DPP8_HUMAN - dbPTM
DPP8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPP8_HUMAN
UniProt AC Q6V1X1
Protein Name Dipeptidyl peptidase 8
Gene Name DPP8
Organism Homo sapiens (Human).
Sequence Length 898
Subcellular Localization Cytoplasm .
Protein Description Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. May play a role in T-cell activation and immune function..
Protein Sequence MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI
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
62UbiquitinationRYSWSQLKKLLADTR
ECCHHHHHHHHHHHH		33.47-
120UbiquitinationLFYSEIPKTINRAAV
EECCCCCHHHCHHHH		68.64-
169PhosphorylationGTVGIASYDYHQGSG
CCEEEEEEEECCCCE		16.1118083107
187PhosphorylationFQAGSGIYHVKDGGP
EECCCCEEEECCCCC		12.2318083107
297UbiquitinationETTPSGGKILRILYE
EECCCCCEEEEEEEE		41.93-
317PhosphorylationEVEIIHVTSPMLETR
CEEEEEEECCCCCCC		16.9827251275
318PhosphorylationVEIIHVTSPMLETRR
EEEEEEECCCCCCCC		13.7627251275
328PhosphorylationLETRRADSFRYPKTG
CCCCCCCCCCCCCCC		15.6127251275
331PhosphorylationRRADSFRYPKTGTAN
CCCCCCCCCCCCCCC		13.6814729942
333UbiquitinationADSFRYPKTGTANPK
CCCCCCCCCCCCCCE		51.13-
334PhosphorylationDSFRYPKTGTANPKV
CCCCCCCCCCCCCEE		34.9517924679
336PhosphorylationFRYPKTGTANPKVTF
CCCCCCCCCCCEEEE		28.6127251275
340UbiquitinationKTGTANPKVTFKMSE
CCCCCCCEEEEEEEE		54.43-
342PhosphorylationGTANPKVTFKMSEIM
CCCCCEEEEEEEEEE		24.5427251275
372 (in isoform 4)Ubiquitination-10.6321890473
372 (in isoform 3)Ubiquitination-10.6321890473
388 (in isoform 2)Ubiquitination-30.0821890473
388 (in isoform 1)Ubiquitination-30.0821890473
388 (in isoform 5)Ubiquitination-30.0821890473
388UbiquitinationAGWTPEGKYAWSILL
CCCCCCCCEEEEEEE		30.0821890473
389PhosphorylationGWTPEGKYAWSILLD
CCCCCCCEEEEEEEC		24.9429449344
392PhosphorylationPEGKYAWSILLDRSQ
CCCCEEEEEEECCCC		8.6629449344
398PhosphorylationWSILLDRSQTRLQIV
EEEEECCCCCEEEEE		35.2529449344
400PhosphorylationILLDRSQTRLQIVLI
EEECCCCCEEEEEEE		34.2929449344
474PhosphorylationIFASECKTGFRHLYK
EEEECCCCCHHHHHH		53.8929396449
480PhosphorylationKTGFRHLYKITSILK
CCCHHHHHHHHHHHH		8.3329396449
483PhosphorylationFRHLYKITSILKESK
HHHHHHHHHHHHHHC		12.9329396449
484PhosphorylationRHLYKITSILKESKY
HHHHHHHHHHHHHCC		29.4224719451
487UbiquitinationYKITSILKESKYKRS
HHHHHHHHHHCCCCC		59.27-
494PhosphorylationKESKYKRSSGGLPAP
HHHCCCCCCCCCCCC		29.23-
495PhosphorylationESKYKRSSGGLPAPS
HHCCCCCCCCCCCCC		40.7021815630
502PhosphorylationSGGLPAPSDFKCPIK
CCCCCCCCCCCCCCC		58.76-
527PhosphorylationEVLGRHGSNIQVDEV
EEEECCCCCCCHHHE		25.32-
543PhosphorylationRLVYFEGTKDSPLEH
EEEEEECCCCCCCCE		25.20-
572PhosphorylationRLTDRGYSHSCCISQ
EEECCCCCCCEEHHH		16.2628348404
574PhosphorylationTDRGYSHSCCISQHC
ECCCCCCCEEHHHCC		12.5428348404
578PhosphorylationYSHSCCISQHCDFFI
CCCCEEHHHCCCEEH		10.4328348404
592UbiquitinationISKYSNQKNPHCVSL
HHHCCCCCCCCEEEE		76.36-
601UbiquitinationPHCVSLYKLSSPEDD
CCEEEEEECCCCCCC		47.38-
614UbiquitinationDDPTCKTKEFWATIL
CCCCCCCHHHHHHHH		36.09-
680 (in isoform 6)Ubiquitination-29.4721906983
691PhosphorylationVKYFRLNTLASLGYV
CEEEEEEECHHCCEE		28.44-
719UbiquitinationLKFEGAFKYKMGQIE
CEEECCEEEECCEEE		43.35-
737 (in isoform 4)Ubiquitination-1.9421890473
802 (in isoform 2)Ubiquitination-51.4421890473
804 (in isoform 5)Ubiquitination-53.3821890473
817UbiquitinationSVAMQAEKFPSEPNR
HHHEEEHHCCCCCCE		66.64-
837 (in isoform 3)Ubiquitination-26.2621890473
853 (in isoform 1)Ubiquitination-39.1421890473
853UbiquitinationSFLVRAGKPYDLQIY
HHHHHCCCCCCEEEC		39.142190698
896UbiquitinationGSRIAALKVI-----
CHHEEEEEEC-----		32.91-
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 DPP8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPP8_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 DPP8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARMC9_HUMANARMC9physical
22863883
CD44_HUMANCD44physical
22863883
SRP14_HUMANSRP14physical
22863883
SRP09_HUMANSRP9physical
22863883
UBXN7_HUMANUBXN7physical
22863883
WDR4_HUMANWDR4physical
22863883
RIN1_HUMANRIN1physical
27173435
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 DPP8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334, AND MASSSPECTROMETRY.

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