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Presenilin-2 (PS-2) (EC 3.4.23.-) (AD3LP) (AD5) (E5-1) (STM-2) [Cleaved into: Presenilin-2 NTF subunit; Presenilin-2 CTF subunit]

 PSN2_HUMAN              Reviewed;         448 AA.
P49810; A8K8D4; B1AP21; Q96P32;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 191.
RecName: Full=Presenilin-2;
Short=PS-2;
EC=3.4.23.-;
AltName: Full=AD3LP;
AltName: Full=AD5;
AltName: Full=E5-1;
AltName: Full=STM-2;
Contains:
RecName: Full=Presenilin-2 NTF subunit;
Contains:
RecName: Full=Presenilin-2 CTF subunit;
Name=PSEN2; Synonyms=AD4, PS2, PSNL2, STM2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AD4 ILE-141.
PubMed=7638622; DOI=10.1126/science.7638622;
Levy-Lahad E., Wasco W., Poorkaj P., Romano D.M., Oshima J.,
Pettingell W.H. Jr., Yu C.-E., Jondro P.D., Schmidt S.D., Wang K.,
Crowley A.C., Fu Y.-H., Guenette S.Y., Galas D., Nemens E.,
Wijsman E.M., Bird T.D., Schellenberg G.D., Tanzi R.E.;
"Candidate gene for the chromosome 1 familial Alzheimer's disease
locus.";
Science 269:973-977(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS AD4 ILE-141 AND VAL-239.
TISSUE=Brain, and Colon;
PubMed=7651536; DOI=10.1038/376775a0;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8618867; DOI=10.1073/pnas.92.26.12180;
Li J., Ma J., Potter H.;
"Identification and expression analysis of a potential familial
Alzheimer disease gene on chromosome 1 related to AD3.";
Proc. Natl. Acad. Sci. U.S.A. 92:12180-12184(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8661049; DOI=10.1006/geno.1996.0266;
Levy-Lahad E., Poorkaj P., Wang K., Fu Y.H., Oshima J., Mulligan J.,
Schellenberg G.D.;
"Genomic structure and expression of STM2, the chromosome 1 familial
Alzheimer disease gene.";
Genomics 34:198-204(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[10]
NUCLEOTIDE SEQUENCE OF 1-390.
Xu Y., Hu X., Zhou Y., Peng X., Yuan J., Qiang B.;
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8574969; DOI=10.1038/nm0296-224;
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]
INTERACTION WITH FLNA AND FLNB.
PubMed=9437013;
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).
[13]
FUNCTION, ACTIVE SITE ASP-366, AND MUTAGENESIS OF ASP-366.
PubMed=10497236; DOI=10.1074/jbc.274.40.28669;
Steiner H., Duff K., Capell A., Romig H., Grim M.G., Lincoln S.,
Hardy J., Yu X., Picciano M., Fechteler K., Citron M., Kopan R.,
Pesold B., Keck S., Baader M., Tomita T., Iwatsubo T., Baumeister R.,
Haass C.;
"A loss of function mutation of presenilin-2 interferes with amyloid
beta-peptide production and notch signaling.";
J. Biol. Chem. 274:28669-28673(1999).
[14]
FUNCTION, ACTIVE SITES ASP-263 AND ASP-366, AND MUTAGENESIS OF ASP-263
AND ASP-366.
PubMed=10652302; DOI=10.1074/jbc.275.5.3173;
Kimberly W.T., Xia W., Rahmati T., Wolfe M.S., Selkoe D.J.;
"The transmembrane aspartates in presenilin 1 and 2 are obligatory for
gamma-secretase activity and amyloid beta-protein generation.";
J. Biol. Chem. 275:3173-3178(2000).
[15]
INTERACTION WITH HERPUD1.
PubMed=11799129; DOI=10.1074/jbc.M112372200;
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).
[16]
REVIEW ON VARIANTS.
PubMed=9521418;
DOI=10.1002/(SICI)1098-1004(1998)11:3<183::AID-HUMU1>3.0.CO;2-J;
Cruts M., van Broeckhoven C.;
"Presenilin mutations in Alzheimer's disease.";
Hum. Mutat. 11:183-190(1998).
[17]
TOPOLOGY.
PubMed=15385547; DOI=10.1074/jbc.M407898200;
Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U.,
Rovelli G., Martoglio B.;
"Consensus analysis of signal peptide peptidase and homologous human
aspartic proteases reveals opposite topology of catalytic domains
compared with presenilins.";
J. Biol. Chem. 279:50790-50798(2004).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-25, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-25, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
VARIANT AD4 HIS-62.
PubMed=9384602; DOI=10.1093/hmg/7.1.43;
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).
[24]
VARIANT AD4 ILE-148.
PubMed=10732806; DOI=10.1007/s100480050044;
Lao J.I., Beyer K., Fernandez-Novoa L., Cacabelos R.;
"A novel mutation in the predicted TM2 domain of the presenilin 2 gene
in Spanish patient with late-onset Alzheimer's disease.";
Neurogenetics 1:293-296(1998).
[25]
VARIANTS AD4 PRO-122 AND ILE-239.
PubMed=10631141; DOI=10.1086/302702;
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).
[26]
VARIANT CMD1V LEU-130.
PubMed=17186461; DOI=10.1086/509900;
Li D., Parks S.B., Kushner J.D., Nauman D., Burgess D., Ludwigsen S.,
Partain J., Nixon R.R., Allen C.N., Irwin R.P., Jakobs P.M., Litt M.,
Hershberger R.E.;
"Mutations of presenilin genes in dilated cardiomyopathy and heart
failure.";
Am. J. Hum. Genet. 79:1030-1039(2006).
[27]
VARIANTS AD4 HIS-62; TRP-71 AND LEU-130.
PubMed=22503161; DOI=10.1016/j.neurobiolaging.2012.02.020;
Lohmann E., Guerreiro R.J., Erginel-Unaltuna N., Gurunlian N.,
Bilgic B., Gurvit H., Hanagasi H.A., Luu N., Emre M., Singleton A.;
"Identification of PSEN1 and PSEN2 gene mutations and variants in
Turkish dementia patients.";
Neurobiol. Aging 33:1850.E17-1850.E27(2012).
-!- 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 (amyloid-beta 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. May function in the
cytoplasmic partitioning of proteins.
{ECO:0000269|PubMed:10497236, ECO:0000269|PubMed:10652302}.
-!- SUBUNIT: Interacts with DOCK3 (By similarity). 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, although other components may exist. Interacts
with HERPUD1, FLNA, FLNB and PARL. {ECO:0000250,
ECO:0000269|PubMed:11799129, ECO:0000269|PubMed:9437013}.
-!- INTERACTION:
Q14204:DYNC1H1; NbExp=3; IntAct=EBI-2010251, EBI-356015;
Q9BQ95:ECSIT; NbExp=4; IntAct=EBI-2010251, EBI-712452;
Q53EL6:PDCD4; NbExp=3; IntAct=EBI-2010251, EBI-935824;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:8574969}; Multi-pass membrane protein
{ECO:0000269|PubMed:8574969}. Golgi apparatus membrane
{ECO:0000269|PubMed:8574969}; Multi-pass membrane protein
{ECO:0000269|PubMed:8574969}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P49810-1; Sequence=Displayed;
Name=2;
IsoId=P49810-2; Sequence=VSP_005194;
Name=3;
IsoId=P49810-3; Sequence=VSP_043648;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 is seen in the placenta, skeletal
muscle and heart while isoform 2 is seen in the heart, brain,
placenta, liver, skeletal muscle and kidney.
{ECO:0000269|PubMed:8574969}.
-!- DOMAIN: The PAL motif is required for normal active site
conformation. {ECO:0000250}.
-!- PTM: Heterogeneous proteolytic processing generates N-terminal and
C-terminal fragments.
-!- PTM: Phosphorylated on serine residues.
-!- DISEASE: Alzheimer disease 4 (AD4) [MIM:606889]: A familial early-
onset form of Alzheimer disease. Alzheimer disease is a
neurodegenerative disorder characterized by progressive dementia,
loss of cognitive abilities, and deposition of fibrillar amyloid
proteins as intraneuronal neurofibrillary tangles, extracellular
amyloid plaques and vascular amyloid deposits. The major
constituents of these plaques are neurotoxic amyloid-beta protein
40 and amyloid-beta protein 42, that are produced by the
proteolysis of the transmembrane APP protein. The cytotoxic C-
terminal fragments (CTFs) and the caspase-cleaved products, such
as C31, are also implicated in neuronal death.
{ECO:0000269|PubMed:10631141, ECO:0000269|PubMed:10732806,
ECO:0000269|PubMed:22503161, ECO:0000269|PubMed:7638622,
ECO:0000269|PubMed:7651536, ECO:0000269|PubMed:9384602}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cardiomyopathy, dilated 1V (CMD1V) [MIM:613697]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:17186461}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Alzheimer Research Forum; Note=Presenilins
mutations;
URL="http://www.alzforum.org/mutations/search?genes%255B%255D=348";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PSEN2ID41883ch1q42.html";
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EMBL; L43964; AAB59557.1; -; mRNA.
EMBL; L44577; AAC42012.1; -; mRNA.
EMBL; U34349; AAC50290.1; -; mRNA.
EMBL; U50871; AAB50054.1; -; Genomic_DNA.
EMBL; BT006984; AAP35630.1; -; mRNA.
EMBL; AK292299; BAF84988.1; -; mRNA.
EMBL; AL391628; CAH73110.1; -; Genomic_DNA.
EMBL; CH471098; EAW69798.1; -; Genomic_DNA.
EMBL; CH471098; EAW69800.1; -; Genomic_DNA.
EMBL; BC006365; AAH06365.1; -; mRNA.
EMBL; AF416718; AAL16812.1; -; mRNA.
CCDS; CCDS1556.1; -. [P49810-1]
CCDS; CCDS44324.1; -. [P49810-3]
PIR; A56993; A56993.
PIR; I39174; I39174.
RefSeq; NP_000438.2; NM_000447.2. [P49810-1]
RefSeq; NP_036618.2; NM_012486.2. [P49810-3]
RefSeq; XP_005273256.1; XM_005273199.3. [P49810-1]
RefSeq; XP_016857324.1; XM_017001835.1. [P49810-1]
RefSeq; XP_016857325.1; XM_017001836.1. [P49810-3]
UniGene; Hs.25363; -.
ProteinModelPortal; P49810; -.
SMR; P49810; -.
BioGrid; 111643; 58.
CORUM; P49810; -.
IntAct; P49810; 24.
MINT; MINT-95242; -.
STRING; 9606.ENSP00000355747; -.
BindingDB; P49810; -.
ChEMBL; CHEMBL3708; -.
MEROPS; A22.002; -.
TCDB; 1.A.54.1.2; the presenilin er ca(2+) leak channel (presenilin) family.
iPTMnet; P49810; -.
PhosphoSitePlus; P49810; -.
SwissPalm; P49810; -.
BioMuta; PSEN2; -.
DMDM; 1709858; -.
EPD; P49810; -.
MaxQB; P49810; -.
PaxDb; P49810; -.
PeptideAtlas; P49810; -.
PRIDE; P49810; -.
DNASU; 5664; -.
Ensembl; ENST00000366783; ENSP00000355747; ENSG00000143801. [P49810-1]
Ensembl; ENST00000422240; ENSP00000403737; ENSG00000143801. [P49810-3]
GeneID; 5664; -.
KEGG; hsa:5664; -.
UCSC; uc009xeo.2; human. [P49810-1]
CTD; 5664; -.
DisGeNET; 5664; -.
EuPathDB; HostDB:ENSG00000143801.16; -.
GeneCards; PSEN2; -.
GeneReviews; PSEN2; -.
HGNC; HGNC:9509; PSEN2.
HPA; CAB013634; -.
MalaCards; PSEN2; -.
MIM; 600759; gene.
MIM; 606889; phenotype.
MIM; 613697; phenotype.
neXtProt; NX_P49810; -.
OpenTargets; ENSG00000143801; -.
Orphanet; 1020; Early-onset autosomal dominant Alzheimer disease.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
PharmGKB; PA33856; -.
eggNOG; KOG2736; Eukaryota.
eggNOG; ENOG410XPZD; LUCA.
GeneTree; ENSGT00390000016593; -.
HOGENOM; HOG000240228; -.
HOVERGEN; HBG011375; -.
InParanoid; P49810; -.
KO; K04522; -.
PhylomeDB; P49810; -.
TreeFam; TF315040; -.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
Reactome; R-HSA-1980148; Signaling by NOTCH3.
Reactome; R-HSA-1980150; Signaling by NOTCH4.
Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; P49810; -.
SIGNOR; P49810; -.
ChiTaRS; PSEN2; human.
GeneWiki; PSEN2; -.
GenomeRNAi; 5664; -.
PRO; PR:P49810; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143801; -.
CleanEx; HS_PSEN2; -.
ExpressionAtlas; P49810; baseline and differential.
Genevisible; P49810; HS.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005938; C:cell cortex; IBA:GO_Central.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:HGNC.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:HGNC.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0042987; P:amyloid precursor protein catabolic process; TAS:HGNC.
GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:HGNC.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007220; P:Notch receptor processing; TAS:HGNC.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:HGNC.
GO; GO:0016485; P:protein processing; IDA:HGNC.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
InterPro; IPR001493; Pept_A22A_PS2.
InterPro; IPR001108; Peptidase_A22A.
InterPro; IPR006639; Preselin/SPP.
PANTHER; PTHR10202; PTHR10202; 2.
Pfam; PF01080; Presenilin; 2.
PRINTS; PR01072; PRESENILIN.
PRINTS; PR01074; PRESENILIN2.
SMART; SM00730; PSN; 1.
1: Evidence at protein level;
Alternative splicing; Alzheimer disease; Amyloidosis; Cardiomyopathy;
Complete proteome; Disease mutation; Endoplasmic reticulum;
Golgi apparatus; Hydrolase; Membrane; Neurodegeneration;
Notch signaling pathway; Phosphoprotein; Protease; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 297 Presenilin-2 NTF subunit. {ECO:0000250}.
/FTId=PRO_0000025603.
CHAIN 298 448 Presenilin-2 CTF subunit. {ECO:0000250}.
/FTId=PRO_0000025604.
TOPO_DOM 1 87 Cytoplasmic. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TOPO_DOM 109 138 Lumenal. {ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TOPO_DOM 160 166 Cytoplasmic. {ECO:0000255}.
TRANSMEM 167 187 Helical. {ECO:0000255}.
TOPO_DOM 188 200 Lumenal. {ECO:0000255}.
TRANSMEM 201 221 Helical. {ECO:0000255}.
TOPO_DOM 222 223 Cytoplasmic. {ECO:0000255}.
TRANSMEM 224 244 Helical. {ECO:0000255}.
TOPO_DOM 245 249 Lumenal. {ECO:0000255}.
TRANSMEM 250 270 Helical. {ECO:0000255}.
TOPO_DOM 271 361 Cytoplasmic. {ECO:0000255}.
TRANSMEM 362 382 Helical. {ECO:0000255}.
TOPO_DOM 383 388 Lumenal. {ECO:0000255}.
TRANSMEM 389 409 Helical. {ECO:0000255}.
TOPO_DOM 410 413 Cytoplasmic. {ECO:0000255}.
INTRAMEM 414 434 Helical. {ECO:0000255}.
TOPO_DOM 435 448 Cytoplasmic. {ECO:0000255}.
MOTIF 414 416 PAL.
ACT_SITE 263 263 {ECO:0000305|PubMed:10652302}.
ACT_SITE 366 366 {ECO:0000305|PubMed:10497236,
ECO:0000305|PubMed:10652302}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:Q61144}.
VAR_SEQ 263 296 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_005194.
VAR_SEQ 324 324 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043648.
VARIANT 62 62 R -> H (in AD4; uncertain pathological
significance; dbSNP:rs58973334).
{ECO:0000269|PubMed:22503161,
ECO:0000269|PubMed:9384602}.
/FTId=VAR_006461.
VARIANT 71 71 R -> W (in AD4; unknown pathological
significance; dbSNP:rs140501902).
{ECO:0000269|PubMed:22503161}.
/FTId=VAR_070027.
VARIANT 122 122 T -> P (in AD4; dbSNP:rs63749851).
{ECO:0000269|PubMed:10631141}.
/FTId=VAR_009214.
VARIANT 130 130 S -> L (in CMD1V and AD4; unknown
pathological significance;
dbSNP:rs63750197).
{ECO:0000269|PubMed:17186461,
ECO:0000269|PubMed:22503161}.
/FTId=VAR_064903.
VARIANT 141 141 N -> I (in AD4; dbSNP:rs63750215).
{ECO:0000269|PubMed:7638622,
ECO:0000269|PubMed:7651536}.
/FTId=VAR_006462.
VARIANT 148 148 V -> I (in AD4; late-onset Alzheimer
disease; dbSNP:rs63750812).
{ECO:0000269|PubMed:10732806}.
/FTId=VAR_007958.
VARIANT 239 239 M -> I (in AD4; dbSNP:rs63749884).
{ECO:0000269|PubMed:10631141}.
/FTId=VAR_009215.
VARIANT 239 239 M -> V (in AD4; Italian patients;
dbSNP:rs28936379).
{ECO:0000269|PubMed:7651536}.
/FTId=VAR_006463.
MUTAGEN 263 263 D->A: Reduces production of amyloid-beta
in APP processing.
{ECO:0000269|PubMed:10652302}.
MUTAGEN 366 366 D->A: Reduces production of amyloid-beta
in APP processing and of NICD in NOTCH1
processing. {ECO:0000269|PubMed:10497236,
ECO:0000269|PubMed:10652302}.
CONFLICT 123 123 P -> T (in Ref. 1 and 10). {ECO:0000305}.
CONFLICT 295 295 S -> L (in Ref. 10; AAL16812).
{ECO:0000305}.
CONFLICT 325 325 Missing (in Ref. 3; AAC50290).
{ECO:0000305}.
CONFLICT 358 358 R -> SQG (in Ref. 3; AAC50290).
{ECO:0000305}.
CONFLICT 432 448 NLVRPFMDTLASHQLYI -> RKHSRFIQMN (in Ref.
3). {ECO:0000305}.
SEQUENCE 448 AA; 50140 MW; A927EEC623468116 CRC64;
MLTFMASDSE EEVCDERTSL MSAESPTPRS CQEGRQGPED GENTAQWRSQ ENEEDGEEDP
DRYVCSGVPG RPPGLEEELT LKYGAKHVIM LFVPVTLCMI VVVATIKSVR FYTEKNGQLI
YTPFTEDTPS VGQRLLNSVL NTLIMISVIV VMTIFLVVLY KYRCYKFIHG WLIMSSLMLL
FLFTYIYLGE VLKTYNVAMD YPTLLLTVWN FGAVGMVCIH WKGPLVLQQA YLIMISALMA
LVFIKYLPEW SAWVILGAIS VYDLVAVLCP KGPLRMLVET AQERNEPIFP ALIYSSAMVW
TVGMAKLDPS SQGALQLPYD PEMEEDSYDS FGEPSYPEVF EPPLTGYPGE ELEEEEERGV
KLGLGDFIFY SVLVGKAAAT GSGDWNTTLA CFVAILIGLC LTLLLLAVFK KALPALPISI
TFGLIFYFST DNLVRPFMDT LASHQLYI


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