PSN2_HUMAN - dbPTM
PSN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSN2_HUMAN
UniProt AC P49810
Protein Name Presenilin-2
Gene Name PSEN2
Organism Homo sapiens (Human).
Sequence Length 448
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein .
Protein Description 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 (amyloid-beta 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. May function in the cytoplasmic partitioning of proteins..
Protein Sequence MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGPEDGENTAQWRSQENEEDGEEDPDRYVCSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEVFEPPLTGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGSGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI
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
3Phosphorylation-----MLTFMASDSE
-----CCEEECCCCH
15.2929759185
7Phosphorylation-MLTFMASDSEEEVC
-CCEEECCCCHHHHH
29.868972483
9PhosphorylationLTFMASDSEEEVCDE
CEEECCCCHHHHHHH
44.408972483
18PhosphorylationEEVCDERTSLMSAES
HHHHHHHHCCCCCCC
24.9429255136
19PhosphorylationEVCDERTSLMSAESP
HHHHHHHCCCCCCCC
28.4429255136
22PhosphorylationDERTSLMSAESPTPR
HHHHCCCCCCCCCCC
33.8930266825
25PhosphorylationTSLMSAESPTPRSCQ
HCCCCCCCCCCCCCC
33.5229255136
27PhosphorylationLMSAESPTPRSCQEG
CCCCCCCCCCCCCCC
40.3830266825
30PhosphorylationAESPTPRSCQEGRQG
CCCCCCCCCCCCCCC
22.73-
49PhosphorylationENTAQWRSQENEEDG
CCCHHHHCCCCCCCC
38.6025850435
63PhosphorylationGEEDPDRYVCSGVPG
CCCCCCCEEECCCCC
17.1229978859
66PhosphorylationDPDRYVCSGVPGRPP
CCCCEEECCCCCCCC
32.5529978859
82UbiquitinationLEEELTLKYGAKHVI
CHHHHHHHHCCCHHH
36.0821963094
86UbiquitinationLTLKYGAKHVIMLFV
HHHHHCCCHHHHHHH
33.7622817900
115UbiquitinationSVRFYTEKNGQLIYT
HHEEEECCCCEEEEE
59.592190698
115 (in isoform 1)Ubiquitination-59.5921906983
115 (in isoform 2)Ubiquitination-59.5921906983
147PhosphorylationLNTLIMISVIVVMTI
HHHHHHHHHHHHHHH
6.6026434776
153PhosphorylationISVIVVMTIFLVVLY
HHHHHHHHHHHHHHH
9.2926434776
160PhosphorylationTIFLVVLYKYRCYKF
HHHHHHHHHHHHHHH
8.3826434776
162PhosphorylationFLVVLYKYRCYKFIH
HHHHHHHHHHHHHHH
7.7426434776
165PhosphorylationVLYKYRCYKFIHGWL
HHHHHHHHHHHHHHH
10.4326434776
294PhosphorylationPIFPALIYSSAMVWT
CCHHHHHHHHHCHHE
9.45-
306AcetylationVWTVGMAKLDPSSQG
HHEECCCCCCCCCCC
44.5230591601
327PhosphorylationDPEMEEDSYDSFGEP
CCCCCCCCCCCCCCC
33.839558331
329 (in isoform 3)Phosphorylation-41.259558331
330PhosphorylationMEEDSYDSFGEPSYP
CCCCCCCCCCCCCCC
27.249558331
335PhosphorylationYDSFGEPSYPEVFEP
CCCCCCCCCCCCCCC
49.369558331

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
7SPhosphorylationKinaseCSNK2A1P68400
GPS
7SPhosphorylationKinaseCK2_GROUP-PhosphoELM
7SPhosphorylationKinaseCK1_GROUP-PhosphoELM
7SPhosphorylationKinaseCK2-FAMILY-GPS
7SPhosphorylationKinaseCK1-FAMILY-GPS
9SPhosphorylationKinaseCK2-FAMILY-GPS
9SPhosphorylationKinaseCK2_GROUP-PhosphoELM
9SPhosphorylationKinaseCK1_GROUP-PhosphoELM
9SPhosphorylationKinaseCK1-FAMILY-GPS
9SPhosphorylationKinaseCSNK2A1P68400
GPS
19SPhosphorylationKinaseCK1-FAMILY-GPS
19SPhosphorylationKinaseAURKAO14965
GPS
19SPhosphorylationKinaseCK2-FAMILY-GPS
19SPhosphorylationKinaseCK1_GROUP-PhosphoELM
19SPhosphorylationKinaseCK2_GROUP-PhosphoELM
327SPhosphorylationKinaseCSNK1DP48730
GPS
330SPhosphorylationKinaseCSNK1DP48730
GPS
330SPhosphorylationKinaseCSNK2A1P68400
GPS
335SPhosphorylationKinaseCK2-FAMILY-GPS
335SPhosphorylationKinaseCSNK2A1P68400
GPS
335SPhosphorylationKinaseCK2_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSN2_HUMAN !!

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 PSN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAN1_HUMANCAPN1physical
9852298
CSEN_HUMANKCNIP3physical
9771752
GFAP_HUMANGFAPphysical
12058025
APBA1_HUMANAPBA1physical
12196555
APBA2_HUMANAPBA2physical
12196555
APBA3_HUMANAPBA3physical
12196555
FLNB_HUMANFLNBphysical
9437013
ICAM5_HUMANICAM5physical
11719200
CSEN_HUMANKCNIP3physical
11278424
SORCN_HUMANSRIphysical
10748169
B2CL1_HUMANBCL2L1physical
10446169
FHL2_HUMANFHL2physical
11001931
KCIP4_HUMANKCNIP4physical
11847232
CIB1_HUMANCIB1physical
10366599
UBQL1_HUMANUBQLN1physical
17614368
RHEB_HUMANRHEBphysical
21163940
PDCD4_HUMANPDCD4physical
21163940
FXL12_HUMANFBXL12physical
21163940
EXOC6_HUMANEXOC6physical
21163940
DNJB1_HUMANDNAJB1physical
21163940
LIPG_HUMANLIPFphysical
21163940
RNF32_HUMANRNF32physical
21163940
CEP55_HUMANCEP55physical
21163940
ELAV1_HUMANELAVL1physical
21163940
EVI5L_HUMANEVI5Lphysical
21163940
GCDH_HUMANGCDHphysical
21163940
IFIT3_HUMANIFIT3physical
21163940
IFIT5_HUMANIFIT5physical
21163940
OGA_HUMANMGEA5physical
21163940
SPC24_HUMANSPC24physical
21163940
DYHC1_HUMANDYNC1H1physical
21163940
EID1_HUMANEID1physical
21163940
AAMP_HUMANAAMPphysical
21163940
ACTG_HUMANACTG1physical
21163940
CHKA_HUMANCHKAphysical
21163940
ECD_HUMANECDphysical
21163940
HPS1_HUMANHPS1physical
21163940
NICA_HUMANNCSTNphysical
15474363
PEN2_HUMANPSENENphysical
15474363
APH1A_HUMANAPH1Aphysical
15474363
PSN1_HUMANPSEN1physical
15474363
PSN2_HUMANPSEN2physical
15474363
TRAF6_HUMANTRAF6physical
23707529
CLK1_HUMANCLK1physical
26496610
RN115_HUMANRNF115physical
28514442
NPL4_HUMANNPLOC4physical
28514442

Drug and Disease Associations
Kegg Disease
H00056 Alzheimer's disease (AD)
H00294 Dilated cardiomyopathy (DCM)
OMIM Disease
606889Alzheimer disease 4 (AD4)
613697Cardiomyopathy, dilated 1V (CMD1V)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSN2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-25, AND MASSSPECTROMETRY.

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