TPP2_HUMAN - dbPTM
TPP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPP2_HUMAN
UniProt AC P29144
Protein Name Tripeptidyl-peptidase 2
Gene Name TPP2
Organism Homo sapiens (Human).
Sequence Length 1249
Subcellular Localization Cytoplasm . Nucleus . Translocates to the nucleus in responce to gamma-irradiation.
Protein Description Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity)..
Protein Sequence MATAATEEPFPFHGLLPKKETGAASFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIVDIIDTTGSGDVNTATEVEPKDGEIVGLSGRVLKIPASWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPVHRVALAEACRKQEEFDVANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGEVWRACIDSNEDGDLSKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKHNIIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALILSGLKANNIDYTVHSVRRALENTAVKADNIEVFAQGHGIIQVDKAYDYLVQNTSFANKLGFTVTVGNNRGIYLRDPVQVAAPSDHGVGIEPVFPENTENSEKISLQLHLALTSNSSWVQCPSHLELMNQCRHINIRVDPRGLREGLHYTEVCGYDIASPNAGPLFRVPITAVIAAKVNESSHYDLAFTDVHFKPGQIRRHFIEVPEGATWAEVTVCSCSSEVSAKFVLHAVQLVKQRAYRSHEFYKFCSLPEKGTLTEAFPVLGGKAIEFCIARWWASLSDVNIDYTISFHGIVCTAPQLNIHASEGINRFDVQSSLKYEDLAPCITLKNWVQTLRPVSAKTKPLGSRDVLPNNRQLYEMVLTYNFHQPKSGEVTPSCPLLCELLYESEFDSQLWIIFDQNKRQMGSGDAYPHQYSLKLEKGDYTIRLQIRHEQISDLERLKDLPFIVSHRLSNTLSLDIHENHSFALLGKKKSSNLTLPPKYNQPFFVTSLPDDKIPKGAGPGCYLAGSLTLSKTELGKKADVIPVHYYLIPPPTKTKNGSKDKEKDSEKEKDLKEEFTEALRDLKIQWMTKLDSSDIYNELKETYPNYLPLYVARLHQLDAEKERMKRLNEIVDAANAVISHIDQTALAVYIAMKTDPRPDAATIKNDMDKQKSTLVDALCRKGCALADHLLHTQAQDGAISTDAEGKEEEGESPLDSLAETFWETTKWTDLFDNKVLTFAYKHALVNKMYGRGLKFATKLVEEKPTKENWKNCIQLMKLLGWTHCASFTENWLPIMYPPDYCVF
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------MATAATEEP
------CCCCCCCCC
19.76-
3Phosphorylation-----MATAATEEPF
-----CCCCCCCCCC
28.7825867546
6Phosphorylation--MATAATEEPFPFH
--CCCCCCCCCCCCC
38.1225867546
19UbiquitinationFHGLLPKKETGAASF
CCCCCCCCCCCCCEE
59.58-
21PhosphorylationGLLPKKETGAASFLC
CCCCCCCCCCCEEEE
40.7921406692
25PhosphorylationKKETGAASFLCRYPE
CCCCCCCEEEEECCC
20.4421406692
28GlutathionylationTGAASFLCRYPEYDG
CCCCEEEEECCCCCC
3.5522555962
61UbiquitinationMQVTTDGKPKIVDII
CEEECCCCCCEEEEE
46.0421906983
93PhosphorylationDGEIVGLSGRVLKIP
CCCEEEEECCEEEEC
20.7221712546
109UbiquitinationSWTNPSGKYHIGIKN
CCCCCCCCEEEEEEC
37.68-
118PhosphorylationHIGIKNGYDFYPKAL
EEEEECCCCCCHHHH
16.5725839225
123AcetylationNGYDFYPKALKERIQ
CCCCCCHHHHHHHHH
55.7826051181
136AcetylationIQKERKEKIWDPVHR
HHHHHHHHCCCHHHH
52.7325953088
136MethylationIQKERKEKIWDPVHR
HHHHHHHHCCCHHHH
52.7372608713
136UbiquitinationIQKERKEKIWDPVHR
HHHHHHHHCCCHHHH
52.73-
152UbiquitinationALAEACRKQEEFDVA
HHHHHHHHHCCCCCC
63.04-
168UbiquitinationNGSSQANKLIKEELQ
CCCHHHHHHHHHHHH
55.39-
171UbiquitinationSQANKLIKEELQSQV
HHHHHHHHHHHHHHH
56.42-
186AcetylationELLNSFEKKYSDPGP
HHHHHHHHHCCCCCC
55.8125953088
186UbiquitinationELLNSFEKKYSDPGP
HHHHHHHHHCCCCCC
55.81-
187AcetylationLLNSFEKKYSDPGPV
HHHHHHHHCCCCCCE
42.6725038526
195PhosphorylationYSDPGPVYDCLVWHD
CCCCCCEEEEEEECC
12.2228064214
220UbiquitinationNEDGDLSKSTVLRNY
CCCCCCCHHHHHHCH
58.40-
221PhosphorylationEDGDLSKSTVLRNYK
CCCCCCHHHHHHCHH
22.0020068231
222PhosphorylationDGDLSKSTVLRNYKE
CCCCCHHHHHHCHHH
27.5724719451
227PhosphorylationKSTVLRNYKEAQEYG
HHHHHHCHHHHHHHC
12.0820068231
293PhosphorylationAPGAQILSIKIGDTR
CCCCEEEEEEECCEE
24.3824719451
304SulfoxidationGDTRLSTMETGTGLI
CCEEECCCHHCHHHH
3.7921406390
321UbiquitinationMIEVINHKCDLVNYS
HHHHHHCCCCCCCCC
25.59-
397PhosphorylationDMMVAEYSLREKLPA
CCEEEEECHHHCCCC
16.6824719451
401AcetylationAEYSLREKLPANQYT
EEECHHHCCCCCCCC
54.0225953088
401MalonylationAEYSLREKLPANQYT
EEECHHHCCCCCCCC
54.0226320211
401UbiquitinationAEYSLREKLPANQYT
EEECHHHCCCCCCCC
54.02-
442PhosphorylationPNWTLRGTQLMNGTS
CCEEEECEEECCCCC
16.4623532336
448PhosphorylationGTQLMNGTSMSSPNA
CEEECCCCCCCCCCC
19.0923532336
449PhosphorylationTQLMNGTSMSSPNAC
EEECCCCCCCCCCCH
20.3327251275
451PhosphorylationLMNGTSMSSPNACGG
ECCCCCCCCCCCHHH
42.2727251275
452PhosphorylationMNGTSMSSPNACGGI
CCCCCCCCCCCHHHH
17.3327251275
485PhosphorylationVRRALENTAVKADNI
HHHHHHHCCCCCCCE
24.3720068231
610PhosphorylationGLREGLHYTEVCGYD
HHHCCCCEEEECCCC
15.0517360941
614GlutathionylationGLHYTEVCGYDIASP
CCCEEEECCCCCCCC
3.2122555962
642PhosphorylationIAAKVNESSHYDLAF
EEEECCCCCCCEEEE
19.7428152594
643PhosphorylationAAKVNESSHYDLAFT
EEECCCCCCCEEEEE
21.6428152594
645PhosphorylationKVNESSHYDLAFTDV
ECCCCCCCEEEEEEC
18.0128152594
655AcetylationAFTDVHFKPGQIRRH
EEEECCCCCCCEEEE
33.1025038526
655UbiquitinationAFTDVHFKPGQIRRH
EEEECCCCCCCEEEE
33.10-
697AcetylationLHAVQLVKQRAYRSH
HHHHHHHHHHHHHCC
42.5325953088
697UbiquitinationLHAVQLVKQRAYRSH
HHHHHHHHHHHHHCC
42.53-
708AcetylationYRSHEFYKFCSLPEK
HHCCCHHHHCCCCCC
45.2623749302
708MalonylationYRSHEFYKFCSLPEK
HHCCCHHHHCCCCCC
45.2626320211
708UbiquitinationYRSHEFYKFCSLPEK
HHCCCHHHHCCCCCC
45.2619608861
715AcetylationKFCSLPEKGTLTEAF
HHCCCCCCCCCCCCE
56.0825953088
715UbiquitinationKFCSLPEKGTLTEAF
HHCCCCCCCCCCCCE
56.08-
717PhosphorylationCSLPEKGTLTEAFPV
CCCCCCCCCCCCEEC
41.3928258704
719PhosphorylationLPEKGTLTEAFPVLG
CCCCCCCCCCEECCC
25.7128258704
748PhosphorylationLSDVNIDYTISFHGI
CCCCCCCEEEEECEE
11.3723879269
749PhosphorylationSDVNIDYTISFHGIV
CCCCCCEEEEECEEE
13.3423879269
751PhosphorylationVNIDYTISFHGIVCT
CCCCEEEEECEEEEE
11.9123879269
767PhosphorylationPQLNIHASEGINRFD
CCCEEEECCCCCCCC
23.3823879269
791AcetylationLAPCITLKNWVQTLR
HHHHEEEHHHHHHHC
39.8625953088
791UbiquitinationLAPCITLKNWVQTLR
HHHHEEEHHHHHHHC
39.86-
796PhosphorylationTLKNWVQTLRPVSAK
EEHHHHHHHCCCCCC
18.3428348404
801PhosphorylationVQTLRPVSAKTKPLG
HHHHCCCCCCCCCCC
27.0828348404
869PhosphorylationQNKRQMGSGDAYPHQ
CCCCCCCCCCCCCCE
28.32-
878PhosphorylationDAYPHQYSLKLEKGD
CCCCCEEEEEECCCC
16.6824719451
880AcetylationYPHQYSLKLEKGDYT
CCCEEEEEECCCCEE
48.9723236377
883AcetylationQYSLKLEKGDYTIRL
EEEEEECCCCEEEEE
68.4723954790
883MalonylationQYSLKLEKGDYTIRL
EEEEEECCCCEEEEE
68.4726320211
883UbiquitinationQYSLKLEKGDYTIRL
EEEEEECCCCEEEEE
68.47-
886PhosphorylationLKLEKGDYTIRLQIR
EEECCCCEEEEEEEE
16.8524505115
887PhosphorylationKLEKGDYTIRLQIRH
EECCCCEEEEEEEEH
12.3624719451
898PhosphorylationQIRHEQISDLERLKD
EEEHHHCCCHHHHCC
35.52-
904AcetylationISDLERLKDLPFIVS
CCCHHHHCCCCEEEE
64.5426051181
904MalonylationISDLERLKDLPFIVS
CCCHHHHCCCCEEEE
64.5426320211
904UbiquitinationISDLERLKDLPFIVS
CCCHHHHCCCCEEEE
64.54-
911PhosphorylationKDLPFIVSHRLSNTL
CCCCEEEEEECCCCC
9.70-
915PhosphorylationFIVSHRLSNTLSLDI
EEEEEECCCCCEEEE
27.9424275569
917PhosphorylationVSHRLSNTLSLDIHE
EEEECCCCCEEEEEC
17.8524275569
936PhosphorylationALLGKKKSSNLTLPP
EECCCCCCCCCCCCC
33.0821406692
937PhosphorylationLLGKKKSSNLTLPPK
ECCCCCCCCCCCCCC
44.7521406692
940PhosphorylationKKKSSNLTLPPKYNQ
CCCCCCCCCCCCCCC
41.2821406692
945PhosphorylationNLTLPPKYNQPFFVT
CCCCCCCCCCCEEEE
25.4623286773
952PhosphorylationYNQPFFVTSLPDDKI
CCCCEEEEECCCCCC
21.2723286773
953PhosphorylationNQPFFVTSLPDDKIP
CCCEEEEECCCCCCC
32.3829978859
958AcetylationVTSLPDDKIPKGAGP
EEECCCCCCCCCCCC
69.1825038526
958UbiquitinationVTSLPDDKIPKGAGP
EEECCCCCCCCCCCC
69.18-
961AcetylationLPDDKIPKGAGPGCY
CCCCCCCCCCCCCCE
65.9426051181
968PhosphorylationKGAGPGCYLAGSLTL
CCCCCCCEEECEEEE
12.9028258704
972PhosphorylationPGCYLAGSLTLSKTE
CCCEEECEEEECHHH
16.7528258704
974PhosphorylationCYLAGSLTLSKTELG
CEEECEEEECHHHCC
30.5924719451
976PhosphorylationLAGSLTLSKTELGKK
EECEEEECHHHCCCC
32.0923286773
983MalonylationSKTELGKKADVIPVH
CHHHCCCCCCEEEEE
48.2826320211
998PhosphorylationYYLIPPPTKTKNGSK
EEECCCCCCCCCCCC
58.0620860994
999AcetylationYLIPPPTKTKNGSKD
EECCCCCCCCCCCCC
64.3725953088
1005UbiquitinationTKTKNGSKDKEKDSE
CCCCCCCCCCCCCCH
74.3717370265
1013UbiquitinationDKEKDSEKEKDLKEE
CCCCCCHHHHHHHHH
74.2117370265
1018UbiquitinationSEKEKDLKEEFTEAL
CHHHHHHHHHHHHHH
66.39-
1029UbiquitinationTEALRDLKIQWMTKL
HHHHHHHHHHHHHCC
36.82-
1038PhosphorylationQWMTKLDSSDIYNEL
HHHHCCCHHHHHHHH
40.1028348404
1039PhosphorylationWMTKLDSSDIYNELK
HHHCCCHHHHHHHHH
27.9125159151
1042PhosphorylationKLDSSDIYNELKETY
CCCHHHHHHHHHHHC
13.94-
1046UbiquitinationSDIYNELKETYPNYL
HHHHHHHHHHCCCHH
41.66-
1048PhosphorylationIYNELKETYPNYLPL
HHHHHHHHCCCHHHH
42.5725072903
1049PhosphorylationYNELKETYPNYLPLY
HHHHHHHCCCHHHHH
7.2025072903
1052PhosphorylationLKETYPNYLPLYVAR
HHHHCCCHHHHHHHH
12.7525072903
1056PhosphorylationYPNYLPLYVARLHQL
CCCHHHHHHHHHHHH
7.0723917254
1067UbiquitinationLHQLDAEKERMKRLN
HHHHHHHHHHHHHHH
52.95-
11172-HydroxyisobutyrylationKNDMDKQKSTLVDAL
CCCHHHHHHHHHHHH
51.66-
1127UbiquitinationLVDALCRKGCALADH
HHHHHHHHCCHHHHH
58.29-
1180UbiquitinationWTDLFDNKVLTFAYK
HHHCCCCCHHHHHHH
40.2321890473
1183PhosphorylationLFDNKVLTFAYKHAL
CCCCCHHHHHHHHHH
14.81-
1186PhosphorylationNKVLTFAYKHALVNK
CCHHHHHHHHHHHHH
10.10-
1187AcetylationKVLTFAYKHALVNKM
CHHHHHHHHHHHHHH
20.9725953088
1187UbiquitinationKVLTFAYKHALVNKM
CHHHHHHHHHHHHHH
20.9721890473
1193UbiquitinationYKHALVNKMYGRGLK
HHHHHHHHHHHHCCH
26.48-
1200AcetylationKMYGRGLKFATKLVE
HHHHHCCHHHHHHHH
35.4625953088
1200UbiquitinationKMYGRGLKFATKLVE
HHHHHCCHHHHHHHH
35.46-
1204AcetylationRGLKFATKLVEEKPT
HCCHHHHHHHHCCCC
47.2923749302
1204UbiquitinationRGLKFATKLVEEKPT
HCCHHHHHHHHCCCC
47.29-
1209AcetylationATKLVEEKPTKENWK
HHHHHHCCCCHHHHH
44.4725953088
1209UbiquitinationATKLVEEKPTKENWK
HHHHHHCCCCHHHHH
44.47-
1212UbiquitinationLVEEKPTKENWKNCI
HHHCCCCHHHHHHHH
58.54-
1216UbiquitinationKPTKENWKNCIQLMK
CCCHHHHHHHHHHHH
54.23-

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 TPP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPP2_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 TPP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLOD2_HUMANPLOD2physical
22863883
TRI47_HUMANTRIM47physical
22863883
PP16A_HUMANPPP1R16Aphysical
25416956
ADAM8_HUMANADAM8physical
26344197
HXK2_HUMANHK2physical
26344197
TIPRL_HUMANTIPRLphysical
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 TPP2_HUMAN

loading...

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-708, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1005 AND LYS-1013, ANDMASS SPECTROMETRY.

TOP