DPP2_HUMAN - dbPTM
DPP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPP2_HUMAN
UniProt AC Q9UHL4
Protein Name Dipeptidyl peptidase 2
Gene Name DPP7
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Lysosome . Cytoplasmic vesicle . Secreted .
Protein Description Plays an important role in the degradation of some oligopeptides..
Protein Sequence MGSAPWAPVLLLALGLRGLQAGARRAPDPGFQERFFQQRLDHFNFERFGNKTFPQRFLVSDRFWVRGEGPIFFYTGNEGDVWAFANNSAFVAELAAERGALLVFAEHRYYGKSLPFGAQSTQRGHTELLTVEQALADFAELLRALRRDLGAQDAPAIAFGGSYGGMLSAYLRMKYPHLVAGALAASAPVLAVAGLGDSNQFFRDVTADFEGQSPKCTQGVREAFRQIKDLFLQGAYDTVRWEFGTCQPLSDEKDLTQLFMFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCDRLLSEAQRITGLRALAGLVYNASGSEHCYDIYRLYHSCADPTGCGTGPDARAWDYQACTEINLTFASNNVTDMFPDLPFTDELRQRYCLDTWGVWPRPDWLLTSFWGGDLRAASNIIFSNGNLDPWAGGGIRRNLSASVIAVTIQGGAHHLDLRASHPEDPASVVEARKLEATIIGEWVKAARREQQPALRGGPRLSL
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
50N-linked_GlycosylationFNFERFGNKTFPQRF
CCHHHHCCCCCCCCE
37.1719159218
86N-linked_GlycosylationGDVWAFANNSAFVAE
CCEEEEECCHHHHHH
36.21UniProtKB CARBOHYD
104UbiquitinationERGALLVFAEHRYYG
HCCCEEEEEECCCCC
7.1421890473
112UbiquitinationAEHRYYGKSLPFGAQ
EECCCCCCCCCCCCC
32.4721906983
134UbiquitinationELLTVEQALADFAEL
EEECHHHHHHHHHHH
7.3921890473
162PhosphorylationPAIAFGGSYGGMLSA
CEEEECCCHHHHHHH
22.4528348404
163PhosphorylationAIAFGGSYGGMLSAY
EEEECCCHHHHHHHH
22.4528348404
168PhosphorylationGSYGGMLSAYLRMKY
CCHHHHHHHHHHHHC
13.1328348404
170PhosphorylationYGGMLSAYLRMKYPH
HHHHHHHHHHHHCHH
7.4628348404
206PhosphorylationNQFFRDVTADFEGQS
HHHHHHHHCCCCCCC
25.46-
207UbiquitinationQFFRDVTADFEGQSP
HHHHHHHCCCCCCCC
21.2421963094
213PhosphorylationTADFEGQSPKCTQGV
HCCCCCCCCCHHHHH
36.86-
215UbiquitinationDFEGQSPKCTQGVRE
CCCCCCCCHHHHHHH
55.9821906983
220UbiquitinationSPKCTQGVREAFRQI
CCCHHHHHHHHHHHH
3.4321890473
228UbiquitinationREAFRQIKDLFLQGA
HHHHHHHHHHHHCCC
39.7921906983
237UbiquitinationLFLQGAYDTVRWEFG
HHHCCCCCEEEEECC
37.8921963094
238PhosphorylationFLQGAYDTVRWEFGT
HHCCCCCEEEEECCC
10.17-
250UbiquitinationFGTCQPLSDEKDLTQ
CCCCCCCCCCCHHHH
50.8621890473
288UbiquitinationLGPLPANPVKVGCDR
CCCCCCCCCCCCHHH
29.4321963094
301UbiquitinationDRLLSEAQRITGLRA
HHHHHHHHHHHHHHH
33.0021890473
304PhosphorylationLSEAQRITGLRALAG
HHHHHHHHHHHHHHH
32.1424719451
315N-linked_GlycosylationALAGLVYNASGSEHC
HHHHHEECCCCCCHH
21.8316399764
315N-linked_GlycosylationALAGLVYNASGSEHC
HHHHHEECCCCCCHH
21.8316399764
356N-linked_GlycosylationYQACTEINLTFASNN
HHHCCEEEEEEECCC
27.14UniProtKB CARBOHYD
363N-linked_GlycosylationNLTFASNNVTDMFPD
EEEEECCCCCCCCCC
35.25UniProtKB CARBOHYD
428N-linked_GlycosylationAGGGIRRNLSASVIA
CCCHHHHCCCEEEEE
28.62UniProtKB CARBOHYD
463UbiquitinationASVVEARKLEATIIG
HHHHHHHHHHHHHHH
58.70-
474UbiquitinationTIIGEWVKAARREQQ
HHHHHHHHHHHHHCC
37.08-

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 DPP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPP2_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 DPP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SBP1_HUMANSELENBP1physical
22939629
MYCBP_HUMANMYCBPphysical
22939629
CYTB_HUMANCSTBphysical
22863883
PLCG1_HUMANPLCG1physical
22863883
RIC8A_HUMANRIC8Aphysical
22863883
SARNP_HUMANSARNPphysical
22863883
WDR61_HUMANWDR61physical
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 DPP2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-315, AND MASSSPECTROMETRY.

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