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Protein

Presenilin-1

Gene

Psen1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 presence of the other members of the gamma-secretase complex for protease activity (By similarity). Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (PubMed:10421573, PubMed:11517342). Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin) (PubMed:11226248). Under conditions of apoptosis or calcium influx, cleaves CDH1 (PubMed:11953314). This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling (PubMed:11226248). Required for normal embryonic brain and skeleton development, and for normal angiogenesis (PubMed:9160754, PubMed:10421573, PubMed:12834865).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei257By similarity1
Active sitei385By similarity1

GO - Molecular functioni

GO - Biological processi

  • activation of MAPKK activity Source: MGI
  • amyloid precursor protein catabolic process Source: MGI
  • amyloid precursor protein metabolic process Source: UniProtKB
  • autophagosome assembly Source: MGI
  • autophagy Source: MGI
  • beta-amyloid formation Source: UniProtKB
  • beta-amyloid metabolic process Source: MGI
  • blood vessel development Source: MGI
  • brain development Source: MGI
  • brain morphogenesis Source: MGI
  • Cajal-Retzius cell differentiation Source: MGI
  • calcium ion transport Source: GO_Central
  • canonical Wnt signaling pathway Source: GO_Central
  • cell fate specification Source: MGI
  • cellular calcium ion homeostasis Source: MGI
  • cellular protein metabolic process Source: MGI
  • cellular response to DNA damage stimulus Source: MGI
  • cerebral cortex cell migration Source: MGI
  • cerebral cortex development Source: MGI
  • choline transport Source: MGI
  • dorsal/ventral neural tube patterning Source: MGI
  • embryonic limb morphogenesis Source: MGI
  • endoplasmic reticulum calcium ion homeostasis Source: MGI
  • epithelial cell proliferation Source: MGI
  • forebrain development Source: MGI
  • heart development Source: MGI
  • heart looping Source: MGI
  • hematopoietic progenitor cell differentiation Source: MGI
  • intracellular signal transduction Source: InterPro
  • learning or memory Source: MGI
  • L-glutamate transport Source: MGI
  • locomotion Source: MGI
  • membrane protein ectodomain proteolysis Source: UniProtKB
  • memory Source: MGI
  • mitochondrial transport Source: MGI
  • myeloid dendritic cell differentiation Source: MGI
  • myeloid leukocyte differentiation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of apoptotic signaling pathway Source: MGI
  • negative regulation of axonogenesis Source: MGI
  • negative regulation of epidermal growth factor-activated receptor activity Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of protein kinase activity Source: MGI
  • negative regulation of protein phosphorylation Source: MGI
  • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  • neural retina development Source: Ensembl
  • neurogenesis Source: MGI
  • neuron apoptotic process Source: MGI
  • neuron development Source: MGI
  • neuron differentiation Source: MGI
  • neuron migration Source: MGI
  • Notch receptor processing Source: MGI
  • Notch signaling pathway Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of catalytic activity Source: UniProtKB
  • positive regulation of coagulation Source: MGI
  • positive regulation of dendritic spine development Source: MGI
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • positive regulation of protein kinase activity Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of receptor recycling Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: MGI
  • post-embryonic development Source: MGI
  • protein glycosylation Source: MGI
  • protein maturation Source: MGI
  • protein processing Source: UniProtKB
  • protein transport Source: MGI
  • regulation of canonical Wnt signaling pathway Source: UniProtKB
  • regulation of epidermal growth factor-activated receptor activity Source: MGI
  • regulation of phosphorylation Source: MGI
  • regulation of protein binding Source: MGI
  • regulation of resting membrane potential Source: MGI
  • regulation of synaptic plasticity Source: MGI
  • regulation of synaptic transmission, glutamatergic Source: MGI
  • response to oxidative stress Source: MGI
  • segmentation Source: MGI
  • single organismal cell-cell adhesion Source: MGI
  • skeletal system morphogenesis Source: MGI
  • skin morphogenesis Source: BHF-UCL
  • smooth endoplasmic reticulum calcium ion homeostasis Source: MGI
  • somitogenesis Source: MGI
  • synaptic vesicle targeting Source: MGI
  • T cell activation involved in immune response Source: MGI
  • T cell receptor signaling pathway Source: MGI
  • thymus development Source: MGI

Keywordsi

Molecular functionHydrolase, Protease
Biological processApoptosis, Cell adhesion, Notch signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-MMU-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiA22.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Presenilin-1 (EC:3.4.23.-)
Short name:
PS-1
Alternative name(s):
Protein S182
Cleaved into the following 3 chains:
Gene namesi
Name:Psen1
Synonyms:Ad3h, Psnl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1202717. Psen1.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Golgi apparatus membrane By similarity; Multi-pass membrane protein By similarity
  • Cytoplasmic granule By similarity
  • Cell membrane 2 Publications
  • Cytoplasmic vesicle 1 Publication1 Publication

  • Note: Translocates with bound NOTCH1 from the endoplasmic reticulum and/or Golgi to 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. Colocalizes with UBQLN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 82CytoplasmicBy similarityAdd BLAST82
Transmembranei83 – 103HelicalBy similarityAdd BLAST21
Topological domaini104 – 132LumenalBy similarityAdd BLAST29
Transmembranei133 – 153HelicalBy similarityAdd BLAST21
Topological domaini154 – 166CytoplasmicBy similarityAdd BLAST13
Transmembranei167 – 189HelicalBy similarityAdd BLAST23
Topological domaini190 – 194LumenalBy similarity5
Transmembranei195 – 216HelicalBy similarityAdd BLAST22
Topological domaini217 – 220CytoplasmicBy similarity4
Transmembranei221 – 241HelicalBy similarityAdd BLAST21
Topological domaini242 – 248LumenalBy similarity7
Transmembranei249 – 272HelicalBy similarityAdd BLAST24
Topological domaini273 – 380CytoplasmicBy similarityAdd BLAST108
Transmembranei381 – 401HelicalBy similarityAdd BLAST21
Topological domaini402 – 407LumenalBy similarity6
Transmembranei408 – 428HelicalBy similarityAdd BLAST21
Topological domaini429 – 432CytoplasmicBy similarity4
Transmembranei433 – 453HelicalBy similarityAdd BLAST21
Topological domaini454 – 467LumenalBy similarityAdd BLAST14

GO - Cellular componenti

  • aggresome Source: UniProtKB
  • axon Source: MGI
  • cell cortex Source: UniProtKB
  • cell junction Source: MGI
  • cell surface Source: Ensembl
  • centrosome Source: MGI
  • ciliary rootlet Source: MGI
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: MGI
  • dendrite Source: MGI
  • dendritic shaft Source: MGI
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • gamma-secretase complex Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • growth cone Source: MGI
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • intracellular Source: MGI
  • kinetochore Source: MGI
  • lysosomal membrane Source: Ensembl
  • membrane Source: MGI
  • membrane-bounded organelle Source: MGI
  • membrane raft Source: MGI
  • mitochondrial inner membrane Source: Ensembl
  • mitochondrion Source: UniProtKB
  • neuromuscular junction Source: Ensembl
  • neuronal cell body Source: MGI
  • nuclear membrane Source: MGI
  • nuclear outer membrane Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: GO_Central
  • plasma membrane Source: UniProtKB
  • presynapse Source: GOC
  • rough endoplasmic reticulum Source: MGI
  • smooth endoplasmic reticulum Source: MGI
  • Z disc Source: GO_Central

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Perinatal lethality; all of the homozygous mutants die within 30 minutes after birth (PubMed:9160754). Heterozygotes have no visible phenotype (PubMed:9160754). Mutant mice display important skeletal malformations (PubMed:9160754, PubMed:10421573). After 12.5 dpc, they exhibit important defects in embryonic brain development, with a decrease in the number of neural progenitor cells in specific brain regions (PubMed:9160754, PubMed:10421573). The cell density in the marginal zone is normal at 13 dpc, but then becomes much reduced, including a strong reduction in the number of Cajal-Retzius cells (PubMed:10421573). At the same time, Notch1 expression is reduced in the developing brain cortex (PubMed:10421573). At 17.5 dpc, all layers of the ventricular zone in the ventrolateral region at the posterior portion of the lateral ventricles have disappeared, giving rise to symmetric cavitation in the posterior part of the brain (PubMed:9160754). They also display cranial hemorrhages that are first observed at 12.5 dpc (PubMed:9160754, PubMed:10421573, PubMed:12834865). This is due to defects in angiogenesis, with increased blood vessel diameter and abnormal morphology and increased proliferation of capillary endothelial cells that lead to stenosis of the capillary lumen (PubMed:12834865). Psen1-deficient mice can be rescued by neuronal expression of human PSEN1; these mice lack any detectable PSEN1 in their skin and display increased levels of cytosolic and nuclear CTNNB1 in skin, which leads to aberrant Wnt signaling (PubMed:11517342). Mutant mice display epidermal hyperplasia and hyperkeratosis that gives rise to skin tumors (PubMed:11517342).4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000255971 – 298Presenilin-1 NTF subunitBy similarityAdd BLAST298
ChainiPRO_0000025598299 – 467Presenilin-1 CTF subunitBy similarityAdd BLAST169
ChainiPRO_0000236058346 – 467Presenilin-1 CTF12By similarityAdd BLAST122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei51PhosphoserineBy similarity1
Modified residuei329PhosphoserineCombined sources1
Modified residuei346Phosphoserine; by PKCBy similarity1
Modified residuei367PhosphoserineCombined sources1
Modified residuei370PhosphothreonineCombined sources1
Modified residuei371PhosphoserineCombined sources1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei291 – 292Cleavage; alternateBy similarity2
Sitei292 – 293Cleavage; alternateBy similarity2
Sitei298 – 299CleavageBy similarity2
Sitei345 – 346Cleavage; by caspaseBy similarity2

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP49769.
PaxDbiP49769.
PeptideAtlasiP49769.
PRIDEiP49769.

PTM databases

iPTMnetiP49769.
PhosphoSitePlusiP49769.
SwissPalmiP49769.

Expressioni

Tissue specificityi

Detected in embryonic brain (PubMed:10421573). Detected in adult skin epidermis (at protein level) (PubMed:11517342).2 Publications

Gene expression databases

BgeeiENSMUSG00000019969.
CleanExiMM_PSEN1.
ExpressionAtlasiP49769. baseline and differential.
GenevisibleiP49769. MM.

Interactioni

Subunit structurei

Homodimer. The functional gamma-secretase complex is composed of at least four polypeptides: 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 (PubMed:11226248). 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, CTNND1, JUP, HERPUD1, FLNA, FLNB, MTCH1, PKP4 and PARL. Interacts through its N-terminus with isoform 3 of GFAP (By similarity). Interacts with DOCK3 (PubMed:10854253). Interacts with isoform 1 and isoform 3 of UBQLN1 (By similarity).By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • beta-catenin binding Source: MGI
  • cadherin binding Source: MGI
  • PDZ domain binding Source: MGI

Protein-protein interaction databases

BioGridi202414. 23 interactors.
DIPiDIP-36237N.
IntActiP49769. 17 interactors.
MINTiMINT-193580.
STRINGi10090.ENSMUSP00000048363.

Structurei

3D structure databases

ProteinModelPortaliP49769.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni322 – 450Required for interaction with CTNNB1By similarityAdd BLAST129
Regioni372 – 399Required for interaction with CTNND2By similarityAdd BLAST28
Regioni464 – 467Interaction with MTCH1By similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi433 – 435PAL3

Domaini

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

Sequence similaritiesi

Belongs to the peptidase A22A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
HOGENOMiHOG000240228.
HOVERGENiHBG011375.
InParanoidiP49769.
KOiK04505.
OMAiNTNDNRE.
OrthoDBiEOG091G0C72.
PhylomeDBiP49769.
TreeFamiTF315040.

Family and domain databases

InterProiView protein in InterPro
IPR002031. Pept_A22A_PS1.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
PANTHERiPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF27. PTHR10202:SF27. 1 hit.
PfamiView protein in Pfam
PF01080. Presenilin. 1 hit.
PRINTSiPR01072. PRESENILIN.
PR01073. PRESENILIN1.
SMARTiView protein in SMART
SM00730. PSN. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49769-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTEIPAPLSY FQNAQMSEDS HSSSAIRSQN DSQERQQQHD RQRLDNPEPI
60 70 80 90 100
SNGRPQSNSR QVVEQDEEED EELTLKYGAK HVIMLFVPVT LCMVVVVATI
110 120 130 140 150
KSVSFYTRKD GQLIYTPFTE DTETVGQRAL HSILNAAIMI SVIVIMTILL
160 170 180 190 200
VVLYKYRCYK VIHAWLIISS LLLLFFFSFI YLGEVFKTYN VAVDYVTVAL
210 220 230 240 250
LIWNFGVVGM IAIHWKGPLR LQQAYLIMIS ALMALVFIKY LPEWTAWLIL
260 270 280 290 300
AVISVYDLVA VLCPKGPLRM LVETAQERNE TLFPALIYSS TMVWLVNMAE
310 320 330 340 350
GDPEAQRRVP KNPKYNTQRA ERETQDSGSG NDDGGFSEEW EAQRDSHLGP
360 370 380 390 400
HRSTPESRAA VQELSGSILT SEDPEERGVK LGLGDFIFYS VLVGKASATA
410 420 430 440 450
SGDWNTTIAC FVAILIGLCL TLLLLAIFKK ALPALPISIT FGLVFYFATD
460
YLVQPFMDQL AFHQFYI
Length:467
Mass (Da):52,640
Last modified:October 1, 1996 - v1
Checksum:iD07215B4BAD2D549
GO
Isoform 2 (identifier: P49769-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:261
Mass (Da):29,849
Checksum:i16FB53FBE20EA4EB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti9S → T in strain: SAM P8. 1
Natural varianti40D → E in strain: SAM P8. 1
Natural varianti67E → CM in strain: SAM P8. 1
Natural varianti196V → L in strain: SAM P8. 1
Natural varianti321 – 322ER → RRD in strain: SAM P8. 2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008381257 – 261DLVAV → GKAQD in isoform 2. 1 Publication5
Alternative sequenceiVSP_008382262 – 467Missing in isoform 2. 1 PublicationAdd BLAST206

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26030.1. [P49769-1]
PIRiI78388.
RefSeqiNP_032969.1. NM_008943.2. [P49769-1]
XP_006515668.1. XM_006515605.3. [P49769-1]
UniGeneiMm.998.

Genome annotation databases

EnsembliENSMUST00000041806; ENSMUSP00000048363; ENSMUSG00000019969. [P49769-1]
ENSMUST00000101225; ENSMUSP00000098786; ENSMUSG00000019969. [P49769-1]
GeneIDi19164.
KEGGimmu:19164.
UCSCiuc007odo.1. mouse. [P49769-2]
uc007odp.1. mouse. [P49769-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26030.1. [P49769-1]
PIRiI78388.
RefSeqiNP_032969.1. NM_008943.2. [P49769-1]
XP_006515668.1. XM_006515605.3. [P49769-1]
UniGeneiMm.998.

3D structure databases

ProteinModelPortaliP49769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202414. 23 interactors.
DIPiDIP-36237N.
IntActiP49769. 17 interactors.
MINTiMINT-193580.
STRINGi10090.ENSMUSP00000048363.

Protein family/group databases

MEROPSiA22.001.

PTM databases

iPTMnetiP49769.
PhosphoSitePlusiP49769.
SwissPalmiP49769.

Proteomic databases

EPDiP49769.
PaxDbiP49769.
PeptideAtlasiP49769.
PRIDEiP49769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041806; ENSMUSP00000048363; ENSMUSG00000019969. [P49769-1]
ENSMUST00000101225; ENSMUSP00000098786; ENSMUSG00000019969. [P49769-1]
GeneIDi19164.
KEGGimmu:19164.
UCSCiuc007odo.1. mouse. [P49769-2]
uc007odp.1. mouse. [P49769-1]

Organism-specific databases

CTDi5663.
MGIiMGI:1202717. Psen1.

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
HOGENOMiHOG000240228.
HOVERGENiHBG011375.
InParanoidiP49769.
KOiK04505.
OMAiNTNDNRE.
OrthoDBiEOG091G0C72.
PhylomeDBiP49769.
TreeFamiTF315040.

Enzyme and pathway databases

ReactomeiR-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiPR:P49769.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019969.
CleanExiMM_PSEN1.
ExpressionAtlasiP49769. baseline and differential.
GenevisibleiP49769. MM.

Family and domain databases

InterProiView protein in InterPro
IPR002031. Pept_A22A_PS1.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
PANTHERiPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF27. PTHR10202:SF27. 1 hit.
PfamiView protein in Pfam
PF01080. Presenilin. 1 hit.
PRINTSiPR01072. PRESENILIN.
PR01073. PRESENILIN1.
SMARTiView protein in SMART
SM00730. PSN. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPSN1_MOUSE
AccessioniPrimary (citable) accession number: P49769
Secondary accession number(s): Q91WK6, Q9JLP9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 15, 2017
This is version 175 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.