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Protein Page:
PSEN1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PSEN1 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. Regulates epithelial- cadherin function. Five alternative splice isoforms have been identified. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.23.-; Membrane protein, multi-pass; Protease; Mitochondrial; Membrane protein, integral; Cell surface
Chromosomal Location of Human Ortholog: 14q24.3
Cellular Component: axon; cell junction; cell soma; cell surface; centrosome; ciliary rootlet; cytoplasmic vesicle; dendritic shaft; endoplasmic reticulum; endoplasmic reticulum membrane; Golgi apparatus; Golgi membrane; growth cone; integral to membrane; integral to plasma membrane; kinetochore; lipid raft; lysosomal membrane; membrane; mitochondrial inner membrane; mitochondrion; neuromuscular junction; nuclear membrane; nuclear outer membrane; nucleus; plasma membrane; rough endoplasmic reticulum; smooth endoplasmic reticulum
Molecular Function: aspartic-type endopeptidase activity; beta-catenin binding; cadherin binding; calcium channel activity; endopeptidase activity; PDZ domain binding; protein binding
Biological Process: activation of MAPKK activity; amyloid precursor protein catabolic process; autophagic vacuole formation; beta-amyloid formation; blood vessel development; brain morphogenesis; Cajal-Retzius cell differentiation; cell fate specification; cell-cell adhesion; cerebral cortex cell migration; choline transport; dorsoventral neural tube patterning; embryonic limb morphogenesis; endoplasmic reticulum calcium ion homeostasis; epithelial cell proliferation; heart looping; hemopoietic progenitor cell differentiation; L-glutamate transport; membrane protein ectodomain proteolysis; memory; mitochondrial transport; myeloid dendritic cell differentiation; negative regulation of apoptosis; negative regulation of axonogenesis; negative regulation of epidermal growth factor receptor activity; negative regulation of neuron apoptosis; negative regulation of transcription from RNA polymerase II promoter; negative regulation of ubiquitin-protein ligase activity; neuron apoptosis; neuron development; neuron migration; Notch receptor processing; Notch signaling pathway; positive regulation of apoptosis; positive regulation of catalytic activity; positive regulation of coagulation; positive regulation of MAP kinase activity; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of receptor recycling; positive regulation of transcription, DNA-dependent; post-embryonic development; protein amino acid glycosylation; protein processing; protein transport; regulation of phosphorylation; regulation of protein binding; regulation of resting membrane potential; regulation of synaptic plasticity; regulation of synaptic transmission, glutamatergic; response to DNA damage stimulus; response to oxidative stress; skeletal morphogenesis; skin morphogenesis; smooth endoplasmic reticulum calcium ion homeostasis; somitogenesis; synaptic vesicle targeting; T cell activation during immune response; T cell receptor signaling pathway; thymus development; Wnt receptor signaling pathway through beta-catenin
Disease: Acne Inversa, Familial, 3; Alzheimer Disease 3; Cardiomyopathy, Dilated, 1u; Frontotemporal Dementia; Pick Disease Of Brain
Reference #:  P49768 (UniProtKB)
Alt. Names/Synonyms: AD3; FAD; presenilin 1; Presenilin-1; Presenilin-1 CTF subunit; Presenilin-1 CTF12; Presenilin-1 NTF subunit; Protein S182; PS-1; PS1; PS1-CTF12; PSEN1; PSN1; PSNL1; S182
Gene Symbols: PSEN1
Molecular weight: 52,668 Da
Basal Isoelectric point: 5.18  Predict pI for various phosphorylation states
CST Pathways:  Alzheimer's Disease  |  ErbB/HER Signaling  |  ESC Pluripotency and Differentiation  |  Notch Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PSEN1

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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Sites Implicated In
apoptosis, inhibited: S346‑p
cell growth, altered: S353‑p, S357‑p
enzymatic activity, induced: S319‑p, T320‑p, T354‑p
intracellular localization: S353‑p, S357‑p
molecular association, regulation: S353‑p, S357‑p
protein conformation: S353‑p, S357‑p
protein stabilization: S319‑p, T320‑p, T354‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 N32 TVRSQNDNRERQEHN
0 11 S43‑p QEHNDRRsLGHPEPL
0 4 S51‑p LGHPEPLsNGRPQGN
0 2 S59‑p NGRPQGNsRQVVEQD
0 1 S102‑p VVVATIKsVsFYTRk
0 1 S104‑p VATIKsVsFYTRkDG
0 2 K109‑ub sVsFYTRkDGQLIYT
0 1 Y154‑p TILLVVLyKYRCYKV
0 1 Y240‑p MALVFIKyLPEWTAW
0 1 Y256‑p ILAVISVyDLVAVLC
1 0 S310‑p PEAQRRVsKNSkYNA
0 1 K314‑ub RRVsKNSkYNAEstE
1 0 S319‑p NSkYNAEstEREsQD
1 0 T320‑p SkYNAEstEREsQDT
0 4 S324‑p AEstEREsQDTVAEN
0 1 T327 tEREsQDTVAENDDG
0 10 A329 REsQDTVAENDDGGF
0 2 N331 sQDTVAENDDGGFSE
1 0 S346‑p EWEAQRDsHLGPHRs
3 3 S353‑p sHLGPHRstPEsRAA
2 14 T354‑p HLGPHRstPEsRAAV
3 3 S357‑p PHRstPEsRAAVQEL
0 14 S365‑p RAAVQELsssILAGE
0 10 S366‑p AAVQELsssILAGED
0 38 S367‑p AVQELsssILAGEDP
0 24 A370 ELsssILAGEDPEER
0 16 G371 LsssILAGEDPEERG
0 1 - gap
  PSEN1 iso2  
N28 HLSNTNDNRERQEHN
S39 QEHNDRRSLGHPEPL
S47 LGHPEPLSNGRPQGN
S55 NGRPQGNSRQVVEQD
S98 VVVATIKSVSFYTRK
S100 VATIKSVSFYTRKDG
K105 SVSFYTRKDGQLIYT
Y150 TILLVVLYKYRCYKV
Y236 MALVFIKYLPEWTAW
Y252 ILAVISVYDLVAVLC
S306 PEAQRRVSKNSKYNA
K310 RRVSKNSKYNAESTE
S315 NSKYNAESTERESQD
T316 SKYNAESTERESQDT
S320 AESTERESQDTVAEN
T323 TERESQDTVAENDDG
A325 RESQDTVAENDDGGF
N327 SQDTVAENDDGGFSE
S342 EWEAQRDSHLGPHRS
S349 SHLGPHRSTPESRAA
T350 HLGPHRSTPESRAAV
S353 PHRSTPESRAAVQEL
S361 RAAVQELSSSILAGE
S362 AAVQELSSSILAGED
S363 AVQELSSSILAGEDP
A366 ELSSSILAGEDPEER
G367 LSSSILAGEDPEERG
- gap
  PSEN1 iso3  
N28 HLSNTNDNRERQEHN
S39 QEHNDRRSLGHPEPL
S47 LGHPEPLSNGRPQGN
S55 NGRPQGNSRQVVEQD
S98 VVVATIKSVSFYTRK
S100 VATIKSVSFYTRKDG
K105 SVSFYTRKDGQLIYT
Y150 TILLVVLYKYRCYKV
Y236 MALVFIKYLPEWTAW
Y252 ILAVISVYDLVAVLC
S306 PEAQRRVSKNSKYNA
K310 RRVSKNSKYNAERAC
R315 NSKYNAERACLPPAA
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S363‑p QRMMMAGsVRNGKPR
  mouse

 
S32‑p AIRSQNDsQERQQQH
R43 QQQHDRQRLDNPEPI
S51 LDNPEPISNGRPQSN
S59 NGRPQSNSRQVVEQD
S102 VVVATIKSVSFYTRK
S104 VATIKSVSFYTRKDG
K109 SVSFYTRKDGQLIYT
Y154 TILLVVLYKYRCYKV
Y240 MALVFIKYLPEWTAW
Y256 ILAVISVYDLVAVLC
P310 PEAQRRVPKNPKYNT
K314 RRVPKNPKYNTQRAE
R319 NPKYNTQRAEREtQD
A320 PKYNTQRAEREtQDs
T324‑p TQRAEREtQDsGsGN
S327‑p AEREtQDsGsGNDDG
S329‑p REtQDsGsGNDDGGF
N331 tQDsGsGNDDGGFSE
S346 EWEAQRDSHLGPHRS
S353 SHLGPHRStPESRAA
T354‑p HLGPHRStPESRAAV
S357 PHRStPESRAAVQEL
S365‑p RAAVQELsGsILtsE
G366 AAVQELsGsILtsED
S367‑p AVQELsGsILtsEDP
T370‑p ELsGsILtsEDPEER
S371‑p LsGsILtsEDPEERG
- gap
  rat

 
N31 SVRSQNDNQERQQHH
R42 QQHHDRQRLDNPESI
S50‑p LDNPESIsNGRPQSN
T59 GRPQSNFTRQVIEQD
S102 VVVATIKSVSFYTRK
S104 VATIKSVSFYTRKDG
K109 SVSFYTRKDGQLIYT
Y154 TILLVVLYKYRCYKV
Y240 MALVFIKYLPEWTAW
Y256 ILAVISVYDLVAVLC
P310 PEAQRRVPKNPKYST
K314 RRVPKNPKYSTQGTE
G319 NPKYSTQGTEREETQ
T320 PKYSTQGTEREETQD
T325 QGTEREETQDTGtGs
T328 EREETQDTGtGsDDG
T330‑p EETQDTGtGsDDGGF
S332‑p TQDTGtGsDDGGFSE
S347 EWEAQRDSHLGPHRS
S354 SHLGPHRSTPESRAA
T355 HLGPHRSTPESRAAV
S358 PHRSTPESRAAVQEL
S366 RAAVQELSGsILtsE
G367 AAVQELSGsILtsED
S368‑p AVQELSGsILtsEDP
T371‑p ELSGsILtsEDPEER
S372‑p LSGsILtsEDPEERG
- gap
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