UniProtKB - Q96PU5 (NED4L_HUMAN)
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- BLAST>sp|Q96PU5|NED4L_HUMAN E3 ubiquitin-protein ligase NEDD4-like OS=Homo sapiens OX=9606 GN=NEDD4L PE=1 SV=2 MATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELAL VQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDP TMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSDQRDDMEHGWEVVDSN DSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQI NQEAAHRRFRSRRHISEDLEPEPSEGGDVPEPWETISEEVNIAGDSLGLALPPPPASPGS RTSPQELSEELSRRLQITPDSNGEQFSSLIQREPSSRLRSCSVTDAVAEQGHLPPPSAPA GRARSSTVTGGEEPTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQL AEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSP QPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKT SLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQK YDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDY GGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLA VFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEE NFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLI KIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQ FVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREK LLMAVENAQGFEGVD
- Align
E3 ubiquitin-protein ligase NEDD4-like
NEDD4L
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
12 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.44"Regulation of the human ether-a-go-go-related gene (hERG) potassium channel by Nedd4 family interacting proteins (Ndfips)."
Kang Y., Guo J., Yang T., Li W., Zhang S.
Biochem. J. 472:71-82(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NDFIP1 AND NDFIP2, SUBCELLULAR LOCATION. - Ref.45"Nedd4 family interacting protein 1 (Ndfip1) is required for ubiquitination and nuclear trafficking of BRCA1-associated ATM activator 1 (BRAT1) during the DNA damage response."
Low L.H., Chow Y.L., Li Y., Goh C.P., Putz U., Silke J., Ouchi T., Howitt J., Tan S.S.
J. Biol. Chem. 290:7141-7150(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN UBIQUITINATION OF BRAT1. - Ref.46"Ubiquitin-specific Protease 36 (USP36) Controls Neuronal Precursor Cell-expressed Developmentally Down-regulated 4-2 (Nedd4-2) Actions over the Neurotrophin Receptor TrkA and Potassium Voltage-gated Channels 7.2/3 (Kv7.2/3)."
Anta B., Martin-Rodriguez C., Gomis-Perez C., Calvo L., Lopez-Benito S., Calderon-Garcia A.A., Vicente-Garcia C., Villarroel A., Arevalo J.C.
J. Biol. Chem. 291:19132-19145(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH USP36, DEUBIQUITINATION BY USP36, MUTAGENESIS OF CYS-942. - Ref.47"Mutations in the HECT domain of NEDD4L lead to AKT-mTOR pathway deregulation and cause periventricular nodular heterotopia."
Deciphering Developmental Disorders study
Broix L., Jagline H., Ivanova L.E., Schmucker S., Drouot N., Clayton-Smith J., Pagnamenta A.T., Metcalfe K.A., Isidor B., Louvier U.W., Poduri A., Taylor J.C., Tilly P., Poirier K., Saillour Y., Lebrun N., Stemmelen T., Rudolf G. , Muraca G., Saintpierre B., Elmorjani A., Moise M., Weirauch N.B., Guerrini R., Boland A., Olaso R., Masson C., Tripathy R., Keays D., Beldjord C., Nguyen L., Godin J., Kini U., Nischke P., Deleuze J.F., Bahi-Buisson N., Sumara I., Hinckelmann M.V., Chelly J.
Nat. Genet. 48:1349-1358(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN PVNH7, VARIANTS PVNH7 CYS-679; HIS-694; LYS-893 AND GLN-897, CHARACTERIZATION OF VARIANTS PVNH7 HIS-694; LYS-893 AND GLN-897.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 942 | Glycyl thioester intermediate | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ion channel binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- potassium channel inhibitor activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- potassium channel regulator activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- sodium channel inhibitor activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- sodium channel regulator activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin protein ligase activity Source: GO_Central
- ubiquitin-protein transferase activity Source: ReactomeInferred from experimenti
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cellular sodium ion homeostasis Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- excretion Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- ion transmembrane transport Source: Reactome
- negative regulation of potassium ion transmembrane transport Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of potassium ion transmembrane transporter activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of protein localization to cell surface Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of sodium ion transmembrane transport Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of sodium ion transmembrane transporter activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of transcription by RNA polymerase II Source: Reactome
- positive regulation of caveolin-mediated endocytosis Source: BHF-UCL <p>Inferred from Sequence or Structural Similarity <br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityi
- positive regulation of dendrite extension Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of endocytosis Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- positive regulation of protein catabolic process Source: Ensembl
- proteasome-mediated ubiquitin-dependent protein catabolic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein K48-linked ubiquitination Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein monoubiquitination Source: Ensembl
- protein polyubiquitination Source: Reactome
- protein ubiquitination Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of ion transmembrane transport Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of membrane depolarization Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of membrane potential Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of membrane repolarization Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of potassium ion transmembrane transporter activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of protein catabolic process Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- regulation of protein stability Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- response to metal ion Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- sodium ion transport Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- ubiquitin-dependent protein catabolic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ventricular cardiac muscle cell action potential Source: BHF-UCL <p>Inferred from Sequence or Structural Similarity <br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityi
- viral life cycle Source: Reactome
- water homeostasis Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Transferase |
| Biological process | Differentiation, Host-virus interaction, Ubl conjugation pathway |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:ENSG00000049759-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.2.B8 2681 6.3.2.19 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-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 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q96PU5 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q96PU5 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00143 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: E3 ubiquitin-protein ligase NEDD4-like (EC:2.3.2.26)Alternative name(s): HECT-type E3 ubiquitin transferase NED4L NEDD4.2 Nedd4-2 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:NEDD4L Synonyms:KIAA0439, NEDL3 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000049759.16 |
Human Gene Nomenclature Database More...HGNCi | HGNC:7728 NEDD4L |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606384 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96PU5 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endosome
- multivesicular body 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.44"Regulation of the human ether-a-go-go-related gene (hERG) potassium channel by Nedd4 family interacting proteins (Ndfips)."
Kang Y., Guo J., Yang T., Li W., Zhang S.
Biochem. J. 472:71-82(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NDFIP1 AND NDFIP2, SUBCELLULAR LOCATION.
- multivesicular body 1 Publication
Golgi apparatus
- Golgi apparatus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.44"Regulation of the human ether-a-go-go-related gene (hERG) potassium channel by Nedd4 family interacting proteins (Ndfips)."
Kang Y., Guo J., Yang T., Li W., Zhang S.
Biochem. J. 472:71-82(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NDFIP1 AND NDFIP2, SUBCELLULAR LOCATION.
- Golgi apparatus 1 Publication
Other locations
- Cytoplasm 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.47"Mutations in the HECT domain of NEDD4L lead to AKT-mTOR pathway deregulation and cause periventricular nodular heterotopia."
Deciphering Developmental Disorders study
Broix L., Jagline H., Ivanova L.E., Schmucker S., Drouot N., Clayton-Smith J., Pagnamenta A.T., Metcalfe K.A., Isidor B., Louvier U.W., Poduri A., Taylor J.C., Tilly P., Poirier K., Saillour Y., Lebrun N., Stemmelen T., Rudolf G. , Muraca G., Saintpierre B., Elmorjani A., Moise M., Weirauch N.B., Guerrini R., Boland A., Olaso R., Masson C., Tripathy R., Keays D., Beldjord C., Nguyen L., Godin J., Kini U., Nischke P., Deleuze J.F., Bahi-Buisson N., Sumara I., Hinckelmann M.V., Chelly J.
Nat. Genet. 48:1349-1358(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN PVNH7, VARIANTS PVNH7 CYS-679; HIS-694; LYS-893 AND GLN-897, CHARACTERIZATION OF VARIANTS PVNH7 HIS-694; LYS-893 AND GLN-897.
Note: May be recruited to exosomes by NDFIP1.- Cytoplasm 3 Publications
Cytosol
- cytosol Source: Reactome
Endosome
- multivesicular body Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- Golgi apparatus Source: UniProtKB-SubCell
Nucleus
- nucleoplasm Source: Reactome
Other locations
- cytoplasm Source: GO_Central
- intracellular Source: UniProtKB <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatori
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Endosome, Golgi apparatus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Periventricular nodular heterotopia 7 (PVNH7)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.47"Mutations in the HECT domain of NEDD4L lead to AKT-mTOR pathway deregulation and cause periventricular nodular heterotopia."
Deciphering Developmental Disorders study
Broix L., Jagline H., Ivanova L.E., Schmucker S., Drouot N., Clayton-Smith J., Pagnamenta A.T., Metcalfe K.A., Isidor B., Louvier U.W., Poduri A., Taylor J.C., Tilly P., Poirier K., Saillour Y., Lebrun N., Stemmelen T., Rudolf G. , Muraca G., Saintpierre B., Elmorjani A., Moise M., Weirauch N.B., Guerrini R., Boland A., Olaso R., Masson C., Tripathy R., Keays D., Beldjord C., Nguyen L., Godin J., Kini U., Nischke P., Deleuze J.F., Bahi-Buisson N., Sumara I., Hinckelmann M.V., Chelly J.
Nat. Genet. 48:1349-1358(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN PVNH7, VARIANTS PVNH7 CYS-679; HIS-694; LYS-893 AND GLN-897, CHARACTERIZATION OF VARIANTS PVNH7 HIS-694; LYS-893 AND GLN-897.
Deciphering Developmental Disorders study
Broix L., Jagline H., Ivanova L.E., Schmucker S., Drouot N., Clayton-Smith J., Pagnamenta A.T., Metcalfe K.A., Isidor B., Louvier U.W., Poduri A., Taylor J.C., Tilly P., Poirier K., Saillour Y., Lebrun N., Stemmelen T., Rudolf G. , Muraca G., Saintpierre B., Elmorjani A., Moise M., Weirauch N.B., Guerrini R., Boland A., Olaso R., Masson C., Tripathy R., Keays D., Beldjord C., Nguyen L., Godin J., Kini U., Nischke P., Deleuze J.F., Bahi-Buisson N., Sumara I., Hinckelmann M.V., Chelly J.
Nat. Genet. 48:1349-1358(2016) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077880 | 679 | Y → C in PVNH7. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077881 | 694 | Q → H in PVNH7; increased degradation; changed function in regulation of TOR signaling. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077882 | 893 | E → K in PVNH7; increased degradation; changed function in regulation of TOR signaling. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077883 | 897 | R → Q in PVNH7; increased degradation; changed function in regulation of TOR signaling. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 448 | S → A: Abolishes interaction with 1433F. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 942 | C → S: Abolishes activity. No effect on USP36 protein levels. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 23327 |
MalaCards human disease database More...MalaCardsi | NEDD4L |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 617201 phenotype |
Open Targets More...OpenTargetsi | ENSG00000049759 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31534 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NEDD4L |
Domain mapping of disease mutations (DMDM) More...DMDMi | 73921204 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000120323 | 2 – 975 | E3 ubiquitin-protein ligase NEDD4-likeAdd BLAST | 974 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 312 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 318 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 342 | Phosphoserine; by WNK1 and WNK4Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 367 | Phosphothreonine; by SGK11 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 446 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 448 | Phosphoserine; by PKA and SGK1Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 449 | Phosphoserine; by WNK1 and WNK4Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 464 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 475 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 479 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 483 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 487 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.46"Ubiquitin-specific Protease 36 (USP36) Controls Neuronal Precursor Cell-expressed Developmentally Down-regulated 4-2 (Nedd4-2) Actions over the Neurotrophin Receptor TrkA and Potassium Voltage-gated Channels 7.2/3 (Kv7.2/3)."
Anta B., Martin-Rodriguez C., Gomis-Perez C., Calvo L., Lopez-Benito S., Calderon-Garcia A.A., Vicente-Garcia C., Villarroel A., Arevalo J.C.
J. Biol. Chem. 291:19132-19145(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH USP36, DEUBIQUITINATION BY USP36, MUTAGENESIS OF CYS-942.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q96PU5 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q96PU5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96PU5 |
PeptideAtlas More...PeptideAtlasi | Q96PU5 |
PRoteomics IDEntifications database More...PRIDEi | Q96PU5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 77752 77753 [Q96PU5-2] 77754 [Q96PU5-3] 77755 [Q96PU5-4] 77756 [Q96PU5-5] 77757 [Q96PU5-6] 77758 [Q96PU5-7] 77760 [Q96PU5-9] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96PU5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96PU5 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.28"Identification of NPC2 protein as interaction molecule with C2 domain of human Nedd4L."
Araki N., Ishigami T., Ushio H., Minegishi S., Umemura M., Miyagi Y., Aoki I., Morinaga H., Tamura K., Toya Y., Uchino K., Umemura S.
Biochem. Biophys. Res. Commun. 388:290-296(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NPC2, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000049759 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q96PU5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96PU5 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA024618 HPA064730 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
17 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.28"Identification of NPC2 protein as interaction molecule with C2 domain of human Nedd4L."
Araki N., Ishigami T., Ushio H., Minegishi S., Umemura M., Miyagi Y., Aoki I., Morinaga H., Tamura K., Toya Y., Uchino K., Umemura S.
Biochem. Biophys. Res. Commun. 388:290-296(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NPC2, TISSUE SPECIFICITY. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.38"Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated downregulation of KCNQ1 potassium channels."
Krzystanek K., Rasmussen H.B., Grunnet M., Staub O., Olesen S.P., Abriel H., Jespersen T.
Heart Rhythm 9:440-448(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KCNQ1. - Ref.39"Mammalian alpha arrestins link activated seven transmembrane receptors to Nedd4 family e3 ubiquitin ligases and interact with beta arrestins."
Shea F.F., Rowell J.L., Li Y., Chang T.H., Alvarez C.E.
PLoS ONE 7:E50557-E50557(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ARRDC4. - Ref.44"Regulation of the human ether-a-go-go-related gene (hERG) potassium channel by Nedd4 family interacting proteins (Ndfips)."
Kang Y., Guo J., Yang T., Li W., Zhang S.
Biochem. J. 472:71-82(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NDFIP1 AND NDFIP2, SUBCELLULAR LOCATION. - Ref.46"Ubiquitin-specific Protease 36 (USP36) Controls Neuronal Precursor Cell-expressed Developmentally Down-regulated 4-2 (Nedd4-2) Actions over the Neurotrophin Receptor TrkA and Potassium Voltage-gated Channels 7.2/3 (Kv7.2/3)."
Anta B., Martin-Rodriguez C., Gomis-Perez C., Calvo L., Lopez-Benito S., Calderon-Garcia A.A., Vicente-Garcia C., Villarroel A., Arevalo J.C.
J. Biol. Chem. 291:19132-19145(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH USP36, DEUBIQUITINATION BY USP36, MUTAGENESIS OF CYS-942.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| DAZAP2 | Q15038 | 3 | EBI-717962,EBI-724310 | |
| SLC11A2 | P49281 | 2 | EBI-717962,EBI-4319335 | |
| SMAD7 | O15105 | 3 | EBI-7196393,EBI-3861591 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ion channel binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116915, 212 interactors |
Database of interacting proteins More...DIPi | DIP-41935N |
Protein interaction database and analysis system More...IntActi | Q96PU5, 28 interactors |
Molecular INTeraction database More...MINTi | Q96PU5 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000383199 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 9 – 11 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 16 – 18 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 20 – 31 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 43 – 51 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 52 – 55 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 56 – 62 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 73 – 82 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 84 – 86 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 87 – 95 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 98 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 103 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 129 – 132 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 145 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 391 – 396 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 397 – 399 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 400 – 405 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 406 – 409 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 410 – 414 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 417 – 419 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 503 – 508 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 509 – 511 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 512 – 517 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 518 – 521 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 522 – 526 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 528 – 534 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 594 – 607 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 612 – 614 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 616 – 622 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 624 – 626 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 627 – 637 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 641 – 645 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 646 – 652 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 653 – 655 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 660 – 675 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 678 – 680 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 681 – 687 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 688 – 690 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 693 – 695 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 699 – 702 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 706 – 723 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 728 – 731 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 733 – 739 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 746 – 749 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 750 – 752 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 754 – 765 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 769 – 771 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 774 – 781 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 784 – 791 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 794 – 796 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 801 – 803 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 804 – 816 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 817 – 819 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 821 – 834 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 837 – 840 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 845 – 853 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 860 – 865 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 868 – 870 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 878 – 889 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 892 – 903 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 913 – 915 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 919 – 922 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 926 – 929 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 933 – 935 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 938 – 940 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 941 – 943 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 945 – 948 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 954 – 965 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96PU5 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96PU5 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q96PU5 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 7 – 109 | C2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 103 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 193 – 226 | WW 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 34 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 385 – 418 | WW 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 34 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 497 – 530 | WW 3PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 34 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 548 – 581 | WW 4PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 34 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 640 – 974 | HECTPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 335 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0940 Eukaryota COG5021 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118966 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004134 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96PU5 |
KEGG Orthology (KO) More...KOi | K13305 |
Identification of Orthologs from Complete Genome Data More...OMAi | SEQRDDM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0SS8 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96PU5 |
TreeFam database of animal gene trees More...TreeFami | TF323658 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00078 HECTc, 1 hit cd00201 WW, 4 hits |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.150, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000008 C2_dom IPR035892 C2_domain_sf IPR024928 E3_ub_ligase_SMURF1 IPR000569 HECT_dom IPR035983 Hect_E3_ubiquitin_ligase IPR001202 WW_dom IPR036020 WW_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00168 C2, 1 hit PF00632 HECT, 1 hit PF00397 WW, 4 hits |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF001569 E3_ub_ligase_SMURF1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00360 C2DOMAIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00239 C2, 1 hit SM00119 HECTc, 1 hit SM00456 WW, 4 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51045 SSF51045, 4 hits SSF56204 SSF56204, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50004 C2, 1 hit PS50237 HECT, 1 hit PS01159 WW_DOMAIN_1, 4 hits PS50020 WW_DOMAIN_2, 4 hits |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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.
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
The sequence of this isoform differs from the canonical sequence as follows:
356-419: Missing.
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
GHLPPLAEDG ASGSATNSNN HLIEPQIRRP RSLSSPTVTL SAPLEGAKDS
410 420 430 440 450
PVRRAVKDTL SNPQSPQPSP YNSPKPQHKV TQSFLPPGWE MRIAPNGRPF
460 470 480 490 500
FIDHNTKTTT WEDPRLKFPV HMRSKTSLNP NDLGPLPPGW EERIHLDGRT
510 520 530 540 550
FYIDHNSKIT QWEDPRLQNP AITGPAVPYS REFKQKYDYF RKKLKKPADI
560 570 580 590 600
PNRFEMKLHR NNIFEESYRR IMSVKRPDVL KARLWIEFES EKGLDYGGVA
610 620 630 640 650
REWFFLLSKE MFNPYYGLFE YSATDNYTLQ INPNSGLCNE DHLSYFTFIG
660 670 680 690 700
RVAGLAVFHG KLLDGFFIRP FYKMMLGKQI TLNDMESVDS EYYNSLKWIL
710 720 730 740 750
ENDPTELDLM FCIDEENFGQ TYQVDLKPNG SEIMVTNENK REYIDLVIQW
760 770 780 790 800
RFVNRVQKQM NAFLEGFTEL LPIDLIKIFD ENELELLMCG LGDVDVNDWR
810 820 830 840 850
QHSIYKNGYC PNHPVIQWFW KAVLLMDAEK RIRLLQFVTG TSRVPMNGFA
860 870 880 890 900
ELYGSNGPQL FTIEQWGSPE KLPRAHTCFN RLDLPPYETF EDLREKLLMA
910
VENAQGFEGV D
The sequence of this isoform differs from the canonical sequence as follows:
356-459: Missing.
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
GHLPPGAKDS PVRRAVKDTL SNPQSPQPSP YNSPKPQHKV TQSFLPPGWE
410 420 430 440 450
MRIAPNGRPF FIDHNTKTTT WEDPRLKFPV HMRSKTSLNP NDLGPLPPGW
460 470 480 490 500
EERIHLDGRT FYIDHNSKIT QWEDPRLQNP AITGPAVPYS REFKQKYDYF
510 520 530 540 550
RKKLKKPADI PNRFEMKLHR NNIFEESYRR IMSVKRPDVL KARLWIEFES
560 570 580 590 600
EKGLDYGGVA REWFFLLSKE MFNPYYGLFE YSATDNYTLQ INPNSGLCNE
610 620 630 640 650
DHLSYFTFIG RVAGLAVFHG KLLDGFFIRP FYKMMLGKQI TLNDMESVDS
660 670 680 690 700
EYYNSLKWIL ENDPTELDLM FCIDEENFGQ TYQVDLKPNG SEIMVTNENK
710 720 730 740 750
REYIDLVIQW RFVNRVQKQM NAFLEGFTEL LPIDLIKIFD ENELELLMCG
760 770 780 790 800
LGDVDVNDWR QHSIYKNGYC PNHPVIQWFW KAVLLMDAEK RIRLLQFVTG
810 820 830 840 850
TSRVPMNGFA ELYGSNGPQL FTIEQWGSPE KLPRAHTCFN RLDLPPYETF
860 870
EDLREKLLMA VENAQGFEGV D
The sequence of this isoform differs from the canonical sequence as follows:
1-121: Missing.
10 20 30 40 50
MERPYTFKDF LLRPRSHKSR VKGFLRLKMA YMPKNGGQDE ENSDQRDDME
60 70 80 90 100
HGWEVVDSND SASQHQEELP PPPLPPGWEE KVDNLGRTYY VNHNNRTTQW
110 120 130 140 150
HRPSLMDVSS ESDNNIRQIN QEAAHRRFRS RRHISEDLEP EPSEGGDVPE
160 170 180 190 200
PWETISEEVN IAGDSLGLAL PPPPASPGSR TSPQELSEEL SRRLQITPDS
210 220 230 240 250
NGEQFSSLIQ REPSSRLRSC SVTDAVAEQG HLPPPSAPAG RARSSTVTGG
260 270 280 290 300
EEPTPSVAYV HTTPGLPSGW EERKDAKGRT YYVNHNNRTT TWTRPIMQLA
310 320 330 340 350
EDGASGSATN SNNHLIEPQI RRPRSLSSPT VTLSAPLEGA KDSPVRRAVK
360 370 380 390 400
DTLSNPQSPQ PSPYNSPKPQ HKVTQSFLPP GWEMRIAPNG RPFFIDHNTK
410 420 430 440 450
TTTWEDPRLK FPVHMRSKTS LNPNDLGPLP PGWEERIHLD GRTFYIDHNS
460 470 480 490 500
KITQWEDPRL QNPAITGPAV PYSREFKQKY DYFRKKLKKP ADIPNRFEMK
510 520 530 540 550
LHRNNIFEES YRRIMSVKRP DVLKARLWIE FESEKGLDYG GVAREWFFLL
560 570 580 590 600
SKEMFNPYYG LFEYSATDNY TLQINPNSGL CNEDHLSYFT FIGRVAGLAV
610 620 630 640 650
FHGKLLDGFF IRPFYKMMLG KQITLNDMES VDSEYYNSLK WILENDPTEL
660 670 680 690 700
DLMFCIDEEN FGQTYQVDLK PNGSEIMVTN ENKREYIDLV IQWRFVNRVQ
710 720 730 740 750
KQMNAFLEGF TELLPIDLIK IFDENELELL MCGLGDVDVN DWRQHSIYKN
760 770 780 790 800
GYCPNHPVIQ WFWKAVLLMD AEKRIRLLQF VTGTSRVPMN GFAELYGSNG
810 820 830 840 850
PQLFTIEQWG SPEKLPRAHT CFNRLDLPPY ETFEDLREKL LMAVENAQGF
EGVD
The sequence of this isoform differs from the canonical sequence as follows:
356-375: Missing.
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
GHLPPPSVAY VHTTPGLPSG WEERKDAKGR TYYVNHNNRT TTWTRPIMQL
410 420 430 440 450
AEDGASGSAT NSNNHLIEPQ IRRPRSLSSP TVTLSAPLEG AKDSPVRRAV
460 470 480 490 500
KDTLSNPQSP QPSPYNSPKP QHKVTQSFLP PGWEMRIAPN GRPFFIDHNT
510 520 530 540 550
KTTTWEDPRL KFPVHMRSKT SLNPNDLGPL PPGWEERIHL DGRTFYIDHN
560 570 580 590 600
SKITQWEDPR LQNPAITGPA VPYSREFKQK YDYFRKKLKK PADIPNRFEM
610 620 630 640 650
KLHRNNIFEE SYRRIMSVKR PDVLKARLWI EFESEKGLDY GGVAREWFFL
660 670 680 690 700
LSKEMFNPYY GLFEYSATDN YTLQINPNSG LCNEDHLSYF TFIGRVAGLA
710 720 730 740 750
VFHGKLLDGF FIRPFYKMML GKQITLNDME SVDSEYYNSL KWILENDPTE
760 770 780 790 800
LDLMFCIDEE NFGQTYQVDL KPNGSEIMVT NENKREYIDL VIQWRFVNRV
810 820 830 840 850
QKQMNAFLEG FTELLPIDLI KIFDENELEL LMCGLGDVDV NDWRQHSIYK
860 870 880 890 900
NGYCPNHPVI QWFWKAVLLM DAEKRIRLLQ FVTGTSRVPM NGFAELYGSN
910 920 930 940 950
GPQLFTIEQW GSPEKLPRAH TCFNRLDLPP YETFEDLREK LLMAVENAQG
FEGVD
The sequence of this isoform differs from the canonical sequence as follows:
1-16: MATGLGEPVYGLSEDE → MRRLAFEQ
356-375: Missing.
10 20 30 40 50
MRRLAFEQGE SRILRVKVVS GIDLAKKDIF GASDPYVKLS LYVADENREL
60 70 80 90 100
ALVQTKTIKK TLNPKWNEEF YFRVNPSNHR LLFEVFDENR LTRDDFLGQV
110 120 130 140 150
DVPLSHLPTE DPTMERPYTF KDFLLRPRSH KSRVKGFLRL KMAYMPKNGG
160 170 180 190 200
QDEENSDQRD DMEHGWEVVD SNDSASQHQE ELPPPPLPPG WEEKVDNLGR
210 220 230 240 250
TYYVNHNNRT TQWHRPSLMD VSSESDNNIR QINQEAAHRR FRSRRHISED
260 270 280 290 300
LEPEPSEGGD VPEPWETISE EVNIAGDSLG LALPPPPASP GSRTSPQELS
310 320 330 340 350
EELSRRLQIT PDSNGEQFSS LIQREPSSRL RSCSVTDAVA EQGHLPPPSV
360 370 380 390 400
AYVHTTPGLP SGWEERKDAK GRTYYVNHNN RTTTWTRPIM QLAEDGASGS
410 420 430 440 450
ATNSNNHLIE PQIRRPRSLS SPTVTLSAPL EGAKDSPVRR AVKDTLSNPQ
460 470 480 490 500
SPQPSPYNSP KPQHKVTQSF LPPGWEMRIA PNGRPFFIDH NTKTTTWEDP
510 520 530 540 550
RLKFPVHMRS KTSLNPNDLG PLPPGWEERI HLDGRTFYID HNSKITQWED
560 570 580 590 600
PRLQNPAITG PAVPYSREFK QKYDYFRKKL KKPADIPNRF EMKLHRNNIF
610 620 630 640 650
EESYRRIMSV KRPDVLKARL WIEFESEKGL DYGGVAREWF FLLSKEMFNP
660 670 680 690 700
YYGLFEYSAT DNYTLQINPN SGLCNEDHLS YFTFIGRVAG LAVFHGKLLD
710 720 730 740 750
GFFIRPFYKM MLGKQITLND MESVDSEYYN SLKWILENDP TELDLMFCID
760 770 780 790 800
EENFGQTYQV DLKPNGSEIM VTNENKREYI DLVIQWRFVN RVQKQMNAFL
810 820 830 840 850
EGFTELLPID LIKIFDENEL ELLMCGLGDV DVNDWRQHSI YKNGYCPNHP
860 870 880 890 900
VIQWFWKAVL LMDAEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQLFTIE
910 920 930 940
QWGSPEKLPR AHTCFNRLDL PPYETFEDLR EKLLMAVENA QGFEGVD
The sequence of this isoform differs from the canonical sequence as follows:
1-16: MATGLGEPVYGLSEDE → MRRLAFEQ
10 20 30 40 50
MRRLAFEQGE SRILRVKVVS GIDLAKKDIF GASDPYVKLS LYVADENREL
60 70 80 90 100
ALVQTKTIKK TLNPKWNEEF YFRVNPSNHR LLFEVFDENR LTRDDFLGQV
110 120 130 140 150
DVPLSHLPTE DPTMERPYTF KDFLLRPRSH KSRVKGFLRL KMAYMPKNGG
160 170 180 190 200
QDEENSDQRD DMEHGWEVVD SNDSASQHQE ELPPPPLPPG WEEKVDNLGR
210 220 230 240 250
TYYVNHNNRT TQWHRPSLMD VSSESDNNIR QINQEAAHRR FRSRRHISED
260 270 280 290 300
LEPEPSEGGD VPEPWETISE EVNIAGDSLG LALPPPPASP GSRTSPQELS
310 320 330 340 350
EELSRRLQIT PDSNGEQFSS LIQREPSSRL RSCSVTDAVA EQGHLPPPSA
360 370 380 390 400
PAGRARSSTV TGGEEPTPSV AYVHTTPGLP SGWEERKDAK GRTYYVNHNN
410 420 430 440 450
RTTTWTRPIM QLAEDGASGS ATNSNNHLIE PQIRRPRSLS SPTVTLSAPL
460 470 480 490 500
EGAKDSPVRR AVKDTLSNPQ SPQPSPYNSP KPQHKVTQSF LPPGWEMRIA
510 520 530 540 550
PNGRPFFIDH NTKTTTWEDP RLKFPVHMRS KTSLNPNDLG PLPPGWEERI
560 570 580 590 600
HLDGRTFYID HNSKITQWED PRLQNPAITG PAVPYSREFK QKYDYFRKKL
610 620 630 640 650
KKPADIPNRF EMKLHRNNIF EESYRRIMSV KRPDVLKARL WIEFESEKGL
660 670 680 690 700
DYGGVAREWF FLLSKEMFNP YYGLFEYSAT DNYTLQINPN SGLCNEDHLS
710 720 730 740 750
YFTFIGRVAG LAVFHGKLLD GFFIRPFYKM MLGKQITLND MESVDSEYYN
760 770 780 790 800
SLKWILENDP TELDLMFCID EENFGQTYQV DLKPNGSEIM VTNENKREYI
810 820 830 840 850
DLVIQWRFVN RVQKQMNAFL EGFTELLPID LIKIFDENEL ELLMCGLGDV
860 870 880 890 900
DVNDWRQHSI YKNGYCPNHP VIQWFWKAVL LMDAEKRIRL LQFVTGTSRV
910 920 930 940 950
PMNGFAELYG SNGPQLFTIE QWGSPEKLPR AHTCFNRLDL PPYETFEDLR
960
EKLLMAVENA QGFEGVD
The sequence of this isoform differs from the canonical sequence as follows:
1-121: Missing.
356-375: Missing.
10 20 30 40 50
MERPYTFKDF LLRPRSHKSR VKGFLRLKMA YMPKNGGQDE ENSDQRDDME
60 70 80 90 100
HGWEVVDSND SASQHQEELP PPPLPPGWEE KVDNLGRTYY VNHNNRTTQW
110 120 130 140 150
HRPSLMDVSS ESDNNIRQIN QEAAHRRFRS RRHISEDLEP EPSEGGDVPE
160 170 180 190 200
PWETISEEVN IAGDSLGLAL PPPPASPGSR TSPQELSEEL SRRLQITPDS
210 220 230 240 250
NGEQFSSLIQ REPSSRLRSC SVTDAVAEQG HLPPPSVAYV HTTPGLPSGW
260 270 280 290 300
EERKDAKGRT YYVNHNNRTT TWTRPIMQLA EDGASGSATN SNNHLIEPQI
310 320 330 340 350
RRPRSLSSPT VTLSAPLEGA KDSPVRRAVK DTLSNPQSPQ PSPYNSPKPQ
360 370 380 390 400
HKVTQSFLPP GWEMRIAPNG RPFFIDHNTK TTTWEDPRLK FPVHMRSKTS
410 420 430 440 450
LNPNDLGPLP PGWEERIHLD GRTFYIDHNS KITQWEDPRL QNPAITGPAV
460 470 480 490 500
PYSREFKQKY DYFRKKLKKP ADIPNRFEMK LHRNNIFEES YRRIMSVKRP
510 520 530 540 550
DVLKARLWIE FESEKGLDYG GVAREWFFLL SKEMFNPYYG LFEYSATDNY
560 570 580 590 600
TLQINPNSGL CNEDHLSYFT FIGRVAGLAV FHGKLLDGFF IRPFYKMMLG
610 620 630 640 650
KQITLNDMES VDSEYYNSLK WILENDPTEL DLMFCIDEEN FGQTYQVDLK
660 670 680 690 700
PNGSEIMVTN ENKREYIDLV IQWRFVNRVQ KQMNAFLEGF TELLPIDLIK
710 720 730 740 750
IFDENELELL MCGLGDVDVN DWRQHSIYKN GYCPNHPVIQ WFWKAVLLMD
760 770 780 790 800
AEKRIRLLQF VTGTSRVPMN GFAELYGSNG PQLFTIEQWG SPEKLPRAHT
810 820 830
CFNRLDLPPY ETFEDLREKL LMAVENAQGF EGVD
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 52 | A → P in AAM76729 (PubMed:14615060).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 52 | A → P in AAM76730 (PubMed:14615060).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 188 | E → K in AAP75706 (PubMed:14556380).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_023415 | 355 | P → L Common polymorphism; impaired ability to inhibit SCNN. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_023416 | 497 | S → R1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077880 | 679 | Y → C in PVNH7. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077881 | 694 | Q → H in PVNH7; increased degradation; changed function in regulation of TOR signaling. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077882 | 893 | E → K in PVNH7; increased degradation; changed function in regulation of TOR signaling. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_077883 | 897 | R → Q in PVNH7; increased degradation; changed function in regulation of TOR signaling. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_015444 | 1 – 121 | Missing in isoform 4 and isoform 8. 4 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 121 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_015446 | 1 – 16 | MATGL…LSEDE → MRRLAFEQ in isoform 6 and isoform 7. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 16 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_015447 | 356 – 459 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 104 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_015448 | 356 – 419 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 64 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043848 | 356 – 375 | Missing in isoform 5, isoform 6 and isoform 8. 5 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 20 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
The Consensus CDS (CCDS) project More...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] |
Protein sequence database of the Protein Information Resource More...PIRi | T46412 |
NCBI Reference Sequences More...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] XP_016881168.1, XM_017025679.1 [Q96PU5-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.185677 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...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] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23327 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23327 |
UCSC genome browser More...UCSCi | uc002lgx.4 human [Q96PU5-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q96PU5 | NEDD4L isoform 5 | 975 | |||
| Uncharacterized protein | 975 | ||||
| Q96PU5-2 | E3 ubiquitin-protein ligase | 911 | |||
| E3 ubiquitin-protein ligase | 911 | ||||
| Q96PU5-3 | E3 ubiquitin-protein ligase | 871 | |||
| E3 ubiquitin-protein ligase | 871 | ||||
| Q96PU5-4 | E3 ubiquitin-protein ligase NEDD4-like | 1254 | |||
| E3 ubiquitin-protein ligase | 854 | ||||
| E3 ubiquitin-protein ligase | 854 | ||||
| UPI0005D004E4 | 942 | ||||
| Q96PU5-5 | NEDD4L isoform 2 | 955 | |||
| Uncharacterized protein | 955 | ||||
| Q96PU5-7 | NEDD4L isoform 7 | 967 | |||
| Uncharacterized protein | 967 | ||||
| Q96PU5-9 | E3 ubiquitin-protein ligase | 834 | |||
| E3 ubiquitin-protein ligase | 834 | ||||
| UPI000512647C | 1234 | ||||
| UPI0005CFFDD0 | 922 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
The Consensus CDS (CCDS) project More...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] |
Protein sequence database of the Protein Information Resource More...PIRi | T46412 |
NCBI Reference Sequences More...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] XP_016881168.1, XM_017025679.1 [Q96PU5-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.185677 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2LAJ | NMR | - | A | 496-535 | [»] | |
| 2LB2 | NMR | - | A | 386-420 | [»] | |
| 2LTY | NMR | - | A | 385-417 | [»] | |
| 2MPT | NMR | - | A | 496-539 | [»] | |
| B | 945-957 | [»] | ||||
| 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 | [»] | |
| 5HPK | X-ray | 2.43 | A | 594-975 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96PU5 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96PU5 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116915, 212 interactors |
Database of interacting proteins More...DIPi | DIP-41935N |
Protein interaction database and analysis system More...IntActi | Q96PU5, 28 interactors |
Molecular INTeraction database More...MINTi | Q96PU5 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000383199 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96PU5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96PU5 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NEDD4L |
Domain mapping of disease mutations (DMDM) More...DMDMi | 73921204 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q96PU5 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q96PU5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96PU5 |
PeptideAtlas More...PeptideAtlasi | Q96PU5 |
PRoteomics IDEntifications database More...PRIDEi | Q96PU5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 77752 77753 [Q96PU5-2] 77754 [Q96PU5-3] 77755 [Q96PU5-4] 77756 [Q96PU5-5] 77757 [Q96PU5-6] 77758 [Q96PU5-7] 77760 [Q96PU5-9] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 23327 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...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] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23327 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23327 |
UCSC genome browser More...UCSCi | uc002lgx.4 human [Q96PU5-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 23327 |
DisGeNET More...DisGeNETi | 23327 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000049759.16 |
GeneCards: human genes, protein and diseases More...GeneCardsi | NEDD4L |
Human Gene Nomenclature Database More...HGNCi | HGNC:7728 NEDD4L |
Human Protein Atlas More...HPAi | HPA024618 HPA064730 |
MalaCards human disease database More...MalaCardsi | NEDD4L |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606384 gene 617201 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96PU5 |
Open Targets More...OpenTargetsi | ENSG00000049759 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31534 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0940 Eukaryota COG5021 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118966 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004134 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96PU5 |
KEGG Orthology (KO) More...KOi | K13305 |
Identification of Orthologs from Complete Genome Data More...OMAi | SEQRDDM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0SS8 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96PU5 |
TreeFam database of animal gene trees More...TreeFami | TF323658 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00143 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:ENSG00000049759-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.2.B8 2681 6.3.2.19 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-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 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q96PU5 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q96PU5 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | NEDD4L human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q96PU5 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | NEDD4L |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 23327 |
Protein Ontology More...PROi | PR:Q96PU5 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000049759 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q96PU5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96PU5 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00078 HECTc, 1 hit cd00201 WW, 4 hits |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.150, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000008 C2_dom IPR035892 C2_domain_sf IPR024928 E3_ub_ligase_SMURF1 IPR000569 HECT_dom IPR035983 Hect_E3_ubiquitin_ligase IPR001202 WW_dom IPR036020 WW_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00168 C2, 1 hit PF00632 HECT, 1 hit PF00397 WW, 4 hits |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF001569 E3_ub_ligase_SMURF1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00360 C2DOMAIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00239 C2, 1 hit SM00119 HECTc, 1 hit SM00456 WW, 4 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51045 SSF51045, 4 hits SSF56204 SSF56204, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50004 C2, 1 hit PS50237 HECT, 1 hit PS01159 WW_DOMAIN_1, 4 hits PS50020 WW_DOMAIN_2, 4 hits |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | NED4L_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q96PU5Primary (citable) accession number: Q96PU5 Secondary accession number(s): O43165 , Q3LSM7, Q7Z5F1, Q7Z5F2, Q7Z5N3, Q8N5A7, Q8WUU9, Q9BW58, Q9H2W4, Q9NT88 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 30, 2005 |
| Last sequence update: | August 30, 2005 | |
| Last modified: | July 18, 2018 | |
| This is version 170 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 18
Human chromosome 18: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
