UniProtKB - Q92542 (NICA_HUMAN)
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- BLAST>sp|Q92542|NICA_HUMAN Nicastrin OS=Homo sapiens OX=9606 GN=NCSTN PE=1 SV=2 MATAGGGSGADPGSRGLLRLLSFCVLLAGLCRGNSVERKIYIPLNKTAPCVRLLNATHQI GCQSSISGDTGVIHVVEKEEDLQWVLTDGPNPPYMVLLESKHFTRDLMEKLKGRTSRIAG LAVSLTKPSPASGFSPSVQCPNDGFGVYSNSYGPEFAHCREIQWNSLGNGLAYEDFSFPI FLLEDENETKVIKQCYQDHNLSQNGSAPTFPLCAMQLFSHMHAVISTATCMRRSSIQSTF SINPEIVCDPLSDYNVWSMLKPINTTGTLKPDDRVVVAATRLDSRSFFWNVAPGAESAVA SFVTQLAAAEALQKAPDVTTLPRNVMFVFFQGETFDYIGSSRMVYDMEKGKFPVQLENVD SFVELGQVALRTSLELWMHTDPVSQKNESVRNQVEDLLATLEKSGAGVPAVILRRPNQSQ PLPPSSLQRFLRARNISGVVLADHSGAFHNKYYQSIYDTAENINVSYPEWLSPEEDLNFV TDTAKALADVATVLGRALYELAGGTNFSDTVQADPQTVTRLLYGFLIKANNSWFQSILRQ DLRSYLGDGPLQHYIAVSSPTNTTYVVQYALANLTGTVVNLTREQCQDPSKVPSENKDLY EYSWVQGPLHSNETDRLPRCVRSTARLARALSPAFELSQWSSTEYSTWTESRWKDIRARI FLIASKELELITLTVGFGILIFSLIVTYCINAKADVLFIAPREPGAVSY
- Align
Nicastrin
NCSTN
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 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.1"Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing."
Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., Yu H., Yang D.-S., Holmes E., Milman P., Liang Y., Zhang D.M. , Xu D.H., Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.
Nature 407:48-54(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE GAMMA-SECRETASE COMPLEX, INTERACTION WITH PSEN1 AND PSEN2, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF 336-ASP-TYR-337. - Ref.11"Reconstitution of gamma-secretase activity."
Edbauer D., Winkler E., Regula J.T., Pesold B., Steiner H., Haass C.
Nat. Cell Biol. 5:486-488(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME ACTIVITY OF A GAMMA-SECRETASE COMPLEX. - Ref.18"Three-dimensional structure of human gamma-secretase."
Lu P., Bai X.C., Ma D., Xie T., Yan C., Sun L., Yang G., Zhao Y., Zhou R., Scheres S.H., Shi Y.
Nature 512:166-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION. - Ref.20"An atomic structure of human gamma-secretase."
Bai X.C., Yan C., Yang G., Lu P., Ma D., Sun L., Zhou R., Scheres S.H., Shi Y.
Nature 525:212-217(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-45; ASN-55; ASN-187; ASN-264; ASN-387; ASN-435; ASN-464; ASN-506; ASN-530; ASN-562 AND ASN-573.
<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
- endopeptidase activity Source: GO_Central
<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
- amyloid-beta formation 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
- amyloid precursor protein catabolic process Source: HGNC <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- amyloid precursor protein metabolic process 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
- epithelial cell proliferation Source: Ensembl
- membrane protein ectodomain proteolysis Source: HGNC <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
- myeloid cell homeostasis Source: Ensembl
- neutrophil degranulation Source: Reactome
- Notch receptor processing Source: HGNC <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- Notch receptor processing, ligand-dependent Source: Reactome
- Notch signaling pathway Source: Reactome
- positive regulation of catalytic activity Source: HGNC <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 processing Source: HGNC <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
- proteolysis 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
- T cell proliferation Source: Ensembl
<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
| Biological process | Notch signaling pathway |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1251985 Nuclear signaling by ERBB4 R-HSA-1474228 Degradation of the extracellular matrix R-HSA-193692 Regulated proteolysis of p75NTR R-HSA-1980150 Signaling by NOTCH4 R-HSA-205043 NRIF signals cell death from the nucleus R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants R-HSA-2979096 NOTCH2 Activation and Transmission of Signal to the Nucleus R-HSA-3928665 EPH-ephrin mediated repulsion of cells R-HSA-6798695 Neutrophil degranulation R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus R-HSA-9017802 Noncanonical activation of NOTCH3 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q92542 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q92542 |
<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: Nicastrin |
| <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:NCSTN Synonyms:KIAA0253 ORF Names:UNQ1874/PRO4317 |
| <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:ENSG00000162736.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:17091 NCSTN |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605254 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q92542 |
<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
Other locations
- Membrane 6 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.1"Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing."
Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., Yu H., Yang D.-S., Holmes E., Milman P., Liang Y., Zhang D.M. , Xu D.H., Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.
Nature 407:48-54(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE GAMMA-SECRETASE COMPLEX, INTERACTION WITH PSEN1 AND PSEN2, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF 336-ASP-TYR-337. - Ref.18"Three-dimensional structure of human gamma-secretase."
Lu P., Bai X.C., Ma D., Xie T., Yan C., Sun L., Yang G., Zhao Y., Zhou R., Scheres S.H., Shi Y.
Nature 512:166-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION. - Ref.19"Sampling the conformational space of the catalytic subunit of human gamma-secretase."
Bai X.C., Rajendra E., Yang G., Shi Y., Scheres S.H.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT. - Ref.20"An atomic structure of human gamma-secretase."
Bai X.C., Yan C., Yang G., Lu P., Ma D., Sun L., Zhou R., Scheres S.H., Shi Y.
Nature 525:212-217(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-45; ASN-55; ASN-187; ASN-264; ASN-387; ASN-435; ASN-464; ASN-506; ASN-530; ASN-562 AND ASN-573. - Ref.21"Structural basis of human gamma-secretase assembly."
Sun L., Zhao L., Yang G., Yan C., Zhou R., Zhou X., Xie T., Zhao Y., Wu S., Li X., Shi Y.
Proc. Natl. Acad. Sci. U.S.A. 112:6003-6008(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS) OF 42-665, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT. - Ref.22"Structure of the transmembrane domain of human nicastrin-a component of gamma-secretase."
Li Y., Liew L.S., Li Q., Kang C.
Sci. Rep. 6:19522-19522(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 664-709, SUBCELLULAR LOCATION.
<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.18"Three-dimensional structure of human gamma-secretase."
Lu P., Bai X.C., Ma D., Xie T., Yan C., Sun L., Yang G., Zhao Y., Zhou R., Scheres S.H., Shi Y.
Nature 512:166-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION. - Ref.19"Sampling the conformational space of the catalytic subunit of human gamma-secretase."
Bai X.C., Rajendra E., Yang G., Shi Y., Scheres S.H.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT. - Ref.20"An atomic structure of human gamma-secretase."
Bai X.C., Yan C., Yang G., Lu P., Ma D., Sun L., Zhou R., Scheres S.H., Shi Y.
Nature 525:212-217(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-45; ASN-55; ASN-187; ASN-264; ASN-387; ASN-435; ASN-464; ASN-506; ASN-530; ASN-562 AND ASN-573. - Ref.21"Structural basis of human gamma-secretase assembly."
Sun L., Zhao L., Yang G., Yan C., Zhou R., Zhou X., Xie T., Zhao Y., Wu S., Li X., Shi Y.
Proc. Natl. Acad. Sci. U.S.A. 112:6003-6008(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS) OF 42-665, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT.
- Cytoplasmic vesicle membrane 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.1"Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing."
Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., Yu H., Yang D.-S., Holmes E., Milman P., Liang Y., Zhang D.M. , Xu D.H., Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.
Nature 407:48-54(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE GAMMA-SECRETASE COMPLEX, INTERACTION WITH PSEN1 AND PSEN2, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF 336-ASP-TYR-337.
<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.18"Three-dimensional structure of human gamma-secretase."
Lu P., Bai X.C., Ma D., Xie T., Yan C., Sun L., Yang G., Zhao Y., Zhou R., Scheres S.H., Shi Y.
Nature 512:166-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION. - Ref.19"Sampling the conformational space of the catalytic subunit of human gamma-secretase."
Bai X.C., Rajendra E., Yang G., Shi Y., Scheres S.H.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT. - Ref.20"An atomic structure of human gamma-secretase."
Bai X.C., Yan C., Yang G., Lu P., Ma D., Sun L., Zhou R., Scheres S.H., Shi Y.
Nature 525:212-217(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-45; ASN-55; ASN-187; ASN-264; ASN-387; ASN-435; ASN-464; ASN-506; ASN-530; ASN-562 AND ASN-573. - Ref.21"Structural basis of human gamma-secretase assembly."
Sun L., Zhao L., Yang G., Yan C., Zhou R., Zhou X., Xie T., Zhao Y., Wu S., Li X., Shi Y.
Proc. Natl. Acad. Sci. U.S.A. 112:6003-6008(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS) OF 42-665, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT.
- Melanosome 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
- Ref.9"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. - Ref.13"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.- Membrane 6 Publications
Endoplasmic reticulum
- endoplasmic reticulum Source: HGNC <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
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- Golgi apparatus Source: HGNC <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
Lysosome
- azurophil granule membrane Source: Reactome
- lysosomal membrane Source: UniProtKBInferred from high throughput direct assayi
Plasma Membrane
- gamma-secretase complex 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
- integral component of plasma membrane Source: HGNC <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
- plasma membrane Source: Reactome
Other locations
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- integral component of membrane 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
- melanosome Source: UniProtKB-SubCell
- membrane Source: UniProtKBInferred from high throughput direct assayi
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 34 – 669 | Extracellular2 Publications <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
| 636 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 670 – 690 | Helical2 Publications <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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 691 – 709 | Cytoplasmic2 Publications <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
| 19 |
<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
Cytoplasmic vesicle, Membrane<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
Acne inversa, familial, 1 (ACNINV1)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.24"Confirmation by exome sequencing of the pathogenic role of NCSTN mutations in acne inversa (hidradenitis suppurativa)."
Liu Y., Gao M., Lv Y.M., Yang X., Ren Y.Q., Jiang T., Zhang X., Guo B.R., Li M., Zhang Q., Zhang P., Zhou F.S., Chen G., Yin X.Y., Zuo X.B., Sun L.D., Zheng X.D., Zhang S.M. , Liu J.J., Zhou Y., Li Y.R., Wang J., Wang J., Yang H.M., Yang S., Li R.Q., Zhang X.J.
J. Invest. Dermatol. 131:1570-1572(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN ACNINV1. - Ref.25"Two novel mutations of the nicastrin gene in Chinese patients with acne inversa."
Li C.R., Jiang M.J., Shen D.B., Xu H.X., Wang H.S., Yao X., Zhang Y., Zhou W.Q., Wang B.
Br. J. Dermatol. 165:415-418(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ACNINV1 ARG-211.
Liu Y., Gao M., Lv Y.M., Yang X., Ren Y.Q., Jiang T., Zhang X., Guo B.R., Li M., Zhang Q., Zhang P., Zhou F.S., Chen G., Yin X.Y., Zuo X.B., Sun L.D., Zheng X.D., Zhang S.M. , Liu J.J., Zhou Y., Li Y.R., Wang J., Wang J., Yang H.M., Yang S., Li R.Q., Zhang X.J.
J. Invest. Dermatol. 131:1570-1572(2011) [PubMed] [Europe PMC] [Abstract]
Li C.R., Jiang M.J., Shen D.B., Xu H.X., Wang H.S., Yao X., Zhang Y., Zhou W.Q., Wang B.
Br. J. Dermatol. 165:415-418(2011) [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_067756 | 211 | P → R in ACNINV1. 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 | 336 – 337 | DY → AA: Increases production of amyloid-beta (beta-APP40 and beta-APP42) in APP processing. 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
| 2 |
<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 - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 23385 |
MalaCards human disease database More...MalaCardsi | NCSTN |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 142690 phenotype |
Open Targets More...OpenTargetsi | ENSG00000162736 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 387 Hidradenitis suppurativa |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142671271 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3418 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NCSTN |
Domain mapping of disease mutations (DMDM) More...DMDMi | 12231037 |
<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 ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 33 | Sequence analysisAdd BLAST | 33 | |
| <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_0000019681 | 34 – 709 | NicastrinAdd BLAST | 676 |
Amino acid modifications
| 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 specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 45 | N-linked (GlcNAc...) asparagineCombined 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 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 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 50 ↔ 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 2 Publications<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
<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
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 55 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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 PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 140 ↔ 159 | 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 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
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 187 | N-linked (GlcNAc...) asparagineCombined 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 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 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 195 ↔ 213 | 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 1 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
<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
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 200 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 204 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 230 ↔ 248 | 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 1 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
<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
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 264 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 387 | N-linked (GlcNAc...) asparagineCombined 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 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 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 417 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 435 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 464 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 506 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 530 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 562 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 573 | N-linked (GlcNAc...) asparagineSequence analysisCombined 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 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 580 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 586 ↔ 620 | 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 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
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 612 | N-linked (GlcNAc...) asparagine1 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/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.1"Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing."
Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., Yu H., Yang D.-S., Holmes E., Milman P., Liang Y., Zhang D.M. , Xu D.H., Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.
Nature 407:48-54(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE GAMMA-SECRETASE COMPLEX, INTERACTION WITH PSEN1 AND PSEN2, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF 336-ASP-TYR-337. - Ref.18"Three-dimensional structure of human gamma-secretase."
Lu P., Bai X.C., Ma D., Xie T., Yan C., Sun L., Yang G., Zhao Y., Zhou R., Scheres S.H., Shi Y.
Nature 512:166-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION. - Ref.20"An atomic structure of human gamma-secretase."
Bai X.C., Yan C., Yang G., Lu P., Ma D., Sun L., Zhou R., Scheres S.H., Shi Y.
Nature 525:212-217(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-45; ASN-55; ASN-187; ASN-264; ASN-387; ASN-435; ASN-464; ASN-506; ASN-530; ASN-562 AND ASN-573.
<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
Disulfide bond, GlycoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q92542 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q92542 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q92542 |
PeptideAtlas More...PeptideAtlasi | Q92542 |
PRoteomics IDEntifications database More...PRIDEi | Q92542 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 75302 75303 [Q92542-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q92542-2 [Q92542-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q92542 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q92542 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q92542 |
<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.1"Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing."
Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., Yu H., Yang D.-S., Holmes E., Milman P., Liang Y., Zhang D.M. , Xu D.H., Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.
Nature 407:48-54(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE GAMMA-SECRETASE COMPLEX, INTERACTION WITH PSEN1 AND PSEN2, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF 336-ASP-TYR-337. - Ref.8"Nicastrin, a key regulator of presenilin function, is expressed constitutively in human neural cell lines."
Satoh J., Kuroda Y.
Neuropathology 21:115-122(2001) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION.
<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.8"Nicastrin, a key regulator of presenilin function, is expressed constitutively in human neural cell lines."
Satoh J., Kuroda Y.
Neuropathology 21:115-122(2001) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000162736 |
CleanEx database of gene expression profiles More...CleanExi | HS_NCSTN |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q92542 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q92542 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB021982 HPA054846 HPA070642 |
<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 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.1"Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing."
Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., Yu H., Yang D.-S., Holmes E., Milman P., Liang Y., Zhang D.M. , Xu D.H., Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.
Nature 407:48-54(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE GAMMA-SECRETASE COMPLEX, INTERACTION WITH PSEN1 AND PSEN2, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF 336-ASP-TYR-337. - Ref.10"Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2."
Kimberly W.T., LaVoie M.J., Ostaszewski B.L., Ye W., Wolfe M.S., Selkoe D.J.
Proc. Natl. Acad. Sci. U.S.A. 100:6382-6387(2003) [PubMed] [Europe PMC] [Abstract]Cited for: COMPONENT OF A GAMMA-SECRETASE COMPLEX WITH PEN2; PSEN1/PSEN2 AND APH1A. - Ref.18"Three-dimensional structure of human gamma-secretase."
Lu P., Bai X.C., Ma D., Xie T., Yan C., Sun L., Yang G., Zhao Y., Zhou R., Scheres S.H., Shi Y.
Nature 512:166-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION. - Ref.19"Sampling the conformational space of the catalytic subunit of human gamma-secretase."
Bai X.C., Rajendra E., Yang G., Shi Y., Scheres S.H.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT. - Ref.20"An atomic structure of human gamma-secretase."
Bai X.C., Yan C., Yang G., Lu P., Ma D., Sun L., Zhou R., Scheres S.H., Shi Y.
Nature 525:212-217(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-45; ASN-55; ASN-187; ASN-264; ASN-387; ASN-435; ASN-464; ASN-506; ASN-530; ASN-562 AND ASN-573. - Ref.21"Structural basis of human gamma-secretase assembly."
Sun L., Zhao L., Yang G., Yan C., Zhou R., Zhou X., Xie T., Zhao Y., Wu S., Li X., Shi Y.
Proc. Natl. Acad. Sci. U.S.A. 112:6003-6008(2015) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS) OF 42-665, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT.
<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 |
|---|---|---|---|---|
| APH1A | Q96BI3 | 4 | EBI-998440,EBI-2606935 | |
| PSEN1 | P49768 | 3 | EBI-998440,EBI-297277 | |
| PSENEN | Q9NZ42 | 3 | EBI-998440,EBI-998468 | |
| TMED10 | P49755 | 5 | EBI-998440,EBI-998422 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116961, 136 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q92542 |
Database of interacting proteins More...DIPi | DIP-36336N |
Protein interaction database and analysis system More...IntActi | Q92542, 67 interactors |
Molecular INTeraction database More...MINTi | Q92542 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000294785 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q92542 |
<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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 35 – 40 | 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 | 41 – 44 | 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 | 46 – 49 | 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 | 59 – 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 | 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 | 70 – 78 | 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 | 79 – 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 | 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 | 90 – 99 | 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 | 100 – 102 | 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 | 105 – 113 | 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 | 114 – 117 | 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 | 121 – 124 | 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 | 141 – 145 | 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 | 150 – 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 | 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 | 154 – 156 | 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 | 174 – 178 | 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 | 180 – 183 | 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 | 186 – 199 | 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 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 | 204 – 206 | 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 | 210 – 218 | 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 | 220 – 222 | 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 | 227 – 239 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 241 – 243 | 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 | 248 – 250 | 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 | 253 – 261 | 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 | 271 – 273 | 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 | 275 – 281 | 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 | 287 – 290 | 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 | 295 – 298 | 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 | 299 – 314 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 322 – 331 | 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 | 333 – 339 | 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 | 340 – 349 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 352 – 354 | 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 | 356 – 358 | 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 | 359 – 367 | 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 | 374 – 379 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 382 – 386 | 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 | 388 – 406 | 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 | 19 | |
| <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 | 411 – 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 | 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 | 426 – 433 | 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 | 438 – 443 | 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 | 445 – 447 | 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 | 460 – 463 | 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 | 475 – 478 | 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 | 482 – 502 | 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 | 21 | |
| <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 | 508 – 510 | 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 | 515 – 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 | 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 | 529 – 532 | 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 | 535 – 537 | 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 | 542 – 545 | 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 | 557 – 560 | 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 | 562 – 575 | 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 | 576 – 579 | 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 | 583 – 587 | 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 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 | 589 – 591 | 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 | 592 – 595 | 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 | 597 – 599 | 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 | 601 – 605 | 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 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 | 611 – 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 | 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 | 619 – 623 | 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 | 627 – 630 | 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 | 633 – 636 | 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 | 643 – 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 | 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 | 649 – 651 | 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 | 657 – 664 | 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 | 666 – 692 | 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 | 27 | |
| <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 | 694 – 697 | 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 | 698 – 700 | 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 | 704 – 706 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q92542 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q92542 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<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
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<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
Signal, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2657 Eukaryota ENOG410XT6X LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000014633 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000044212 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006497 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q92542 |
KEGG Orthology (KO) More...KOi | K06171 |
Identification of Orthologs from Complete Genome Data More...OMAi | HMHAVIS |
Database of Orthologous Groups More...OrthoDBi | EOG091G03DV |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q92542 |
TreeFam database of animal gene trees More...TreeFami | TF317086 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR008710 Nicastrin |
The PANTHER Classification System More...PANTHERi | PTHR21092 PTHR21092, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF05450 Nicastrin, 1 hit |
<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 (2)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 2 <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
MATAGGGSGA DPGSRGLLRL LSFCVLLAGL CRGNSVERKI YIPLNKTAPC
60 70 80 90 100
VRLLNATHQI GCQSSISGDT GVIHVVEKEE DLQWVLTDGP NPPYMVLLES
110 120 130 140 150
KHFTRDLMEK LKGRTSRIAG LAVSLTKPSP ASGFSPSVQC PNDGFGVYSN
160 170 180 190 200
SYGPEFAHCR EIQWNSLGNG LAYEDFSFPI FLLEDENETK VIKQCYQDHN
210 220 230 240 250
LSQNGSAPTF PLCAMQLFSH MHAVISTATC MRRSSIQSTF SINPEIVCDP
260 270 280 290 300
LSDYNVWSML KPINTTGTLK PDDRVVVAAT RLDSRSFFWN VAPGAESAVA
310 320 330 340 350
SFVTQLAAAE ALQKAPDVTT LPRNVMFVFF QGETFDYIGS SRMVYDMEKG
360 370 380 390 400
KFPVQLENVD SFVELGQVAL RTSLELWMHT DPVSQKNESV RNQVEDLLAT
410 420 430 440 450
LEKSGAGVPA VILRRPNQSQ PLPPSSLQRF LRARNISGVV LADHSGAFHN
460 470 480 490 500
KYYQSIYDTA ENINVSYPEW LSPEEDLNFV TDTAKALADV ATVLGRALYE
510 520 530 540 550
LAGGTNFSDT VQADPQTVTR LLYGFLIKAN NSWFQSILRQ DLRSYLGDGP
560 570 580 590 600
LQHYIAVSSP TNTTYVVQYA LANLTGTVVN LTREQCQDPS KVPSENKDLY
610 620 630 640 650
EYSWVQGPLH SNETDRLPRC VRSTARLARA LSPAFELSQW SSTEYSTWTE
660 670 680 690 700
SRWKDIRARI FLIASKELEL ITLTVGFGIL IFSLIVTYCI NAKADVLFIA
PREPGAVSY
The sequence of this isoform differs from the canonical sequence as follows:
1-20: Missing.
21-29: LSFCVLLAG → MDFNLILES
10 20 30 40 50
MDFNLILESL CRGNSVERKI YIPLNKTAPC VRLLNATHQI GCQSSISGDT
60 70 80 90 100
GVIHVVEKEE DLQWVLTDGP NPPYMVLLES KHFTRDLMEK LKGRTSRIAG
110 120 130 140 150
LAVSLTKPSP ASGFSPSVQC PNDGFGVYSN SYGPEFAHCR EIQWNSLGNG
160 170 180 190 200
LAYEDFSFPI FLLEDENETK VIKQCYQDHN LSQNGSAPTF PLCAMQLFSH
210 220 230 240 250
MHAVISTATC MRRSSIQSTF SINPEIVCDP LSDYNVWSML KPINTTGTLK
260 270 280 290 300
PDDRVVVAAT RLDSRSFFWN VAPGAESAVA SFVTQLAAAE ALQKAPDVTT
310 320 330 340 350
LPRNVMFVFF QGETFDYIGS SRMVYDMEKG KFPVQLENVD SFVELGQVAL
360 370 380 390 400
RTSLELWMHT DPVSQKNESV RNQVEDLLAT LEKSGAGVPA VILRRPNQSQ
410 420 430 440 450
PLPPSSLQRF LRARNISGVV LADHSGAFHN KYYQSIYDTA ENINVSYPEW
460 470 480 490 500
LSPEEDLNFV TDTAKALADV ATVLGRALYE LAGGTNFSDT VQADPQTVTR
510 520 530 540 550
LLYGFLIKAN NSWFQSILRQ DLRSYLGDGP LQHYIAVSSP TNTTYVVQYA
560 570 580 590 600
LANLTGTVVN LTREQCQDPS KVPSENKDLY EYSWVQGPLH SNETDRLPRC
610 620 630 640 650
VRSTARLARA LSPAFELSQW SSTEYSTWTE SRWKDIRARI FLIASKELEL
660 670 680
ITLTVGFGIL IFSLIVTYCI NAKADVLFIA PREPGAVSY
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 | 657 | R → H in AAH47621 (PubMed:15489334).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_050274 | 75 | V → I. Corresponds to variant dbSNP:rs12045198Ensembl. | 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_050275 | 77 | E → D. Corresponds to variant dbSNP:rs35603924Ensembl. | 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_067756 | 211 | P → R in ACNINV1. 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_008385 | 1 – 20 | 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
| 20 | |
| <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_008386 | 21 – 29 | LSFCVLLAG → MDFNLILES 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
| 9 |
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 | AF240468 mRNA Translation: AAG11412.1 AY359120 mRNA Translation: AAQ89478.1 AK314764 mRNA Translation: BAG37302.1 AL445230 Genomic DNA No translation available. CH471121 Genomic DNA Translation: EAW52720.1 CH471121 Genomic DNA Translation: EAW52721.1 CH471121 Genomic DNA Translation: EAW52722.1 BC047621 mRNA Translation: AAH47621.1 D87442 mRNA Translation: BAA13383.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1203.1 [Q92542-1] CCDS76228.1 [Q92542-2] |
NCBI Reference Sequences More...RefSeqi | NP_001277113.1, NM_001290184.1 [Q92542-2] NP_001277115.1, NM_001290186.1 NP_056146.1, NM_015331.2 [Q92542-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.517249 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000294785; ENSP00000294785; ENSG00000162736 [Q92542-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23385 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23385 |
UCSC genome browser More...UCSCi | uc001fvx.4 human [Q92542-1] |
<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 |
|---|
<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 | AF240468 mRNA Translation: AAG11412.1 AY359120 mRNA Translation: AAQ89478.1 AK314764 mRNA Translation: BAG37302.1 AL445230 Genomic DNA No translation available. CH471121 Genomic DNA Translation: EAW52720.1 CH471121 Genomic DNA Translation: EAW52721.1 CH471121 Genomic DNA Translation: EAW52722.1 BC047621 mRNA Translation: AAH47621.1 D87442 mRNA Translation: BAA13383.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1203.1 [Q92542-1] CCDS76228.1 [Q92542-2] |
NCBI Reference Sequences More...RefSeqi | NP_001277113.1, NM_001290184.1 [Q92542-2] NP_001277115.1, NM_001290186.1 NP_056146.1, NM_015331.2 [Q92542-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.517249 |
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 |
| 2N7Q | NMR | - | A | 664-709 | [»] | |
| 2N7R | NMR | - | A | 664-709 | [»] | |
| 4UIS | electron microscopy | 4.40 | A | 42-665 | [»] | |
| 5A63 | electron microscopy | 3.40 | A | 1-709 | [»] | |
| 5FN2 | electron microscopy | 4.20 | A | 1-709 | [»] | |
| 5FN3 | electron microscopy | 4.10 | A | 1-709 | [»] | |
| 5FN4 | electron microscopy | 4.00 | A | 1-709 | [»] | |
| 5FN5 | electron microscopy | 4.30 | A | 1-709 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q92542 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q92542 | |||||
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 | 116961, 136 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q92542 |
Database of interacting proteins More...DIPi | DIP-36336N |
Protein interaction database and analysis system More...IntActi | Q92542, 67 interactors |
Molecular INTeraction database More...MINTi | Q92542 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000294785 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q92542 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3418 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q92542 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q92542 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q92542 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NCSTN |
Domain mapping of disease mutations (DMDM) More...DMDMi | 12231037 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q92542 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q92542 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q92542 |
PeptideAtlas More...PeptideAtlasi | Q92542 |
PRoteomics IDEntifications database More...PRIDEi | Q92542 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 75302 75303 [Q92542-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q92542-2 [Q92542-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 23385 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000294785; ENSP00000294785; ENSG00000162736 [Q92542-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23385 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23385 |
UCSC genome browser More...UCSCi | uc001fvx.4 human [Q92542-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 23385 |
DisGeNET More...DisGeNETi | 23385 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000162736.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | NCSTN |
Human Gene Nomenclature Database More...HGNCi | HGNC:17091 NCSTN |
Human Protein Atlas More...HPAi | CAB021982 HPA054846 HPA070642 |
MalaCards human disease database More...MalaCardsi | NCSTN |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 142690 phenotype 605254 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q92542 |
Open Targets More...OpenTargetsi | ENSG00000162736 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 387 Hidradenitis suppurativa |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142671271 |
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 | KOG2657 Eukaryota ENOG410XT6X LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000014633 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000044212 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006497 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q92542 |
KEGG Orthology (KO) More...KOi | K06171 |
Identification of Orthologs from Complete Genome Data More...OMAi | HMHAVIS |
Database of Orthologous Groups More...OrthoDBi | EOG091G03DV |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q92542 |
TreeFam database of animal gene trees More...TreeFami | TF317086 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1251985 Nuclear signaling by ERBB4 R-HSA-1474228 Degradation of the extracellular matrix R-HSA-193692 Regulated proteolysis of p75NTR R-HSA-1980150 Signaling by NOTCH4 R-HSA-205043 NRIF signals cell death from the nucleus R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants R-HSA-2979096 NOTCH2 Activation and Transmission of Signal to the Nucleus R-HSA-3928665 EPH-ephrin mediated repulsion of cells R-HSA-6798695 Neutrophil degranulation R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus R-HSA-9017802 Noncanonical activation of NOTCH3 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q92542 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q92542 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | NCSTN human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Nicastrin |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 23385 |
Protein Ontology More...PROi | PR:Q92542 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000162736 |
CleanEx database of gene expression profiles More...CleanExi | HS_NCSTN |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q92542 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q92542 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR008710 Nicastrin |
The PANTHER Classification System More...PANTHERi | PTHR21092 PTHR21092, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF05450 Nicastrin, 1 hit |
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 | NICA_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 | Q92542Primary (citable) accession number: Q92542 Secondary accession number(s): Q5T207, Q5T208, Q86VV5 | |
| <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: | July 15, 1998 |
| Last sequence update: | January 11, 2001 | |
| Last modified: | July 18, 2018 | |
| This is version 173 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, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: 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 - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
