[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANTS AD3 LEU-146; ARG-163; GLU-246 AND VAL-286. TISSUE=Brain; DOI=10.1038/375754a0; PubMed=7596406 [NCBI, ExPASy, EBI, Israel, Japan] Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M., St George-Hyslop P.H.; "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease."; Nature 375:754-760(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). TISSUE=Blood, and Brain; DOI=10.1016/0014-5793(96)00054-3; PubMed=8641442 [NCBI, ExPASy, EBI, Israel, Japan] Sahara N., Yahagi Y., Takagi H., Kondo T., Okochi M., Usami M., Shirasawa T., Mori H.; "Identification and characterization of presenilin I-467, I-463 and I-374."; FEBS Lett. 381:7-11(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). Powell C.S., Gegg M.E., Palmer M.S.; "Human presenilin 1 gene encodes an alternative protein-minilin."; Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Rowen L., Madan A., Qin S., Abbasi N., Dors M., Ratcliffe A., Madan A., Dickhoff R., Shaffer T., James R., Lasky S., Hood L.; "Complete sequence of the gene for presenilin 1."; Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Kang L., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.; Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan] Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.; "The DNA sequence and analysis of human chromosome 14."; Nature 421:601-607(2003).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113. DOI=10.1006/bbrc.1996.6043; PubMed=9070286 [NCBI, ExPASy, EBI, Israel, Japan] Tsujimura A., Yasojima K., Hashimoto-Gotoh T.; "Cloning of Xenopus presenilin-alpha and -beta cDNAs and their differential expression in oogenesis and embryogenesis."; Biochem. Biophys. Res. Commun. 231:392-396(1997).
[9]	NUCLEOTIDE SEQUENCE [MRNA] OF 24-32; 254-255; 290-292; 316-317 AND 376-379 (ISOFORM 6). TISSUE=Megakaryocyte, and Platelet; DOI=10.1016/0014-5793(96)00845-9; PubMed=8804415 [NCBI, ExPASy, EBI, Israel, Japan] Vidal R., Ghiso J., Wisniewski T., Frangione B.; "Alzheimer's presenilin 1 gene expression in platelets and megakaryocytes. Identification of a novel splice variant."; FEBS Lett. 393:19-23(1996).
[10]	PROTEIN SEQUENCE OF 36-42; 61-76; 109-129; 217-239; 270-278; 315-320; 345-352 AND 381-395 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, AND CHARACTERIZATION OF GAMMA-SECRETASE COMPLEX. DOI=10.1021/bi0494976; PubMed=15274632 [NCBI, ExPASy, EBI, Israel, Japan] Fraering P.C., Ye W., Strub J.-M., Dolios G., LaVoie M.J., Ostaszewski B.L., van Dorsselaer A., Wang R., Selkoe D.J., Wolfe M.S.; "Purification and characterization of the human gamma-secretase complex."; Biochemistry 43:9774-9789(2004).
[11]	SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1038/nm0296-224; PubMed=8574969 [NCBI, ExPASy, EBI, Israel, Japan] Kovacs D.M., Fausett H.J., Page K.J., Kim T.-W., Moir R.D., Merriam D.E., Hollister R.D., Hallmark O.G., Mancini R., Felsenstein K.M., Hyman B.T., Tanzi R.E., Wasco W.; "Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells."; Nat. Med. 2:224-229(1996).
[12]	PROTEOLYTIC PROCESSING. DOI=10.1006/nbdi.1997.0129; PubMed=9173929 [NCBI, ExPASy, EBI, Israel, Japan] Podlisny M.B., Citron M., Amarante P., Sherrington R., Xia W., Zhang J., Diehl T., Levesque G., Fraser P., Haass C., Koo E.H., Seubert P., St George-Hyslop P.H., Teplow D.B., Selkoe D.J.; "Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue."; Neurobiol. Dis. 3:325-337(1997).
[13]	PHOSPHORYLATION. DOI=10.1073/pnas.94.10.5349; PubMed=9144240 [NCBI, ExPASy, EBI, Israel, Japan] Walter J., Gruenberg J., Capell A., Pesold B., Schindzielorz A., Citron M., Mendla K., St George-Hyslop P.H., Multhaup G., Selkoe D.J., Haass C.; "Proteolytic processing of the Alzheimer disease-associated presenilin-1 generates an in vivo substrate for protein kinase C."; Proc. Natl. Acad. Sci. U.S.A. 94:5349-5354(1997).
[14]	CASPASE CLEAVAGE SITE, AND MUTAGENESIS OF ASP-345; ASP-373 AND ASP-385. DOI=10.1021/bi972106l; PubMed=9485372 [NCBI, ExPASy, EBI, Israel, Japan] Gruenberg J., Walter J., Loetscher H., Deuschle U., Jacobsen H., Haass C.; "Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family."; Biochemistry 37:2263-2270(1998).
[15]	INTERACTION WITH CTNNB1, AND SUBCELLULAR LOCATION. DOI=10.1016/S0014-5793(98)00886-2; PubMed=9738936 [NCBI, ExPASy, EBI, Israel, Japan] Murayama M., Tanaka S., Palacino J., Murayama O., Honda T., Sun X., Yasutake K., Nihonmatsu N., Wolozin B., Takashima A.; "Direct association of presenilin-1 with beta-catenin."; FEBS Lett. 433:73-77(1998).
[16]	INTERACTION WITH FLNA AND FLNB. PubMed=9437013 [NCBI, ExPASy, EBI, Israel, Japan] Zhang W., Han S.W., McKeel D.W., Goate A., Wu J.Y.; "Interaction of presenilins with the filamin family of actin-binding proteins."; J. Neurosci. 18:914-922(1998).
[17]	FUNCTION, AND MUTAGENESIS OF MET-292. DOI=10.1021/bi9914210; PubMed=10545183 [NCBI, ExPASy, EBI, Israel, Japan] Steiner H., Romig H., Pesold B., Philipp U., Baader M., Citron M., Loetscher H., Jacobsen H., Haass C.; "Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis."; Biochemistry 38:14600-14605(1999).
[18]	INTERACTION WITH MTCH1. DOI=10.1074/jbc.274.46.32543; PubMed=10551805 [NCBI, ExPASy, EBI, Israel, Japan] Xu X., Shi Y.-C., Wu X., Gambetti P., Sui D., Cui M.-Z.; "Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1."; J. Biol. Chem. 274:32543-32546(1999).
[19]	FUNCTION. DOI=10.1074/jbc.274.51.36801; PubMed=10593990 [NCBI, ExPASy, EBI, Israel, Japan] Ray W.J., Yao M., Mumm J., Schroeter E.H., Saftig P., Wolfe M., Selkoe D.J., Kopan R., Goate A.M.; "Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch."; J. Biol. Chem. 274:36801-36807(1999).
[20]	INTERACTION WITH CTNND2. DOI=10.1046/j.1471-4159.1999.0720999.x; PubMed=10037471 [NCBI, ExPASy, EBI, Israel, Japan] Levesque G., Yu G., Nishimura M., Zhang D.M., Levesque L., Yu H., Xu D., Liang Y., Rogaeva E.A., Ikeda M., Duthie M., Murgolo N., Wang L., VanderVere P., Bayne M.L., Strader C.D., Rommens J.M., Fraser P.E., St George-Hyslop P.H.; "Presenilins interact with armadillo proteins including neural-specific plakophilin-related protein and beta-catenin."; J. Neurochem. 72:999-1008(1999).
[21]	COMPONENT OF THE PSEN1/E-CADHERIN/CATENIN ADHESION COMPLEX WITH PSEN1; CDH1; CTNNA1 AND CTNNB1/CTNND1. DOI=10.1016/S1097-2765(00)80219-1; PubMed=10635315 [NCBI, ExPASy, EBI, Israel, Japan] Georgakopoulos A., Marambaud P., Efthimiopoulos S., Shioi J., Cui W., Li H.-C., Schutte M., Gordon R., Holstein G.R., Martinelli G., Mehta P., Friedrich V.L. Jr., Robakis N.K.; "Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts."; Mol. Cell 4:893-902(1999).
[22]	FUNCTION, AND MUTAGENESIS OF ASP-257 AND ASP-385. DOI=10.1038/19077; PubMed=10206644 [NCBI, ExPASy, EBI, Israel, Japan] Wolfe M.S., Xia W., Ostaszewski B.L., Diehl T.S., Kimberly W.T., Selkoe D.J.; "Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity."; Nature 398:513-517(1999).
[23]	FUNCTION, AND MUTAGENESIS OF ASP-257 AND ASP-385. DOI=10.1046/j.1471-4159.2000.0750583.x; PubMed=10899933 [NCBI, ExPASy, EBI, Israel, Japan] Berezovska O., Jack C., McLean P., Aster J.C., Hicks C., Xia W., Wolfe M.S., Kimberly W.T., Weinmaster G., Selkoe D.J., Hyman B.T.; "Aspartate mutations in presenilin and gamma-secretase inhibitors both impair notch1 proteolysis and nuclear translocation with relative preservation of notch1 signaling."; J. Neurochem. 75:583-593(2000).
[24]	FUNCTION, AND MUTAGENESIS OF LEU-286. DOI=10.1073/pnas.100049897; PubMed=10811883 [NCBI, ExPASy, EBI, Israel, Japan] Kulic L., Walter J., Multhaup G., Teplow D.B., Baumeister R., Romig H., Capell A., Steiner H., Haass C.; "Separation of presenilin function in amyloid beta-peptide generation and endoproteolysis of Notch."; Proc. Natl. Acad. Sci. U.S.A. 97:5913-5918(2000).
[25]	FUNCTION, AND INTERACTION WITH CDH1. DOI=10.1073/pnas.041603398; PubMed=11226248 [NCBI, ExPASy, EBI, Israel, Japan] Baki L., Marambaud P., Efthimiopoulos S., Georgakopoulos A., Wen P., Cui W., Shioi J., Koo E., Ozawa M., Friedrich V.L., Robakis N.K.; "Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex."; Proc. Natl. Acad. Sci. U.S.A. 98:2381-2386(2001).
[26]	TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. DOI=10.1006/bcmd.2002.0486; PubMed=11987239 [NCBI, ExPASy, EBI, Israel, Japan] Mirinics Z.K., Calafat J., Udby L., Lovelock J., Kjeldsen L., Rothermund K., Sisodia S.S., Borregaard N., Corey S.J.; "Identification of the presenilins in hematopoietic cells with localization of presenilin 1 to neutrophil and platelet granules."; Blood Cells Mol. Dis. 28:28-38(2002).
[27]	INTERACTION WITH HERPUD1. DOI=10.1074/jbc.M112372200; PubMed=11799129 [NCBI, ExPASy, EBI, Israel, Japan] Sai X., Kawamura Y., Kokame K., Yamaguchi H., Shiraishi H., Suzuki R., Suzuki T., Kawaichi M., Miyata T., Kitamura T., De Strooper B., Yanagisawa K., Komano H.; "Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid beta-protein."; J. Biol. Chem. 277:12915-12920(2002).
[28]	INTERACTION WITH GFAP, MUTAGENESIS OF 66-ASP--ASP-72; 76-LYS-TYR-77; 82-VAL-ILE-83; VAL-82 AND 84-MET-LEU-85, AND CHARACTERIZATION OF VARIANTS AD3 VAL-79 AND LEU-82. DOI=10.1074/jbc.M112121200; PubMed=12058025 [NCBI, ExPASy, EBI, Israel, Japan] Nielsen A.L., Holm I.E., Johansen M., Bonven B., Jorgensen P., Jorgensen A.L.; "A new splice variant of glial fibrillary acidic protein GFAPepsilon, interacts with the presenilin proteins."; J. Biol. Chem. 277:29983-29991(2002).
[29]	INTERACTION WITH CDH2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-385. DOI=10.1002/jnr.10753; PubMed=14515347 [NCBI, ExPASy, EBI, Israel, Japan] Uemura K., Kitagawa N., Kohno R., Kuzuya A., Kageyama T., Chonabayashi K., Shibasaki H., Shimohama S.; "Presenilin 1 is involved in maturation and trafficking of N-cadherin to the plasma membrane."; J. Neurosci. Res. 74:184-191(2003).
[30]	ENZYME ACTIVITY OF A GAMMA-SECRETASE COMPLEX. DOI=10.1038/ncb960; PubMed=12679784 [NCBI, ExPASy, EBI, Israel, Japan] Edbauer D., Winkler E., Regula J.T., Pesold B., Steiner H., Haass C.; "Reconstitution of gamma-secretase activity."; Nat. Cell Biol. 5:486-488(2003).
[31]	COMPONENT OF A GAMMA-SECRETASE COMPLEX WITH PEN2; PSEN1/PSEN2 AND NCSTN. DOI=10.1073/pnas.1037392100; PubMed=12740439 [NCBI, ExPASy, EBI, Israel, Japan] Kimberly W.T., LaVoie M.J., Ostaszewski B.L., Ye W., Wolfe M.S., Selkoe D.J.; "Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2."; Proc. Natl. Acad. Sci. U.S.A. 100:6382-6387(2003).
[32]	SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). DOI=10.1186/gb-2004-5-2-r8; PubMed=14759258 [NCBI, ExPASy, EBI, Israel, Japan] Hillman R.T., Green R.E., Brenner S.E.; "An unappreciated role for RNA surveillance."; Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004).
[33]	PHOSPHORYLATION AT SER-310 AND SER-346, AND MUTAGENESIS OF SER-310 AND SER-346. DOI=10.1074/jbc.M306653200; PubMed=14576165 [NCBI, ExPASy, EBI, Israel, Japan] Fluhrer R., Friedlein A., Haass C., Walter J.; "Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis."; J. Biol. Chem. 279:1585-1593(2004).
[34]	FUNCTION, ACTIVE SITES ASP-257 AND ASP-385, AND MUTAGENESIS OF TYR-256; ASP-257; ASP-385 AND TYR-389. DOI=10.1111/j.1471-4159.2004.02596.x; PubMed=15341515 [NCBI, ExPASy, EBI, Israel, Japan] Wrigley J.D., Nunn E.J., Nyabi O., Clarke E.E., Hunt P., Nadin A., De Strooper B., Shearman M.S., Beher D.; "Conserved residues within the putative active site of gamma-secretase differentially influence enzyme activity and inhibitor binding."; J. Neurochem. 90:1312-1320(2004).
[35]	INTERACTION WITH CDH1. DOI=10.1074/jbc.M507503200; PubMed=16126725 [NCBI, ExPASy, EBI, Israel, Japan] Serban G., Kouchi Z., Baki L., Georgakopoulos A., Litterst C.M., Shioi J., Robakis N.K.; "Cadherins mediate both the association between PS1 and beta-catenin and the effects of PS1 on beta-catenin stability."; J. Biol. Chem. 280:36007-36012(2005).
[36]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[37]	FUNCTION OF PAL MOTIF, AND MUTAGENESIS OF PRO-433; ALA-434 AND LEU-435. DOI=10.1111/j.1471-4159.2005.03548.x; PubMed=16305624 [NCBI, ExPASy, EBI, Israel, Japan] Wang J., Beher D., Nyborg A.C., Shearman M.S., Golde T.E., Goate A.; "C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation."; J. Neurochem. 96:218-227(2006).
[38]	REVIEW ON VARIANTS. PubMed=8875251 [NCBI, ExPASy, EBI, Israel, Japan] Cruts M., Hendriks L., Van Broeckhoven C.; "The presenilin genes: a new gene family involved in Alzheimer disease pathology."; Hum. Mol. Genet. 5:1449-1455(1996).
[39]	REVIEW ON VARIANTS. DOI=10.1002/(SICI)1098-1004(1998)11:3<183::AID-HUMU1>3.3.CO;2-M; PubMed=9521418 [NCBI, ExPASy, EBI, Israel, Japan] Cruts M., van Broeckhoven C.; "Presenilin mutations in Alzheimer's disease."; Hum. Mutat. 11:183-190(1998).
[40]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-365 AND SER-367, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.; "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."; Mol. Cell 31:438-448(2008).
[41]	VARIANTS AD3 THR-143 AND ALA-384. DOI=10.1093/hmg/4.12.2363; PubMed=8634711 [NCBI, ExPASy, EBI, Israel, Japan] Cruts M., Backhovens H., Wang S.-Y., van Gassen G., Theuns J., de Jonghe C., Wehnert A., de Voecht J., de Winter G., Cras P., Bruyland M., Datson N., Weissenbach J., den Dunnen J.T., Martin J.-J., Hendriks L., Van Broeckhoven C.; "Molecular genetic analysis of familial early-onset Alzheimer's disease linked to chromosome 14q24.3."; Hum. Mol. Genet. 4:2363-2372(1995).
[42]	VARIANTS AD3 LEU-82; HIS-115; THR-139; ARG-163; THR-231; LEU-264; VAL-392 AND TYR-410. DOI=10.1093/hmg/4.12.2373; PubMed=8634712 [NCBI, ExPASy, EBI, Israel, Japan] Campion D., Flaman J.-M., Brice A., Hannequin D., Dubois B., Martin C., Moreau V., Charbonnier F., Didierjean O., Tardieu S., Penet C., Puel M., Pasquier F., le Doze F., Bellis G., Calenda A., Heilig R., Martinez M., Mallet J., Bellis M., Clerget-Darpoux F., Agid Y., Frebourg T.; "Mutations of the presenilin I gene in families with early-onset Alzheimer's disease."; Hum. Mol. Genet. 4:2373-2377(1995).
[43]	VARIANTS AD3 VAL-260; VAL-285 AND VAL-392. DOI=10.1038/376775a0; PubMed=7651536 [NCBI, ExPASy, EBI, Israel, Japan] Rogaev E.I., Sherrington R., Rogaeva E.A., Levesque G., Ikeda M., Liang Y., Chi H., Lin C., Holman K., Tsuda T., Mar L., Sorbi S., Nacmias B., Piacentini S., Amaducci L., Chumakov I., Cohen D., Lannfelt L., Fraser P.E., Rommens J.M., St George-Hyslop P.H.; "Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene."; Nature 376:775-778(1995).
[44]	VARIANTS AD3 VAL-139; VAL-146; TYR-163; THR-267; ALA-280 AND GLY-280. PubMed=7550356 [NCBI, ExPASy, EBI, Israel, Japan] Clark R.F., Hutton M., Fuldner R.A., Froelich S., Karran E., Talbot C., Crook R., Lendon C.L., Prihar G., He C., Korenblat K., Martinez A., Wragg M., Busfield F., Behrens M.I., Myers A., Norton J., Morris J., Mehta N., Pearson C., Lincoln S., Baker M., Duff K., Zehr C., Perez-Tur J., Houlden H., Ruiz A., Ossa J., Lopera F., Arcos M., Madrigal L., Collinge J., Humphreys C., Asworth T., Sarner S., Fox N.C., Harvey R., Kennedy A., Roques P.K., Cline R.T., Phillips C.A., Venter J.C., Forsel L., Axelman K., Lilius L., Johnston J., Cowburn R., Viitanen M., Winblad B., Kosik K.S., Haltia M., Poyhonen M., Dickson D., Mann D., Neary D., Snowden J., Lantos P., Lannfelt L., Rossor M.N., Roberts G.W., Adams M.D., Hardy J., Goate A.M.; "The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families."; Nat. Genet. 11:219-222(1995).
[45]	VARIANTS AD3 PHE-96; ARG-163 AND THR-213. DOI=10.1016/0304-3940(96)12587-8; PubMed=8733303 [NCBI, ExPASy, EBI, Israel, Japan] Kamino K., Sato S., Sakaki Y., Yoshiiwa A., Nishiwaki Y., Takeda H., Tanabe H., Nishimura T., Li K., St George-Hyslop P.H., Miki T., Ogihara T.; "Three different mutations of presenilin 1 gene in early-onset Alzheimer's disease families."; Neurosci. Lett. 208:195-198(1996).
[46]	VARIANT AD3 ASP-135. DOI=10.1002/ana.410420121; PubMed=9225696 [NCBI, ExPASy, EBI, Israel, Japan] Crook R., Ellis R., Shanks M., Thal L.J., Perez-Tur J., Baker M., Hutton M., Haltia T., Hardy J., Galasko D.; "Early-onset Alzheimer's disease with a presenilin-1 mutation at the site corresponding to the Volga German presenilin-2 mutation."; Ann. Neurol. 42:124-128(1997).
[47]	VARIANT AD3 ALA-280. DOI=10.1002/(SICI)1098-1004(1997)10:3<186::AID-HUMU2>3.3.CO;2-K; PubMed=9298817 [NCBI, ExPASy, EBI, Israel, Japan] Lendon C.L., Martinez A., Behrens I.M., Kosik K.S., Madrigal L., Norton J., Neuman R., Myers A., Busfield F., Wragg M., Arcos M., Arango-Viana J.C., Ossa J., Ruiz A., Goate A.M., Lopera F.; "E280A PS-1 mutation causes Alzheimer's disease but age of onset is not modified by ApoE alleles."; Hum. Mutat. 10:186-195(1997).
[48]	VARIANTS AD3 THR-233 AND THR-278. PubMed=9172170 [NCBI, ExPASy, EBI, Israel, Japan] Kwok J.B.J., Taddei K., Hallupp M., Fisher C., Brooks W.S., Broe G.A., Hardy J., Fulham M.J., Nicholson G.A., Stell R., St George-Hyslop P.H., Fraser P.E., Kakulas B., Clarnette R., Relkin N., Gandy S.E., Schofield P.R., Martins R.N.; "Two novel (M233T and R278T) presenilin-1 mutations in early-onset Alzheimer's disease pedigrees and preliminary evidence for association of presenilin-1 mutations with a novel phenotype."; NeuroReport 8:1537-1542(1997).
[49]	VARIANT AD3 PRO-171. PubMed=9833068 [NCBI, ExPASy, EBI, Israel, Japan] Ramirez-Duenas M.G., Rogaeva E.A., Leal C.A., Lin C., Ramirez-Casillas G.A., Hernandez-Romo J.A., St George-Hyslop P.H., Cantu J.M.; "A novel Leu171Pro mutation in presenilin-1 gene in a Mexican family with early onset Alzheimer disease."; Ann. Genet. 41:149-153(1998).
[50]	VARIANT GLY-318. DOI=10.1002/ana.410440617; PubMed=9851443 [NCBI, ExPASy, EBI, Israel, Japan] Mattila K.M., Forsell C., Pirttila T., Rinne J.O., Lehtimaki T., Roytta M., Lilius L., Eerola A., St George-Hyslop P.H., Frey H., Lannfelt L.; "The Glu318Gly mutation of the presenilin-1 gene does not necessarily cause Alzheimer's disease."; Ann. Neurol. 44:965-967(1998).
[51]	VARIANT GLY-318. DOI=10.1002/ana.410440624; PubMed=9851450 [NCBI, ExPASy, EBI, Israel, Japan] Aldudo J., Bullido M.J., Frank A., Valdivieso F.; "Missense mutation E318G of the presenilin-1 gene appears to be a nonpathogenic polymorphism."; Ann. Neurol. 44:985-986(1998).
[52]	VARIANTS AD3 VAL-79; CYS-115 AND VAL-231, AND VARIANT GLY-318. DOI=10.1093/hmg/7.1.43; PubMed=9384602 [NCBI, ExPASy, EBI, Israel, Japan] Cruts M., van Duijn C.M., Backhovens H., van den Broeck M., Wehnert A., Serneels S., Sherrington R., Hutton M., Hardy J., St George-Hyslop P.H., Hofman A., van Broeckhoven C.; "Estimation of the genetic contribution of presenilin-1 and -2 mutations in a population-based study of presenile Alzheimer disease."; Hum. Mol. Genet. 7:43-51(1998).
[53]	VARIANTS AD3 ASP-120; ARG-163; VAL-209; VAL-260; LEU-264; TYR-410 AND PRO-426. DOI=10.1002/(SICI)1098-1004(1998)11:3<216::AID-HUMU6>3.3.CO;2-O; PubMed=9521423 [NCBI, ExPASy, EBI, Israel, Japan] Poorkaj P., Sharma V., Anderson L., Nemens E., Alonso M.E., Orr H., White J., Heston L., Bird T.D., Schellenberg G.D.; "Missense mutations in the chromosome 14 familial Alzheimer's disease presenilin 1 gene."; Hum. Mutat. 11:216-221(1998).
[54]	VARIANT AD3 GLU-378. DOI=10.1002/(SICI)1098-1004(1998)11:6<481::AID-HUMU13>3.3.CO;2-E; PubMed=10200054 [NCBI, ExPASy, EBI, Israel, Japan] Besancon R., Lorenzi A., Cruts M., Radawiec S., Sturtz F., Broussolle E., Chazot G., van Broeckhoven C., Chamba G., Vandenberghe A.; "Missense mutation in exon 11 (codon 378) of the presenilin-1 gene in a French family with early-onset Alzheimer's disease and transmission study by mismatch enhanced allele specific amplification."; Hum. Mutat. 11:481-481(1998).
[55]	VARIANT AD3 LYS-139. PubMed=9719376 [NCBI, ExPASy, EBI, Israel, Japan] Dumanchin C., Brice A., Campion D., Hannequin D., Martin C., Moreau V., Agid Y., Martinez M., Clerget-Darpoux F., Frebourg T.; "De novo presenilin 1 mutations are rare in clinically sporadic, early onset Alzheimer's disease cases."; J. Med. Genet. 35:672-673(1998).
[56]	VARIANT AD3 LEU-117. PubMed=9507958 [NCBI, ExPASy, EBI, Israel, Japan] Wisniewski T., Dowjat W.K., Buxbaum J.D., Khorkova O., Efthimiopoulos S., Kulczycki J., Lojkowska W., Wegiel J., Wisniewski H.M., Frangione B.; "A novel Polish presenilin-1 mutation (P117L) is associated with familial Alzheimer's disease and leads to death as early as the age of 28 years."; NeuroReport 9:217-221(1998).
[57]	VARIANTS AD3 LEU-169 AND GLN-436. PubMed=9831473 [NCBI, ExPASy, EBI, Israel, Japan] Taddei K., Kwok J.B., Kril J.J., Halliday G.M., Creasey H., Hallupp M., Fisher C., Brooks W.S., Chung C., Andrews C., Masters C.L., Schofield P.R., Martins R.N.; "Two novel presenilin-1 mutations (Ser169Leu and Pro436Gln) associated with very early onset Alzheimer's disease."; NeuroReport 9:3335-3339(1998).
[58]	VARIANT GLY-318. DOI=10.1086/302200; PubMed=9915968 [NCBI, ExPASy, EBI, Israel, Japan] Dermaut B., Cruts M., Slooter A.J.C., van Gestel S., de Jonghe C., Vanderstichele H., Vanmechelen E., Breteler M.M., Hofman A., van Duijn C.M., van Broeckhoven C.; "The Glu318Gly substitution in presenilin 1 is not causally related to Alzheimer disease."; Am. J. Hum. Genet. 64:290-292(1999).
[59]	VARIANTS AD3 LEU-82; HIS-115; ASP-120; THR-139; LEU-146; ILE-147; ARG-163; CYS-165; TRP-173; THR-231; THR-233; PRO-235; LEU-264; ILE-390; VAL-392 AND TYR-410, AND VARIANT GLY-318. DOI=10.1086/302553; PubMed=10441572 [NCBI, ExPASy, EBI, Israel, Japan] Campion D., Dumanchin C., Hannequin D., Dubois B., Belliard S., Puel M., Thomas-Anterion C., Michon A., Martin C., Charbonnier F., Raux G., Camuzat A., Penet C., Mesnage V., Martinez M., Clerget-Darpoux F., Brice A., Frebourg T.; "Early-onset autosomal dominant Alzheimer disease: prevalence, genetic heterogeneity, and mutation spectrum."; Am. J. Hum. Genet. 65:664-670(1999).
[60]	VARIANTS AD3 PHE-143 AND SER-436. DOI=10.1002/(SICI)1098-1004(1999)13:3<256::AID-HUMU11>3.0.CO;2-P; PubMed=10090481 [NCBI, ExPASy, EBI, Israel, Japan] Palmer M.S., Beck J.A., Campbell T.A., Humphries C.B., Roques P.K., Fox N.C., Harvey R., Rossor M.N., Collinge J.; "Pathogenic presenilin 1 mutations (P436S and I143F) in early-onset Alzheimer's disease in the UK."; Hum. Mutat. 13:256-256(1999).
[61]	VARIANT AD3 ARG-209. DOI=10.1002/(SICI)1098-1004(1999)14:1<90::AID-HUMU19>3.0.CO;2-S; PubMed=10447269 [NCBI, ExPASy, EBI, Israel, Japan] Sugiyama N., Suzuki K., Matsumura T., Kawanishi C., Onishi H., Yamada Y., Iseki E., Kosaka K.; "A novel missense mutation (G209R) in exon 8 of the presenilin 1 gene in a Japanese family with presenile familial Alzheimer's disease."; Hum. Mutat. 14:90-90(1999).
[62]	VARIANTS AD3 LEU-233; ARG-282 AND THR-409, AND VARIANT GLY-318. DOI=10.1002/(SICI)1098-1004(199911)14:5<433::AID-HUMU10>3.0.CO;2-K; PubMed=10533070 [NCBI, ExPASy, EBI, Israel, Japan] Aldudo J., Bullido M.J., Valdivieso F.; "DGGE method for the mutational analysis of the coding and proximal promoter regions of the Alzheimer's disease presenilin-1 gene: two novel mutations."; Hum. Mutat. 14:433-439(1999).
[63]	VARIANT AD3 PRO-169. PubMed=10025789 [NCBI, ExPASy, EBI, Israel, Japan] Ezquerra M., Carnero C., Blesa R., Gelpi J.L., Ballesta F., Oliva R.; "A presenilin 1 mutation (Ser169Pro) associated with early-onset AD and myoclonic seizures."; Neurology 52:566-570(1999).
[64]	VARIANT AD3 PRO-219. PubMed=10208579 [NCBI, ExPASy, EBI, Israel, Japan] Smith M.J., Gardner R.J., Knight M.A., Forrest S.M., Beyreuther K., Storey E., McLean C.A., Cotton R.G., Cappal R., Masters C.L.; "Early-onset Alzheimer's disease caused by a novel mutation at codon 219 of the presenilin-1 gene."; NeuroReport 10:503-507(1999).
[65]	VARIANT AD3 ASN-116. PubMed=10439444 [NCBI, ExPASy, EBI, Israel, Japan] Romero I., Joergensen P., Bolwig G., Fraser P.E., Rogaeva E., Mann D., Havsager A.-M., Joergensen A.L.; "A presenilin-1 Thr116Asn substitution in a family with early-onset Alzheimer's disease."; NeuroReport 10:2255-2260(1999).
[66]	VARIANTS AD3 VAL-79; LEU-105 AND VAL-139, AND VARIANT GLY-318. DOI=10.1086/302702; PubMed=10631141 [NCBI, ExPASy, EBI, Israel, Japan] Finckh U., Mueller-Thomsen T., Mann U., Eggers C., Marksteiner J., Meins W., Binetti G., Alberici A., Hock C., Nitsch R.M., Gal A.; "High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes."; Am. J. Hum. Genet. 66:110-117(2000).
[67]	VARIANT AD3 SER-405. DOI=10.1136/jnnp.68.2.220; PubMed=10644793 [NCBI, ExPASy, EBI, Israel, Japan] Yasuda M., Maeda S., Kawamata T., Tamaoka A., Yamamoto Y., Kuroda S., Maeda K., Tanaka C.; "Novel presenilin-1 mutation with widespread cortical amyloid deposition but limited cerebral amyloid angiopathy."; J. Neurol. Neurosurg. Psych. 68:220-223(2000).
[68]	VARIANT AD3 SER-92. DOI=10.1006/bbrc.2000.3646; PubMed=11027672 [NCBI, ExPASy, EBI, Israel, Japan] Lewis P.A., Perez-Tur J., Golde T.E., Hardy J.; "The presenilin 1 C92S mutation increases abeta 42 production."; Biochem. Biophys. Res. Commun. 277:261-263(2000).
[69]	VARIANT FRONTOTEMPORAL DEMENTIA PRO-113. PubMed=11094121 [NCBI, ExPASy, EBI, Israel, Japan] Raux G., Gantier R., Thomas-Anterion C., Boulliat J., Verpillat P., Hannequin D., Brice A., Frebourg T., Campion D.; "Dementia with prominent frontotemporal features associated with L113P presenilin 1 mutation."; Neurology 55:1577-1578(2000).
[70]	VARIANT AD3 GLU-431. Ringman J.M., Jain V., Murrell J., Ghetti B., Cochran E.J.; Hum. Genet. 109:242-242(2001).
[71]	VARIANT AD3 ALA-206. DOI=10.1001/jama.286.18.2257; PubMed=11710891 [NCBI, ExPASy, EBI, Israel, Japan] Athan E.S., Williamson J., Ciappa A., Santana V., Romas S.N., Lee J.H., Rondon H., Lantigua R.A., Medrano M., Torres M., Arawaka S., Rogaeva E., Song Y.-Q., Sato C., Kawarai T., Fafel K.C., Boss M.A., Seltzer W.K., Stern Y., St George-Hyslop P.H., Tycko B., Mayeux R.; "A founder mutation in presenilin 1 causing early-onset Alzheimer disease in unrelated Caribbean Hispanic families."; JAMA 286:2257-2263(2001).
[72]	VARIANT AD3 SER-266. DOI=10.1002/ajmg.10250; PubMed=11920851 [NCBI, ExPASy, EBI, Israel, Japan] Matsubara-Tsutsui M., Yasuda M., Yamagata H., Nomura T., Taguchi K., Kohara K., Miyoshi K., Miki T.; "Molecular evidence of presenilin 1 mutation in familial early onset dementia."; Am. J. Med. Genet. 114:292-298(2002).
[73]	VARIANT AD3 PRO-166. DOI=10.1073/pnas.112686799; PubMed=12048239 [NCBI, ExPASy, EBI, Israel, Japan] Moehlmann T., Winkler E., Xia X., Edbauer D., Murrell J., Capell A., Kaether C., Zheng H., Ghetti B., Haass C., Steiner H.; "Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 production."; Proc. Natl. Acad. Sci. U.S.A. 99:8025-8030(2002).
[74]	VARIANT AD3 MET-174. DOI=10.1007/s10048-002-0136-6; PubMed=12484344 [NCBI, ExPASy, EBI, Israel, Japan] Bertoli-Avella A.M., Marcheco Teruel B., Llibre Rodriguez J.J., Gomez Viera N., Borrajero-Martinez I., Severijnen E.A., Joosse M., van Duijn C.M., Heredero Baute L., Heutink P.; "A novel presenilin 1 mutation (L174 M) in a large Cuban family with early onset Alzheimer disease."; Neurogenetics 4:97-104(2002).
[75]	VARIANT AD3 VAL-271. DOI=10.1074/jbc.M211827200; PubMed=12493737 [NCBI, ExPASy, EBI, Israel, Japan] Kwok J.B.J., Halliday G.M., Brooks W.S., Dolios G., Laudon H., Murayama O., Hallupp M., Badenhop R.F., Vickers J., Wang R., Naslund J., Takashima A., Gandy S.E., Schofield P.R.; "Presenilin-1 mutation L271V results in altered exon 8 splicing and Alzheimer's disease with non-cored plaques and no neuritic dystrophy."; J. Biol. Chem. 278:6748-6754(2003).
[76]	VARIANT GLY-318. DOI=10.1016/j.ajhg.2008.04.014; PubMed=18485326 [NCBI, ExPASy, EBI, Israel, Japan] Cornier A.S., Staehling-Hampton K., Delventhal K.M., Saga Y., Caubet J.-F., Sasaki N., Ellard S., Young E., Ramirez N., Carlo S.E., Torres J., Emans J.B., Turnpenny P.D., Pourquie O.; "Mutations in the MESP2 gene cause spondylothoracic dysostosis/Jarcho-Levin syndrome."; Am. J. Hum. Genet. 82:1334-1341(2008).

Comments

FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx, cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin, thus negatively regulating Wnt signaling. May also play a role in hematopoiesis.
SUBUNIT: Homodimer. Component of the gamma-secretase complex, a complex composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for secretase activity. Other components which are associated with the complex include SLC25A64, SLC5A7, PHB and PSEN1 isoform 3. Predominantly heterodimer of a N-terminal (NTF) and a C-terminal (CTF) endoproteolytical fragment. Associates with proteolytic processed C-terminal fragments C83 and C99 of the amyloid precursor protein (APP). Associates with NOTCH1. Component of cadherin/catenin adhesion complexes through direct binding to CDH1 or CDH2. Interaction with CDH1 stabilizes the complex and stimulates cell-cell aggregation. Interaction with CDH2 is essential for trafficking of CDH2 from the endoplasmic reticulum to the plasma membrane. Interacts with CTNND2, CTNNB1, HERPUD1, FLNA, FLNB, MTCH1, PKP4 and PARL. Interacts through its N-terminus with isoform 3 of GFAP. Interacts with DOCK3 (By similarity).
INTERACTION:
P05067:APP; NbExp=1; IntAct=EBI-297277, EBI-77613;
P05067-4:APP; NbExp=1; IntAct=EBI-297277, EBI-302641;
P05067-8:APP; NbExp=1; IntAct=EBI-297277, EBI-302661;
P35222:CTNNB1; NbExp=2; IntAct=EBI-297277, EBI-491549;
Q02248:Ctnnb1 (xeno); NbExp=1; IntAct=EBI-297277, EBI-397872;
P14923:JUP; NbExp=3; IntAct=EBI-297277, EBI-702484;
Q9NZJ7:MTCH1; NbExp=1; IntAct=EBI-297277, EBI-297455;
P49755:TMED10; NbExp=2; IntAct=EBI-297277, EBI-998422;
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell surface. Note=Bound to NOTCH1 also at the cell surface. Colocalizes with CDH1/2 at sites of cell-cell contact. Colocalizes with CTNNB1 in the endoplasmic reticulum and the proximity of the plasma membrane. Also present in azurophil granules of neutrophils.

ALTERNATIVE PRODUCTS: 6 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	I-467
Isoform ID	P49768-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	I-463
Isoform ID	P49768-2
Features which should be applied to build the isoform sequence: VSP_005191.

Name	3
Synonyms	I-374
Isoform ID	P49768-3
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Features which should be applied to build the isoform sequence: VSP_005191, VSP_005192.

Name	4
Synonyms	Minilin
Isoform ID	P49768-4
Features which should be applied to build the isoform sequence: VSP_007986, VSP_007987.

Name	5
Isoform ID	P49768-5
Features which should be applied to build the isoform sequence: VSP_005192.

Name	6
Isoform ID	P49768-6
Features which should be applied to build the isoform sequence: VSP_012288.

TISSUE SPECIFICITY: Expressed in a wide range of tissues including various regions of the brain, liver, spleen and lymph nodes.
DOMAIN: The PAL motif is required for normal active site conformation.
PTM: Heterogeneous proteolytic processing generates N-terminal (NTF) and C-terminal (CTF) fragments of approximately 35 and 20 kDa, respectively. During apoptosis, the C-terminal fragment (CTF) is further cleaved by caspase-3 to produce the fragment, PS1-CTF12.
PTM: After endoproteolysis, the C-terminal fragment (CTF) is phosphorylated on serine residues by PKA and/or PKC. Phosphorylation on Ser-346 inhibits endoproteolysis.
DISEASE: Defects in PSEN1 are a cause of Alzheimer disease type 3 (AD3) [MIM:607822]. AD3 is a familial early-onset form of Alzheimer disease. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitve abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
DISEASE: Defects in PSEN1 are a cause of frontotemporal dementia [MIM:600274].
SIMILARITY: Belongs to the peptidase A22A family [view classification].
WEB RESOURCE: Name=Alzheimer Research Forum; Note=Presenilins mutations; URL="http://www.alzforum.org/res/com/mut/pre/default.asp";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=PSEN1";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L42110; AAB46416.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76517; AAB46370.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76528; AAB46371.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76519; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76520; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76521; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76522; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76523; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76524; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76525; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76526; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L76527; AAB46371.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U40379; AAB05894.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U40380; AAB05895.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ008005; CAA07825.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109907; AAC97960.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF416717; AAL16811.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004858; AAF19253.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004858; AAF19254.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011729; AAH11729.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D84149; BAA20883.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00028077; -.
IPI00068752; -.
IPI00219934; -.
IPI00289615; -.
IPI00337671; -.
IPI00514137; -.

PIR

S58396; S58396.
S63683; S63683.
S63684; S63684.

RefSeq

NP_000012.1; -.
NP_015557.2; -.

UniGene

Hs.3260

3D structure databases

ModBase

P49768.

Protein-protein interaction databases

DIP

DIP:1134N; -.

IntAct

P49768; 10.

Protein family/group databases

MEROPS

A22.001; -.

TCDB

1.A.54.1.1; presenilin ER Ca2+ leak channel (Presenilin) family.

PTM databases

PhosphoSite

P49768; -.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway; p75(NTR)-mediated signaling.
ps1pathway; Presenilin action in Notch and Wnt signaling.
syndecan_3_pathway; Syndecan-3-mediated signaling events.

Reactome

REACT_11061; Signalling by NGF.
REACT_299; Signaling by Notch.

Organism-specific databases

GC14P072672; -.

HIX0011789; -.

HGNC:9508; PSEN1.

CAB006844; -.

104311; gene. [NCBI / EBI]
600274; phenotype. [NCBI / EBI]
607822; phenotype. [NCBI / EBI]

Orphanet

1020; Alzheimer disease, familial.
154; Cardiomyopathy, familial dilated.
36385; Fronto-temporal dementia and Parkinsonism linked to chromosome 17 (FTDP-17).
282; Frontotemporal dementia.
2883; Pick disease of brain.

PharmGKB

PA33855; -.

Gene expression databases

P49768; -.

P49768; -.

HS_PSEN1; -.

ENSG00000080815; Homo sapiens.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000139;	Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005639;	Cellular component: integral to nuclear inner membrane (traceable author statement from ProtInc).
GO:0005887;	Cellular component: integral to plasma membrane (inferred from direct assay from HGNC).
GO:0000776;	Cellular component: kinetochore (traceable author statement from ProtInc).
GO:0005624;	Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0005640;	Cellular component: nuclear outer membrane (inferred from direct assay from MGI).
GO:0008013;	Molecular function: beta-catenin binding (inferred from physical interaction from MGI).
GO:0004175;	Molecular function: endopeptidase activity (inferred from direct assay from MGI).
GO:0030165;	Molecular function: PDZ domain binding (inferred from physical interaction from UniProtKB).
GO:0042987;	Biological process: amyloid precursor protein catabolic process (traceable author statement from HGNC).
GO:0006916;	Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0016337;	Biological process: cell-cell adhesion (inferred from mutant phenotype from MGI).
GO:0007059;	Biological process: chromosome segregation (traceable author statement from ProtInc).
GO:0032469;	Biological process: endoplasmic reticulum calcium ion homeostasis (inferred from direct assay from MGI).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0006509;	Biological process: membrane protein ectodomain proteolysis (inferred from direct assay from HGNC).
GO:0007220;	Biological process: Notch receptor processing (traceable author statement from HGNC).
GO:0043085;	Biological process: positive regulation of catalytic activity (inferred from direct assay from HGNC).
GO:0042325;	Biological process: regulation of phosphorylation (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002031; Pept_A22A_PS1.
IPR006639; Peptidase_A22.
IPR001108; Peptidase_A22A.
Graphical view of domain structure.

PANTHER

PTHR10202:SF7; Pept_A22A_PS1; 1.
PTHR10202; Peptidase_A22A; 1.

Pfam

PF01080; Presenilin; 1.
Pfam graphical view of domain structure.

PRINTS

PR01072; PRESENILIN.
PR01073; PRESENILIN1.

SMART

SM00730; PSN; 1.
SMART graphical view of domain structure.

Proteomic databases

PRIDE

P49768; -.

Genome annotation databases

Ensembl

ENSG00000080815; Homo sapiens. [Contig view]

GeneID

5663; -.

KEGG

hsa:5663; -.

Phylogenomic databases

HOVERGEN

P49768; -.

Other

22006; -.

P49768; -.

PSEN1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Alzheimer disease; Amyloidosis; Apoptosis; Cell adhesion; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Golgi apparatus; Hydrolase; Membrane; Neurodegeneration; Notch signaling pathway; Phosphoprotein; Polymorphism; Protease; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 298`	`298`	`Presenilin-1 NTF subunit.`	`PRO_0000025591`
`CHAIN`	`299 467`	`169`	`Presenilin-1 CTF subunit.`	`PRO_0000025592`
`CHAIN`	`346 467`	`122`	`Presenilin-1 CTF12.`	`PRO_0000236055`
`TOPO_DOM`	`1 82`	`82`	`Cytoplasmic (Potential).`
`TRANSMEM`	`83 103`	`21`	`Potential.`
`TOPO_DOM`	`104 132`	`29`	`Lumenal (Potential).`
`TRANSMEM`	`133 153`	`21`	`Potential.`
`TOPO_DOM`	`154 160`	`7`	`Cytoplasmic (Potential).`
`TRANSMEM`	`161 181`	`21`	`Potential.`
`TOPO_DOM`	`182 190`	`9`	`Lumenal (Potential).`
`TRANSMEM`	`191 211`	`21`	`Potential.`
`TOPO_DOM`	`212 220`	`9`	`Cytoplasmic (Potential).`
`TRANSMEM`	`221 241`	`21`	`Potential.`
`TOPO_DOM`	`242 243`	`2`	`Lumenal (Potential).`
`TRANSMEM`	`244 264`	`21`	`Potential.`
`TOPO_DOM`	`265 407`	`143`	`Cytoplasmic (Potential).`
`TRANSMEM`	`408 428`	`21`	`Potential.`
`TRANSMEM`	`433 453`	`21`	`Potential.`
`TOPO_DOM`	`454 467`	`14`	`Cytoplasmic (Potential).`
`REGION`	`322 450`	`129`	`Required for interaction with CTNNB1.`
`REGION`	`372 399`	`28`	`Required for interaction with CTNND2.`
`REGION`	`464 467`	`4`	`Interaction with MTCH1.`
`MOTIF`	`433 435`	`3`	`PAL.`
`COMPBIAS`	`94 97`	`4`	`Poly-Val.`
`COMPBIAS`	`171 174`	`4`	`Poly-Leu.`
`COMPBIAS`	`418 425`	`8`	`Poly-Leu.`
`ACT_SITE`	`257 257`		`Probable.`
`ACT_SITE`	`385 385`		`Probable.`
`SITE`	`291 292`	`2`	`Cleavage; alternate.`
`SITE`	`292 293`	`2`	`Cleavage; alternate.`
`SITE`	`298 299`	`2`	`Cleavage.`
`SITE`	`345 346`	`2`	`Cleavage; by caspase.`
`MOD_RES`	`43 43`		`Phosphoserine.`
`MOD_RES`	`310 310`		`Phosphoserine; by PKA.`
`MOD_RES`	`346 346`		`Phosphoserine; by PKC.`
`MOD_RES`	`365 365`		`Phosphoserine.`
`MOD_RES`	`367 367`		`Phosphoserine.`
`VAR_SEQ`	`26 29`		`Missing (in isoform 2 and isoform 3).`	`VSP_005191`
`VAR_SEQ`	`162 184`		`IHAWLIISSLLLLFFFSFIYLGE -> SMRHRSLLSTLFFLWLGILVTVT (in isoform 4).`	`VSP_007986`
`VAR_SEQ`	`185 467`		`Missing (in isoform 4).`	`VSP_007987`
`VAR_SEQ`	`319 467`		`STERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESR` `AAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASA` `TASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPIS` `ITFGLVFYFATDYLVQPFMDQLAFHQFYI -> RACLPPAAINLLSIAPMAPRLFMPKGACRPTAQKGSHKTL` `LQRMMMAGSVRNGKPRGTVI (in isoform 3 and isoform 5).`	`VSP_005192`
`VAR_SEQ`	`319 376`		`Missing (in isoform 6).`	`VSP_012288`
`VARIANT`	`79 79`	`1`	`A -> V (in AD3; no effect on interaction with GFAP).`	`VAR_006413`
`VARIANT`	`82 82`	`1`	`V -> L (in AD3; no effect on interaction with GFAP).`	`VAR_006414`
`VARIANT`	`92 92`	`1`	`C -> S (in AD3).`	`VAR_016214`
`VARIANT`	`96 96`	`1`	`V -> F (in AD3).`	`VAR_006415`
`VARIANT`	`105 105`	`1`	`F -> L (in AD3).`	`VAR_009208`
`VARIANT`	`113 113`	`1`	`L -> P (in frontotemporal dementia).`	`VAR_016215`
`VARIANT`	`115 115`	`1`	`Y -> C (in AD3).`	`VAR_006416`
`VARIANT`	`115 115`	`1`	`Y -> H (in AD3).`	`VAR_006417`
`VARIANT`	`116 116`	`1`	`T -> N (in AD3).`	`VAR_010120`
`VARIANT`	`117 117`	`1`	`P -> L (in AD3).`	`VAR_009209`
`VARIANT`	`120 120`	`1`	`E -> D (in AD3).`	`VAR_006418`
`VARIANT`	`120 120`	`1`	`E -> K (in AD3).`	`VAR_006419`
`VARIANT`	`135 135`	`1`	`N -> D (in AD3).`	`VAR_010121`
`VARIANT`	`139 139`	`1`	`M -> I (in AD3).`	`VAR_006420`
`VARIANT`	`139 139`	`1`	`M -> K (in AD3).`	`VAR_010122`
`VARIANT`	`139 139`	`1`	`M -> T (in AD3).`	`VAR_006421`
`VARIANT`	`139 139`	`1`	`M -> V (in AD3).`	`VAR_006422`
`VARIANT`	`143 143`	`1`	`I -> F (in AD3).`	`VAR_006423`
`VARIANT`	`143 143`	`1`	`I -> T (in AD3).`	`VAR_006424`
`VARIANT`	`146 146`	`1`	`M -> I (in AD3).`	`VAR_006425`
`VARIANT`	`146 146`	`1`	`M -> L (in AD3).`	`VAR_006426`
`VARIANT`	`146 146`	`1`	`M -> V (in AD3).`	`VAR_006427`
`VARIANT`	`147 147`	`1`	`T -> I (in AD3).`	`VAR_010123`
`VARIANT`	`163 163`	`1`	`H -> R (in AD3).`	`VAR_006428`
`VARIANT`	`163 163`	`1`	`H -> Y (in AD3).`	`VAR_006429`
`VARIANT`	`165 165`	`1`	`W -> C (in AD3).`	`VAR_010124`
`VARIANT`	`166 166`	`1`	`L -> P (in AD3; onset in adolescence).`	`VAR_016216`
`VARIANT`	`169 169`	`1`	`S -> L (in AD3).`	`VAR_006430`
`VARIANT`	`169 169`	`1`	`S -> P (in AD3).`	`VAR_006431`
`VARIANT`	`171 171`	`1`	`L -> P (in AD3).`	`VAR_006432`
`VARIANT`	`173 173`	`1`	`L -> W (in AD3).`	`VAR_010125`
`VARIANT`	`174 174`	`1`	`L -> M (in AD3).`	`VAR_016217`
`VARIANT`	`205 205`	`1`	`F -> L (in dbSNP:rs1042864 [NCBI]).`	`VAR_011876`
`VARIANT`	`206 206`	`1`	`G -> A (in AD3).`	`VAR_016218`
`VARIANT`	`209 209`	`1`	`G -> R (in AD3).`	`VAR_009210`
`VARIANT`	`209 209`	`1`	`G -> V (in AD3).`	`VAR_006433`
`VARIANT`	`213 213`	`1`	`I -> T (in AD3).`	`VAR_006434`
`VARIANT`	`219 219`	`1`	`L -> P (in AD3).`	`VAR_010126`
`VARIANT`	`231 231`	`1`	`A -> T (in AD3).`	`VAR_006435`
`VARIANT`	`231 231`	`1`	`A -> V (in AD3).`	`VAR_006436`
`VARIANT`	`233 233`	`1`	`M -> L (in AD3).`	`VAR_009211`
`VARIANT`	`233 233`	`1`	`M -> T (in AD3).`	`VAR_006437`
`VARIANT`	`235 235`	`1`	`L -> P (in A3D).`	`VAR_006438`
`VARIANT`	`246 246`	`1`	`A -> E (in AD3).`	`VAR_006439`
`VARIANT`	`250 250`	`1`	`L -> S (in AD3).`	`VAR_006440`
`VARIANT`	`260 260`	`1`	`A -> V (in AD3).`	`VAR_006441`
`VARIANT`	`262 262`	`1`	`L -> F (in AD3).`	`VAR_006442`
`VARIANT`	`263 263`	`1`	`C -> R (in AD3).`	`VAR_006443`
`VARIANT`	`264 264`	`1`	`P -> L (in AD3).`	`VAR_006444`
`VARIANT`	`266 266`	`1`	`G -> S (in AD3).`	`VAR_016219`
`VARIANT`	`267 267`	`1`	`P -> S (in AD3).`	`VAR_006445`
`VARIANT`	`267 267`	`1`	`P -> T (in AD3).`	`VAR_006446`
`VARIANT`	`269 269`	`1`	`R -> G (in AD3).`	`VAR_006447`
`VARIANT`	`269 269`	`1`	`R -> H (in AD3).`	`VAR_006448`
`VARIANT`	`271 271`	`1`	`L -> V (in AD3).`	`VAR_016220`
`VARIANT`	`278 278`	`1`	`R -> T (in AD3).`	`VAR_006449`
`VARIANT`	`280 280`	`1`	`E -> A (in AD3).`	`VAR_006450`
`VARIANT`	`280 280`	`1`	`E -> G (in AD3).`	`VAR_006451`
`VARIANT`	`282 282`	`1`	`L -> R (in AD3).`	`VAR_009212`
`VARIANT`	`285 285`	`1`	`A -> V (in AD3).`	`VAR_006452`
`VARIANT`	`286 286`	`1`	`L -> V (in AD3).`	`VAR_006453`
`VARIANT`	`289 289`	`1`	`S -> C (in AD3).`	`VAR_010127`
`VARIANT`	`318 318`	`1`	`E -> G (in dbSNP:rs17125721 [NCBI]).`	`VAR_006454`
`VARIANT`	`378 378`	`1`	`G -> E (in AD3).`	`VAR_006455`
`VARIANT`	`384 384`	`1`	`G -> A (in AD3).`	`VAR_006456`
`VARIANT`	`390 390`	`1`	`S -> I (in AD3).`	`VAR_010128`
`VARIANT`	`392 392`	`1`	`L -> V (in AD3).`	`VAR_006457`
`VARIANT`	`405 405`	`1`	`N -> S (in AD3).`	`VAR_010129`
`VARIANT`	`409 409`	`1`	`A -> T (in AD3).`	`VAR_009213`
`VARIANT`	`410 410`	`1`	`C -> Y (in AD3).`	`VAR_006458`
`VARIANT`	`426 426`	`1`	`A -> P (in AD3).`	`VAR_006459`
`VARIANT`	`431 431`	`1`	`A -> E (in AD3).`	`VAR_025605`
`VARIANT`	`436 436`	`1`	`P -> Q (in AD3).`	`VAR_006460`
`VARIANT`	`436 436`	`1`	`P -> S (in AD3).`	`VAR_008141`
`MUTAGEN`	`66 72`		`Missing: No effect on interaction with GFAP.`
`MUTAGEN`	`76 77`		`KY->AA: No effect on interaction with GFAP.`
`MUTAGEN`	`82 83`		`VI->EE: Loss of interaction with GFAP.`
`MUTAGEN`	`82 82`		`V->K,E: Loss of interaction with GFAP.`
`MUTAGEN`	`84 85`		`ML->EE: Loss of interaction with GFAP.`
`MUTAGEN`	`256 256`		`Y->F: Alters gamma-secretase cleavage specificity. Increased production of amyloid beta(42). No effect on enzymatic activity.`
`MUTAGEN`	`257 257`		`D->A: Loss of endoproteolytic cleavage; reduces production of amyloid beta in APP processing and of NICD in NOTCH1 processing.`
`MUTAGEN`	`257 257`		`D->E: Abolishes gamma-secretase activity. Reduces production of amyloid beta in APP processing. Accumulation of full-length PS1. Loss of binding of transition state analog gamma-secretase inhibitor.`
`MUTAGEN`	`286 286`		`L->A,E,P,Q,R,W: Increases production of amyloid beta in APP processing.`
`MUTAGEN`	`286 286`		`L->E,R: Reduces production of NICD in NOTCH1 processing.`
`MUTAGEN`	`292 292`		`M->D: Loss of endoproteolytic cleavage.`
`MUTAGEN`	`310 310`		`S->A: Abolishes PKA-mediated phosphorylation; no effect on caspase-mediated cleavage.`
`MUTAGEN`	`345 345`		`D->N: Abolishes caspase cleavage.`
`MUTAGEN`	`346 346`		`S->A: Abolishes PKC-mediated phosphorylation; no effect on PKA-mediated phosphorylation.`
`MUTAGEN`	`346 346`		`S->E: Inhibits caspase-mediated cleavage. Modulates progression of apoptosis.`
`MUTAGEN`	`373 373`		`D->N: No effect on caspase cleavage.`
`MUTAGEN`	`385 385`		`D->A: Loss of endoproteolytic cleavage. Reduces production of amyloid beta in APP processing. Disassembly of the N-cadherin/PS1 complex at the cell surface. Impairs CDH2 processing.`
`MUTAGEN`	`385 385`		`D->E: Abolishes gamma-secretase activity. Reduces production of amyloid beta in APP processing. Accumulation of full-length PS1. Loss of binding of transition state analog gamma-secretase inhibitor.`
`MUTAGEN`	`385 385`		`D->N: No effect on caspase cleavage.`
`MUTAGEN`	`389 389`		`Y->F: Alters gamma-secretase cleavage specificity. Increased production of amyloid beta(42). No effect on enzymatic activity.`
`MUTAGEN`	`433 433`		`P->A: No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing. Slightly increased Abeta42/Abeta40 ratio.`
`MUTAGEN`	`433 433`		`P->D,F,L,N,V: No endoproteolytic cleavage; no APP nor NOTCH1 processing. No detectable Abetano detectable Abeta.`
`MUTAGEN`	`433 433`		`P->G: Very little endoproteolysis. Little APP processing. No NOTCH1 processing. Very low levels Abeta40 and no detectable Abeta42.`
`MUTAGEN`	`434 434`		`A->C: Some loss of endoproteolytic cleavage. Some loss of APP and NOTCH1 processing. Six-fold increase in Abeta42/Abeta40 ratio.`
`MUTAGEN`	`434 434`		`A->D,I,L,V: No endoproteolytic cleavage. No APP nor NOTCH1 processing. No detectable Abeta.`
`MUTAGEN`	`434 434`		`A->G: No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing. Reduced Abeta42/Abeta40 ratio.`
`MUTAGEN`	`435 435`		`L->A: No effect on endoproteolytic cleavage. No effect on APP processing. Impaired NOTCH1 processing. Greatly reduced Abeta42/Abeta40 ratio.`
`MUTAGEN`	`435 435`		`L->F: No endoproteolytic cleavage. No APP nor NOTCH1 processing. No detectable Abeta.`
`MUTAGEN`	`435 435`		`L->G: Greatly reduced endoproteolytic cleavage. Very little APP and NOTCH1 processing. Very low levels of Abeta40 and no detectable Abeta42.`
`MUTAGEN`	`435 435`		`L->I: No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing.`
`MUTAGEN`	`435 435`		`L->V: No effect on endoproteolytic cleavage. No effect on APP processing. Impaired NOTCH1 processing. Some increase in Abeta42/Abeta40 ratio.`
`CONFLICT`	`128 128`		`R -> G (in Ref. 6; AAL16811).`

Sequence information

Length: 467 AA [This is the length of the unprocessed precursor]

Molecular weight: 52668 Da [This is the MW of the unprocessed precursor]

CRC64: 5E0F451EF82BCF20 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTELPAPLSY FQNAQMSEDN HLSNTVRSQN DNRERQEHND RRSLGHPEPL SNGRPQGNSR 

        70         80         90        100        110        120 
QVVEQDEEED EELTLKYGAK HVIMLFVPVT LCMVVVVATI KSVSFYTRKD GQLIYTPFTE 

       130        140        150        160        170        180 
DTETVGQRAL HSILNAAIMI SVIVVMTILL VVLYKYRCYK VIHAWLIISS LLLLFFFSFI 

       190        200        210        220        230        240 
YLGEVFKTYN VAVDYITVAL LIWNFGVVGM ISIHWKGPLR LQQAYLIMIS ALMALVFIKY 

       250        260        270        280        290        300 
LPEWTAWLIL AVISVYDLVA VLCPKGPLRM LVETAQERNE TLFPALIYSS TMVWLVNMAE 

       310        320        330        340        350        360 
GDPEAQRRVS KNSKYNAEST ERESQDTVAE NDDGGFSEEW EAQRDSHLGP HRSTPESRAA 

       370        380        390        400        410        420 
VQELSSSILA GEDPEERGVK LGLGDFIFYS VLVGKASATA SGDWNTTIAC FVAILIGLCL 

       430        440        450        460 
TLLLLAIFKK ALPALPISIT FGLVFYFATD YLVQPFMDQL AFHQFYI

P49768 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools