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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
62 | Phosphorylation | LLTPDELTNSSETRL HCCHHHCCCCCCCCC | 30.89 | 29083192 | |
64 | Phosphorylation | TPDELTNSSETRLSL CHHHCCCCCCCCCCH | 25.06 | 29083192 | |
65 | Phosphorylation | PDELTNSSETRLSLE HHHCCCCCCCCCCHH | 45.09 | 29083192 | |
67 | Phosphorylation | ELTNSSETRLSLEDL HCCCCCCCCCCHHHH | 38.57 | 29083192 | |
90 | N-linked_Glycosylation | DPEARWINDTDVVYK CCCCCEECCCCEEEE | 38.89 | 22387313 | |
111 | N-linked_Glycosylation | IKLNIETNATTLLLE EEEEEECCCEEEEEE | 23.62 | 22387313 | |
119 | N-linked_Glycosylation | ATTLLLENTTFVTFK CEEEEEECCEEEEEE | 44.37 | 22387313 | |
131 | Phosphorylation | TFKASRHSVSPDLKY EEEECCCCCCCCHHH | 24.15 | 25278378 | |
133 | Phosphorylation | KASRHSVSPDLKYVL EECCCCCCCCHHHEE | 18.73 | 18669648 | |
138 | Phosphorylation | SVSPDLKYVLLAYDV CCCCCHHHEEEEEEH | 12.02 | 18669648 | |
143 | Phosphorylation | LKYVLLAYDVKQIFH HHHEEEEEEHHHHHC | 22.65 | 12662155 | |
257 | N-linked_Glycosylation | RLAFLMINDSLVPTM EEEEEEECCCCCCCC | 20.89 | 22387313 | |
270 | Phosphorylation | TMVIPRFTGALYPKG CCCCCCCCCCCCCCC | 23.87 | - | |
274 | Phosphorylation | PRFTGALYPKGKQYP CCCCCCCCCCCCCCC | 11.45 | - | |
280 | Phosphorylation | LYPKGKQYPYPKAGQ CCCCCCCCCCCCCCC | 14.28 | - | |
282 | Phosphorylation | PKGKQYPYPKAGQVN CCCCCCCCCCCCCCC | 16.66 | - | |
291 | Phosphorylation | KAGQVNPTIKLYVVN CCCCCCCEEEEEEEE | 26.07 | 28060719 | |
316 | Phosphorylation | MPPDSFKSREYYITM CCCCCCCCCCEEEEE | 28.47 | - | |
319 | Phosphorylation | DSFKSREYYITMVKW CCCCCCCEEEEEEEE | 10.08 | - | |
320 | Phosphorylation | SFKSREYYITMVKWV CCCCCCEEEEEEEEH | 5.78 | - | |
328 | Phosphorylation | ITMVKWVSNTKTVVR EEEEEEHHCHHHHHH | 37.35 | - | |
342 | N-linked_Glycosylation | RWLNRAQNISILTVC HHHHHHCCEEEEEEE | 29.05 | 22387313 | |
414 | Phosphorylation | QSKSEQITVRHLTSG ECCCCEEEEEEECCC | 15.92 | 23312004 | |
467 | Phosphorylation | LLNRQCISCNFMKEQ HCCCCCCCCCCCHHH | 15.61 | 17081983 | |
481 | Phosphorylation | QCTYFDASFSPMNQH HCCEEECCCCCCCCE | 28.27 | 17081983 | |
483 | Phosphorylation | TYFDASFSPMNQHFL CEEECCCCCCCCEEE | 22.27 | 17081983 | |
512 | Phosphorylation | STDNPAKYFILESNS CCCCCCCEEEEECCH | 9.65 | - | |
519 | Phosphorylation | YFILESNSMLKEAIL EEEEECCHHHHHHHH | 34.47 | 24076635 | |
639 | Phosphorylation | KFLLKLPYIDSKRLS HHHHCCCCCCCCCEE | 28.00 | 23909892 | |
642 | Phosphorylation | LKLPYIDSKRLSIFG HCCCCCCCCCEEECC | 15.32 | 23909892 | |
669 | Acetylation | KSDEKLFKCGSVVAP CCCHHHCCCCCEEEE | 48.39 | 7366057 | |
729 | Acetylation | IHGTADTKVHFQHSA EEECCCCCHHCHHHH | 33.97 | 30588301 | |
748 | N-linked_Glycosylation | HLIKAGVNYTMQVYP HHHHHCCCEEEEECC | 26.16 | 22387313 | |
754 | Phosphorylation | VNYTMQVYPDEGHNV CCEEEEECCCCCCCC | 6.51 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
257 | N | Glycosylation |
| 22387313 |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DPP10_HUMAN | DPP10 | physical | 22387313 | |
KCND2_HUMAN | KCND2 | physical | 15454437 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
600807 | Asthma (ASTHMA) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
N-linked Glycosylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |