PPIL4_HUMAN - dbPTM
PPIL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIL4_HUMAN
UniProt AC Q8WUA2
Protein Name Peptidyl-prolyl cis-trans isomerase-like 4
Gene Name PPIL4
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Nucleus .
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity)..
Protein Sequence MAVLLETTLGDVVIDLYTEERPRACLNFLKLCKIKYYNYCLIHNVQRDFIIQTGDPTGTGRGGESIFGQLYGDQASFFEAEKVPRIKHKKKGTVSMVNNGSDQHGSQFLITTGENLDYLDGVHTVFGEVTEGMDIIKKINETFVDKDFVPYQDIRINHTVILDDPFDDPPDLLIPDRSPEPTREQLDSGRIGADEEIDDFKGRSAEEVEEIKAEKEAKTQAILLEMVGDLPDADIKPPENVLFVCKLNPVTTDEDLEIIFSRFGPIRSCEVIRDWKTGESLCYAFIEFEKEEDCEKAFFKMDNVLIDDRRIHVDFSQSVAKVKWKGKGGKYTKSDFKEYEKEQDKPPNLVLKDKVKPKQDTKYDLILDEQAEDSKSSHSHTSKKHKKKTHHCSEEKEDEDYMPIKNTNQDIYREMGFGHYEEEESCWEKQKSEKRDRTQNRSRSRSRERDGHYSNSHKSKYQTDLYERERSKKRDRSRSPKKSKDKEKSKYR
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
7Phosphorylation-MAVLLETTLGDVVI
-CCEEEEEECCCHHE		27.5626270265
8PhosphorylationMAVLLETTLGDVVID
CCEEEEEECCCHHEE		21.2626270265
17PhosphorylationGDVVIDLYTEERPRA
CCHHEECCCCCCHHH		14.3526270265
18PhosphorylationDVVIDLYTEERPRAC
CHHEECCCCCCHHHH		38.3726270265
21MethylationIDLYTEERPRACLNF
EECCCCCCHHHHHHH		21.55115387835
23MethylationLYTEERPRACLNFLK
CCCCCCHHHHHHHHH		44.12115387843
35AcetylationFLKLCKIKYYNYCLI
HHHHHCCCEEEEEEE		27.4626051181
93PhosphorylationIKHKKKGTVSMVNNG
CCCCCCCCEEECCCC		20.4922210691
118PhosphorylationTTGENLDYLDGVHTV
ECCCCCHHCCCCCHH		15.1722210691
130PhosphorylationHTVFGEVTEGMDIIK
CHHHEEHHHCHHHHH		23.6322210691
138UbiquitinationEGMDIIKKINETFVD
HCHHHHHHHHHHCCC		40.1132142685
146UbiquitinationINETFVDKDFVPYQD
HHHHCCCCCCCCHHH		48.0029967540
159PhosphorylationQDIRINHTVILDDPF
HHCEEEEEEEECCCC		12.5422167270
178PhosphorylationDLLIPDRSPEPTREQ
CCCCCCCCCCCCHHH		40.7829255136
182PhosphorylationPDRSPEPTREQLDSG
CCCCCCCCHHHHHCC		45.2129255136
188PhosphorylationPTREQLDSGRIGADE
CCHHHHHCCCCCCCH		38.2723898821
201UbiquitinationDEEIDDFKGRSAEEV
CHHCCCCCCCCHHHH		61.4821906983
201SumoylationDEEIDDFKGRSAEEV
CHHCCCCCCCCHHHH		61.4828112733
201SumoylationDEEIDDFKGRSAEEV
CHHCCCCCCCCHHHH		61.48-
204PhosphorylationIDDFKGRSAEEVEEI
CCCCCCCCHHHHHHH		49.0225159151
212UbiquitinationAEEVEEIKAEKEAKT
HHHHHHHHHHHHHHH		54.4921906983
212SumoylationAEEVEEIKAEKEAKT
HHHHHHHHHHHHHHH		54.49-
212SumoylationAEEVEEIKAEKEAKT
HHHHHHHHHHHHHHH		54.4928112733
215UbiquitinationVEEIKAEKEAKTQAI
HHHHHHHHHHHHHHH		68.7622817900
218SumoylationIKAEKEAKTQAILLE
HHHHHHHHHHHHHHH		42.1128112733
236SumoylationDLPDADIKPPENVLF
CCCCCCCCCCCCEEE		55.88-
283PhosphorylationKTGESLCYAFIEFEK
CCCCEEEEEEEEECC		15.16-
296UbiquitinationEKEEDCEKAFFKMDN
CCHHHHHHHHHEECC		57.7522817900
300UbiquitinationDCEKAFFKMDNVLID
HHHHHHHEECCEEEC		38.6022817900
300AcetylationDCEKAFFKMDNVLID
HHHHHHHEECCEEEC		38.6025953088
318PhosphorylationIHVDFSQSVAKVKWK
EECCCCCCEEEEEEC		23.8925627689
321UbiquitinationDFSQSVAKVKWKGKG
CCCCCEEEEEECCCC		42.0433845483
321AcetylationDFSQSVAKVKWKGKG
CCCCCEEEEEECCCC		42.0425953088
321SumoylationDFSQSVAKVKWKGKG
CCCCCEEEEEECCCC		42.0428112733
341UbiquitinationSDFKEYEKEQDKPPN
HHHHHHHHHCCCCCC		60.8329967540
345UbiquitinationEYEKEQDKPPNLVLK
HHHHHCCCCCCCEEC		63.1729967540
352UbiquitinationKPPNLVLKDKVKPKQ
CCCCCEECCCCCCCC		48.2821906983
352SumoylationKPPNLVLKDKVKPKQ
CCCCCEECCCCCCCC		48.28-
354UbiquitinationPNLVLKDKVKPKQDT
CCCEECCCCCCCCCC		51.0422817900
356UbiquitinationLVLKDKVKPKQDTKY
CEECCCCCCCCCCCC		52.8422817900
358UbiquitinationLKDKVKPKQDTKYDL
ECCCCCCCCCCCCEE		55.9022817900
361PhosphorylationKVKPKQDTKYDLILD
CCCCCCCCCCEEEEC		29.0728796482
362SumoylationVKPKQDTKYDLILDE
CCCCCCCCCEEEECH		45.09-
362UbiquitinationVKPKQDTKYDLILDE
CCCCCCCCCEEEECH		45.0921906983
362SumoylationVKPKQDTKYDLILDE
CCCCCCCCCEEEECH		45.0928112733
363PhosphorylationKPKQDTKYDLILDEQ
CCCCCCCCEEEECHH		20.3428796482
374PhosphorylationLDEQAEDSKSSHSHT
ECHHHCCCCCCCCCC		26.4128985074
375UbiquitinationDEQAEDSKSSHSHTS
CHHHCCCCCCCCCCC		69.1932015554
376PhosphorylationEQAEDSKSSHSHTSK
HHHCCCCCCCCCCCH		36.9229449344
377PhosphorylationQAEDSKSSHSHTSKK
HHCCCCCCCCCCCHH		32.5229449344
379PhosphorylationEDSKSSHSHTSKKHK
CCCCCCCCCCCHHHC		30.3429449344
381PhosphorylationSKSSHSHTSKKHKKK
CCCCCCCCCHHHCCC		45.3029449344
382PhosphorylationKSSHSHTSKKHKKKT
CCCCCCCCHHHCCCC		33.9929449344
389PhosphorylationSKKHKKKTHHCSEEK
CHHHCCCCCCCCCCC		26.2329978859
393PhosphorylationKKKTHHCSEEKEDED
CCCCCCCCCCCCCCC		44.4230576142
401PhosphorylationEEKEDEDYMPIKNTN
CCCCCCCCCCCCCCC		11.6228796482
405UbiquitinationDEDYMPIKNTNQDIY
CCCCCCCCCCCHHHH		52.4223000965
405SumoylationDEDYMPIKNTNQDIY
CCCCCCCCCCCHHHH		52.42-
405SumoylationDEDYMPIKNTNQDIY
CCCCCCCCCCCHHHH		52.4228112733
412PhosphorylationKNTNQDIYREMGFGH
CCCCHHHHHHCCCCC		14.6022817900
420PhosphorylationREMGFGHYEEEESCW
HHCCCCCCHHHHHHH		25.9728796482
425PhosphorylationGHYEEEESCWEKQKS
CCCHHHHHHHHHHHH		28.0128796482
429UbiquitinationEEESCWEKQKSEKRD
HHHHHHHHHHHHHHH		38.2332015554
435MethylationEKQKSEKRDRTQNRS
HHHHHHHHHHHHHHH		34.2954558141
437MethylationQKSEKRDRTQNRSRS
HHHHHHHHHHHHHHH		42.0954558147
441MethylationKRDRTQNRSRSRSRE
HHHHHHHHHHHHHHH		24.5154558153
442PhosphorylationRDRTQNRSRSRSRER
HHHHHHHHHHHHHHC		42.0022210691
444PhosphorylationRTQNRSRSRSRERDG
HHHHHHHHHHHHCCC		35.5422210691
446PhosphorylationQNRSRSRSRERDGHY
HHHHHHHHHHCCCCC		39.4822210691
456PhosphorylationRDGHYSNSHKSKYQT
CCCCCCCCHHHHHHH		26.7630576142
459PhosphorylationHYSNSHKSKYQTDLY
CCCCCHHHHHHHHHH		31.0422210691
460SumoylationYSNSHKSKYQTDLYE
CCCCHHHHHHHHHHH		46.2928112733
460UbiquitinationYSNSHKSKYQTDLYE
CCCCHHHHHHHHHHH		46.2932015554
460SumoylationYSNSHKSKYQTDLYE
CCCCHHHHHHHHHHH		46.29-
460AcetylationYSNSHKSKYQTDLYE
CCCCHHHHHHHHHHH		46.2923954790
460MethylationYSNSHKSKYQTDLYE
CCCCHHHHHHHHHHH		46.2930591461
461PhosphorylationSNSHKSKYQTDLYER
CCCHHHHHHHHHHHH		24.6022210691
466PhosphorylationSKYQTDLYERERSKK
HHHHHHHHHHHHHHH		18.7528796482
471PhosphorylationDLYERERSKKRDRSR
HHHHHHHHHHCCCCC		37.4628112733
477PhosphorylationRSKKRDRSRSPKKSK
HHHHCCCCCCCCCCC		41.2026657352
483PhosphorylationRSRSPKKSKDKEKSK
CCCCCCCCCHHHHHC		52.8126657352
489PhosphorylationKSKDKEKSKYR----
CCCHHHHHCCC----		35.6926657352
491PhosphorylationKDKEKSKYR------
CHHHHHCCC------		28.7526657352
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 PPIL4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIL4_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 PPIL4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHERP_HUMANCHERPphysical
22365833
CCAR2_HUMANCCAR2physical
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
There are no disease associations of PTM sites.
Regulatory Network of PPIL4_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-178, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASSSPECTROMETRY.
"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-178, AND MASSSPECTROMETRY.

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