PSN1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSN1_RAT
• UniProt AC: P97887
• Protein Name: Presenilin-1
• Gene Name: Psen1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 468
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Golgi apparatus membrane ; Multi-pass membrane protein . Cytoplasmic granule . Cell membrane . Translocates with bound NOTCH1 from the endoplasmic reticulum and/or Golgi to the cell surfa
• 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. 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. 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). Under conditions of apoptosis or calcium influx, cleaves CDH1. 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 (By similarity). Required for normal embryonic brain and skeleton development, and for normal angiogenesis (By similarity)..
• Protein Sequence: MTEIPAPLSYFQNAQMSEDSHSSSVRSQNDNQERQQHHDRQRLDNPESISNGRPQSNFTRQVIEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIVSSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMIAIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVPKNPKYSTQGTEREETQDTGTGSDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSGSILTSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLIFYFATDYLVQPFMDQLAFHQFYI

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
9	Phosphorylation	TEIPAPLSYFQNAQM CCCCCCCHHHCCCCC	23.89	25575281
10	Phosphorylation	EIPAPLSYFQNAQMS CCCCCCHHHCCCCCC	19.50	25575281
17	Phosphorylation	YFQNAQMSEDSHSSS HHCCCCCCCCCCCHH	26.60	25575281
20	Phosphorylation	NAQMSEDSHSSSVRS CCCCCCCCCCHHCCC	22.63	25575281
22	Phosphorylation	QMSEDSHSSSVRSQN CCCCCCCCHHCCCCC	28.41	25575281
23	Phosphorylation	MSEDSHSSSVRSQND CCCCCCCHHCCCCCC	27.68	25575281
24	Phosphorylation	SEDSHSSSVRSQNDN CCCCCCHHCCCCCCH	25.27	25575281
48	Phosphorylation	QRLDNPESISNGRPQ HHCCCHHHHCCCCCC	32.35	27097102
50	Phosphorylation	LDNPESISNGRPQSN CCCHHHHCCCCCCCC	42.38	29779826
56	Phosphorylation	ISNGRPQSNFTRQVI HCCCCCCCCCCHHHH	36.27	25575281
59	Phosphorylation	GRPQSNFTRQVIEQD CCCCCCCCHHHHHCC	25.17	25575281
315	Phosphorylation	RVPKNPKYSTQGTER CCCCCCCCCCCCCCC	20.43	23984901
316	Phosphorylation	VPKNPKYSTQGTERE CCCCCCCCCCCCCCE	22.00	23984901
317	Phosphorylation	PKNPKYSTQGTEREE CCCCCCCCCCCCCEE	28.11	23984901
320	Phosphorylation	PKYSTQGTEREETQD CCCCCCCCCCEECCC	23.27	23984901
325	Phosphorylation	QGTEREETQDTGTGS CCCCCEECCCCCCCC	27.30	28551015
328	Phosphorylation	EREETQDTGTGSDDG CCEECCCCCCCCCCC	27.16	27097102
330	Phosphorylation	EETQDTGTGSDDGGF EECCCCCCCCCCCCC	35.29	27097102
332	Phosphorylation	TQDTGTGSDDGGFSE CCCCCCCCCCCCCCH	32.16	27097102
338	Phosphorylation	GSDDGGFSEEWEAQR CCCCCCCCHHHHHHC	37.57	23984901
347	Phosphorylation	EWEAQRDSHLGPHRS HHHHHCCCCCCCCCC	23.85	23984901
354	Phosphorylation	SHLGPHRSTPESRAA CCCCCCCCCHHHHHH	45.33	25575281
355	Phosphorylation	HLGPHRSTPESRAAV CCCCCCCCHHHHHHH	30.91	25575281
358	Phosphorylation	PHRSTPESRAAVQEL CCCCCHHHHHHHHHH	28.55	25575281
366	Phosphorylation	RAAVQELSGSILTSE HHHHHHHCCCCCCCC	29.73	27097102
368	Phosphorylation	AVQELSGSILTSEDP HHHHHCCCCCCCCCH	15.85	23712012
371	Phosphorylation	ELSGSILTSEDPEER HHCCCCCCCCCHHHH	28.53	23712012
372	Phosphorylation	LSGSILTSEDPEERG HCCCCCCCCCHHHHC	36.24	27097102

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
347	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
347	S	Phosphorylation	Phosphorylation on Ser-347 inhibits endoproteolysis.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PSN1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERLN2_RAT	Erlin2	physical	22771797

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.