DPP4_HUMAN - dbPTM
DPP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPP4_HUMAN
UniProt AC P27487
Protein Name Dipeptidyl peptidase 4
Gene Name DPP4
Organism Homo sapiens (Human).
Sequence Length 766
Subcellular Localization Dipeptidyl peptidase 4 soluble form: Secreted . Detected in the serum and the seminal fluid.
Cell membrane
Single-pass type II membrane protein. Apical cell membrane
Single-pass type II membrane protein. Cell projection, invadopodium membrane
Protein Description Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline..
Protein Sequence MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP
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
42PhosphorylationATADSRKTYTLTDYL
CCCCCCCEEEHHHHH		22.1926552605
43PhosphorylationTADSRKTYTLTDYLK
CCCCCCEEEHHHHHH		11.6426552605
44PhosphorylationADSRKTYTLTDYLKN
CCCCCEEEHHHHHHH		28.5418510355
46PhosphorylationSRKTYTLTDYLKNTY
CCCEEEHHHHHHHEE		18.1326552605
48PhosphorylationKTYTLTDYLKNTYRL
CEEEHHHHHHHEEEE		17.8426552605
52PhosphorylationLTDYLKNTYRLKLYS
HHHHHHHEEEEEEEE		14.3918510355
58PhosphorylationNTYRLKLYSLRWISD
HEEEEEEEEEEECCC		12.2229396449
59PhosphorylationTYRLKLYSLRWISDH
EEEEEEEEEEECCCC		23.1524719451
85N-linked_GlycosylationVFNAEYGNSSVFLEN
EEECCCCCCEEEEEC		30.1512483204
92N-linked_GlycosylationNSSVFLENSTFDEFG
CCEEEEECCCCCCCC		48.7920684603
150N-linked_GlycosylationITEERIPNNTQWVTW
ECCCCCCCCCCEEEE		62.9112483204
150N-linked_GlycosylationITEERIPNNTQWVTW
ECCCCCCCCCCEEEE		62.9112483204
182PhosphorylationKIEPNLPSYRITWTG
EEECCCCCEEEEEEC		30.1524719451
219N-linked_GlycosylationSALWWSPNGTFLAYA
HCEEECCCCEEEEEE		57.5312483204
229N-linked_GlycosylationFLAYAQFNDTEVPLI
EEEEEEECCCCCEEE		43.1212483204
256PhosphorylationPKTVRVPYPKAGAVN
CCEEECCCCCCCCCC		17.95-
281N-linked_GlycosylationDSLSSVTNATSIQIT
CCCCCCCCCCEEEEE		38.7812483204
321N-linked_GlycosylationQWLRRIQNYSVMDIC
HHHHHHCCCCCEECC		28.7712483204
432PhosphorylationMPGGRNLYKIQLSDY
CCCCCCEEEEECCCC		15.0324719451
439PhosphorylationYKIQLSDYTKVTCLS
EEEECCCCCEEEEEE		12.7024719451
440PhosphorylationKIQLSDYTKVTCLSC
EEECCCCCEEEEEEE		24.8324719451
460PhosphorylationRCQYYSVSFSKEAKY
HCEEEEEEECCCEEE		20.1924719451
520N-linked_GlycosylationKLDFIILNETKFWYQ
CCCEEEECCCCEEEE		44.4712483204
630PhosphorylationRIAIWGWSYGGYVTS
EEEEEEECCCCEEEE		15.2324114839
631PhosphorylationIAIWGWSYGGYVTSM
EEEEEECCCCEEEEE		14.2024114839
636PhosphorylationWSYGGYVTSMVLGSG
ECCCCEEEEEEECCC		11.5624114839
683PhosphorylationPEDNLDHYRNSTVMS
CCCCCHHHHCHHHHH		15.91-
685N-linked_GlycosylationDNLDHYRNSTVMSRA
CCCHHHHCHHHHHHH		34.5616335952
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 DPP4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPP4_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 DPP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCL22_HUMANCCL22physical
9933589
CAR11_HUMANCARD11physical
17287217
BCL10_HUMANBCL10physical
17287217
IKKB_HUMANIKBKBphysical
17287217
SEPR_HUMANFAPphysical
26209915
ADA_HUMANADAphysical
26209915
Drug and Disease Associations
Kegg Disease
H00032 Thyroid cancer
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D06553 Alogliptin benzoate (JAN/USAN)
D06578 Denagliptin tosylate (USAN)
D06645 Sitagliptin phosphate hydrate (JAN); Sitagliptin phosphate (USAN); Sitagliptin phosphate monohydrate
D07080 Vildagliptin (JAN/USAN/INN); Equa (TN); Galvus (TN)
D08516 Sitagliptin (Prop.INN)
D08616 Teneligliptin (INN)
D08631 Carmegliptin (USAN/INN)
D08996 Saxagliptin (INN)
D09326 Carmegliptin dihydrochloride (USAN)
D09333 Dutogliptin (USAN)
D09334 Dutogliptin tartrate (USAN)
D09566 Linagliptin (JAN/USAN/INN); Tradjenta (TN)
D09625 Gosogliptin (USAN/INN)
D09753 Saxagliptin hydrate (JAN/USAN); ONGLYZA (TN)
D09756 Teneligliptin hydrobromide hydrate (JAN)
D09780 Anagliptin (JAN/INN)
D10178 Trelagliptin (USAN)
D10179 Trelagliptin succinate (USAN)
D10262 Saxagliptin hydrochloride; Onglyza (TN)
D10317 Omarigliptin (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPP4_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selectivedipeptidyl peptidase-4 (DPP4) inhibitors.";
Meng W., Brigance R.P., Chao H.J., Fura A., Harrity T.,Marcinkeviciene J., O'Connor S.P., Tamura J.K., Xie D., Zhang Y.,Klei H.E., Kish K., Weigelt C.A., Turdi H., Wang A., Zahler R.,Kirby M.S., Hamann L.G.;
J. Med. Chem. 53:5620-5628(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 39-766, AND GLYCOSYLATION ATASN-85; ASN-92; ASN-150; ASN-219; ASN-229 AND ASN-520.
"Structural basis of proline-specific exopeptidase activity asobserved in human dipeptidyl peptidase-IV.";
Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M.;
Structure 11:947-959(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION,GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, AND DISULFIDEBONDS.
"Crystal structure of human dipeptidyl peptidase IV/CD26 in complexwith a substrate analog.";
Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N.;
Nat. Struct. Biol. 10:19-25(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION,GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321AND ASN-520, AND DISULFIDE BONDS.
"The structure and function of human dipeptidyl peptidase IV,possessing a unique eight-bladed beta-propeller fold.";
Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H.,Sugiyama S., Inaka K., Yamamoto A., Shimizu R.;
Biochem. Biophys. Res. Commun. 302:849-854(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION,GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, ANDDISULFIDE BONDS.
"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-92; ASN-150; ASN-520 ANDASN-685, AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-520 AND ASN-685, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory