UniProt ID | NICA_CAEEL | |
---|---|---|
UniProt AC | Q23316 | |
Protein Name | Nicastrin | |
Gene Name | aph-2 | |
Organism | Caenorhabditis elegans. | |
Sequence Length | 723 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein . |
|
Protein Description | Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch (glp-1 or lin-12). It may represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.. | |
Protein Sequence | MKKWLVIVLIIAGIRCDGFSDQVFRTLFIGEGNACYRTFNKTHEFGCQANRENENGLIVRIDKQEDFKNLDSCWNSFYPKYSGKYWALLPVNLIRRDTISQLKSSKCLSGIVLYNSGESIHPGDESTAASHDAECPNAASDYYLQDKNEEYCERKINSRGAITRDGLMKIDWRIQMVFIDNSTDLEIIEKCYSMFNKPKEDGSSGYPYCGMSFRLANMAAGNSEICYRRGKNDAKLFQMNIDSGDAPQLCGAMHSDNIFAFPTPIPTSPTNETIITSKYMMVTARMDSFGMIPEISVGEVSVLTSIISVLAAARSMGTQIEKWQKASNTSNRNVFFAFFNGESLDYIGSGAAAYQMENGKFPQMIRSDRTHIHPIRPNELDYILEVQQIGVAKGRKYYVHVDGERYQQNKTQTDRVIDRIERGLRSHAFDLEKPSGSGDRVPPASWHSFAKADAHVQSVLLAPYGKEYEYQRVNSILDKNEWTEDEREKAIQEIEAVSTAILAAAADYVGVETDEVVAKVDKKLITTIFDCLITSNFWFDCDFMQKLDGGRYHKLFNSYGFNQKSTYISMESHTAFPTVLHWLTIFALGSDKETLNVKSEKSCSHLGQFQAFQMYTYTWQPNPYTGNFSCLKSAIVKKVMVSPAVDSQTPEEEMNTRYSTWMESVYIIESVNLYLMEDASFEYTMILIAVISALLSIFAVGRCSETTFIVDEGEPAAEGGEPL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
40 | N-linked_Glycosylation | NACYRTFNKTHEFGC CCEEECCCCCCCCCC | 47.94 | - | |
181 | N-linked_Glycosylation | IQMVFIDNSTDLEII EEEEEECCCCCHHHH | 41.83 | 17761667 | |
271 | N-linked_Glycosylation | PIPTSPTNETIITSK CCCCCCCCCCEEECC | 48.04 | - | |
328 | N-linked_Glycosylation | EKWQKASNTSNRNVF HHHHHHCCCCCCCEE | 53.00 | - | |
409 | N-linked_Glycosylation | DGERYQQNKTQTDRV CCHHHHCCCCHHHHH | 33.54 | - | |
627 | N-linked_Glycosylation | QPNPYTGNFSCLKSA CCCCCCCCCHHHHHH | 20.19 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of NICA_CAEEL !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NICA_CAEEL !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of NICA_CAEEL !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of NICA_CAEEL !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditiselegans and suggests an atypical translocation mechanism for integralmembrane proteins."; Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,Taoka M., Takahashi N., Isobe T.; Mol. Cell. Proteomics 6:2100-2109(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181, AND MASSSPECTROMETRY. |