XPP1_HUMAN - dbPTM
XPP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPP1_HUMAN
UniProt AC Q9NQW7
Protein Name Xaa-Pro aminopeptidase 1
Gene Name XPNPEP1 {ECO:0000312|EMBL:AAH05126.1}
Organism Homo sapiens (Human).
Sequence Length 623
Subcellular Localization Cytoplasm.
Protein Description Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro..
Protein Sequence MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQKQGRQEALEWLIRETQPISKQH
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
6Methylation--MPPKVTSELLRQL
--CCHHHHHHHHHHH		23.70-
20MethylationLRQAMRNSEYVTEPI
HHHHHHCCCCCCCCE		21.68-
54PhosphorylationDCRRAFVSGFDGSAG
CCHHEECCCCCCCCC		27.5624719451
74PhosphorylationEEHAAMWTDGRYFLQ
HHHHCCCCCCHHHHH		18.5824719451
84UbiquitinationRYFLQAAKQMDSNWT
HHHHHHHHHCCCCCE		49.52-
88PhosphorylationQAAKQMDSNWTLMKM
HHHHHCCCCCEEEEC		28.9928857561
91PhosphorylationKQMDSNWTLMKMGLK
HHCCCCCEEEECCCC		22.6429759185
97PhosphorylationWTLMKMGLKDTPTQE
CEEEECCCCCCCCCC		3.9824719451
98UbiquitinationTLMKMGLKDTPTQED
EEEECCCCCCCCCCH		54.5521906983
98 (in isoform 2)Ubiquitination-54.5521906983
117PhosphorylationVLPEGSRVGVDPLII
ECCCCCCCCCCCEEC		10.5724719451
127UbiquitinationDPLIIPTDYWKKMAK
CCEECCHHHHHHHHH		41.77-
127UbiquitinationDPLIIPTDYWKKMAK
CCEECCHHHHHHHHH		41.77-
130 (in isoform 2)Ubiquitination-26.8321906983
130UbiquitinationIIPTDYWKKMAKVLR
ECCHHHHHHHHHHHH		26.8321906983
130AcetylationIIPTDYWKKMAKVLR
ECCHHHHHHHHHHHH		26.8325953088
131UbiquitinationIPTDYWKKMAKVLRS
CCHHHHHHHHHHHHH		29.91-
131AcetylationIPTDYWKKMAKVLRS
CCHHHHHHHHHHHHH		29.9126051181
134AcetylationDYWKKMAKVLRSAGH
HHHHHHHHHHHHCCC		38.0026051181
141UbiquitinationKVLRSAGHHLIPVKE
HHHHHCCCCEEECCH		16.5821906983
141UbiquitinationKVLRSAGHHLIPVKE
HHHHHCCCCEEECCH		16.58-
141 (in isoform 1)Ubiquitination-16.5821906983
147 (in isoform 2)Ubiquitination-35.2121906983
147UbiquitinationGHHLIPVKENLVDKI
CCCEEECCHHHHHHH		35.2121906983
173AcetylationLLTLGLDYTGISWKD
CEEECCCCCCCCHHH		16.35-
173UbiquitinationLLTLGLDYTGISWKD
CEEECCCCCCCCHHH		16.3521906983
173UbiquitinationLLTLGLDYTGISWKD
CEEECCCCCCCCHHH		16.3519608861
173AcetylationLLTLGLDYTGISWKD
CEEECCCCCCCCHHH		16.3519608861
173 (in isoform 1)Ubiquitination-16.3521906983
174UbiquitinationLTLGLDYTGISWKDK
EEECCCCCCCCHHHH		27.92-
190 (in isoform 1)Ubiquitination-15.8321906983
190UbiquitinationADLRLKMAERNVMWF
HHHHHHHHHHHHHHH		15.8321906983
190UbiquitinationADLRLKMAERNVMWF
HHHHHHHHHHHHHHH		15.83-
269AcetylationRIQVHPYKSILSELK
EEECCCHHHHHHHHH		35.1625953088
276UbiquitinationKSILSELKALCADLS
HHHHHHHHHHHCCCC		34.95-
283PhosphorylationKALCADLSPREKVWV
HHHHCCCCCCCCEEE		23.5821815630
287MalonylationADLSPREKVWVSDKA
CCCCCCCCEEECCHH		42.5526320211
287UbiquitinationADLSPREKVWVSDKA
CCCCCCCCEEECCHH		42.55-
287AcetylationADLSPREKVWVSDKA
CCCCCCCCEEECCHH		42.5525825284
296PhosphorylationWVSDKASYAVSETIP
EECCHHHHEEECCCC		18.8422817900
304MalonylationAVSETIPKDHRCCMP
EEECCCCCCCCCCCC		63.4226320211
304AcetylationAVSETIPKDHRCCMP
EEECCCCCCCCCCCC		63.4219608861
312PhosphorylationDHRCCMPYTPICIAK
CCCCCCCCCHHHHHH		9.77-
319UbiquitinationYTPICIAKAVKNSAE
CCHHHHHHHHHCCHH		33.53-
319UbiquitinationYTPICIAKAVKNSAE
CCHHHHHHHHHCCHH		33.53-
319AcetylationYTPICIAKAVKNSAE
CCHHHHHHHHHCCHH		33.5325953088
326PhosphorylationKAVKNSAESEGMRRA
HHHHCCHHCCCCCHH		49.49-
330UbiquitinationNSAESEGMRRAHIKD
CCHHCCCCCHHHHHH		1.99-
330UbiquitinationNSAESEGMRRAHIKD
CCHHCCCCCHHHHHH		1.99-
330AcetylationNSAESEGMRRAHIKD
CCHHCCCCCHHHHHH		1.99-
330AcetylationNSAESEGMRRAHIKD
CCHHCCCCCHHHHHH		1.99-
336UbiquitinationGMRRAHIKDAVALCE
CCCHHHHHHHHHHHH		29.75-
336UbiquitinationGMRRAHIKDAVALCE
CCCHHHHHHHHHHHH		29.75-
339PhosphorylationRAHIKDAVALCELFN
HHHHHHHHHHHHHHH		6.32-
347UbiquitinationALCELFNWLEKEVPK
HHHHHHHHHHHHCCC		9.8819608861
347AcetylationALCELFNWLEKEVPK
HHHHHHHHHHHHCCC		9.8819608861
347AcetylationALCELFNWLEKEVPK
HHHHHHHHHHHHCCC		9.88-
358PhosphorylationEVPKGGVTEISAADK
HCCCCCCCEEEHHHH		30.7624719451
361PhosphorylationKGGVTEISAADKAEE
CCCCCEEEHHHHHHH		15.9224719451
365UbiquitinationTEISAADKAEEFRRQ
CEEEHHHHHHHHHHH		53.63-
365UbiquitinationTEISAADKAEEFRRQ
CEEEHHHHHHHHHHH		53.63-
380O-linked_GlycosylationQADFVDLSFPTISST
HCCEEECCCCCCCCC		25.3923301498
401PhosphorylationIHYAPVPETNRTLSL
EEEECCCCCCCEECC		59.9724719451
404PhosphorylationAPVPETNRTLSLDEV
ECCCCCCCEECCCEE		44.4524719451
405PhosphorylationPVPETNRTLSLDEVY
CCCCCCCEECCCEEE		23.8322817900
407PhosphorylationPETNRTLSLDEVYLI
CCCCCEECCCEEEEE		32.9122817900
408UbiquitinationETNRTLSLDEVYLID
CCCCEECCCEEEEEC		7.97-
408UbiquitinationETNRTLSLDEVYLID
CCCCEECCCEEEEEC		7.97-
416PhosphorylationDEVYLIDSGAQYKDG
CEEEEECCCCCCCCC		29.0922468782
420PhosphorylationLIDSGAQYKDGTTDV
EECCCCCCCCCCCCE		15.5422468782
421UbiquitinationIDSGAQYKDGTTDVT
ECCCCCCCCCCCCEE		37.292190698
424PhosphorylationGAQYKDGTTDVTRTM
CCCCCCCCCCEEEEE		29.9222468782
425PhosphorylationAQYKDGTTDVTRTMH
CCCCCCCCCEEEEEE		33.7222817900
431SulfoxidationTTDVTRTMHFGTPTA
CCCEEEEEECCCCCC		1.9130846556
435PhosphorylationTRTMHFGTPTAYEKE
EEEEECCCCCCCCHH		19.2728985074
437PhosphorylationTMHFGTPTAYEKECF
EEECCCCCCCCHHHH		41.5327732954
439PhosphorylationHFGTPTAYEKECFTY
ECCCCCCCCHHHHHH		29.9727732954
441UbiquitinationGTPTAYEKECFTYVL
CCCCCCCHHHHHHHH		47.29-
460UbiquitinationAVSAAVFPTGTKGHL
EEEEEEECCCCCCHH		24.26-
464UbiquitinationAVFPTGTKGHLLDSF
EEECCCCCCHHHHHH		45.75-
464 (in isoform 1)Ubiquitination-45.7521906983
478PhosphorylationFARSALWDSGLDYLH
HHHHHHHHCCCCCCC		33.4127251275
484UbiquitinationWDSGLDYLHGTGHGV
HHCCCCCCCCCCCCH		2.76-
518SulfoxidationDEPLEAGMIVTDEPG
CCCCCCCCEEECCCC		2.6130846556
546AcetylationVVLVVPVKTKYNFNN
EEEEEEECCCCCCCC		32.9825953088
556PhosphorylationYNFNNRGSLTFEPLT
CCCCCCCCEEEEEEE		22.4625850435
558PhosphorylationFNNRGSLTFEPLTLV
CCCCCCEEEEEEEEE		27.8725850435
565UbiquitinationTFEPLTLVPIQTKMI
EEEEEEEEEECCCCC		3.10-
567UbiquitinationEPLTLVPIQTKMIDV
EEEEEEEECCCCCCH		6.74-
576PhosphorylationTKMIDVDSLTDKECD
CCCCCHHHCCHHCCH		32.77-
591UbiquitinationWLNNYHLTCRDVIGK
HHHHCCEEHHHHHCH		7.68-
599PhosphorylationCRDVIGKELQKQGRQ
HHHHHCHHHHHHHHH		51.74-
623UbiquitinationTQPISKQH-------
HCCCCCCC-------		43.30-
641Ubiquitination-------------------------
-------------------------		-
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 XPP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPP1_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 XPP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPOA2_HUMANPOLA2physical
16169070
PUR8_HUMANADSLphysical
22863883
API5_HUMANAPI5physical
22863883
ASB6_HUMANASB6physical
22863883
DCTP1_HUMANDCTPP1physical
22863883
GNPI1_HUMANGNPDA1physical
22863883
NOL3_HUMANNOL3physical
22863883
NUCB1_HUMANNUCB1physical
22863883
PCNA_HUMANPCNAphysical
22863883
PDE12_HUMANPDE12physical
22863883
PSMD9_HUMANPSMD9physical
22863883
RD23B_HUMANRAD23Bphysical
22863883
UBA6_HUMANUBA6physical
22863883
SYWC_HUMANWARSphysical
22863883
VATA_HUMANATP6V1Aphysical
26344197
XPO2_HUMANCSE1Lphysical
26344197
SYDC_HUMANDARSphysical
26344197
M2GD_HUMANDMGDHphysical
26344197
IRGQ_HUMANIRGQphysical
26344197
SYMC_HUMANMARSphysical
26344197
NAGK_HUMANNAGKphysical
26344197
NTF2_HUMANNUTF2physical
26344197
PUF60_HUMANPUF60physical
26344197
TADBP_HUMANTARDBPphysical
26344197
ELOC_HUMANTCEB1physical
26344197
TIPRL_HUMANTIPRLphysical
26344197
UCHL5_HUMANUCHL5physical
26344197
PFD3_HUMANVBP1physical
26344197
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 XPP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304, AND MASS SPECTROMETRY.

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