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Protein

E3 ubiquitin-protein ligase NEDD4-like

Gene

NEDD4L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). Plays a role in dendrite formation by melanocytes (PubMed:23999003).By similarity9 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.

Enzyme regulationi

Activated by NDFIP1- and NDFIP2-binding.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei942Glycyl thioester intermediate1

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL
  • potassium channel inhibitor activity Source: BHF-UCL
  • potassium channel regulator activity Source: BHF-UCL
  • sodium channel inhibitor activity Source: BHF-UCL
  • sodium channel regulator activity Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • cellular sodium ion homeostasis Source: UniProtKB
  • excretion Source: UniProtKB
  • ion transmembrane transport Source: Reactome
  • negative regulation of potassium ion transmembrane transport Source: BHF-UCL
  • negative regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  • negative regulation of protein localization to cell surface Source: BHF-UCL
  • negative regulation of sodium ion transmembrane transport Source: BHF-UCL
  • negative regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  • positive regulation of caveolin-mediated endocytosis Source: BHF-UCL
  • positive regulation of dendrite extension Source: UniProtKB
  • positive regulation of endocytosis Source: UniProtKB
  • positive regulation of protein catabolic process Source: Ensembl
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • protein K48-linked ubiquitination Source: BHF-UCL
  • protein monoubiquitination Source: Ensembl
  • protein polyubiquitination Source: Reactome
  • protein ubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • regulation of ion transmembrane transport Source: BHF-UCL
  • regulation of membrane depolarization Source: BHF-UCL
  • regulation of membrane potential Source: BHF-UCL
  • regulation of membrane repolarization Source: BHF-UCL
  • regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  • regulation of protein catabolic process Source: UniProtKB
  • response to metal ion Source: UniProtKB
  • sodium ion transport Source: UniProtKB
  • ventricular cardiac muscle cell action potential Source: BHF-UCL
  • viral life cycle Source: Reactome
  • water homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Differentiation, Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi2.3.2.B8. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-162588. Budding and maturation of HIV virion.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2672351. Stimuli-sensing channels.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96PU5.
SIGNORiQ96PU5.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase NEDD4-like (EC:2.3.2.26)
Alternative name(s):
HECT-type E3 ubiquitin transferase NED4L
NEDD4.2
Nedd4-2
Gene namesi
Name:NEDD4L
Synonyms:KIAA0439, NEDL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:7728. NEDD4L.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • intracellular Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi448S → A: Abolishes interaction with 1433F. 1 Publication1
Mutagenesisi942C → S: Abolishes activity. 1 Publication1

Organism-specific databases

DisGeNETi23327.
OpenTargetsiENSG00000049759.
PharmGKBiPA31534.

Polymorphism and mutation databases

BioMutaiNEDD4L.
DMDMi73921204.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001203232 – 975E3 ubiquitin-protein ligase NEDD4-likeAdd BLAST974

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Modified residuei318PhosphothreonineCombined sources1
Modified residuei342Phosphoserine; by WNK1 and WNK4Combined sources2 Publications1
Modified residuei367Phosphothreonine; by SGK11 Publication1
Modified residuei446PhosphoserineCombined sources1
Modified residuei448Phosphoserine; by PKA and SGK1Combined sources2 Publications1
Modified residuei449Phosphoserine; by WNK1 and WNK4Combined sources1 Publication1
Modified residuei464PhosphoserineCombined sources1
Modified residuei475PhosphoserineCombined sources1
Modified residuei479PhosphoserineCombined sources1
Modified residuei483PhosphoserineCombined sources1
Modified residuei487PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by SGK1 or PKA; which impairs interaction with SCNN. Interaction with YWHAH inhibits dephosphorylation.5 Publications
Auto-ubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96PU5.
MaxQBiQ96PU5.
PaxDbiQ96PU5.
PeptideAtlasiQ96PU5.
PRIDEiQ96PU5.

PTM databases

iPTMnetiQ96PU5.
PhosphoSitePlusiQ96PU5.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in prostate, pancreas and kidney (PubMed:14615060, PubMed:15496141, PubMed:19664597). Expressed in melanocytes (PubMed:23999003).4 Publications

Inductioni

By androgens in prostate, and by albumin in kidney.2 Publications

Gene expression databases

BgeeiENSG00000049759.
ExpressionAtlasiQ96PU5. baseline and differential.
GenevisibleiQ96PU5. HS.

Organism-specific databases

HPAiHPA024618.
HPA064730.

Interactioni

Subunit structurei

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. Interacts with ARRDC4 (PubMed:23236378). Interacts with KCNQ1; promotes internalization of KCNQ1 (PubMed:22024150).By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAZAP2Q150383EBI-717962,EBI-724310

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116915. 188 interactors.
DIPiDIP-41935N.
IntActiQ96PU5. 25 interactors.
MINTiMINT-148327.
STRINGi9606.ENSP00000383199.

Structurei

Secondary structure

1975
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Turni16 – 18Combined sources3
Beta strandi20 – 31Combined sources12
Beta strandi43 – 51Combined sources9
Turni52 – 55Combined sources4
Beta strandi56 – 62Combined sources7
Beta strandi73 – 82Combined sources10
Turni84 – 86Combined sources3
Beta strandi87 – 95Combined sources9
Beta strandi98 – 100Combined sources3
Beta strandi103 – 111Combined sources9
Beta strandi129 – 132Combined sources4
Beta strandi145 – 152Combined sources8
Beta strandi391 – 396Combined sources6
Turni397 – 399Combined sources3
Beta strandi400 – 405Combined sources6
Turni406 – 409Combined sources4
Beta strandi410 – 414Combined sources5
Helixi417 – 419Combined sources3
Beta strandi503 – 508Combined sources6
Turni509 – 511Combined sources3
Beta strandi512 – 517Combined sources6
Turni518 – 521Combined sources4
Beta strandi522 – 526Combined sources5
Helixi528 – 534Combined sources7
Helixi594 – 607Combined sources14
Beta strandi612 – 614Combined sources3
Beta strandi616 – 622Combined sources7
Helixi624 – 626Combined sources3
Helixi627 – 637Combined sources11
Helixi641 – 645Combined sources5
Beta strandi646 – 652Combined sources7
Beta strandi653 – 655Combined sources3
Helixi660 – 675Combined sources16
Helixi678 – 680Combined sources3
Beta strandi681 – 687Combined sources7
Turni688 – 690Combined sources3
Beta strandi693 – 695Combined sources3
Helixi699 – 702Combined sources4
Helixi706 – 723Combined sources18
Beta strandi728 – 731Combined sources4
Helixi733 – 739Combined sources7
Helixi746 – 749Combined sources4
Turni750 – 752Combined sources3
Helixi754 – 765Combined sources12
Helixi769 – 771Combined sources3
Beta strandi774 – 781Combined sources8
Beta strandi784 – 791Combined sources8
Helixi794 – 796Combined sources3
Turni801 – 803Combined sources3
Helixi804 – 816Combined sources13
Turni817 – 819Combined sources3
Helixi821 – 834Combined sources14
Helixi837 – 840Combined sources4
Helixi845 – 853Combined sources9
Helixi860 – 865Combined sources6
Beta strandi868 – 870Combined sources3
Helixi878 – 889Combined sources12
Helixi892 – 903Combined sources12
Helixi913 – 915Combined sources3
Beta strandi919 – 922Combined sources4
Beta strandi926 – 929Combined sources4
Beta strandi933 – 935Combined sources3
Beta strandi938 – 940Combined sources3
Helixi941 – 943Combined sources3
Beta strandi945 – 948Combined sources4
Helixi954 – 965Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LAJNMR-A496-535[»]
2LB2NMR-A386-420[»]
2LTYNMR-A385-417[»]
2MPTNMR-A496-539[»]
B945-957[»]
2NSQX-ray1.85A1-154[»]
2ONIX-ray2.20A594-967[»]
3JVZX-ray3.30C/D596-975[»]
3JW0X-ray3.10C/D596-975[»]
5HPKX-ray2.43A594-975[»]
ProteinModelPortaliQ96PU5.
SMRiQ96PU5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96PU5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 109C2PROSITE-ProRule annotationAdd BLAST103
Domaini193 – 226WW 1PROSITE-ProRule annotationAdd BLAST34
Domaini385 – 418WW 2PROSITE-ProRule annotationAdd BLAST34
Domaini497 – 530WW 3PROSITE-ProRule annotationAdd BLAST34
Domaini548 – 581WW 4PROSITE-ProRule annotationAdd BLAST34
Domaini640 – 974HECTPROSITE-ProRule annotationAdd BLAST335

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

eggNOGiKOG0940. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00760000118966.
HOVERGENiHBG004134.
InParanoidiQ96PU5.
KOiK13305.
OMAiFDENRLX.
OrthoDBiEOG091G0SS8.
PhylomeDBiQ96PU5.
TreeFamiTF323658.

Family and domain databases

CDDicd00078. HECTc. 1 hit.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
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 (8)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96PU5-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MATGLGEPVY GLSEDEGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY
60 70 80 90 100
VADENRELAL VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT
110 120 130 140 150
RDDFLGQVDV PLSHLPTEDP TMERPYTFKD FLLRPRSHKS RVKGFLRLKM
160 170 180 190 200
AYMPKNGGQD EENSDQRDDM EHGWEVVDSN DSASQHQEEL PPPPLPPGWE
210 220 230 240 250
EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS SESDNNIRQI NQEAAHRRFR
260 270 280 290 300
SRRHISEDLE PEPSEGGDVP EPWETISEEV NIAGDSLGLA LPPPPASPGS
310 320 330 340 350
RTSPQELSEE LSRRLQITPD SNGEQFSSLI QREPSSRLRS CSVTDAVAEQ
360 370 380 390 400
GHLPPPSAPA GRARSSTVTG GEEPTPSVAY VHTTPGLPSG WEERKDAKGR
410 420 430 440 450
TYYVNHNNRT TTWTRPIMQL AEDGASGSAT NSNNHLIEPQ IRRPRSLSSP
460 470 480 490 500
TVTLSAPLEG AKDSPVRRAV KDTLSNPQSP QPSPYNSPKP QHKVTQSFLP
510 520 530 540 550
PGWEMRIAPN GRPFFIDHNT KTTTWEDPRL KFPVHMRSKT SLNPNDLGPL
560 570 580 590 600
PPGWEERIHL DGRTFYIDHN SKITQWEDPR LQNPAITGPA VPYSREFKQK
610 620 630 640 650
YDYFRKKLKK PADIPNRFEM KLHRNNIFEE SYRRIMSVKR PDVLKARLWI
660 670 680 690 700
EFESEKGLDY GGVAREWFFL LSKEMFNPYY GLFEYSATDN YTLQINPNSG
710 720 730 740 750
LCNEDHLSYF TFIGRVAGLA VFHGKLLDGF FIRPFYKMML GKQITLNDME
760 770 780 790 800
SVDSEYYNSL KWILENDPTE LDLMFCIDEE NFGQTYQVDL KPNGSEIMVT
810 820 830 840 850
NENKREYIDL VIQWRFVNRV QKQMNAFLEG FTELLPIDLI KIFDENELEL
860 870 880 890 900
LMCGLGDVDV NDWRQHSIYK NGYCPNHPVI QWFWKAVLLM DAEKRIRLLQ
910 920 930 940 950
FVTGTSRVPM NGFAELYGSN GPQLFTIEQW GSPEKLPRAH TCFNRLDLPP
960 970
YETFEDLREK LLMAVENAQG FEGVD
Length:975
Mass (Da):111,932
Last modified:August 30, 2005 - v2
Checksum:i2C958625B4A1AB3F
GO
Isoform 2 (identifier: Q96PU5-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:911
Mass (Da):104,922
Checksum:iCE04AAED677AA506
GO
Isoform 3 (identifier: Q96PU5-3) [UniParc]FASTAAdd to basket
Also known as: NEDD4Le

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

Note: No experimental confirmation available.
Show »
Length:871
Mass (Da):100,752
Checksum:i5E2AB9B510060D4A
GO
Isoform 4 (identifier: Q96PU5-4) [UniParc]FASTAAdd to basket
Also known as: NEDD4La, NEDD4Lb, NEDD4Lf

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

Show »
Length:854
Mass (Da):98,181
Checksum:i00C74E1661F52E7F
GO
Isoform 5 (identifier: Q96PU5-5) [UniParc]FASTAAdd to basket
Also known as: NEDD4Ld

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

Show »
Length:955
Mass (Da):110,022
Checksum:iA8BB278A37F6A6B5
GO
Isoform 6 (identifier: Q96PU5-6) [UniParc]FASTAAdd to basket
Also known as: NEDD4Lh

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

Show »
Length:947
Mass (Da):109,404
Checksum:iF107E5A8E0C3BB8D
GO
Isoform 7 (identifier: Q96PU5-7) [UniParc]FASTAAdd to basket
Also known as: NEDD4Lg

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

Show »
Length:967
Mass (Da):111,314
Checksum:i9786AC67C8CD165F
GO
Isoform 8 (identifier: Q96PU5-9) [UniParc]FASTAAdd to basket

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

Show »
Length:834
Mass (Da):96,271
Checksum:i47C33C4FB577C3DB
GO

Sequence cautioni

The sequence BAA23711 differs from that shown. Probable cloning artifact.Curated
The sequence BAA23711 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52A → P in AAM76729 (PubMed:14615060).Curated1
Sequence conflicti52A → P in AAM76730 (PubMed:14615060).Curated1
Sequence conflicti188E → K in AAP75706 (PubMed:14556380).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023415355P → L Common polymorphism; impaired ability to inhibit SCNN. 1 PublicationCorresponds to variant rs767136811dbSNPEnsembl.1
Natural variantiVAR_023416497S → R.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0154441 – 121Missing in isoform 4 and isoform 8. 4 PublicationsAdd BLAST121
Alternative sequenceiVSP_0154461 – 16MATGL…LSEDE → MRRLAFEQ in isoform 6 and isoform 7. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_015447356 – 459Missing in isoform 3. 1 PublicationAdd BLAST104
Alternative sequenceiVSP_015448356 – 419Missing in isoform 2. 1 PublicationAdd BLAST64
Alternative sequenceiVSP_043848356 – 375Missing in isoform 5, isoform 6 and isoform 8. 5 PublicationsAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45872.1. [Q96PU5-1]
CCDS45873.1. [Q96PU5-5]
CCDS45874.1. [Q96PU5-7]
CCDS45875.1. [Q96PU5-4]
CCDS45876.1. [Q96PU5-9]
CCDS58632.1. [Q96PU5-2]
CCDS59323.1. [Q96PU5-6]
PIRiT46412.
RefSeqiNP_001138436.1. NM_001144964.1. [Q96PU5-4]
NP_001138437.1. NM_001144965.1. [Q96PU5-4]
NP_001138438.1. NM_001144966.2. [Q96PU5-4]
NP_001138439.1. NM_001144967.2. [Q96PU5-1]
NP_001138440.1. NM_001144968.1. [Q96PU5-7]
NP_001138441.1. NM_001144969.1. [Q96PU5-6]
NP_001138442.1. NM_001144970.2. [Q96PU5-9]
NP_001138443.1. NM_001144971.1. [Q96PU5-9]
NP_001230889.1. NM_001243960.1. [Q96PU5-2]
NP_056092.2. NM_015277.5. [Q96PU5-5]
XP_016881168.1. XM_017025679.1. [Q96PU5-4]
UniGeneiHs.185677.

Genome annotation databases

EnsembliENST00000256830; ENSP00000256830; ENSG00000049759. [Q96PU5-3]
ENST00000356462; ENSP00000348847; ENSG00000049759. [Q96PU5-2]
ENST00000357895; ENSP00000350569; ENSG00000049759. [Q96PU5-7]
ENST00000382850; ENSP00000372301; ENSG00000049759. [Q96PU5-5]
ENST00000400345; ENSP00000383199; ENSG00000049759. [Q96PU5-1]
ENST00000431212; ENSP00000389406; ENSG00000049759. [Q96PU5-4]
ENST00000435432; ENSP00000393395; ENSG00000049759. [Q96PU5-9]
ENST00000456173; ENSP00000405440; ENSG00000049759. [Q96PU5-9]
ENST00000456986; ENSP00000411947; ENSG00000049759. [Q96PU5-4]
ENST00000586263; ENSP00000468546; ENSG00000049759. [Q96PU5-6]
GeneIDi23327.
KEGGihsa:23327.
UCSCiuc002lgx.4. human. [Q96PU5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45872.1. [Q96PU5-1]
CCDS45873.1. [Q96PU5-5]
CCDS45874.1. [Q96PU5-7]
CCDS45875.1. [Q96PU5-4]
CCDS45876.1. [Q96PU5-9]
CCDS58632.1. [Q96PU5-2]
CCDS59323.1. [Q96PU5-6]
PIRiT46412.
RefSeqiNP_001138436.1. NM_001144964.1. [Q96PU5-4]
NP_001138437.1. NM_001144965.1. [Q96PU5-4]
NP_001138438.1. NM_001144966.2. [Q96PU5-4]
NP_001138439.1. NM_001144967.2. [Q96PU5-1]
NP_001138440.1. NM_001144968.1. [Q96PU5-7]
NP_001138441.1. NM_001144969.1. [Q96PU5-6]
NP_001138442.1. NM_001144970.2. [Q96PU5-9]
NP_001138443.1. NM_001144971.1. [Q96PU5-9]
NP_001230889.1. NM_001243960.1. [Q96PU5-2]
NP_056092.2. NM_015277.5. [Q96PU5-5]
XP_016881168.1. XM_017025679.1. [Q96PU5-4]
UniGeneiHs.185677.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LAJNMR-A496-535[»]
2LB2NMR-A386-420[»]
2LTYNMR-A385-417[»]
2MPTNMR-A496-539[»]
B945-957[»]
2NSQX-ray1.85A1-154[»]
2ONIX-ray2.20A594-967[»]
3JVZX-ray3.30C/D596-975[»]
3JW0X-ray3.10C/D596-975[»]
5HPKX-ray2.43A594-975[»]
ProteinModelPortaliQ96PU5.
SMRiQ96PU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116915. 188 interactors.
DIPiDIP-41935N.
IntActiQ96PU5. 25 interactors.
MINTiMINT-148327.
STRINGi9606.ENSP00000383199.

PTM databases

iPTMnetiQ96PU5.
PhosphoSitePlusiQ96PU5.

Polymorphism and mutation databases

BioMutaiNEDD4L.
DMDMi73921204.

Proteomic databases

EPDiQ96PU5.
MaxQBiQ96PU5.
PaxDbiQ96PU5.
PeptideAtlasiQ96PU5.
PRIDEiQ96PU5.

Protocols and materials databases

DNASUi23327.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256830; ENSP00000256830; ENSG00000049759. [Q96PU5-3]
ENST00000356462; ENSP00000348847; ENSG00000049759. [Q96PU5-2]
ENST00000357895; ENSP00000350569; ENSG00000049759. [Q96PU5-7]
ENST00000382850; ENSP00000372301; ENSG00000049759. [Q96PU5-5]
ENST00000400345; ENSP00000383199; ENSG00000049759. [Q96PU5-1]
ENST00000431212; ENSP00000389406; ENSG00000049759. [Q96PU5-4]
ENST00000435432; ENSP00000393395; ENSG00000049759. [Q96PU5-9]
ENST00000456173; ENSP00000405440; ENSG00000049759. [Q96PU5-9]
ENST00000456986; ENSP00000411947; ENSG00000049759. [Q96PU5-4]
ENST00000586263; ENSP00000468546; ENSG00000049759. [Q96PU5-6]
GeneIDi23327.
KEGGihsa:23327.
UCSCiuc002lgx.4. human. [Q96PU5-1]

Organism-specific databases

CTDi23327.
DisGeNETi23327.
GeneCardsiNEDD4L.
HGNCiHGNC:7728. NEDD4L.
HPAiHPA024618.
HPA064730.
MIMi606384. gene.
neXtProtiNX_Q96PU5.
OpenTargetsiENSG00000049759.
PharmGKBiPA31534.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0940. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00760000118966.
HOVERGENiHBG004134.
InParanoidiQ96PU5.
KOiK13305.
OMAiFDENRLX.
OrthoDBiEOG091G0SS8.
PhylomeDBiQ96PU5.
TreeFamiTF323658.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B8. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-162588. Budding and maturation of HIV virion.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2672351. Stimuli-sensing channels.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96PU5.
SIGNORiQ96PU5.

Miscellaneous databases

ChiTaRSiNEDD4L. human.
EvolutionaryTraceiQ96PU5.
GeneWikiiNEDD4L.
GenomeRNAii23327.
PROiQ96PU5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000049759.
ExpressionAtlasiQ96PU5. baseline and differential.
GenevisibleiQ96PU5. HS.

Family and domain databases

CDDicd00078. HECTc. 1 hit.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
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]
ProtoNetiSearch...

Entry informationi

Entry nameiNED4L_HUMAN
AccessioniPrimary (citable) accession number: Q96PU5
Secondary accession number(s): O43165
, Q3LSM7, Q7Z5F1, Q7Z5F2, Q7Z5N3, Q8N5A7, Q8WUU9, Q9BW58, Q9H2W4, Q9NT88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: November 30, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.