PSN1_HUMAN - dbPTM
PSN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSN1_HUMAN
UniProt AC P49768
Protein Name Presenilin-1
Gene Name PSEN1
Organism Homo sapiens (Human).
Sequence Length 467
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). [PubMed: 15274632]
Protein Sequence MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI
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
39 (in isoform 3)Phosphorylation-43.6725849741
39 (in isoform 2)Phosphorylation-43.6725849741
43PhosphorylationQEHNDRRSLGHPEPL
HHHHCHHCCCCCCCC		39.3325159151
51PhosphorylationLGHPEPLSNGRPQGN
CCCCCCCCCCCCCCC		48.2125159151
59PhosphorylationNGRPQGNSRQVVEQD
CCCCCCCCCCCCCCC		30.8023927012
74PhosphorylationEEEDEELTLKYGAKH
HHHCHHHHHHHCCHH		25.20-
76UbiquitinationEDEELTLKYGAKHVI
HCHHHHHHHCCHHHH		36.08-
77PhosphorylationDEELTLKYGAKHVIM
CHHHHHHHCCHHHHH		25.9826074081
90PhosphorylationIMLFVPVTLCMVVVV
HHHHHHHHHHHHHHH		14.2626074081
99PhosphorylationCMVVVVATIKSVSFY
HHHHHHHHHHHCEEE		19.8226074081
102PhosphorylationVVVATIKSVSFYTRK
HHHHHHHHCEEEECC		21.1026074081
104PhosphorylationVATIKSVSFYTRKDG
HHHHHHCEEEECCCC		21.4526074081
105 (in isoform 2)Ubiquitination-7.2821906983
105 (in isoform 3)Ubiquitination-7.2821906983
106PhosphorylationTIKSVSFYTRKDGQL
HHHHCEEEECCCCEE		9.7226074081
107PhosphorylationIKSVSFYTRKDGQLI
HHHCEEEECCCCEEE		29.2726074081
109 (in isoform 6)Ubiquitination-59.4121906983
109 (in isoform 1)Ubiquitination-59.4121906983
109 (in isoform 4)Ubiquitination-59.4121906983
109 (in isoform 5)Ubiquitination-59.4121906983
109UbiquitinationSVSFYTRKDGQLIYT
HCEEEECCCCEEEEE		59.4121906983
154PhosphorylationTILLVVLYKYRCYKV
HHHHHHHHHHHHHHH		8.38-
240PhosphorylationMALVFIKYLPEWTAW
HHHHHHHHCHHHHHH		23.75-
256PhosphorylationILAVISVYDLVAVLC
HHHHHHHHHHHHHHC		9.21-
310 (in isoform 2)Ubiquitination-25.0621906983
310PhosphorylationPEAQRRVSKNSKYNA
HHHHHHHCCCCCCCC		25.0629496963
311UbiquitinationEAQRRVSKNSKYNAE
HHHHHHCCCCCCCCC		63.48-
313PhosphorylationQRRVSKNSKYNAEST
HHHHCCCCCCCCCCC		40.0129496963
314UbiquitinationRRVSKNSKYNAESTE
HHHCCCCCCCCCCCC		52.502190698
314 (in isoform 1)Ubiquitination-52.5021906983
315PhosphorylationRVSKNSKYNAESTER
HHCCCCCCCCCCCCC		21.3030576142
319PhosphorylationNSKYNAESTERESQD
CCCCCCCCCCCHHHC		32.9129255136
320PhosphorylationSKYNAESTERESQDT
CCCCCCCCCCHHHCC		30.4829255136
324PhosphorylationAESTERESQDTVAEN
CCCCCCHHHCCCCCC		39.3125849741
327PhosphorylationTERESQDTVAENDDG
CCCHHHCCCCCCCCC		17.6130576142
337PhosphorylationENDDGGFSEEWEAQR
CCCCCCCCHHHHHHC		37.5725849741
346PhosphorylationEWEAQRDSHLGPHRS
HHHHHCCCCCCCCCC		23.8523403867
353 (in isoform 3)Phosphorylation-45.3320068231
353PhosphorylationSHLGPHRSTPESRAA
CCCCCCCCCHHHHHH		45.3323401153
354PhosphorylationHLGPHRSTPESRAAV
CCCCCCCCHHHHHHH		30.9112056836
357 (in isoform 5)Phosphorylation-28.5520068231
357PhosphorylationPHRSTPESRAAVQEL
CCCCCHHHHHHHHHH		28.5526055452
363 (in isoform 3)Phosphorylation-43.9820068231
365PhosphorylationRAAVQELSSSILAGE
HHHHHHHHHHHHCCC		22.6829255136
366PhosphorylationAAVQELSSSILAGED
HHHHHHHHHHHCCCC		33.7429255136
367 (in isoform 5)Phosphorylation-20.4620068231
367PhosphorylationAVQELSSSILAGEDP
HHHHHHHHHHCCCCH		20.4629255136
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
310SPhosphorylationKinasePKA_GROUP-PhosphoELM
310SPhosphorylationKinasePRKACAP00517
GPS
310SPhosphorylationKinasePKA-Uniprot
310SPhosphorylationKinasePKA-FAMILY-GPS
319SPhosphorylationKinaseMAPK9P45984
GPS
320TPhosphorylationKinaseMAPK9P45984
GPS
346SPhosphorylationKinasePKC-Uniprot
346SPhosphorylationKinaseKPCAP17252
PhosphoELM
346SPhosphorylationKinasePRKCAP05696
GPS
346SPhosphorylationKinasePKC-FAMILY-GPS
353SPhosphorylationKinaseGSK3BP49841
PSP
354TPhosphorylationKinaseCDK_GROUP-PhosphoELM
354TPhosphorylationKinaseCDK5Q00535
PSP
354TPhosphorylationKinaseCDK-FAMILY-GPS
354TPhosphorylationKinaseDYRK1AQ61214
PSP
357SPhosphorylationKinaseGSK3BP49841
PSP
397SPhosphorylationKinaseGSK3BP49841
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:12354302
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:23707529
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
346SPhosphorylation

14576165
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
9852041
CTNB1_HUMANCTNNB1physical
10341227
NICA_HUMANNCSTNphysical
14572442
PEN2_HUMANPSENENphysical
14572442
APH1A_HUMANAPH1Aphysical
14572442
PEN2_HUMANPSENENphysical
12639958
GFAP_HUMANGFAPphysical
12058025
FLNB_HUMANFLNBphysical
9437013
ICAM5_HUMANICAM5physical
11719200
PKP4_HUMANPKP4physical
10092585
FBXW7_HUMANFBXW7physical
12354302
APH1A_HUMANAPH1Aphysical
12471034
PSN2_HUMANPSEN2physical
12471034
NICA_HUMANNCSTNphysical
12471034
BCL2_HUMANBCL2physical
10521466
CTNA1_HUMANCTNNA1physical
10635315
NOTC1_HUMANNOTCH1physical
10077672
B2CL1_HUMANBCL2L1physical
10446169
HERP1_HUMANHERPUD1physical
11799129
CTND1_HUMANCTNND1physical
10208590
TAU_HUMANMAPTphysical
9689133
KCIP4_HUMANKCNIP4physical
11847232
CIB1_HUMANCIB1physical
10366599
PSN1_HUMANPSEN1physical
12535650
YMEL1_HUMANYME1L1physical
12214059
CTNB1_HUMANCTNNB1physical
17360711
PSB1_HUMANPSMB1physical
10527805
PSA5_HUMANPSMA5physical
10527805
UBQL1_HUMANUBQLN1physical
16815845
TRAF6_HUMANTRAF6physical
18996842
IRAK2_HUMANIRAK2physical
18996842
HERP1_HUMANHERPUD1physical
14550564
APOE_HUMANAPOEphysical
21163940
PSN2_HUMANPSEN2physical
21163940
CDC37_HUMANCDC37physical
21163940
RAB3A_HUMANRAB3Aphysical
21163940
PRAM_HUMANPRAM1physical
21163940
GCDH_HUMANGCDHphysical
21163940
KANK2_HUMANKANK2physical
21163940
CDK5_HUMANCDK5physical
21163940
AP1M2_HUMANAP1M2physical
21163940
CP2CI_HUMANCYP2C18physical
21163940
CP2C8_HUMANCYP2C8physical
21163940
FXL12_HUMANFBXL12physical
21163940
NOS3_HUMANNOS3physical
21163940
PDCD4_HUMANPDCD4physical
21163940
PRDX2_HUMANPRDX2physical
21163940
RD23A_HUMANRAD23Aphysical
21163940
RHEB_HUMANRHEBphysical
21163940
STALP_HUMANSTAMBPL1physical
21163940
E41L3_HUMANEPB41L3physical
21163940
ACTN1_HUMANACTN1physical
21163940
EFHD1_HUMANEFHD1physical
21163940
G3P_HUMANGAPDHphysical
21163940
RMD3_HUMANRMDN3physical
21163940
F10A1_HUMANST13physical
21163940
ENSA_HUMANENSAphysical
21163940
COF1_HUMANCFL1physical
21163940
UMPS_HUMANUMPSphysical
21163940
SCOT1_HUMANOXCT1physical
21163940
FGF13_HUMANFGF13physical
21163940
HMGB1_HUMANHMGB1physical
21163940
ITSN2_HUMANITSN2physical
21163940
SCN1A_HUMANSCN1Aphysical
21163940
TBA1B_HUMANTUBA1Bphysical
21163940
ECSIT_HUMANECSITphysical
21163940
NICA_HUMANNCSTNphysical
15474363
PEN2_HUMANPSENENphysical
15474363
APH1A_HUMANAPH1Aphysical
15474363
PSN1_HUMANPSEN1physical
15474363
PSN2_HUMANPSEN2physical
15474363
TRAF6_HUMANTRAF6physical
23707529
TYDP2_HUMANTDP2physical
21988832
ETFA_HUMANETFAphysical
10527805
ERLN2_HUMANERLIN2physical
22771797
TGFR1_HUMANTGFBR1physical
24399296
TRAF6_HUMANTRAF6physical
24399296
UBC_HUMANUBCphysical
24399296
CTNB1_HUMANCTNNB1physical
16306047
DESP_HUMANDSPphysical
16306047
ITF2_HUMANTCF4physical
16306047
NICA_HUMANNCSTNphysical
17911105
CADH2_HUMANCDH2physical
20696212
Drug and Disease Associations
Kegg Disease
H00056 Alzheimer's disease (AD)
H00078 Frontotemporal lobar degeneration (FTLD), including: Pick disease of brain; Frontotemporal dementia
H00294 Dilated cardiomyopathy (DCM)
H00681 Acne inversa; Hidradenitis supprativa
OMIM Disease
607822Alzheimer disease 3 (AD3)
600274Frontotemporal dementia (FTD)
613694Cardiomyopathy, dilated 1U (CMD1U)
613737Acne inversa, familial, 3 (ACNINV3)
Kegg Drug
D08869 Begacestat (USAN/INN)
D09010 Tarenflurbil (USAN/INN); R-Flurbiprofen
D09377 Semagacestat (USAN/INN)
D09869 Avagacestat (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-365 AND SER-367,AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.
"Phosphorylation of presenilin 1 at the caspase recognition siteregulates its proteolytic processing and the progression ofapoptosis.";
Fluhrer R., Friedlein A., Haass C., Walter J.;
J. Biol. Chem. 279:1585-1593(2004).
Cited for: PHOSPHORYLATION AT SER-310 AND SER-346, AND MUTAGENESIS OF SER-310 ANDSER-346.

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