMNGFAE 850 860 870 880 890 900 LYGSNGPQSF TVEQWGTPEK LPRAHTCFNR LDLPPYESFE ELWDKLQMAI ENTQGFDGVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN." Wang X., Trotman L.C., Koppie T., Alimonti A., Chen Z., Gao Z., Wang J., Erdjument-Bromage H., Tempst P., Cordon-Cardo C., Pandolfi P.P., Jiang X. Cell 128:129-139(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, UBIQUITIN LIGASE ACTIVITY, INTERACTION WITH PTEN.
[2]	"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N. DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS GLN-679 AND SER-698. Tissue: Bone marrow.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS GLN-679 AND SER-698. Tissue: Trachea.
[4]	"Identification of a human cell proliferation inducing gene." Kim J.W. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS GLN-679 AND SER-698.
[5]	"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 [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Adipose tissue.
[6]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLN-679 AND SER-698.
[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] (ISOFORMS 1; 2 AND 4), VARIANTS GLN-679 AND SER-698. Tissue: Brain and Testis.
[9]	"PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101." Bouamr F., Melillo J.A., Wang M.Q., Nagashima K., de Los Santos M., Rein A., Goff S.P. J. Virol. 77:11882-11895(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTLV-1 MATRIX PROTEIN P19.
[10]	"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.
[11]	"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 SER-747, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization." Fouladkou F., Landry T., Kawabe H., Neeb A., Lu C., Brose N., Stambolic V., Rotin D. Proc. Natl. Acad. Sci. U.S.A. 105:8585-8590(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTEN.
[13]	"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-747, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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: FUNCTION, INTERACTION WITH TNK2.
[15]	"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: INTERACTION WITH RAP2A AND TNIK.
[16]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function." Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D. EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGFR1, FUNCTION IN UBIQUITINATION OF FGFR1.
[19]	"Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression." Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F., Aulmann S., Ben-Chetrit N., Pines G., Navon R., Crosetto N., Kostler W., Carvalho S., Lavi S., Schmitt F., Dikic I., Yakhini Z., Sinn P., Mills G.B., Yarden Y. Oncogene 31:4599-4608(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH OTUD7B.
[20]	"Crystal structure of the C2 domain of the E3 ubiquitin-protein ligase Nedd4." Structural genomics consortium (SGC) Submitted (OCT-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-152 (ISOFORM 4).
[21]	"Human NEDD4 3rd WW domain complex with ebola Zaire virus matrix protein VP40 derived peptide." Iglesias-Bexiga M. Submitted (OCT-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 834-878.
[22]	"Human NEDD4 3rd WW domain complex with human T-cell leukemia virus GAP-Pro polyprotein derived peptide." Iglesias-Bexiga M., Luque I., Macias M. Submitted (OCT-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 834-878.
[23]	"Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation." Maspero E., Mari S., Valentini E., Musacchio A., Fish A., Pasqualato S., Polo S. EMBO Rep. 12:342-349(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 938-1319 IN COMPLEX WITH UBIQUITIN, FUNCTION.
[24]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-627.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D42055 mRNA. Translation: BAA07655.1. Different initiation.
AK304394 mRNA. Translation: BAG65229.1.
AY550969 mRNA. Translation: AAT52215.1.
AL832063 Genomic DNA. No translation available.
AC009997 Genomic DNA. No translation available.
AC039057 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77495.1.
BC136605 mRNA. Translation: AAI36606.1.
BC144284 mRNA. Translation: AAI44285.1.
BC144285 mRNA. Translation: AAI44286.1.
BC152452 mRNA. Translation: AAI52453.1.
BC152562 mRNA. Translation: AAI52563.1.

IPI

IPI00384495.
IPI00940829.
IPI00945379.
IPI00969091.

RefSeq

NP_006145.2. NM_006154.2.
NP_940682.2. NM_198400.2.

UniGene

Hs.1565.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KPZ	NMR	-	A	834-878	[»]
2KQ0	NMR	-	A	834-878	[»]
2XBB	X-ray	2.68	A/B	938-1319	[»]
2XBF	X-ray	2.50	A	938-1319	[»]
3B7Y	X-ray	1.80	A/B	517-571	[»]

ProteinModelPortal

P46934.

SMR

P46934. Positions 517-571, 611-642, 768-1312.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29815N.

IntAct

P46934. 11 interactions.

MINT

MINT-86457.

STRING

9606.ENSP00000345530.

PTM databases

PhosphoSite

P46934.

Polymorphism databases

DMDM

261260094.

Proteomic databases

PaxDb

P46934.

PRIDE

P46934.

Protocols and materials databases

DNASU

4734.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338963; ENSP00000345530; ENSG00000069869.
ENST00000435532; ENSP00000410613; ENSG00000069869.
ENST00000506154; ENSP00000422705; ENSG00000069869.
ENST00000508342; ENSP00000424827; ENSG00000069869.

GeneID

4734.

KEGG

hsa:4734.

UCSC

uc002adi.3. human.
uc002adj.3. human.
uc002adl.3. human.
uc010ugj.2. human.

Organism-specific databases

CTD

4734.

GeneCards

GC15M056119.

HGNC

HGNC:7727. NEDD4.

HPA

CAB001991.
HPA039883.

MIM

602278. gene.

neXtProt

NX_P46934.

PharmGKB

PA31533.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5021.

HOVERGEN

HBG004134.

KO

K10591.

OMA

YRRILSV.

OrthoDB

EOG4P5K8F.

Enzyme and pathway databases

Pathway_Interaction_DB

ps1pathway. Presenilin action in Notch and Wnt signaling.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

SignaLink

P46934.

UniPathway

UPA00143.

Gene expression databases

Bgee

P46934.

CleanEx

HS_NEDD4.

Genevestigator

P46934.

GermOnline

ENSG00000069869. Homo sapiens.

Family and domain databases

InterPro

IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]

SMART

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

SUPFAM

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

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

NEDD4. human.

EvolutionaryTrace

P46934.

GenomeRNAi

4734.

NextBio

18250.

SOURCE

Search...

Entry information

Entry name

NEDD4_HUMAN

Accession

Primary (citable) accession number: P46934
Secondary accession number(s): A1KY35 , A6ND72, A7MD29, B4E2R7, B7ZM59, B7ZM60, B9EGN5, D6RF89

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 30, 2010
Last modified:	May 29, 2013
This is version 136 of the entry and version 4 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.