PSN1_MOUSE - dbPTM
PSN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSN1_MOUSE
UniProt AC P49769
Protein Name Presenilin-1
Gene Name Psen1
Organism Mus musculus (Mouse).
Sequence Length 467
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Cytoplasmic granule . Cell membrane . Cytoplasmic vesicle . Translocates with bound NOTCH1 from the endoplasmic reticulum and/or G
Protein Description 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 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]
Protein Sequence MTEIPAPLSYFQNAQMSEDSHSSSAIRSQNDSQERQQQHDRQRLDNPEPISNGRPQSNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVIMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYVTVALLIWNFGVVGMIAIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVPKNPKYNTQRAERETQDSGSGNDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSGSILTSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
32PhosphorylationAIRSQNDSQERQQQH
HHHCCCCHHHHHHHH
41.3025266776
51PhosphorylationLDNPEPISNGRPQSN
CCCCCCCCCCCCCCC
43.9025367039
57PhosphorylationISNGRPQSNSRQVVE
CCCCCCCCCCCCCCC
39.1825266776
59PhosphorylationNGRPQSNSRQVVEQD
CCCCCCCCCCCCCCC
29.3625266776
324PhosphorylationTQRAERETQDSGSGN
HHHHHHHCCCCCCCC
43.8527087446
327PhosphorylationAERETQDSGSGNDDG
HHHHCCCCCCCCCCC
25.6625521595
329PhosphorylationRETQDSGSGNDDGGF
HHCCCCCCCCCCCCC
38.0725521595
337PhosphorylationGNDDGGFSEEWEAQR
CCCCCCCCHHHHHHC
37.5725619855
346PhosphorylationEWEAQRDSHLGPHRS
HHHHHCCCCCCCCCC
23.8529472430
353PhosphorylationSHLGPHRSTPESRAA
CCCCCCCCCHHHHHH
45.3325266776
354PhosphorylationHLGPHRSTPESRAAV
CCCCCCCCHHHHHHH
30.9125266776
357PhosphorylationPHRSTPESRAAVQEL
CCCCCHHHHHHHHHH
28.5529472430
365PhosphorylationRAAVQELSGSILTSE
HHHHHHHCCCCCCCC
29.7326824392
367PhosphorylationAVQELSGSILTSEDP
HHHHHCCCCCCCCCH
15.8527087446
370PhosphorylationELSGSILTSEDPEER
HHCCCCCCCCCHHHH
28.5327087446
371PhosphorylationLSGSILTSEDPEERG
HCCCCCCCCCHHHHC
36.2427087446

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
346SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
346SPhosphorylation

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Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PSN1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_MOUSECtnnb1physical
11104755
NICA_MOUSENcstnphysical
15474363
PSN1_MOUSEPsen1physical
15474363
PEN2_MOUSEPsenenphysical
15474363
APH1A_MOUSEAph1aphysical
15474363
CADH1_MOUSECdh1physical
11953314
NOTC1_MOUSENotch1physical
11518718
NOTC2_MOUSENotch2physical
11518718
NOTC3_MOUSENotch3physical
11518718
NOTC4_MOUSENotch4physical
11518718
GSK3B_MOUSEGsk3bphysical
12805290
DLL1_MOUSEDll1physical
12794186
P85A_MOUSEPik3r1physical
15192701
NMDZ1_MOUSEGrin1physical
15066262
NMDE1_MOUSEGrin2aphysical
15066262
NICA_MOUSENcstnphysical
11943765
ERLN2_MOUSEErlin2physical
22771797
VPP1_MOUSEAtp6v0a1physical
20541250
CADH2_MOUSECdh2physical
20696212
CTNB1_MOUSECtnnb1physical
20696212

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSN1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367; THR-370AND SER-371, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-370 ANDSER-371, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, AND MASSSPECTROMETRY.

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