| 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 | ||
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* 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 | ||||||
|---|---|---|---|---|---|---|
| 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. | |