PPCE_HUMAN - dbPTM
PPCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPCE_HUMAN
UniProt AC P48147
Protein Name Prolyl endopeptidase
Gene Name PREP
Organism Homo sapiens (Human).
Sequence Length 710
Subcellular Localization Cytoplasm.
Protein Description Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long..
Protein Sequence MLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNILQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYGCSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
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
1Acetylation-------MLSLQYPD
-------CCCCCCCC		5.3122814378
6Phosphorylation--MLSLQYPDVYRDE
--CCCCCCCCCCCCC		13.4927642862
10PhosphorylationSLQYPDVYRDETAVQ
CCCCCCCCCCCCCHH		21.5227642862
19PhosphorylationDETAVQDYHGHKICD
CCCCHHHCCCCCCCC		7.8127642862
23UbiquitinationVQDYHGHKICDPYAW
HHHCCCCCCCCCCEE		50.01-
25GlutathionylationDYHGHKICDPYAWLE
HCCCCCCCCCCEECC		5.2722555962
28PhosphorylationGHKICDPYAWLEDPD
CCCCCCCCEECCCCC		9.3628796482
36PhosphorylationAWLEDPDSEQTKAFV
EECCCCCHHHHHHHH		36.6726552605
39PhosphorylationEDPDSEQTKAFVEAQ
CCCCHHHHHHHHHHH		21.9326552605
40UbiquitinationDPDSEQTKAFVEAQN
CCCHHHHHHHHHHHH		39.25-
48UbiquitinationAFVEAQNKITVPFLE
HHHHHHHCCCCCHHH		27.89-
57GlutathionylationTVPFLEQCPIRGLYK
CCCHHHHCCCCCCCH		1.9022555962
68PhosphorylationGLYKERMTELYDYPK
CCCHHHHHHHHCCCC		29.1229759185
71PhosphorylationKERMTELYDYPKYSC
HHHHHHHHCCCCEEE		13.7522461510
73PhosphorylationRMTELYDYPKYSCHF
HHHHHHCCCCEEEEE		6.5129759185
75AcetylationTELYDYPKYSCHFKK
HHHHCCCCEEEEEEC		43.5025953088
76PhosphorylationELYDYPKYSCHFKKG
HHHCCCCEEEEEECC		16.4226437602
81AcetylationPKYSCHFKKGKRYFY
CCEEEEEECCCEEEE		36.6326051181
86PhosphorylationHFKKGKRYFYFYNTG
EEECCCEEEEEEECC		13.2028152594
88PhosphorylationKKGKRYFYFYNTGLQ
ECCCEEEEEEECCCC		9.0221406692
90PhosphorylationGKRYFYFYNTGLQNQ
CCEEEEEEECCCCCC		10.6321406692
92PhosphorylationRYFYFYNTGLQNQRV
EEEEEEECCCCCCEE		28.0821406692
120PhosphorylationFLDPNILSDDGTVAL
EECCCCCCCCCCEEE		29.83-
1572-HydroxyisobutyrylationWVTIKFMKVDGAKEL
CEEEEEEEECCCCCC		40.06-
157AcetylationWVTIKFMKVDGAKEL
CEEEEEEEECCCCCC		40.0619608861
162UbiquitinationFMKVDGAKELPDVLE
EEEECCCCCCCHHHH		66.37-
172UbiquitinationPDVLERVKFSCMAWT
CHHHHHHCEEEEEEE		37.47-
172AcetylationPDVLERVKFSCMAWT
CHHHHHHCEEEEEEE		37.4725953088
196UbiquitinationSYPQQDGKSDGTETS
CCCCCCCCCCCCCCC		54.38-
197PhosphorylationYPQQDGKSDGTETST
CCCCCCCCCCCCCCC		46.9621406692
200PhosphorylationQDGKSDGTETSTNLH
CCCCCCCCCCCCCHH		40.8721406692
202PhosphorylationGKSDGTETSTNLHQK
CCCCCCCCCCCHHHH		40.4621406692
203PhosphorylationKSDGTETSTNLHQKL
CCCCCCCCCCHHHHH		14.7421406692
204PhosphorylationSDGTETSTNLHQKLY
CCCCCCCCCHHHHHH		49.5821406692
209UbiquitinationTSTNLHQKLYYHVLG
CCCCHHHHHHEHHHC		27.92-
235SulfoxidationFPDEPKWMGGAELSD
CCCCCCCCCCEEECC		4.4230846556
241PhosphorylationWMGGAELSDDGRYVL
CCCCEEECCCCCEEE		25.76-
246PhosphorylationELSDDGRYVLLSIRE
EECCCCCEEEEEEEC		10.8621406692
250PhosphorylationDGRYVLLSIREGCDP
CCCEEEEEEECCCCC		18.5520068231
270PhosphorylationYCDLQQESSGIAGIL
EECCCCCCCCHHHHH		29.5328348404
271PhosphorylationCDLQQESSGIAGILK
ECCCCCCCCHHHHHH		33.2028348404
325UbiquitinationFRDPEESKWKVLVPE
CCCCHHHCCEEECCH		55.07-
327UbiquitinationDPEESKWKVLVPEHE
CCHHHCCEEECCHHH		29.45-
381PhosphorylationTFPLDVGSIVGYSGQ
CCCCCCCCEEECCCC		17.6020068231
428UbiquitinationVFREVTVKGIDASDY
EEEEEEEECCCHHHC		40.5621890473
433PhosphorylationTVKGIDASDYQTVQI
EEECCCHHHCEEEEE		32.8628152594
435PhosphorylationKGIDASDYQTVQIFY
ECCCHHHCEEEEEEE		12.0028152594
437PhosphorylationIDASDYQTVQIFYPS
CCHHHCEEEEEEEEC		14.2428152594
442PhosphorylationYQTVQIFYPSKDGTK
CEEEEEEEECCCCCC		14.28-
449AcetylationYPSKDGTKIPMFIVH
EECCCCCCCEEEEEE		50.7925953088
510PhosphorylationNIRGGGEYGETWHKG
EECCCCCCCCCCCCC		24.44-
516UbiquitinationEYGETWHKGGILANK
CCCCCCCCCCEECCC		50.8521890473
523UbiquitinationKGGILANKQNCFDDF
CCCEECCCCCCCCHH		36.96-
539UbiquitinationCAAEYLIKEGYTSPK
HHHHHHHHCCCCCCC		42.35-
544PhosphorylationLIKEGYTSPKRLTIN
HHHCCCCCCCEEEEC		21.6828985074
546UbiquitinationKEGYTSPKRLTINGG
HCCCCCCCEEEECCC		60.86-
596PhosphorylationYTIGHAWTTDYGCSD
ECCCCEEECCCCCCC		15.57-
614PhosphorylationHFEWLVKYSPLHNVK
HHHHHHHHCCCCCCC		14.1927642862
615PhosphorylationFEWLVKYSPLHNVKL
HHHHHHHCCCCCCCC		18.4425159151
621UbiquitinationYSPLHNVKLPEADDI
HCCCCCCCCCCCCCC		64.74-
643MethylationLTADHDDRVVPLHSL
EEECCCCCEEEHHHH		37.07115488781
658PhosphorylationKFIATLQYIVGRSRK
HHHHHHHHHHCCCCC		10.7322673903
667PhosphorylationVGRSRKQSNPLLIHV
HCCCCCCCCCEEEEE		43.3725849741
703GlutathionylationMFAFIARCLNVDWIP
HHHHHHHHCCCCCCC		2.1022555962
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

Oops, there are no upstream regulatory protein records of PPCE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPCE_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 PPCE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYTC_HUMANTARSphysical
22939629
AIP_HUMANAIPphysical
26344197
LGUL_HUMANGLO1physical
26344197
HSP74_HUMANHSPA4physical
26344197
CH60_HUMANHSPD1physical
26344197
HS105_HUMANHSPH1physical
26344197
KCAB2_HUMANKCNAB2physical
26344197
PABP4_HUMANPABPC4physical
26344197
DHPR_HUMANQDPRphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00107Oxytocin
Regulatory Network of PPCE_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND MASS SPECTROMETRY.

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