UBPE_DROME - dbPTM
UBPE_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBPE_DROME
UniProt AC Q24574
Protein Name Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000250|UniProtKB:Q96K76}
Gene Name Usp47 {ECO:0000303|PubMed:27552662, ECO:0000312|FlyBase:FBgn0016756}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1556
Subcellular Localization Nucleus .
Protein Description Ubiquitin-specific protease that deubiquitinates target proteins to regulate different cellular and developmental pathways. [PubMed: 10949024]
Protein Sequence MTDKESEQCTVSVFDQTPGSEQKKINVVVRSHFTVKRVIDLIGTQFSYEKFELLLQPHDNKDLVNLNALESQLMYEVAGFEPQLKNHLILLPSGSWDGDVTKRFELPIKRVVVKKVMKSDGEKAKSPATGEKKKRVVGEKTKKKPASGSSSPSKAKTTSEDSLAKTSISSESSPEKTSKIKTTAAKISKPGSEKAPRASPEECPELSTEINSKNTSSESPVAKKTAKVTSKPTLELLSPIKPSSPIKELDCEPVDTLSKQQLSEQLQLYPQGRNLISPVDDAPSDLFISDAEQLSDDDLALGASASPTMLGPGYDYGAPTGDSDVEGVTGVTDPSTIGTDDGTYPALSNFYRRKYGGDELRAWQRVNTTGADFVSSATTETEAEARQASLGPRGYVGLVNQAMTCYLNSLLQALFMTPEFRNALYRWEFDNDNEAKNIPYQLQKLFLNLQTSPKAAVETTDLTRSFGWDSTEAWQQHDIQELCRVMFDALEHKFKNTKQANLISNLYEGKMNDYVKCLECNTEKTREDTFLDIPLPVRPFGSSSAYGSIEEALRAFVQPETLDGNNQYLCEKCKKKCDAHKGLHFKSFPYILTLHLKRFDFDYQTMHRIKLNDRVTFPQTLNLNTFINRSGNSGEQNSQLNGTVDDCSTADSGSAMEDDNLSSGVVTTASSSQHENDLNDEDEGIDMSSSTSKSAKQGSGPYLYELFAIMIHSGSASGGHYYAYIKDFDNNEWFCFNDQNVTSITQEDIQRSFGGPNGSYYSSAYTSSTNAYMLMYRQVDAKRNELVAKVADFPEHIKTLLPKLHSEEETRVSRLGRHITVTDLALPDLYKPRVYFYNPSLKKMKITRVYVSQSFNINLVLMSAYEMLNVEQFAPLSRCRLVAYNSSMDTIIQSLESCTDPALTELRAAQNYSLDFLLEYRAEDQEFEVYPPNGITWYVFKVDLSTMAMDGPFLVYSAAREREASDVLRRSIALRLHISEQQFLLATVRATVPKAFVSYDPHPTPEALQHLQNMANTQFKSITYFYLNVPNTDAATLEMLGVPTVESVECASGGDVVDAAMMNGVAPGHMSSSNDYDWRRYKRDLVEPMSQPSPSHGHESNSEDSSLSDGDRTLVETDNMAHRGGGDSQVSSTSHSPQLSSPEDEAASHDAMMRVHAYCNGNGSYAAADVVDPLLLPTSTNHFFYATKVECVDVVGTGSSSGHQSDEEAQLRKPTRAYKLLVGTHMRMGAFKKHIEQLIQVPAAHFKLQRKHDNNLSNNQNNSLVHLIEGETLTVELGKTLEPDEFKAKIHFLRLADIDNETSKLPCVCEWVYNANTTAEQAKKELVAKLHRIDAKYATLSVQNCRIWLKGGRIPIKILSDDETLYCDMRSSIAAEFIVQECEEEVDPQPKDDSLTLFVRRWCPAKLEFGKFQEITLDQDSEIRLSLSQISDIPIDKLSYMKLNSNFPCTSISALSVNESSSWYSVPTTLDKYPLNSTQTGNIYLYKDRTVPARELTLEERRLMNAREKARLDRVGCVSTTRYAQRRERALKIYLDSPEKSSNVTASAPMDVHVNN
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
126PhosphorylationSDGEKAKSPATGEKK
CCCCCCCCCCCCCCH
25.3227626673
147PhosphorylationKTKKKPASGSSSPSK
CCCCCCCCCCCCCCC
47.9719429919
149PhosphorylationKKKPASGSSSPSKAK
CCCCCCCCCCCCCCC
25.7519429919
150PhosphorylationKKPASGSSSPSKAKT
CCCCCCCCCCCCCCC
50.2019429919
151PhosphorylationKPASGSSSPSKAKTT
CCCCCCCCCCCCCCC
34.5819429919
153PhosphorylationASGSSSPSKAKTTSE
CCCCCCCCCCCCCCH
47.3919429919
169PhosphorylationSLAKTSISSESSPEK
HHHHHCCCCCCCHHH
28.0227794539
172PhosphorylationKTSISSESSPEKTSK
HHCCCCCCCHHHHCC
53.8119429919
173PhosphorylationTSISSESSPEKTSKI
HCCCCCCCHHHHCCC
32.7819429919
199PhosphorylationSEKAPRASPEECPEL
CCCCCCCCHHHCCCC
33.8428490779
217PhosphorylationINSKNTSSESPVAKK
CCCCCCCCCCCCCHH
39.8029892262
219PhosphorylationSKNTSSESPVAKKTA
CCCCCCCCCCCHHHC
26.9925749252
229PhosphorylationAKKTAKVTSKPTLEL
CHHHCCCCCCCCHHH
30.2628490779
230PhosphorylationKKTAKVTSKPTLELL
HHHCCCCCCCCHHHC
39.3628490779
233PhosphorylationAKVTSKPTLELLSPI
CCCCCCCCHHHCCCC
36.2828490779
238PhosphorylationKPTLELLSPIKPSSP
CCCHHHCCCCCCCCC
36.8819429919
243PhosphorylationLLSPIKPSSPIKELD
HCCCCCCCCCCCCCC
43.6819429919
244PhosphorylationLSPIKPSSPIKELDC
CCCCCCCCCCCCCCC
38.8919429919
256PhosphorylationLDCEPVDTLSKQQLS
CCCCCCCCCCHHHHH
32.9221082442
389PhosphorylationEAEARQASLGPRGYV
HHHHHHHCCCCCCHH
26.0627626673
820PhosphorylationSRLGRHITVTDLALP
HHHCCCEEEECCCCC
15.9521082442
1093PhosphorylationVEPMSQPSPSHGHES
CCCCCCCCCCCCCCC
31.2530478224
1131PhosphorylationGGGDSQVSSTSHSPQ
CCCCCCCCCCCCCCC
21.9122817900
1132PhosphorylationGGDSQVSSTSHSPQL
CCCCCCCCCCCCCCC
34.7622817900
1134PhosphorylationDSQVSSTSHSPQLSS
CCCCCCCCCCCCCCC
24.7422668510
1136PhosphorylationQVSSTSHSPQLSSPE
CCCCCCCCCCCCCCC
17.7022817900
1140PhosphorylationTSHSPQLSSPEDEAA
CCCCCCCCCCCHHHH
38.3022817900
1141PhosphorylationSHSPQLSSPEDEAAS
CCCCCCCCCCHHHHC
40.6822817900
1197PhosphorylationECVDVVGTGSSSGHQ
EEEEEECCCCCCCCC
23.4529892262
1199PhosphorylationVDVVGTGSSSGHQSD
EEEECCCCCCCCCCH
22.5922817900
1200PhosphorylationDVVGTGSSSGHQSDE
EEECCCCCCCCCCHH
41.5029892262
1201PhosphorylationVVGTGSSSGHQSDEE
EECCCCCCCCCCHHH
41.8329892262
1205PhosphorylationGSSSGHQSDEEAQLR
CCCCCCCCHHHHHHC
41.1222817900

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 UBPE_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBPE_DROME !!

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 UBPE_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TTKB_DROMEttkgenetic
18160715
TTKA_DROMEttkgenetic
18160715

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBPE_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-173; SER-238;SER-1131; SER-1132; SER-1140; SER-1141; SER-1199; SER-1201 ANDSER-1205, AND MASS SPECTROMETRY.

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