UniProt ID | NICA_HUMAN | |
---|---|---|
UniProt AC | Q92542 | |
Protein Name | Nicastrin | |
Gene Name | NCSTN | |
Organism | Homo sapiens (Human). | |
Sequence Length | 709 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein . Cytoplasmic vesicle membrane Single-pass type I membrane protein . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV. |
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Protein Description | Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). [PubMed: 10993067] | |
Protein Sequence | MATAGGGSGADPGSRGLLRLLSFCVLLAGLCRGNSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEEDLQWVLTDGPNPPYMVLLESKHFTRDLMEKLKGRTSRIAGLAVSLTKPSPASGFSPSVQCPNDGFGVYSNSYGPEFAHCREIQWNSLGNGLAYEDFSFPIFLLEDENETKVIKQCYQDHNLSQNGSAPTFPLCAMQLFSHMHAVISTATCMRRSSIQSTFSINPEIVCDPLSDYNVWSMLKPINTTGTLKPDDRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALQKAPDVTTLPRNVMFVFFQGETFDYIGSSRMVYDMEKGKFPVQLENVDSFVELGQVALRTSLELWMHTDPVSQKNESVRNQVEDLLATLEKSGAGVPAVILRRPNQSQPLPPSSLQRFLRARNISGVVLADHSGAFHNKYYQSIYDTAENINVSYPEWLSPEEDLNFVTDTAKALADVATVLGRALYELAGGTNFSDTVQADPQTVTRLLYGFLIKANNSWFQSILRQDLRSYLGDGPLQHYIAVSSPTNTTYVVQYALANLTGTVVNLTREQCQDPSKVPSENKDLYEYSWVQGPLHSNETDRLPRCVRSTARLARALSPAFELSQWSSTEYSTWTESRWKDIRARIFLIASKELELITLTVGFGILIFSLIVTYCINAKADVLFIAPREPGAVSY | |
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 |
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45 | N-linked_Glycosylation | RKIYIPLNKTAPCVR EEEEEECCCCCHHHH | 33.99 | 30598546 | |
55 | N-linked_Glycosylation | APCVRLLNATHQIGC CHHHHHHCCCCCCCC | 47.59 | 30598546 | |
101 | Ubiquitination | YMVLLESKHFTRDLM EEEEEECCCHHHHHH | 33.10 | - | |
110 | 2-Hydroxyisobutyrylation | FTRDLMEKLKGRTSR HHHHHHHHHCCCCCC | 41.35 | - | |
110 | Acetylation | FTRDLMEKLKGRTSR HHHHHHHHHCCCCCC | 41.35 | 19828433 | |
110 | Ubiquitination | FTRDLMEKLKGRTSR HHHHHHHHHCCCCCC | 41.35 | - | |
112 | Acetylation | RDLMEKLKGRTSRIA HHHHHHHCCCCCCCE | 58.37 | 19828441 | |
127 | Ubiquitination | GLAVSLTKPSPASGF EEEEECCCCCCCCCC | 49.11 | - | |
187 | N-linked_Glycosylation | IFLLEDENETKVIKQ EEEECCCCCHHHHHH | 74.65 | 30598546 | |
200 | N-linked_Glycosylation | KQCYQDHNLSQNGSA HHHHHHCCCCCCCCC | 50.07 | UniProtKB CARBOHYD | |
204 | N-linked_Glycosylation | QDHNLSQNGSAPTFP HHCCCCCCCCCCCHH | 42.90 | UniProtKB CARBOHYD | |
264 | N-linked_Glycosylation | WSMLKPINTTGTLKP HHHCCCCCCCCCCCC | 39.86 | 30598546 | |
319 | Phosphorylation | LQKAPDVTTLPRNVM HHHCCCCCCCCCCEE | 29.96 | 22798277 | |
320 | Phosphorylation | QKAPDVTTLPRNVMF HHCCCCCCCCCCEEE | 34.31 | 22798277 | |
331 (in isoform 2) | Ubiquitination | - | 37.03 | 21906983 | |
349 | Ubiquitination | RMVYDMEKGKFPVQL EEEEECCCCCCCEEE | 61.84 | - | |
349 | 2-Hydroxyisobutyrylation | RMVYDMEKGKFPVQL EEEEECCCCCCCEEE | 61.84 | - | |
349 | Acetylation | RMVYDMEKGKFPVQL EEEEECCCCCCCEEE | 61.84 | 12655271 | |
351 (in isoform 1) | Ubiquitination | - | 58.52 | 21906983 | |
351 | Ubiquitination | VYDMEKGKFPVQLEN EEECCCCCCCEEECC | 58.52 | 21906983 | |
383 (in isoform 2) | Ubiquitination | - | 12.02 | 21906983 | |
387 | N-linked_Glycosylation | TDPVSQKNESVRNQV CCCCHHCCHHHHHHH | 38.86 | 30598546 | |
400 | Phosphorylation | QVEDLLATLEKSGAG HHHHHHHHHHHCCCC | 35.10 | 24719451 | |
403 | Ubiquitination | DLLATLEKSGAGVPA HHHHHHHHCCCCCCE | 58.25 | 2190698 | |
403 (in isoform 1) | Ubiquitination | - | 58.25 | 21906983 | |
417 | N-linked_Glycosylation | AVILRRPNQSQPLPP EEEEECCCCCCCCCH | 52.93 | UniProtKB CARBOHYD | |
425 | Phosphorylation | QSQPLPPSSLQRFLR CCCCCCHHHHHHHHH | 41.56 | - | |
426 | Phosphorylation | SQPLPPSSLQRFLRA CCCCCHHHHHHHHHH | 34.00 | - | |
434 | Methylation | LQRFLRARNISGVVL HHHHHHHCCCCCEEE | 34.28 | 12019821 | |
435 | N-linked_Glycosylation | QRFLRARNISGVVLA HHHHHHCCCCCEEEE | 31.62 | 30598546 | |
437 | Phosphorylation | FLRARNISGVVLADH HHHHCCCCCEEEECC | 29.14 | 22590650 | |
464 | N-linked_Glycosylation | YDTAENINVSYPEWL HHHHHHCCCCCCCCC | 28.41 | 30598546 | |
506 | N-linked_Glycosylation | YELAGGTNFSDTVQA HHHHCCCCCHHHCCC | 37.39 | 30598546 | |
530 | N-linked_Glycosylation | YGFLIKANNSWFQSI HHHHHHHCCHHHHHH | 37.76 | 30598546 | |
536 | Phosphorylation | ANNSWFQSILRQDLR HCCHHHHHHHHHHHH | 17.70 | 24719451 | |
562 | N-linked_Glycosylation | IAVSSPTNTTYVVQY EEEECCCCCHHHHHH | 33.53 | 30598546 | |
573 | N-linked_Glycosylation | VVQYALANLTGTVVN HHHHHHHHCCCCEEE | 38.70 | 30598546 | |
580 | N-linked_Glycosylation | NLTGTVVNLTREQCQ HCCCCEEECCHHHCC | 31.21 | 30630874 | |
612 | N-linked_Glycosylation | VQGPLHSNETDRLPR ECCCCCCCCCCCHHH | 45.50 | 19349973 | |
612 | N-linked_Glycosylation | VQGPLHSNETDRLPR ECCCCCCCCCCCHHH | 45.50 | 19349973 | |
632 | Phosphorylation | ARLARALSPAFELSQ HHHHHHHCCHHHHHH | 17.13 | - | |
638 | Phosphorylation | LSPAFELSQWSSTEY HCCHHHHHHCCCCCC | 23.54 | - | |
647 | Phosphorylation | WSSTEYSTWTESRWK CCCCCCCCCCHHHHH | 35.19 | - | |
649 | Phosphorylation | STEYSTWTESRWKDI CCCCCCCCHHHHHHH | 24.95 | - | |
672 | Phosphorylation | SKELELITLTVGFGI CCCCHHHHHHHHHHH | 29.06 | - | |
674 | Phosphorylation | ELELITLTVGFGILI CCHHHHHHHHHHHHH | 15.21 | - | |
689 | S-palmitoylation | FSLIVTYCINAKADV HHHHHHHHHHCCCCE | 1.09 | 19028695 | |
708 | Phosphorylation | PREPGAVSY------ CCCCCCCCC------ | 25.29 | 25159151 | |
708 | O-linked_Glycosylation | PREPGAVSY------ CCCCCCCCC------ | 25.29 | 22503002 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of NICA_HUMAN !! |
* 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_HUMAN !! |
Kegg Disease | ||||||
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H00681 | Acne inversa; Hidradenitis supprativa | |||||
OMIM Disease | ||||||
142690 | Acne inversa, familial, 1 (ACNINV1) | |||||
Kegg Drug | ||||||
D08869 | Begacestat (USAN/INN) | |||||
D09010 | Tarenflurbil (USAN/INN); R-Flurbiprofen | |||||
D09377 | Semagacestat (USAN/INN) | |||||
D09869 | Avagacestat (USAN) | |||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-612, AND MASSSPECTROMETRY. | |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-187 AND ASN-387,AND MASS SPECTROMETRY. | |
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-387. |