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Q96PU5

- NED4L_HUMAN

UniProt

Q96PU5 - NED4L_HUMAN

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Protein

E3 ubiquitin-protein ligase NEDD4-like

Gene
NEDD4L, KIAA0439, NEDL3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK1 and TNK2.7 Publications

Enzyme regulationi

Activated by NDFIP1- and NDFIP2-binding.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei942 – 9421Glycyl thioester intermediate

GO - Molecular functioni

  1. ion channel binding Source: BHF-UCL
  2. ligase activity Source: UniProtKB-KW
  3. potassium channel inhibitor activity Source: BHF-UCL
  4. potassium channel regulator activity Source: BHF-UCL
  5. protein binding Source: UniProtKB
  6. sodium channel inhibitor activity Source: BHF-UCL
  7. sodium channel regulator activity Source: UniProtKB
  8. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cellular sodium ion homeostasis Source: UniProtKB
  2. excretion Source: UniProtKB
  3. gene expression Source: Reactome
  4. ion transmembrane transport Source: Reactome
  5. negative regulation of potassium ion transmembrane transport Source: BHF-UCL
  6. negative regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  7. negative regulation of protein localization to cell surface Source: BHF-UCL
  8. negative regulation of sodium ion transmembrane transport Source: BHF-UCL
  9. negative regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  10. negative regulation of systemic arterial blood pressure Source: Ensembl
  11. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  12. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  13. positive regulation of cation channel activity Source: Ensembl
  14. positive regulation of caveolin-mediated endocytosis Source: BHF-UCL
  15. positive regulation of endocytosis Source: UniProtKB
  16. positive regulation of protein catabolic process Source: Ensembl
  17. positive regulation of sodium ion transport Source: Ensembl
  18. proteasome-mediated ubiquitin-dependent protein catabolic process Source: BHF-UCL
  19. protein K48-linked ubiquitination Source: BHF-UCL
  20. protein monoubiquitination Source: Ensembl
  21. protein ubiquitination Source: UniProtKB
  22. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  23. regulation of ion transmembrane transport Source: BHF-UCL
  24. regulation of membrane depolarization Source: BHF-UCL
  25. regulation of membrane potential Source: BHF-UCL
  26. regulation of membrane repolarization Source: BHF-UCL
  27. regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  28. regulation of protein catabolic process Source: UniProtKB
  29. regulation of tight junction assembly Source: Ensembl
  30. response to metal ion Source: UniProtKB
  31. response to salt stress Source: Ensembl
  32. sodium ion transport Source: UniProtKB
  33. transcription, DNA-templated Source: Reactome
  34. transcription initiation from RNA polymerase II promoter Source: Reactome
  35. transforming growth factor beta receptor signaling pathway Source: Reactome
  36. transmembrane transport Source: Reactome
  37. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: Ensembl
  38. ventricular cardiac muscle cell action potential Source: BHF-UCL
  39. viral life cycle Source: Reactome
  40. viral process Source: Reactome
  41. water homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_160189. Stimuli-sensing channels.
REACT_6359. Budding and maturation of HIV virion.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96PU5.
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
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:7728. NEDD4L.

Subcellular locationi

Cytoplasm
Note: May be recruited to exosomes by NDFIP1.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. intracellular Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: RefGenome
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 975974E3 ubiquitin-protein ligase NEDD4-likePRO_0000120323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei318 – 3181Phosphothreonine1 Publication
Modified residuei342 – 3421Phosphoserine; by WNK1 and WNK43 Publications
Modified residuei367 – 3671Phosphothreonine; by SGK1 Inferred
Modified residuei446 – 4461Phosphoserine2 Publications
Modified residuei448 – 4481Phosphoserine; by PKA and SGK12 Publications
Modified residuei449 – 4491Phosphoserine; by WNK1 and WNK42 Publications
Modified residuei464 – 4641Phosphoserine1 Publication
Modified residuei479 – 4791Phosphoserine4 Publications
Modified residuei483 – 4831Phosphoserine2 Publications
Modified residuei487 – 4871Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96PU5.
PaxDbiQ96PU5.
PRIDEiQ96PU5.

PTM databases

PhosphoSiteiQ96PU5.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in prostate, pancreas and kidney.3 Publications

Inductioni

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

Gene expression databases

ArrayExpressiQ96PU5.
BgeeiQ96PU5.
GenevestigatoriQ96PU5.

Organism-specific databases

HPAiHPA024618.

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 NPC2.14 Publications

Protein-protein interaction databases

BioGridi116915. 160 interactions.
DIPiDIP-41935N.
IntActiQ96PU5. 20 interactions.
MINTiMINT-148327.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LAJNMR-A496-535[»]
2LB2NMR-A386-420[»]
2LTYNMR-A385-417[»]
2NSQX-ray1.85A1-154[»]
2ONIX-ray2.20A594-967[»]
3JVZX-ray3.30C/D596-975[»]
3JW0X-ray3.10C/D596-975[»]
ProteinModelPortaliQ96PU5.
SMRiQ96PU5. Positions 6-154, 193-252, 386-420, 496-966.

Miscellaneous databases

EvolutionaryTraceiQ96PU5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 109103C2Add
BLAST
Domaini193 – 22634WW 1Add
BLAST
Domaini385 – 41834WW 2Add
BLAST
Domaini497 – 53034WW 3Add
BLAST
Domaini548 – 58134WW 4Add
BLAST
Domaini640 – 974335HECTAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.
Contains 4 WW domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5021.
HOVERGENiHBG004134.
KOiK13305.
OMAiSEQRDDM.
OrthoDBiEOG7RFTGT.
PhylomeDBiQ96PU5.
TreeFamiTF323658.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 4 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (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. Align

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

MATGLGEPVY GLSEDEGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY    50
VADENRELAL VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT 100
RDDFLGQVDV PLSHLPTEDP TMERPYTFKD FLLRPRSHKS RVKGFLRLKM 150
AYMPKNGGQD EENSDQRDDM EHGWEVVDSN DSASQHQEEL PPPPLPPGWE 200
EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS SESDNNIRQI NQEAAHRRFR 250
SRRHISEDLE PEPSEGGDVP EPWETISEEV NIAGDSLGLA LPPPPASPGS 300
RTSPQELSEE LSRRLQITPD SNGEQFSSLI QREPSSRLRS CSVTDAVAEQ 350
GHLPPPSAPA GRARSSTVTG GEEPTPSVAY VHTTPGLPSG WEERKDAKGR 400
TYYVNHNNRT TTWTRPIMQL AEDGASGSAT NSNNHLIEPQ IRRPRSLSSP 450
TVTLSAPLEG AKDSPVRRAV KDTLSNPQSP QPSPYNSPKP QHKVTQSFLP 500
PGWEMRIAPN GRPFFIDHNT KTTTWEDPRL KFPVHMRSKT SLNPNDLGPL 550
PPGWEERIHL DGRTFYIDHN SKITQWEDPR LQNPAITGPA VPYSREFKQK 600
YDYFRKKLKK PADIPNRFEM KLHRNNIFEE SYRRIMSVKR PDVLKARLWI 650
EFESEKGLDY GGVAREWFFL LSKEMFNPYY GLFEYSATDN YTLQINPNSG 700
LCNEDHLSYF TFIGRVAGLA VFHGKLLDGF FIRPFYKMML GKQITLNDME 750
SVDSEYYNSL KWILENDPTE LDLMFCIDEE NFGQTYQVDL KPNGSEIMVT 800
NENKREYIDL VIQWRFVNRV QKQMNAFLEG FTELLPIDLI KIFDENELEL 850
LMCGLGDVDV NDWRQHSIYK NGYCPNHPVI QWFWKAVLLM DAEKRIRLLQ 900
FVTGTSRVPM NGFAELYGSN GPQLFTIEQW GSPEKLPRAH TCFNRLDLPP 950
YETFEDLREK LLMAVENAQG FEGVD 975
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 BAA23711.1 differs from that shown. Reason: Probable cloning artifact.
The sequence BAA23711.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti355 – 3551P → L Common polymorphism; impaired ability to inhibit SCNN. 1 Publication
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. VSP_015444Add
BLAST
Alternative sequencei1 – 1616MATGL…LSEDE → MRRLAFEQ in isoform 6 and isoform 7. VSP_015446Add
BLAST
Alternative sequencei356 – 459104Missing in isoform 3. VSP_015447Add
BLAST
Alternative sequencei356 – 41964Missing in isoform 2. VSP_015448Add
BLAST
Alternative sequencei356 – 37520Missing in isoform 5, isoform 6 and isoform 8. VSP_043848Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521A → P in AAM76729. 1 Publication
Sequence conflicti52 – 521A → P in AAM76730. 1 Publication
Sequence conflicti188 – 1881E → K in AAP75706. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [Q96PU5-5]
uc002lgy.3. human. [Q96PU5-1]
uc002lgz.3. human. [Q96PU5-2]
uc002lhb.2. human. [Q96PU5-9]
uc002lhc.2. human. [Q96PU5-7]
uc002lhe.2. human. [Q96PU5-6]
uc002lhh.2. human. [Q96PU5-3]

Polymorphism databases

DMDMi73921204.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS45872.1. [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 ]
PIRi T46412.
RefSeqi NP_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 ]
UniGenei Hs.185677.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q96PU5.
SMRi Q96PU5. Positions 6-154, 193-252, 386-420, 496-966.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116915. 160 interactions.
DIPi DIP-41935N.
IntActi Q96PU5. 20 interactions.
MINTi MINT-148327.

PTM databases

PhosphoSitei Q96PU5.

Polymorphism databases

DMDMi 73921204.

Proteomic databases

MaxQBi Q96PU5.
PaxDbi Q96PU5.
PRIDEi Q96PU5.

Protocols and materials databases

DNASUi 23327.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256830 ; 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 ]
GeneIDi 23327.
KEGGi hsa:23327.
UCSCi uc002lgx.3. human. [Q96PU5-5 ]
uc002lgy.3. human. [Q96PU5-1 ]
uc002lgz.3. human. [Q96PU5-2 ]
uc002lhb.2. human. [Q96PU5-9 ]
uc002lhc.2. human. [Q96PU5-7 ]
uc002lhe.2. human. [Q96PU5-6 ]
uc002lhh.2. human. [Q96PU5-3 ]

Organism-specific databases

CTDi 23327.
GeneCardsi GC18P055711.
HGNCi HGNC:7728. NEDD4L.
HPAi HPA024618.
MIMi 606384. gene.
neXtProti NX_Q96PU5.
PharmGKBi PA31534.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5021.
HOVERGENi HBG004134.
KOi K13305.
OMAi SEQRDDM.
OrthoDBi EOG7RFTGT.
PhylomeDBi Q96PU5.
TreeFami TF323658.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_160189. Stimuli-sensing channels.
REACT_6359. Budding and maturation of HIV virion.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki Q96PU5.

Miscellaneous databases

ChiTaRSi NEDD4L. human.
EvolutionaryTracei Q96PU5.
GeneWikii NEDD4L.
GenomeRNAii 23327.
NextBioi 45240.
PROi Q96PU5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96PU5.
Bgeei Q96PU5.
Genevestigatori Q96PU5.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view ]
PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
PRINTSi PR00360. C2DOMAIN.
SMARTi SM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 4 hits.
SSF56204. SSF56204. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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. 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-342; SER-446; SER-449; SER-464; SER-479 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: INTERACTION WITH NPC2, TISSUE SPECIFICITY.
  29. "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.
  30. "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.
  31. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  32. "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.
  33. "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.
  34. "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.
  35. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  39. "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.

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 3, 2014
This is version 127 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

External Data

Dasty 3

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