DPP3_HUMAN - dbPTM
DPP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPP3_HUMAN
UniProt AC Q9NY33
Protein Name Dipeptidyl peptidase 3
Gene Name DPP3
Organism Homo sapiens (Human).
Sequence Length 737
Subcellular Localization Cytoplasm, cytosol .
Protein Description Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. [PubMed: 3233187]
Protein Sequence MADTQYILPNDIGVSSLDCREAFRLLSPTERLYAYHLSRAAWYGGLAVLLQTSPEAPYIYALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPKEKLERVILGSEAAQQHPEEVRGLWQTCGELMFSLEPRLRHLGLGKEGITTYFSGNCTMEDAKLAQDFLDSQNLSAYNTRLFKEVDGEGKPYYEVRLASVLGSEPSLDSEVTSKLKSYEFRGSPFQVTRGDYAPILQKVVEQLEKAKAYAANSHQGQMLAQYIESFTQGSIEAHKRGSRFWIQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAVVNKAMSAKFERLVASAEQLLKELPWPPTFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATQREKLTFLEEDDKDLYILWKGPSFDVQVGLHELLGHGSGKLFVQDEKGAFNFDQETVINPETGEQIQSWYRSGETWDSKFSTIASSYEECRAESVGLYLCLHPQVLEIFGFEGADAEDVIYVNWLNMVRAGLLALEFYTPEAFNWRQAHMQARFVILRVLLEAGEGLVTITPTTGSDGRPDARVRLDRSKIRSVGKPALERFLRRLQVLKSTGDVAGGRALYEGYATVTDAPPECFLTLRDTVLLRKESRKLIVQPNTRLEGSDVQLLEYEASAAGLIRSFSERFPEDGPELEEILTQLATADARFWKGPSEAPSGQA
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------MADTQYILP
------CCCCCEECC		28.6722223895
4Phosphorylation----MADTQYILPND
----CCCCCEECCCC		17.4624043423
6Phosphorylation--MADTQYILPNDIG
--CCCCCEECCCCCC		13.4024043423
15PhosphorylationLPNDIGVSSLDCREA
CCCCCCCCCCCHHHH		21.7024043423
16PhosphorylationPNDIGVSSLDCREAF
CCCCCCCCCCHHHHH		26.3124043423
27PhosphorylationREAFRLLSPTERLYA
HHHHHHCCHHHHHHH		34.0722210691
29PhosphorylationAFRLLSPTERLYAYH
HHHHCCHHHHHHHHH		30.29-
35PhosphorylationPTERLYAYHLSRAAW
HHHHHHHHHHHHHHH		6.9622210691
113UbiquitinationYKSFGDTKFVPNLPK
CCCCCCCCCCCCCCH		49.4521906983
113 (in isoform 1)Ubiquitination-49.4521906983
113 (in isoform 2)Ubiquitination-49.4521906983
130PhosphorylationLERVILGSEAAQQHP
HHHHHHCHHHHHHCH		22.1823911959
153O-linked_GlycosylationTCGELMFSLEPRLRH
HHHHHHHCCHHHHHH		20.1830379171
165UbiquitinationLRHLGLGKEGITTYF
HHHCCCCCCCCEEEE		58.78-
169 (in isoform 2)Phosphorylation-26.7123663014
170 (in isoform 2)Phosphorylation-22.2023663014
171PhosphorylationGKEGITTYFSGNCTM
CCCCCEEEEECCCCH		6.2623663014
171 (in isoform 2)Phosphorylation-6.2623663014
173 (in isoform 2)Phosphorylation-20.7723663014
177 (in isoform 2)Phosphorylation-27.8223663014
178SulfoxidationYFSGNCTMEDAKLAQ
EEECCCCHHHHHHHH		4.8430846556
202AcetylationAYNTRLFKEVDGEGK
HHHHEEEEEECCCCC		62.5125953088
202UbiquitinationAYNTRLFKEVDGEGK
HHHHEEEEEECCCCC		62.5121906983
202 (in isoform 1)Ubiquitination-62.5121906983
209 (in isoform 1)Ubiquitination-26.0821906983
209 (in isoform 2)Ubiquitination-26.0821906983
209UbiquitinationKEVDGEGKPYYEVRL
EEECCCCCEEEEEEH		26.0821906983
211PhosphorylationVDGEGKPYYEVRLAS
ECCCCCEEEEEEHHH		18.7528796482
212PhosphorylationDGEGKPYYEVRLASV
CCCCCEEEEEEHHHH		19.2428796482
218PhosphorylationYYEVRLASVLGSEPS
EEEEEHHHHHCCCCC		23.59-
233 (in isoform 1)Ubiquitination-51.0421906983
233AcetylationLDSEVTSKLKSYEFR
CCHHHHHHCCCCEEC		51.0425953088
233UbiquitinationLDSEVTSKLKSYEFR
CCHHHHHHCCCCEEC		51.0421906983
235UbiquitinationSEVTSKLKSYEFRGS
HHHHHHCCCCEECCC		55.5221906983
235 (in isoform 1)Ubiquitination-55.5221906983
236PhosphorylationEVTSKLKSYEFRGSP
HHHHHCCCCEECCCC		40.0924719451
257 (in isoform 1)Ubiquitination-44.8121906983
257UbiquitinationDYAPILQKVVEQLEK
CHHHHHHHHHHHHHH		44.8121906983
2642-HydroxyisobutyrylationKVVEQLEKAKAYAAN
HHHHHHHHHHHHHCC		64.87-
264 (in isoform 1)Ubiquitination-64.8721906983
264UbiquitinationKVVEQLEKAKAYAAN
HHHHHHHHHHHHHCC		64.8721906983
272PhosphorylationAKAYAANSHQGQMLA
HHHHHCCCHHHHHHH		16.6826657352
286PhosphorylationAQYIESFTQGSIEAH
HHHHHHHHHCCCCHH		41.10-
289PhosphorylationIESFTQGSIEAHKRG
HHHHHHCCCCHHHCC		13.87-
294UbiquitinationQGSIEAHKRGSRFWI
HCCCCHHHCCCCEEE		66.55-
294AcetylationQGSIEAHKRGSRFWI
HCCCCHHHCCCCEEE		66.5524431683
297PhosphorylationIEAHKRGSRFWIQDK
CCHHHCCCCEEEECC		28.47-
307 (in isoform 2)Ubiquitination-7.9721906983
337UbiquitinationGFVAVVNKAMSAKFE
HHHHHHCHHHHHHHH		33.5821906983
337 (in isoform 1)Ubiquitination-33.5821906983
342UbiquitinationVNKAMSAKFERLVAS
HCHHHHHHHHHHHHC		40.21-
355UbiquitinationASAEQLLKELPWPPT
HCHHHHHHHCCCCCC		66.84-
405UbiquitinationLRQTEGFKNVSLGNV
HHCCCCCCCCCHHHH		68.26-
408PhosphorylationTEGFKNVSLGNVLAV
CCCCCCCCHHHHHHH		39.7021712546
423UbiquitinationAYATQREKLTFLEED
HHHHHHHHCEEEECC		55.82-
425PhosphorylationATQREKLTFLEEDDK
HHHHHHCEEEECCCC		36.9216097034
459UbiquitinationLLGHGSGKLFVQDEK
HHCCCCCEEEEECCC		40.21-
466 (in isoform 1)Ubiquitination-64.9221906983
466UbiquitinationKLFVQDEKGAFNFDQ
EEEEECCCCCCCCCC		64.9221906983
498UbiquitinationSGETWDSKFSTIASS
CCCCCCHHHHHHHHC		40.64-
615UbiquitinationSKIRSVGKPALERFL
HHHHHCCHHHHHHHH		25.59-
629 (in isoform 1)Ubiquitination-47.3021906983
629UbiquitinationLRRLQVLKSTGDVAG
HHHHHHHHHCCCCCC		47.3021906983
630PhosphorylationRRLQVLKSTGDVAGG
HHHHHHHHCCCCCCC		33.2023403867
631PhosphorylationRLQVLKSTGDVAGGR
HHHHHHHCCCCCCCC		35.5023403867
641PhosphorylationVAGGRALYEGYATVT
CCCCCEEEEEEEEEC		13.3123403867
644PhosphorylationGRALYEGYATVTDAP
CCEEEEEEEEECCCC		6.2723403867
646PhosphorylationALYEGYATVTDAPPE
EEEEEEEEECCCCCC		18.5623403867
648PhosphorylationYEGYATVTDAPPECF
EEEEEEECCCCCCCE		23.3023403867
670UbiquitinationLLRKESRKLIVQPNT
EEECCCCCEEECCCC		52.42-
677PhosphorylationKLIVQPNTRLEGSDV
CEEECCCCCCCCCCC		43.23-
682PhosphorylationPNTRLEGSDVQLLEY
CCCCCCCCCCEEEEH		25.8227251275
689PhosphorylationSDVQLLEYEASAAGL
CCCEEEEHHHHHHHH		19.4326074081
692PhosphorylationQLLEYEASAAGLIRS
EEEEHHHHHHHHHHH		13.5026074081
698MethylationASAAGLIRSFSERFP
HHHHHHHHHHHHHCC		36.37-
699PhosphorylationSAAGLIRSFSERFPE
HHHHHHHHHHHHCCC		26.5726074081
701PhosphorylationAGLIRSFSERFPEDG
HHHHHHHHHHCCCCC		29.1626074081
716PhosphorylationPELEEILTQLATADA
HHHHHHHHHHHHCCC		27.4826074081
720PhosphorylationEILTQLATADARFWK
HHHHHHHHCCCCCCC		33.3926074081
727UbiquitinationTADARFWKGPSEAPS
HCCCCCCCCCCCCCC		59.232190698
727 (in isoform 1)Ubiquitination-59.2321906983
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 DPP3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPP3_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 DPP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DLDH_HUMANDLDphysical
22863883
NDRG1_HUMANNDRG1physical
22863883
SPSY_HUMANSMSphysical
22863883
TNG2_HUMANTANGO2physical
26344197
KEAP1_HUMANKEAP1physical
21516116
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 DPP3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-425, AND MASSSPECTROMETRY.

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