UBE2O_MOUSE - dbPTM
UBE2O_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBE2O_MOUSE
UniProt AC Q6ZPJ3
Protein Name (E3-independent) E2 ubiquitin-conjugating enzyme UBE2O
Gene Name Ube2o
Organism Mus musculus (Mouse).
Sequence Length 1288
Subcellular Localization Cytoplasm . Nucleus . Mainly localizes to the cytoplasm.
Protein Description E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins. Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity. Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis. Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location. Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly..
Protein Sequence MADPAAPAPAQAQAAAAPTPAAAPAAAAPPPAPATDSASGPSSDSGPEAGSQRLLFSHDLVSGRYRGSVHFGLVRLIHGEDSDSEGDDDGRGSSGCSEAGGAGHEEGRASPLRRGYVRVQWYPEGVKQHVKETKLKLEDRSVVPRDVVRHMRSTDSQCGTVIDVNIDCAVKLIGTNCIIYPVNSKDLQHIWPFMYGDYIAYDCWLGKVYDLKNQIILKLSNGARCSMNTEDGAKLYDVCPHVSDSGLFFDDSYGFYPGQVLIGPAKIFSSVQWLSGVKPVLSTKSKFRVVVEEVQVVELKVTWITKSFCPGGTDSVSPPPSIITQENLGRVKRLGCFDHAQRQLGERCLYVFPAKVEPAKIAWECPEKNCAQGEGSMAKKVKRLLKKQVVRIMSCTPDTQCPRDHSMEDPDKKGEARAGSEIGSASPEEQPDGSASPVEMQDEGSEELQETCEPLPPFLLKEGGDDGLHSAEQDADDEAADDTDDTSSVTSSASSTTSSQSGSGTGRKKSIPLSIKNLKRKHKRKKNKVTRDFKPGDRVAVEVVTTMTSADVMWQDGSVECNIRSNDLFPVHHLDNNEFCPGDFVVDKRVQSCPDPAVYGVVQSGDHVGRTCMVKWFKLRPSGDDVELIGEEEDVSVYDIADHPDFRFRTTDIVIRIGNTEDGALPKEDEPSVGQVARVDVSSKVEVVWADNSKTIILPQHLYNIESEIEESDYDSVEGSSSGASSDEWEDDSDSWETDNGLVDDEHPKIEELAAILPAEQPTAPEEDKGVVISEEAATAAIQGAVAMAAPVAGLMEKAGKDGPPKSFRELKEAIKILESLKNMTVEQLLTGSPTSPTVEPEKPTREKKFLDDIKKLQENLKKTLDNVAIAEEEKMEAVPDTERKEEKPEVQSPVKAEWPSETPVLCQQCGGRPGVTFTSAKGEVFSVLEFAPSNHSFKKIEFQPPEAKKFFSTVRKEMALLATSLPDGIMVKTFEDRMDLFSALIKGPTRTPYEDGLYLFDIQLPNIYPAVPPHFCYLSQCSGRLNPNLYDNGKVCVSLLGTWIGKGTERWTSKSSLLQVLISIQGLILVNEPYYNEAGFDSDRGLQEGYENSRCYNEMALIRVVQSMTQLVRRPPEVFEQEIRQHFSVGGWRLVNRIESWLETHAMQERAQVMPNGALKDSSSLEPMAAAELSDSGREEPEDVGMAPGEASQGSDSEGGAQGPASASRDHTEQTETAPDASAPPSVRPKRRRKSYRSFLPEKSGYPDIGFPLFPLSKGFIKSIRGVLTQFRAALLEAGMPESTEDK
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
43PhosphorylationDSASGPSSDSGPEAG
CCCCCCCCCCCCCCC
38.6425338131
45PhosphorylationASGPSSDSGPEAGSQ
CCCCCCCCCCCCCCC
59.1925338131
51PhosphorylationDSGPEAGSQRLLFSH
CCCCCCCCCEEEEEE
21.1225338131
68PhosphorylationVSGRYRGSVHFGLVR
CCCCCCCEEEEEEEE
11.9226824392
82PhosphorylationRLIHGEDSDSEGDDD
EEECCCCCCCCCCCC
38.4425521595
84PhosphorylationIHGEDSDSEGDDDGR
ECCCCCCCCCCCCCC
47.6425521595
93PhosphorylationGDDDGRGSSGCSEAG
CCCCCCCCCCCCCCC
23.3822802335
94PhosphorylationDDDGRGSSGCSEAGG
CCCCCCCCCCCCCCC
46.7921659605
97PhosphorylationGRGSSGCSEAGGAGH
CCCCCCCCCCCCCCC
33.7227087446
110PhosphorylationGHEEGRASPLRRGYV
CCCCCCCCCCCCCEE
24.0922817900
127UbiquitinationQWYPEGVKQHVKETK
EECCHHHHHHHHHCC
45.6122790023
131UbiquitinationEGVKQHVKETKLKLE
HHHHHHHHHCCCCCC
58.50-
136UbiquitinationHVKETKLKLEDRSVV
HHHHCCCCCCCCCCC
51.9227667366
171UbiquitinationVNIDCAVKLIGTNCI
EECCCEEEEECCCEE
18.83-
212UbiquitinationLGKVYDLKNQIILKL
CCEEEECCCCEEEEE
43.8622790023
255UbiquitinationFFDDSYGFYPGQVLI
EECCCCCCCCCCEEE
5.1627667366
269PhosphorylationIGPAKIFSSVQWLSG
EECHHHHHCCHHHHC
32.83-
298UbiquitinationVEEVQVVELKVTWIT
EEEEEEEEEEEEEEE
43.9727667366
383UbiquitinationSMAKKVKRLLKKQVV
HHHHHHHHHHHHHCE
48.5227667366
393UbiquitinationKKQVVRIMSCTPDTQ
HHHCEEEEECCCCCC
1.5627667366
394PhosphorylationKQVVRIMSCTPDTQC
HHCEEEEECCCCCCC
16.6825521595
396PhosphorylationVVRIMSCTPDTQCPR
CEEEEECCCCCCCCC
19.5225367039
399PhosphorylationIMSCTPDTQCPRDHS
EEECCCCCCCCCCCC
33.0225367039
406PhosphorylationTQCPRDHSMEDPDKK
CCCCCCCCCCCCCCC
28.3125521595
420PhosphorylationKGEARAGSEIGSASP
CCCCCCCCCCCCCCC
25.6725293948
424PhosphorylationRAGSEIGSASPEEQP
CCCCCCCCCCCCCCC
31.1019060867
426PhosphorylationGSEIGSASPEEQPDG
CCCCCCCCCCCCCCC
34.2422817900
430UbiquitinationGSASPEEQPDGSASP
CCCCCCCCCCCCCCC
39.4627667366
434PhosphorylationPEEQPDGSASPVEMQ
CCCCCCCCCCCCCCC
32.7125293948
436PhosphorylationEQPDGSASPVEMQDE
CCCCCCCCCCCCCCC
31.0422817900
445PhosphorylationVEMQDEGSEELQETC
CCCCCCCCHHHHHHC
26.3321183079
451PhosphorylationGSEELQETCEPLPPF
CCHHHHHHCCCCCCE
14.8125293948
470PhosphorylationGGDDGLHSAEQDADD
CCCCCCCCCCCCCCC
38.2526525534
483PhosphorylationDDEAADDTDDTSSVT
CCCCCCCCCCCCCEE
36.0022817900
486PhosphorylationAADDTDDTSSVTSSA
CCCCCCCCCCEECCC
26.22-
487PhosphorylationADDTDDTSSVTSSAS
CCCCCCCCCEECCCC
29.7922817900
488PhosphorylationDDTDDTSSVTSSASS
CCCCCCCCEECCCCC
31.35-
491UbiquitinationDDTSSVTSSASSTTS
CCCCCEECCCCCCCC
23.0427667366
492PhosphorylationDTSSVTSSASSTTSS
CCCCEECCCCCCCCC
23.8627087446
494PhosphorylationSSVTSSASSTTSSQS
CCEECCCCCCCCCCC
30.11-
501PhosphorylationSSTTSSQSGSGTGRK
CCCCCCCCCCCCCCC
36.55-
510PhosphorylationSGTGRKKSIPLSIKN
CCCCCCCCCCCHHHH
32.2625521595
514PhosphorylationRKKSIPLSIKNLKRK
CCCCCCCHHHHHHHH
26.6025619855
516UbiquitinationKSIPLSIKNLKRKHK
CCCCCHHHHHHHHHH
53.5022790023
588UbiquitinationPGDFVVDKRVQSCPD
CCCEEEECCCCCCCC
42.7422790023
638PhosphorylationEEEDVSVYDIADHPD
CCCCCEEEECCCCCC
8.3022817900
667UbiquitinationTEDGALPKEDEPSVG
CCCCCCCCCCCCCCC
77.8522790023
706UbiquitinationPQHLYNIESEIEESD
CHHHCCCCCCCCCCC
38.3927667366
787UbiquitinationAAIQGAVAMAAPVAG
HHHHHHHHHHHHHHH
4.9527667366
812UbiquitinationPKSFRELKEAIKILE
CHHHHHHHHHHHHHH
40.1122790023
816UbiquitinationRELKEAIKILESLKN
HHHHHHHHHHHHHCC
48.5722790023
822UbiquitinationIKILESLKNMTVEQL
HHHHHHHCCCCHHHH
54.6922790023
824OxidationILESLKNMTVEQLLT
HHHHHCCCCHHHHHH
4.2017242355
825PhosphorylationLESLKNMTVEQLLTG
HHHHCCCCHHHHHHC
30.2224925903
830UbiquitinationNMTVEQLLTGSPTSP
CCCHHHHHHCCCCCC
5.2127667366
831PhosphorylationMTVEQLLTGSPTSPT
CCHHHHHHCCCCCCC
44.1824925903
833PhosphorylationVEQLLTGSPTSPTVE
HHHHHHCCCCCCCCC
21.5525521595
835PhosphorylationQLLTGSPTSPTVEPE
HHHHCCCCCCCCCCC
49.3825521595
836PhosphorylationLLTGSPTSPTVEPEK
HHHCCCCCCCCCCCC
23.2025521595
838PhosphorylationTGSPTSPTVEPEKPT
HCCCCCCCCCCCCCC
36.9525521595
843UbiquitinationSPTVEPEKPTREKKF
CCCCCCCCCCCHHHH
63.5022790023
845PhosphorylationTVEPEKPTREKKFLD
CCCCCCCCCHHHHHH
63.6325619855
849UbiquitinationEKPTREKKFLDDIKK
CCCCCHHHHHHHHHH
46.5422790023
855UbiquitinationKKFLDDIKKLQENLK
HHHHHHHHHHHHHHH
55.1927667366
863UbiquitinationKLQENLKKTLDNVAI
HHHHHHHHHHHHHHH
58.4422790023
864PhosphorylationLQENLKKTLDNVAIA
HHHHHHHHHHHHHHH
37.4429899451
882PhosphorylationKMEAVPDTERKEEKP
HHHCCCCCCCCCCCC
31.4529899451
893PhosphorylationEEKPEVQSPVKAEWP
CCCCCCCCCCCCCCC
36.5125521595
901PhosphorylationPVKAEWPSETPVLCQ
CCCCCCCCCCCEEHH
55.9925777480
903PhosphorylationKAEWPSETPVLCQQC
CCCCCCCCCEEHHHC
24.0425777480
915UbiquitinationQQCGGRPGVTFTSAK
HHCCCCCCEEEECCC
29.7227667366
917PhosphorylationCGGRPGVTFTSAKGE
CCCCCCEEEECCCCC
27.4125777480
919PhosphorylationGRPGVTFTSAKGEVF
CCCCEEEECCCCCEE
20.5725777480
920PhosphorylationRPGVTFTSAKGEVFS
CCCEEEECCCCCEEE
24.6425777480
925UbiquitinationFTSAKGEVFSVLEFA
EECCCCCEEEEEEEC
6.2127667366
940UbiquitinationPSNHSFKKIEFQPPE
CCCCCCCEEEECCHH
45.5222790023
950UbiquitinationFQPPEAKKFFSTVRK
ECCHHHHHHHHHHHH
59.7027667366
962UbiquitinationVRKEMALLATSLPDG
HHHHHHHHHHCCCCC
3.3827667366
987UbiquitinationDLFSALIKGPTRTPY
HHHHHHHCCCCCCCC
60.7422790023
1108PhosphorylationALIRVVQSMTQLVRR
HHHHHHHHHHHHHHC
16.5220531401
1110PhosphorylationIRVVQSMTQLVRRPP
HHHHHHHHHHHHCCH
24.8120531401
1163PhosphorylationPNGALKDSSSLEPMA
CCCCCCCCCCCCHHH
21.9024759943
1164PhosphorylationNGALKDSSSLEPMAA
CCCCCCCCCCCHHHH
49.4224759943
1165PhosphorylationGALKDSSSLEPMAAA
CCCCCCCCCCHHHHH
40.4825521595
1175PhosphorylationPMAAAELSDSGREEP
HHHHHHCCCCCCCCC
22.6425619855
1177PhosphorylationAAAELSDSGREEPED
HHHHCCCCCCCCCCC
36.0525619855
1193PhosphorylationGMAPGEASQGSDSEG
CCCCCCCCCCCCCCC
30.6721082442
1196PhosphorylationPGEASQGSDSEGGAQ
CCCCCCCCCCCCCCC
30.2625521595
1198PhosphorylationEASQGSDSEGGAQGP
CCCCCCCCCCCCCCC
39.5825619855
1207PhosphorylationGGAQGPASASRDHTE
CCCCCCCCCCCCCCC
29.8825619855
1209PhosphorylationAQGPASASRDHTEQT
CCCCCCCCCCCCCCC
35.4325619855
1223PhosphorylationTETAPDASAPPSVRP
CCCCCCCCCCCCCCC
49.0028066266
1227PhosphorylationPDASAPPSVRPKRRR
CCCCCCCCCCCCCCH
29.6923684622
1236PhosphorylationRPKRRRKSYRSFLPE
CCCCCHHHHHHHCCC
24.7822324799
1237PhosphorylationPKRRRKSYRSFLPEK
CCCCHHHHHHHCCCC
17.2029472430
1238UbiquitinationKRRRKSYRSFLPEKS
CCCHHHHHHHCCCCC
28.2027667366
1239PhosphorylationRRRKSYRSFLPEKSG
CCHHHHHHHCCCCCC
23.9326643407
1259UbiquitinationFPLFPLSKGFIKSIR
CCCCCCCHHHHHHHH
66.57-
1263UbiquitinationPLSKGFIKSIRGVLT
CCCHHHHHHHHHHHH
37.2527667366

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 UBE2O_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBE2O_MOUSE !!

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 UBE2O_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPNE1_HUMANCPNE1physical
12522145
CPNE4_HUMANCPNE4physical
12522145

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBE2O_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84 AND SER-893,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 ANDSER-836, AND MASS SPECTROMETRY.

TOP