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P49769 (PSN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Presenilin-1

Short name=PS-1
EC=3.4.23.-
Alternative name(s):
Protein S182

Cleaved into the following 3 chains:

  1. Presenilin-1 NTF subunit
  2. Presenilin-1 CTF subunit
  3. Presenilin-1 CTF12
    Short name=PS1-CTF12
Gene names
Name:Psen1
Synonyms:Ad3h, Psnl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 By similarity.

Subunit structure

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. Associates with 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 3of GFAP. Interacts with DOCK3 By similarity. Ref.5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell surface By similarity.

Domain

The PAL motif is required for normal active site conformation By similarity.

Post-translational modification

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 By similarity.

After endoproteolysis, the C-terminal fragment (CTF) is phosphorylated on serine residues by PKA and/or PKC. Phosphorylation on Ser-346 inhibits endoproteolysis By similarity.

Sequence similarities

Belongs to the peptidase A22A family.

Ontologies

Keywords
   Biological processApoptosis
Cell adhesion
Notch signaling pathway
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCajal-Retzius cell differentiation

Inferred from mutant phenotype PubMed 15548218. Source: MGI

L-glutamate transport

Inferred from mutant phenotype PubMed 15009636. Source: MGI

Notch receptor processing

Inferred from mutant phenotype PubMed 10206645PubMed 12391611PubMed 20130175. Source: MGI

Notch signaling pathway

Inferred from mutant phenotype PubMed 10821758PubMed 11262239PubMed 16715081. Source: MGI

T cell activation involved in immune response

Inferred from genetic interaction PubMed 17698590. Source: MGI

T cell receptor signaling pathway

Inferred from genetic interaction PubMed 17698590. Source: MGI

activation of MAPKK activity

Inferred from mutant phenotype PubMed 15896720. Source: MGI

amyloid precursor protein catabolic process

Inferred from mutant phenotype PubMed 10206645PubMed 11567612PubMed 15452145. Source: MGI

anagen

Inferred from genetic interaction PubMed 15525534. Source: MGI

autophagic vacuole assembly

Inferred from mutant phenotype PubMed 15452145. Source: MGI

autophagy

Inferred from mutant phenotype PubMed 15123735. Source: MGI

beta-amyloid formation

Inferred from mutant phenotype PubMed 20130175. Source: MGI

beta-amyloid metabolic process

Inferred from mutant phenotype PubMed 12684521. Source: MGI

blood vessel development

Inferred from mutant phenotype PubMed 15254914PubMed 16079160PubMed 9153393. Source: MGI

brain development

Inferred from mutant phenotype PubMed 9153393. Source: MGI

brain morphogenesis

Inferred from genetic interaction PubMed 17614943. Source: MGI

calcium ion transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell fate specification

Inferred from genetic interaction PubMed 15525534. Source: MGI

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 12431992. Source: MGI

cellular protein metabolic process

Inferred from direct assay PubMed 17097608. Source: MGI

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 12460542. Source: MGI

cerebral cortex cell migration

Inferred from mutant phenotype PubMed 16079160. Source: MGI

cerebral cortex development

Inferred from mutant phenotype PubMed 16079160. Source: MGI

choline transport

Inferred from mutant phenotype PubMed 17196556. Source: MGI

dorsal/ventral neural tube patterning

Inferred from genetic interaction PubMed 10557208. Source: MGI

embryonic limb morphogenesis

Inferred from genetic interaction PubMed 16169548. Source: MGI

endoplasmic reticulum calcium ion homeostasis

Inferred from mutant phenotype PubMed 10662826PubMed 12460542PubMed 15009636PubMed 15123735. Source: MGI

epithelial cell proliferation

Inferred from genetic interaction PubMed 17913918. Source: MGI

forebrain development

Inferred from genetic interaction PubMed 15148382. Source: MGI

heart development

Inferred from mutant phenotype PubMed 15254914. Source: MGI

heart looping

Inferred from genetic interaction PubMed 10557208. Source: MGI

hematopoietic progenitor cell differentiation

Inferred from genetic interaction PubMed 15122901. Source: MGI

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

learning or memory

Inferred from genetic interaction PubMed 15066262. Source: MGI

locomotion

Inferred from genetic interaction PubMed 15148382. Source: MGI

membrane protein ectodomain proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

memory

Inferred from mutant phenotype PubMed 11567612PubMed 11738035. Source: MGI

mitochondrial transport

Inferred from mutant phenotype PubMed 12805290. Source: MGI

myeloid leukocyte differentiation

Inferred from genetic interaction PubMed 15122901. Source: MGI

negative regulation of apoptotic process

Inferred from direct assay PubMed 15192701. Source: MGI

negative regulation of apoptotic signaling pathway

Inferred from genetic interaction PubMed 15148382. Source: MGI

negative regulation of axonogenesis

Inferred from mutant phenotype PubMed 15548218. Source: MGI

negative regulation of epidermal growth factor-activated receptor activity

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from mutant phenotype PubMed 12805290. Source: MGI

negative regulation of protein phosphorylation

Inferred from genetic interaction PubMed 15148382. Source: MGI

negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

negative regulation of ubiquitin-protein transferase activity

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

neurogenesis

Inferred from mutant phenotype PubMed 11738035PubMed 9160754. Source: MGI

neuron apoptotic process

Inferred from genetic interaction PubMed 16478525. Source: MGI

neuron development

Inferred from mutant phenotype PubMed 12391611. Source: MGI

neuron differentiation

Inferred from mutant phenotype PubMed 10821758. Source: MGI

neuron migration

Inferred from mutant phenotype PubMed 10421573PubMed 10821758PubMed 12391611PubMed 15163631. Source: MGI

positive regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 15896720. Source: MGI

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 16169548. Source: MGI

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of coagulation

Inferred from mutant phenotype PubMed 12646573. Source: MGI

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

positive regulation of protein kinase activity

Inferred from direct assay PubMed 15192701. Source: MGI

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 15896720. Source: MGI

positive regulation of receptor recycling

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

post-embryonic development

Inferred from mutant phenotype PubMed 10518543. Source: MGI

protein glycosylation

Inferred from mutant phenotype PubMed 12646573. Source: MGI

protein maturation

Inferred from genetic interaction PubMed 11943765PubMed 15280425. Source: MGI

protein processing

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from genetic interaction PubMed 11943765. Source: MGI

regulation of epidermal growth factor-activated receptor activity

Inferred from genetic interaction PubMed 17556541. Source: MGI

regulation of protein binding

Inferred from genetic interaction PubMed 17920016. Source: MGI

regulation of resting membrane potential

Inferred from mutant phenotype PubMed 15548218. Source: MGI

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 11814648. Source: MGI

regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 10097174. Source: MGI

response to oxidative stress

Inferred from mutant phenotype PubMed 10097174. Source: MGI

segmentation

Inferred from mutant phenotype PubMed 11262239PubMed 16079160. Source: MGI

single organismal cell-cell adhesion

Inferred from sequence orthology PubMed 11953314. Source: MGI

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 9160754. Source: MGI

skin morphogenesis

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

smooth endoplasmic reticulum calcium ion homeostasis

Inferred from genetic interaction PubMed 12431992. Source: MGI

somitogenesis

Inferred from mutant phenotype PubMed 9153393. Source: MGI

synaptic vesicle targeting

Inferred from mutant phenotype PubMed 12805290. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 17698590. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Z disc

Inferred from Biological aspect of Ancestor. Source: RefGenome

apical plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

axon

Inferred from direct assay PubMed 11740561. Source: MGI

cell cortex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell surface

Inferred from Biological aspect of Ancestor. Source: RefGenome

centrosome

Inferred from electronic annotation. Source: Ensembl

ciliary rootlet

Inferred from direct assay PubMed 16018997. Source: MGI

cytoplasmic vesicle

Inferred from direct assay PubMed 11740561. Source: MGI

dendrite

Inferred from direct assay PubMed 8922407. Source: MGI

dendritic shaft

Inferred from direct assay PubMed 12805290. Source: MGI

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

gamma-secretase complex

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from direct assay PubMed 12805290. Source: MGI

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Inferred from direct assay PubMed 10421573. Source: MGI

kinetochore

Inferred from electronic annotation. Source: Ensembl

lysosomal membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay Ref.5PubMed 12684521PubMed 15474363PubMed 15634781PubMed 15886206. Source: MGI

membrane raft

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane-bounded organelle

Inferred from direct assay PubMed 12805290. Source: MGI

mitochondrial inner membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuromuscular junction

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuronal cell body

Inferred from direct assay PubMed 12805290PubMed 8922407. Source: MGI

nuclear outer membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 12794186. Source: MGI

perinuclear region of cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from direct assay PubMed 17097608. Source: MGI

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

smooth endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

cadherin binding

Inferred from physical interaction PubMed 11953314. Source: MGI

calcium channel activity

Inferred from electronic annotation. Source: Ensembl

endopeptidase activity

Inferred from mutant phenotype PubMed 10206645PubMed 11262239PubMed 11953314PubMed 12391611PubMed 12684521PubMed 15452145PubMed 17097608PubMed 17556541PubMed 17913918. Source: MGI

protein binding

Inferred from physical interaction PubMed 16511561PubMed 20541250PubMed 22771797PubMed 23585889PubMed 22036569. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49769-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P49769-2)

The sequence of this isoform differs from the canonical sequence as follows:
     257-261: DLVAV → GKAQD
     262-467: Missing.
Note: Due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Presenilin-1 NTF subunit By similarity
PRO_0000025597
Chain299 – 467169Presenilin-1 CTF subunit By similarity
PRO_0000025598
Chain346 – 467122Presenilin-1 CTF12 By similarity
PRO_0000236058

Regions

Topological domain1 – 8282Cytoplasmic Potential
Transmembrane83 – 10321Helical; Potential
Topological domain104 – 13229Lumenal Potential
Transmembrane133 – 15321Helical; Potential
Topological domain154 – 1607Cytoplasmic Potential
Transmembrane161 – 18121Helical; Potential
Topological domain182 – 19413Lumenal Potential
Transmembrane195 – 21521Helical; Potential
Topological domain216 – 2205Cytoplasmic Potential
Transmembrane221 – 24121Helical; Potential
Topological domain242 – 2432Lumenal Potential
Transmembrane244 – 26421Helical; Potential
Topological domain265 – 380116Cytoplasmic Potential
Transmembrane381 – 40121Helical; Potential
Topological domain402 – 4076Lumenal Potential
Transmembrane408 – 42821Helical; Potential
Topological domain429 – 4324Cytoplasmic Potential
Intramembrane433 – 45321Helical; Potential
Topological domain454 – 46714Cytoplasmic Potential
Region322 – 450129Required for interaction with CTNNB1 By similarity
Region372 – 39928Required for interaction with CTNND2 By similarity
Region464 – 4674Interaction with MTCH1 By similarity
Motif433 – 4353PAL

Sites

Active site2571 By similarity
Active site3851 By similarity
Site291 – 2922Cleavage; alternate By similarity
Site292 – 2932Cleavage; alternate By similarity
Site298 – 2992Cleavage By similarity
Site345 – 3462Cleavage; by caspase By similarity

Amino acid modifications

Modified residue3291Phosphoserine Ref.8
Modified residue3461Phosphoserine; by PKC By similarity
Modified residue3671Phosphoserine Ref.7
Modified residue3701Phosphothreonine Ref.7
Modified residue3711Phosphoserine Ref.7

Natural variations

Alternative sequence257 – 2615DLVAV → GKAQD in isoform 2.
VSP_008381
Alternative sequence262 – 467206Missing in isoform 2.
VSP_008382
Natural variant91S → T in strain: SAM P8.
Natural variant401D → E in strain: SAM P8.
Natural variant671E → CM in strain: SAM P8.
Natural variant1961V → L in strain: SAM P8.
Natural variant321 – 3222ER → RRD in strain: SAM P8.

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D07215B4BAD2D549

FASTA46752,640
        10         20         30         40         50         60 
MTEIPAPLSY FQNAQMSEDS HSSSAIRSQN DSQERQQQHD RQRLDNPEPI SNGRPQSNSR 

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

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

       190        200        210        220        230        240 
YLGEVFKTYN VAVDYVTVAL LIWNFGVVGM IAIHWKGPLR LQQAYLIMIS ALMALVFIKY 

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

       310        320        330        340        350        360 
GDPEAQRRVP KNPKYNTQRA ERETQDSGSG NDDGGFSEEW EAQRDSHLGP HRSTPESRAA 

       370        380        390        400        410        420 
VQELSGSILT SEDPEERGVK LGLGDFIFYS VLVGKASATA SGDWNTTIAC FVAILIGLCL 

       430        440        450        460 
TLLLLAIFKK ALPALPISIT FGLVFYFATD YLVQPFMDQL AFHQFYI 

« Hide

Isoform 2 [UniParc].

Checksum: 16FB53FBE20EA4EB
Show »

FASTA26129,849

References

« Hide 'large scale' references
[1]"Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease."
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. expand/collapse author list , 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.
Nature 375:754-760(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Transcriptional regulation of the mouse presenilin-1 gene."
Mitsuda N., Roses A.D., Vitek M.P.
J. Biol. Chem. 272:23489-23497(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Strain: 129/SvJ.
[3]"Molecular cloning and tissue distribution of presenilin-1 in senenscence accelerated mice (SAM P8) mice."
Kumar V.B., Vyas K.C., Choudhary V., Franko M., Flood J.F., Morley J.E.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: SAM P8.
Tissue: Hippocampus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: FVB/N.
Tissue: Eye, Liver, Mammary gland and Retina.
[5]"Isolation and characterization of novel presenilin binding protein."
Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q., Dargusch R., Schubert D., Kimura H.
J. Neurochem. 75:109-116(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOCK3.
Tissue: Brain.
[6]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-370 AND SER-371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42177 mRNA. Translation: AAC42094.1.
AF007560 Genomic DNA. Translation: AAB72049.1.
AF149111 mRNA. Translation: AAF73153.1.
BC014744 mRNA. Translation: AAH14744.1.
BC030409 mRNA. Translation: AAH30409.1.
BC071233 mRNA. Translation: AAH71233.1.
CCDSCCDS26030.1. [P49769-1]
PIRI78388.
RefSeqNP_032969.1. NM_008943.2. [P49769-1]
XP_006515668.1. XM_006515605.1. [P49769-1]
UniGeneMm.998.

3D structure databases

ProteinModelPortalP49769.
SMRP49769. Positions 292-467.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202414. 17 interactions.
DIPDIP-36237N.
IntActP49769. 14 interactions.
MINTMINT-193580.

Chemistry

BindingDBP49769.

Protein family/group databases

MEROPSA22.001.

PTM databases

PhosphoSiteP49769.

Proteomic databases

MaxQBP49769.
PaxDbP49769.
PRIDEP49769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041806; ENSMUSP00000048363; ENSMUSG00000019969. [P49769-1]
ENSMUST00000101225; ENSMUSP00000098786; ENSMUSG00000019969. [P49769-1]
GeneID19164.
KEGGmmu:19164.
UCSCuc007odo.1. mouse. [P49769-2]
uc007odp.1. mouse. [P49769-1]

Organism-specific databases

CTD5663.
MGIMGI:1202717. Psen1.

Phylogenomic databases

eggNOGNOG237920.
HOGENOMHOG000240228.
HOVERGENHBG011375.
InParanoidP49769.
KOK04505.
OMAEAQRKVS.
OrthoDBEOG7NGQBG.
PhylomeDBP49769.
TreeFamTF315040.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.

Gene expression databases

ArrayExpressP49769.
BgeeP49769.
CleanExMM_PSEN1.
GenevestigatorP49769.

Family and domain databases

InterProIPR002031. Pept_A22A_PS1.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF7. PTHR10202:SF7. 1 hit.
PfamPF01080. Presenilin. 1 hit.
[Graphical view]
PRINTSPR01072. PRESENILIN.
PR01073. PRESENILIN1.
SMARTSM00730. PSN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295822.
PROP49769.
SOURCESearch...

Entry information

Entry namePSN1_MOUSE
AccessionPrimary (citable) accession number: P49769
Secondary accession number(s): Q91WK6, Q9JLP9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot