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Q96PU5

- NED4L_HUMAN

UniProt

Q96PU5 - NED4L_HUMAN

Protein

E3 ubiquitin-protein ligase NEDD4-like

Gene

NEDD4L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    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

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

    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

    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 SGK11 Publication
    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.10 Publications
    Auto-ubiquitinated.1 Publication

    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.By similarity14 Publications

    Protein-protein interaction databases

    BioGridi116915. 164 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.
    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

    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.

    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
    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:
    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

    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. 164 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

    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

    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: October 1, 2014
    This is version 128 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