DPP10_HUMAN - dbPTM
DPP10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPP10_HUMAN
UniProt AC Q8N608
Protein Name Inactive dipeptidyl peptidase 10
Gene Name DPP10
Organism Homo sapiens (Human).
Sequence Length 796
Subcellular Localization Cell membrane
Single-pass type II membrane protein .
Protein Description Promotes cell surface expression of the potassium channel KCND2. [PubMed: 15454437 Modulates the activity and gating characteristics of the potassium channel KCND2]
Protein Sequence MNQTASVSHHIKCQPSKTIKELGSNSPPQRNWKGIAIALLVILVVCSLITMSVILLTPDELTNSSETRLSLEDLFRKDFVLHDPEARWINDTDVVYKSENGHVIKLNIETNATTLLLENTTFVTFKASRHSVSPDLKYVLLAYDVKQIFHYSYTASYVIYNIHTREVWELNPPEVEDSVLQYAAWGVQGQQLIYIFENNIYYQPDIKSSSLRLTSSGKEEIIFNGIADWLYEEELLHSHIAHWWSPDGERLAFLMINDSLVPTMVIPRFTGALYPKGKQYPYPKAGQVNPTIKLYVVNLYGPTHTLELMPPDSFKSREYYITMVKWVSNTKTVVRWLNRAQNISILTVCETTTGACSKKYEMTSDTWLSQQNEEPVFSRDGSKFFMTVPVKQGGRGEFHHVAMFLIQSKSEQITVRHLTSGNWEVIKILAYDETTQKIYFLSTESSPRGRQLYSASTEGLLNRQCISCNFMKEQCTYFDASFSPMNQHFLLFCEGPRVPVVSLHSTDNPAKYFILESNSMLKEAILKKKIGKPEIKILHIDDYELPLQLSLPKDFMDRNQYALLLIMDEEPGGQLVTDKFHIDWDSVLIDMDNVIVARFDGRGSGFQGLKILQEIHRRLGSVEVKDQITAVKFLLKLPYIDSKRLSIFGKGYGGYIASMILKSDEKLFKCGSVVAPITDLKLYASAFSERYLGMPSKEESTYQAASVLHNVHGLKEENILIIHGTADTKVHFQHSAELIKHLIKAGVNYTMQVYPDEGHNVSEKSKYHLYSTILKFFSDCLKEEISVLPQEPEEDE
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
62PhosphorylationLLTPDELTNSSETRL
HCCHHHCCCCCCCCC
30.8929083192
64PhosphorylationTPDELTNSSETRLSL
CHHHCCCCCCCCCCH
25.0629083192
65PhosphorylationPDELTNSSETRLSLE
HHHCCCCCCCCCCHH
45.0929083192
67PhosphorylationELTNSSETRLSLEDL
HCCCCCCCCCCHHHH
38.5729083192
90N-linked_GlycosylationDPEARWINDTDVVYK
CCCCCEECCCCEEEE
38.8922387313
111N-linked_GlycosylationIKLNIETNATTLLLE
EEEEEECCCEEEEEE
23.6222387313
119N-linked_GlycosylationATTLLLENTTFVTFK
CEEEEEECCEEEEEE
44.3722387313
131PhosphorylationTFKASRHSVSPDLKY
EEEECCCCCCCCHHH
24.1525278378
133PhosphorylationKASRHSVSPDLKYVL
EECCCCCCCCHHHEE
18.7318669648
138PhosphorylationSVSPDLKYVLLAYDV
CCCCCHHHEEEEEEH
12.0218669648
143PhosphorylationLKYVLLAYDVKQIFH
HHHEEEEEEHHHHHC
22.6512662155
257N-linked_GlycosylationRLAFLMINDSLVPTM
EEEEEEECCCCCCCC
20.8922387313
270PhosphorylationTMVIPRFTGALYPKG
CCCCCCCCCCCCCCC
23.87-
274PhosphorylationPRFTGALYPKGKQYP
CCCCCCCCCCCCCCC
11.45-
280PhosphorylationLYPKGKQYPYPKAGQ
CCCCCCCCCCCCCCC
14.28-
282PhosphorylationPKGKQYPYPKAGQVN
CCCCCCCCCCCCCCC
16.66-
291PhosphorylationKAGQVNPTIKLYVVN
CCCCCCCEEEEEEEE
26.0728060719
316PhosphorylationMPPDSFKSREYYITM
CCCCCCCCCCEEEEE
28.47-
319PhosphorylationDSFKSREYYITMVKW
CCCCCCCEEEEEEEE
10.08-
320PhosphorylationSFKSREYYITMVKWV
CCCCCCEEEEEEEEH
5.78-
328PhosphorylationITMVKWVSNTKTVVR
EEEEEEHHCHHHHHH
37.35-
342N-linked_GlycosylationRWLNRAQNISILTVC
HHHHHHCCEEEEEEE
29.0522387313
414PhosphorylationQSKSEQITVRHLTSG
ECCCCEEEEEEECCC
15.9223312004
467PhosphorylationLLNRQCISCNFMKEQ
HCCCCCCCCCCCHHH
15.6117081983
481PhosphorylationQCTYFDASFSPMNQH
HCCEEECCCCCCCCE
28.2717081983
483PhosphorylationTYFDASFSPMNQHFL
CEEECCCCCCCCEEE
22.2717081983
512PhosphorylationSTDNPAKYFILESNS
CCCCCCCEEEEECCH
9.65-
519PhosphorylationYFILESNSMLKEAIL
EEEEECCHHHHHHHH
34.4724076635
639PhosphorylationKFLLKLPYIDSKRLS
HHHHCCCCCCCCCEE
28.0023909892
642PhosphorylationLKLPYIDSKRLSIFG
HCCCCCCCCCEEECC
15.3223909892
669AcetylationKSDEKLFKCGSVVAP
CCCHHHCCCCCEEEE
48.397366057
729AcetylationIHGTADTKVHFQHSA
EEECCCCCHHCHHHH
33.9730588301
748N-linked_GlycosylationHLIKAGVNYTMQVYP
HHHHHCCCEEEEECC
26.1622387313
754PhosphorylationVNYTMQVYPDEGHNV
CCEEEEECCCCCCCC
6.51-

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 DPP10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
257NGlycosylation

22387313

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 DPP10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPP10_HUMANDPP10physical
22387313
KCND2_HUMANKCND2physical
15454437

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600807Asthma (ASTHMA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPP10_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"N-glycosylation of the mammalian dipeptidyl aminopeptidase-likeprotein 10 (DPP10) regulates trafficking and interaction with Kv4channels.";
Cotella D., Radicke S., Cipriani V., Cavaletto M., Merlin S.,Follenzi A., Ravens U., Wettwer E., Santoro C., Sblattero D.;
Int. J. Biochem. Cell Biol. 44:876-885(2012).
Cited for: GLYCOSYLATION AT ASN-90; ASN-111; ASN-119; ASN-257; ASN-342 ANDASN-748, AND MUTAGENESIS OF ASN-257.
Phosphorylation
ReferencePubMed
"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-133; TYR-138 ANDTYR-143, AND MASS SPECTROMETRY.

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