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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

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei942 – 9421Glycyl thioester intermediate

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL
  • ligase activity Source: UniProtKB-KW
  • 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

Ligase

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:6.3.2.-)
Alternative name(s):
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi448 – 4481S → A: Abolishes interaction with 1433F. 1 Publication
Mutagenesisi942 – 9421C → S: Abolishes activity. 1 Publication

Organism-specific databases

PharmGKBiPA31534.

Polymorphism and mutation databases

BioMutaiNEDD4L.
DMDMi73921204.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 975974E3 ubiquitin-protein ligase NEDD4-likePRO_0000120323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei318 – 3181PhosphothreonineCombined sources
Modified residuei342 – 3421Phosphoserine; by WNK1 and WNK4Combined sources2 Publications
Modified residuei367 – 3671Phosphothreonine; by SGK11 Publication
Modified residuei446 – 4461PhosphoserineCombined sources
Modified residuei448 – 4481Phosphoserine; by PKA and SGK1Combined sources2 Publications
Modified residuei449 – 4491Phosphoserine; by WNK1 and WNK4Combined sources1 Publication
Modified residuei464 – 4641PhosphoserineCombined sources
Modified residuei475 – 4751PhosphoserineCombined sources
Modified residuei479 – 4791PhosphoserineCombined sources
Modified residuei483 – 4831PhosphoserineCombined sources
Modified residuei487 – 4871PhosphoserineCombined sources

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.
PhosphoSiteiQ96PU5.

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. 187 interactions.
DIPiDIP-41935N.
IntActiQ96PU5. 25 interactions.
MINTiMINT-148327.
STRINGi9606.ENSP00000383199.

Structurei

Secondary structure

1
975
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Turni16 – 183Combined sources
Beta strandi20 – 3112Combined sources
Beta strandi43 – 519Combined sources
Turni52 – 554Combined sources
Beta strandi56 – 627Combined sources
Beta strandi73 – 8210Combined sources
Turni84 – 863Combined sources
Beta strandi87 – 959Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi391 – 3966Combined sources
Turni397 – 3993Combined sources
Beta strandi400 – 4056Combined sources
Turni406 – 4094Combined sources
Beta strandi410 – 4145Combined sources
Helixi417 – 4193Combined sources
Beta strandi503 – 5086Combined sources
Turni509 – 5113Combined sources
Beta strandi512 – 5176Combined sources
Turni518 – 5214Combined sources
Beta strandi522 – 5265Combined sources
Helixi528 – 5347Combined sources
Helixi594 – 60714Combined sources
Beta strandi612 – 6143Combined sources
Beta strandi616 – 6227Combined sources
Helixi624 – 6263Combined sources
Helixi627 – 63711Combined sources
Helixi641 – 6455Combined sources
Beta strandi646 – 6527Combined sources
Beta strandi653 – 6553Combined sources
Helixi660 – 67516Combined sources
Helixi678 – 6803Combined sources
Beta strandi681 – 6877Combined sources
Turni688 – 6903Combined sources
Beta strandi693 – 6953Combined sources
Helixi699 – 7024Combined sources
Helixi706 – 72318Combined sources
Beta strandi728 – 7314Combined sources
Helixi733 – 7397Combined sources
Helixi746 – 7494Combined sources
Turni750 – 7523Combined sources
Helixi754 – 76512Combined sources
Helixi769 – 7713Combined sources
Beta strandi774 – 7818Combined sources
Beta strandi784 – 7918Combined sources
Helixi794 – 7963Combined sources
Turni801 – 8033Combined sources
Helixi804 – 81613Combined sources
Turni817 – 8193Combined sources
Helixi821 – 83414Combined sources
Helixi837 – 8404Combined sources
Helixi845 – 8539Combined sources
Helixi860 – 8656Combined sources
Beta strandi868 – 8703Combined sources
Helixi878 – 88912Combined sources
Helixi892 – 90312Combined sources
Helixi913 – 9153Combined sources
Beta strandi919 – 9224Combined sources
Beta strandi926 – 9294Combined sources
Beta strandi933 – 9353Combined sources
Beta strandi938 – 9403Combined sources
Helixi941 – 9433Combined sources
Beta strandi945 – 9484Combined sources
Helixi954 – 96512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-154, 193-252, 386-420, 496-966.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96PU5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 109103C2PROSITE-ProRule annotationAdd
BLAST
Domaini193 – 22634WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini385 – 41834WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini497 – 53034WW 3PROSITE-ProRule annotationAdd
BLAST
Domaini548 – 58134WW 4PROSITE-ProRule annotationAdd
BLAST
Domaini640 – 974335HECTPROSITE-ProRule annotationAdd
BLAST

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521A → P in AAM76729 (PubMed:14615060).Curated
Sequence conflicti52 – 521A → P in AAM76730 (PubMed:14615060).Curated
Sequence conflicti188 – 1881E → K in AAP75706 (PubMed:14556380).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti355 – 3551P → L Common polymorphism; impaired ability to inhibit SCNN. 1 Publication
Corresponds to variant rs767136811 [ dbSNP | Ensembl ].
VAR_023415
Natural varianti497 – 4971S → R.1 Publication
VAR_023416

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 121121Missing in isoform 4 and isoform 8. 4 PublicationsVSP_015444Add
BLAST
Alternative sequencei1 – 1616MATGL…LSEDE → MRRLAFEQ in isoform 6 and isoform 7. 1 PublicationVSP_015446Add
BLAST
Alternative sequencei356 – 459104Missing in isoform 3. 1 PublicationVSP_015447Add
BLAST
Alternative sequencei356 – 41964Missing in isoform 2. 1 PublicationVSP_015448Add
BLAST
Alternative sequencei356 – 37520Missing in isoform 5, isoform 6 and isoform 8. 5 PublicationsVSP_043848Add
BLAST

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]
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]
UniGeneiHs.185677.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-154, 193-252, 386-420, 496-966.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116915. 187 interactions.
DIPiDIP-41935N.
IntActiQ96PU5. 25 interactions.
MINTiMINT-148327.
STRINGi9606.ENSP00000383199.

PTM databases

iPTMnetiQ96PU5.
PhosphoSiteiQ96PU5.

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.
GeneCardsiNEDD4L.
HGNCiHGNC:7728. NEDD4L.
HPAiHPA024618.
HPA064730.
MIMi606384. gene.
neXtProtiNX_Q96PU5.
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

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: September 7, 2016
This is version 150 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.