DPP9_HUMAN - dbPTM
DPP9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPP9_HUMAN
UniProt AC Q86TI2
Protein Name Dipeptidyl peptidase 9
Gene Name DPP9
Organism Homo sapiens (Human).
Sequence Length 863
Subcellular Localization Isoform 1: Cytoplasm, cytosol .
Isoform 2: Nucleus .
Protein Description Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2..
Protein Sequence MATTGTPTADRGDAAATDDPAARFQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVYSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGLSNVLDDPKSAGVATFVIQEEFDRFTGYWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTDSYRYPRTGSKNPKIALKLAEFQTDSQGKIVSTQEKELVQPFSSLFPKVEYIARAGWTRDGKYAWAMFLDRPQQWLQLVLLPPALFIPSTENEEQRLASARAVPRNVQPYVVYEEVTNVWINVHDIFYPFPQSEGEDELCFLRANECKTGFCHLYKVTAVLKSQGYDWSEPFSPGEDEFKCPIKEEIALTSGEWEVLARHGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVRLTTPGFSHSCSMSQNFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAASCPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL
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
2Acetylation------MATTGTPTA
------CCCCCCCCC		17.5419413330
3Phosphorylation-----MATTGTPTAD
-----CCCCCCCCCC		25.1825159151
4Phosphorylation----MATTGTPTADR
----CCCCCCCCCCC		29.5325159151
6Phosphorylation--MATTGTPTADRGD
--CCCCCCCCCCCCC		18.5125159151
8PhosphorylationMATTGTPTADRGDAA
CCCCCCCCCCCCCCC		40.8228450419
17PhosphorylationDRGDAAATDDPAARF
CCCCCCCCCCHHHHH		35.8929514088
19 (in isoform 2)Phosphorylation-30.3124245541
21 (in isoform 2)Phosphorylation-20.4721815630
30PhosphorylationRFQVQKHSWDGLRSI
HHEEEECCHHHHHHH		33.6220873877
32 (in isoform 2)Phosphorylation-49.6228985074
35PhosphorylationKHSWDGLRSIIHGSR
ECCHHHHHHHHHCCC		31.1932645325
35 (in isoform 2)Phosphorylation-31.1928985074
43MalonylationSIIHGSRKYSGLIVN
HHHHCCCCCCCEEEE		45.5326320211
44PhosphorylationIIHGSRKYSGLIVNK
HHHCCCCCCCEEEEC		13.5823312004
45PhosphorylationIHGSRKYSGLIVNKA
HHCCCCCCCEEEECC		30.1122617229
51AcetylationYSGLIVNKAPHDFQF
CCCEEEECCCCCEEE		53.0223236377
51UbiquitinationYSGLIVNKAPHDFQF
CCCEEEECCCCCEEE		53.0221963094
57 (in isoform 2)Ubiquitination-43.59-
61UbiquitinationHDFQFVQKTDESGPH
CCEEEEECCCCCCCC		53.28-
74 (in isoform 2)Phosphorylation-11.0227251275
80AcetylationYYLGMPYGSRENSLL
EEECCCCCCCCCCCC		17.8519608861
80UbiquitinationYYLGMPYGSRENSLL
EEECCCCCCCCCCCC		17.8521963094
80 (in isoform 2)Ubiquitination-17.85-
85PhosphorylationPYGSRENSLLYSEIP
CCCCCCCCCCCCCCC		18.2623403867
88PhosphorylationSRENSLLYSEIPKKV
CCCCCCCCCCCCHHH		15.0023403867
89PhosphorylationRENSLLYSEIPKKVR
CCCCCCCCCCCHHHH		29.0823403867
90UbiquitinationENSLLYSEIPKKVRK
CCCCCCCCCCHHHHH		50.1629967540
90 (in isoform 2)Ubiquitination-50.16-
93UbiquitinationLLYSEIPKKVRKEAL
CCCCCCCHHHHHHHH		70.3527667366
104PhosphorylationKEALLLLSWKQMLDH
HHHHHHHHHHHHHHH		32.0028348404
115PhosphorylationMLDHFQATPHHGVYS
HHHHHHCCCCCCCCC		16.6328555341
122UbiquitinationTPHHGVYSREEELLR
CCCCCCCCHHHHHHH		30.7027667366
123 (in isoform 2)Ubiquitination-37.34-
126 (in isoform 2)Ubiquitination-48.64-
133 (in isoform 2)Phosphorylation-42.7827251275
134UbiquitinationLLRERKRLGVFGITS
HHHHHHHHCCCCEEE		8.4421963094
167AcetylationFHCRDGGKNGFMVSP
EEECCCCCCCEEECC		60.4726051181
167UbiquitinationFHCRDGGKNGFMVSP
EEECCCCCCCEEECC		60.4727667366
173PhosphorylationGKNGFMVSPMKPLEI
CCCCEEECCCCCCEE		13.9022199227
176UbiquitinationGFMVSPMKPLEIKTQ
CEEECCCCCCEEEEC		50.2427667366
181UbiquitinationPMKPLEIKTQCSGPR
CCCCCEEEECCCCCC		24.1433845483
196UbiquitinationMDPKICPADPAFFSF
CCCCCCCCCHHHHHC		30.8927667366
196 (in isoform 2)Ubiquitination-30.89-
205 (in isoform 2)Ubiquitination-39.69-
210UbiquitinationFINNSDLWVANIETG
CCCCCCEEEEECCCC		7.6833845483
210 (in isoform 2)Ubiquitination-7.68-
250UbiquitinationTFVIQEEFDRFTGYW
EEEEEECHHHCCCEE		8.8727667366
271UbiquitinationWEGSEGLKTLRILYE
CCCCCHHHHEEEEEE		57.2621963094
283PhosphorylationLYEEVDESEVEVIHV
EEEECCHHHEEEEEC		42.3428348404
292PhosphorylationVEVIHVPSPALEERK
EEEEECCCHHHHCCC		23.0130624053
300UbiquitinationPALEERKTDSYRYPR
HHHHCCCCCCCCCCC		36.0821963094
305PhosphorylationRKTDSYRYPRTGSKN
CCCCCCCCCCCCCCC		6.7123911959
308PhosphorylationDSYRYPRTGSKNPKI
CCCCCCCCCCCCHHH		41.1023911959
311UbiquitinationRYPRTGSKNPKIALK
CCCCCCCCCHHHHEE		77.8332015554
314AcetylationRTGSKNPKIALKLAE
CCCCCCHHHHEEEEE		50.4320167786
318UbiquitinationKNPKIALKLAEFQTD
CCHHHHEEEEEEEEC		36.3121906983
318 (in isoform 1)Ubiquitination-36.3121906983
318 (in isoform 4)Ubiquitination-36.3121906983
321 (in isoform 2)Phosphorylation-49.0427251275
324PhosphorylationLKLAEFQTDSQGKIV
EEEEEEEECCCCCCC		42.8329396449
326PhosphorylationLAEFQTDSQGKIVST
EEEEEECCCCCCCCC		44.1929396449
329UbiquitinationFQTDSQGKIVSTQEK
EEECCCCCCCCCHHH		32.0921906983
329 (in isoform 1)Ubiquitination-32.0921906983
329 (in isoform 4)Ubiquitination-32.0921906983
332PhosphorylationDSQGKIVSTQEKELV
CCCCCCCCCHHHHHC		28.0429396449
333PhosphorylationSQGKIVSTQEKELVQ
CCCCCCCCHHHHHCC		29.8329396449
336UbiquitinationKIVSTQEKELVQPFS
CCCCCHHHHHCCCHH		46.6721906983
336 (in isoform 1)Ubiquitination-46.6721906983
336 (in isoform 4)Ubiquitination-46.6721906983
340UbiquitinationTQEKELVQPFSSLFP
CHHHHHCCCHHHHCC		46.0432015554
347UbiquitinationQPFSSLFPKVEYIAR
CCHHHHCCHHHHHHC		45.1121963094
347 (in isoform 2)Ubiquitination-45.1121906983
354UbiquitinationPKVEYIARAGWTRDG
CHHHHHHCCCCCCCC		24.8721963094
358PhosphorylationYIARAGWTRDGKYAW
HHHCCCCCCCCCEEE		20.2624719451
358UbiquitinationYIARAGWTRDGKYAW
HHHCCCCCCCCCEEE		20.2621963094
358 (in isoform 2)Ubiquitination-20.2621906983
363PhosphorylationGWTRDGKYAWAMFLD
CCCCCCCEEEEEECC		16.9524719451
365 (in isoform 2)Ubiquitination-5.7921906983
377 (in isoform 2)Ubiquitination-26.94-
401UbiquitinationEQRLASARAVPRNVQ
HHHHHHCCCCCCCCC		33.3521963094
412UbiquitinationRNVQPYVVYEEVTNV
CCCCCEEEEEEECEE		4.0321963094
448UbiquitinationFLRANECKTGFCHLY
EEECCCCCCCCCEEE		45.57-
462UbiquitinationYKVTAVLKSQGYDWS
EEEEEHHHCCCCCCC		33.8521906983
462 (in isoform 1)Ubiquitination-33.8521906983
462 (in isoform 4)Ubiquitination-33.8521906983
477 (in isoform 2)Ubiquitination-72.97-
491UbiquitinationKEEIALTSGEWEVLA
CCEEEECCCCEEHHE		35.2529967540
491 (in isoform 2)Ubiquitination-35.2521906983
509UbiquitinationSKIWVNEETKLVYFQ
CEEEECCCEEEEEEE		46.1429967540
513UbiquitinationVNEETKLVYFQGTKD
ECCCEEEEEEECCCC		4.8529967540
518PhosphorylationKLVYFQGTKDTPLEH
EEEEEECCCCCCCCE		18.2424719451
532UbiquitinationHHLYVVSYEAAGEIV
EEEEEEEHHHCCEEE		9.6629967540
547 (in isoform 2)Phosphorylation-22.0224719451
578PhosphorylationCVHVYKLSGPDDDPL
EEEEEECCCCCCCHH		44.0927470641
587UbiquitinationPDDDPLHKQPRFWAS
CCCCHHHCCHHHHHH		70.4521906983
587 (in isoform 1)Ubiquitination-70.4521906983
587 (in isoform 4)Ubiquitination-70.4521906983
616 (in isoform 2)Ubiquitination-23.4521906983
624SulfoxidationSDVRLYGMIYKPHAL
CCCEEEEEEECCCCC		1.5931801345
694UbiquitinationLRFEGALKNQMGQVE
CCCCHHHHCCCCCEE		44.6021906983
694 (in isoform 1)Ubiquitination-44.6021906983
694 (in isoform 4)Ubiquitination-44.6021906983
716PhosphorylationLQFVAEKYGFIDLSR
HHHHHHHHCCEEECC		14.5822210691
722PhosphorylationKYGFIDLSRVAIHGW
HHCCEEECCEEECCC		22.4422210691
723 (in isoform 2)Ubiquitination-29.2321906983
730PhosphorylationRVAIHGWSYGGFLSL
CEEECCCCHHHHHHH		20.6322210691
731PhosphorylationVAIHGWSYGGFLSLM
EEECCCCHHHHHHHH		18.1122210691
828AcetylationSQLIRAGKPYQLQIY
HHHHHCCCCEEEEEC		39.3026051181
828UbiquitinationSQLIRAGKPYQLQIY
HHHHHCCCCEEEEEC		39.3027667366
828 (in isoform 1)Ubiquitination-39.3021906983
830PhosphorylationLIRAGKPYQLQIYPN
HHHCCCCEEEEECCC		25.91-
841PhosphorylationIYPNERHSIRCPESG
ECCCCCCCEECCCCC		20.2527251275
857UbiquitinationHYEVTLLHFLQEYL-
CEEEEHHHHHHHHC-		25.2027667366
857 (in isoform 2)Ubiquitination-25.2021906983
870 (in isoform 2)Phosphorylation-27251275
911Ubiquitination-------------------------------------------------------
-------------------------------------------------------		27667366
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 DPP9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPP9_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 DPP9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LPP_HUMANLPPphysical
22863883
NIF3L_HUMANNIF3L1physical
22863883
NPL4_HUMANNPLOC4physical
22863883
RPR1B_HUMANRPRD1Bphysical
22863883
SAE1_HUMANSAE1physical
22863883
STA5B_HUMANSTAT5Bphysical
22863883
SURF2_HUMANSURF2physical
22863883
TM1L1_HUMANTOM1L1physical
22863883
PRPK_HUMANTP53RKphysical
22863883
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 DPP9_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-51, AND MASS SPECTROMETRY.

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