OTU7B_HUMAN - dbPTM
OTU7B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTU7B_HUMAN
UniProt AC Q6GQQ9
Protein Name OTU domain-containing protein 7B
Gene Name OTUD7B
Organism Homo sapiens (Human).
Sequence Length 843
Subcellular Localization Cytoplasm . Nucleus . Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner.
Protein Description Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections (By similarity). Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B. [PubMed: 26903241 Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2 (By similarity Mediates deubiquitination of EGFR]
Protein Sequence MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKENTKEQAVIPLTDSEYKLLPLHFAVDPGKGWEWGKDDSDNVRLASVILSLEVKLHLLHSYMNVKWIPLSSDAQAPLAQPESPTASAGDEPRSTPESGDSDKESVGSSSTSNEGGRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGSKPGGVGTGLGGSSGTETLEKKKKNSLKSWKGGKEEAAGDGPVSEKPPAESVGNGGSKYSQEVMQSLSILRTAMQGEGKFIFVGTLKMGHRHQYQEEMIQRYLSDAEERFLAEQKQKEAERKIMNGGIGGGPPPAKKPEPDAREEQPTGPPAESRAMAFSTGYPGDFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPPYATFPRQCPPGRPYPHQDSIPSLEPGSHSKDGLHRGALLPPPYRVADSYSNGYREPPEPDGWAGGLRGLPPTQTKCKQPNCSFYGHPETNNFCSCCYREELRRREREPDGELLVHRF
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
2Phosphorylation------MTLDMDAVL
------CCCCHHHHH
31.3126714015
10PhosphorylationLDMDAVLSDFVRSTG
CCHHHHHHHHHHHHC
23.5426714015
30UbiquitinationARDLLEGKNWDVNAA
HHHHHCCCCCCHHHH
45.5529967540
55PhosphorylationHAGNLPPSFSEGSGG
HCCCCCCCCCCCCCC
39.1930576142
57PhosphorylationGNLPPSFSEGSGGSR
CCCCCCCCCCCCCCC
45.4429396449
60PhosphorylationPPSFSEGSGGSRTPE
CCCCCCCCCCCCCCC
35.6129116813
63PhosphorylationFSEGSGGSRTPEKGF
CCCCCCCCCCCCCCC
36.1825159151
65PhosphorylationEGSGGSRTPEKGFSD
CCCCCCCCCCCCCCC
37.1825159151
76PhosphorylationGFSDREPTRPPRPIL
CCCCCCCCCCCCCCC
51.5629496963
93UbiquitinationQDDIVQEKRLSRGIS
CCHHHHHHHHHHHHC
41.3621906983
94UbiquitinationDDIVQEKRLSRGISH
CHHHHHHHHHHHHCH
36.8222817900
98UbiquitinationQEKRLSRGISHASSS
HHHHHHHHHCHHHHH
23.5222817900
100PhosphorylationKRLSRGISHASSSIV
HHHHHHHCHHHHHHH
18.8029255136
103PhosphorylationSRGISHASSSIVSLA
HHHHCHHHHHHHHHH
21.1321712546
104PhosphorylationRGISHASSSIVSLAR
HHHCHHHHHHHHHHH
25.5223911959
105PhosphorylationGISHASSSIVSLARS
HHCHHHHHHHHHHHH
25.2326055452
108PhosphorylationHASSSIVSLARSHVS
HHHHHHHHHHHHHCC
18.0323403867
115PhosphorylationSLARSHVSSNGGGGG
HHHHHHCCCCCCCCC
16.8022798277
134UbiquitinationPLEMPICAFQLPDLT
CCCCCEEEEECCCCE
8.9221890473
144UbiquitinationLPDLTVYNEDFRSFI
CCCCEEECHHHHHHH
37.7222817900
148UbiquitinationTVYNEDFRSFIERDL
EEECHHHHHHHHHHH
42.8722817900
149PhosphorylationVYNEDFRSFIERDLI
EECHHHHHHHHHHHH
30.48-
159PhosphorylationERDLIEQSMLVALEQ
HHHHHHHHHHHHHHH
10.99-
184UbiquitinationDPTSQRLLPLATTGD
CCCCCCEECEEECCC
3.3921890473
218PhosphorylationLMLRKALYALMEKGV
HHHHHHHHHHHHHCC
11.53-
223UbiquitinationALYALMEKGVEKEAL
HHHHHHHHCCCHHHH
55.0521906983
227UbiquitinationLMEKGVEKEALKRRW
HHHHCCCHHHHHHHH
45.9722817900
243UbiquitinationWQQTQQNKESGLVYT
HHHHHHHHHCCCEEC
49.25-
256UbiquitinationYTEDEWQKEWNELIK
ECHHHHHHHHHHHHH
66.8129967540
263UbiquitinationKEWNELIKLASSEPR
HHHHHHHHHHHCCCC
51.1021890473
263UbiquitinationKEWNELIKLASSEPR
HHHHHHHHHHHCCCC
51.1021890473
371PhosphorylationSMEQKENTKEQAVIP
CHHHHCCCCCCEEEE
36.73-
372UbiquitinationMEQKENTKEQAVIPL
HHHHCCCCCCEEEEC
60.4532015554
376UbiquitinationENTKEQAVIPLTDSE
CCCCCCEEEECCCCC
4.6523000965
382UbiquitinationAVIPLTDSEYKLLPL
EEEECCCCCEEEEEE
37.2823000965
385UbiquitinationPLTDSEYKLLPLHFA
ECCCCCEEEEEEEEE
39.2229967540
387UbiquitinationTDSEYKLLPLHFAVD
CCCCEEEEEEEEEEC
3.5723000965
397UbiquitinationHFAVDPGKGWEWGKD
EEEECCCCCCCCCCC
67.2629967540
426UbiquitinationEVKLHLLHSYMNVKW
HHHHHHHHHHCCCEE
24.2023000965
432UbiquitinationLHSYMNVKWIPLSSD
HHHHCCCEEEECCCC
34.1123000965
435UbiquitinationYMNVKWIPLSSDAQA
HCCCEEEECCCCCCC
25.6923000965
437PhosphorylationNVKWIPLSSDAQAPL
CCEEEECCCCCCCCC
22.3330266825
437UbiquitinationNVKWIPLSSDAQAPL
CCEEEECCCCCCCCC
22.3323000965
438PhosphorylationVKWIPLSSDAQAPLA
CEEEECCCCCCCCCC
44.6530266825
441UbiquitinationIPLSSDAQAPLAQPE
EECCCCCCCCCCCCC
48.8023000965
446UbiquitinationDAQAPLAQPESPTAS
CCCCCCCCCCCCCCC
50.4023000965
449PhosphorylationAPLAQPESPTASAGD
CCCCCCCCCCCCCCC
33.9430266825
451PhosphorylationLAQPESPTASAGDEP
CCCCCCCCCCCCCCC
42.3930266825
453PhosphorylationQPESPTASAGDEPRS
CCCCCCCCCCCCCCC
34.9530266825
460PhosphorylationSAGDEPRSTPESGDS
CCCCCCCCCCCCCCC
60.0623927012
461PhosphorylationAGDEPRSTPESGDSD
CCCCCCCCCCCCCCC
32.1523927012
464PhosphorylationEPRSTPESGDSDKES
CCCCCCCCCCCCHHC
49.4523927012
467PhosphorylationSTPESGDSDKESVGS
CCCCCCCCCHHCCCC
54.8523927012
471O-linked_GlycosylationSGDSDKESVGSSSTS
CCCCCHHCCCCCCCC
37.2023301498
471PhosphorylationSGDSDKESVGSSSTS
CCCCCHHCCCCCCCC
37.2023927012
474PhosphorylationSDKESVGSSSTSNEG
CCHHCCCCCCCCCCC
20.9623927012
475PhosphorylationDKESVGSSSTSNEGG
CHHCCCCCCCCCCCC
31.5423927012
476PhosphorylationKESVGSSSTSNEGGR
HHCCCCCCCCCCCCC
37.2423927012
477PhosphorylationESVGSSSTSNEGGRR
HCCCCCCCCCCCCCC
37.2023403867
478PhosphorylationSVGSSSTSNEGGRRK
CCCCCCCCCCCCCCC
34.5323403867
501PhosphorylationKDKKRADSVANKLGS
HHHHHHHHHHHHHHH
23.3423403867
505AcetylationRADSVANKLGSFGKT
HHHHHHHHHHHHHHH
44.4825953088
505UbiquitinationRADSVANKLGSFGKT
HHHHHHHHHHHHHHH
44.4823000965
508PhosphorylationSVANKLGSFGKTLGS
HHHHHHHHHHHHHHH
41.0625849741
511UbiquitinationNKLGSFGKTLGSKLK
HHHHHHHHHHHHHHH
38.2723000965
512PhosphorylationKLGSFGKTLGSKLKK
HHHHHHHHHHHHHHH
36.4126434776
514UbiquitinationGSFGKTLGSKLKKNM
HHHHHHHHHHHHHHC
28.1523000965
515UbiquitinationSFGKTLGSKLKKNMG
HHHHHHHHHHHHHCC
37.6222817900
516UbiquitinationFGKTLGSKLKKNMGG
HHHHHHHHHHHHCCC
63.6323000965
517UbiquitinationGKTLGSKLKKNMGGL
HHHHHHHHHHHCCCC
11.6322817900
520UbiquitinationLGSKLKKNMGGLMHS
HHHHHHHHCCCCCCC
32.5123000965
522UbiquitinationSKLKKNMGGLMHSKG
HHHHHHCCCCCCCCC
35.1622817900
525UbiquitinationKKNMGGLMHSKGSKP
HHHCCCCCCCCCCCC
3.6623000965
527PhosphorylationNMGGLMHSKGSKPGG
HCCCCCCCCCCCCCC
25.4229449344
530PhosphorylationGLMHSKGSKPGGVGT
CCCCCCCCCCCCCCC
39.1430175587
531UbiquitinationLMHSKGSKPGGVGTG
CCCCCCCCCCCCCCC
57.2429967540
536UbiquitinationGSKPGGVGTGLGGSS
CCCCCCCCCCCCCCC
19.8322817900
537PhosphorylationSKPGGVGTGLGGSSG
CCCCCCCCCCCCCCC
27.1627732954
537UbiquitinationSKPGGVGTGLGGSSG
CCCCCCCCCCCCCCC
27.1622817900
542PhosphorylationVGTGLGGSSGTETLE
CCCCCCCCCCCHHHH
24.6429255136
543PhosphorylationGTGLGGSSGTETLEK
CCCCCCCCCCHHHHH
53.6729255136
545PhosphorylationGLGGSSGTETLEKKK
CCCCCCCCHHHHHHH
27.9529255136
547PhosphorylationGGSSGTETLEKKKKN
CCCCCCHHHHHHHHC
39.8029255136
555PhosphorylationLEKKKKNSLKSWKGG
HHHHHHCCCCCCCCC
46.1624719451
565UbiquitinationSWKGGKEEAAGDGPV
CCCCCCCCCCCCCCC
47.5122817900
567UbiquitinationKGGKEEAAGDGPVSE
CCCCCCCCCCCCCCC
21.6422817900
572UbiquitinationEAAGDGPVSEKPPAE
CCCCCCCCCCCCCHH
16.4522817900
574UbiquitinationAGDGPVSEKPPAESV
CCCCCCCCCCCHHHC
70.5822817900
576UbiquitinationDGPVSEKPPAESVGN
CCCCCCCCCHHHCCC
29.3122817900
581UbiquitinationEKPPAESVGNGGSKY
CCCCHHHCCCCCCHH
5.3422817900
586UbiquitinationESVGNGGSKYSQEVM
HHCCCCCCHHHHHHH
29.8022817900
587UbiquitinationSVGNGGSKYSQEVMQ
HCCCCCCHHHHHHHH
52.8022817900
589PhosphorylationGNGGSKYSQEVMQSL
CCCCCHHHHHHHHHH
24.4922210691
595PhosphorylationYSQEVMQSLSILRTA
HHHHHHHHHHHHHHH
13.1422210691
595UbiquitinationYSQEVMQSLSILRTA
HHHHHHHHHHHHHHH
13.1422817900
596UbiquitinationSQEVMQSLSILRTAM
HHHHHHHHHHHHHHH
1.7622817900
631PhosphorylationQEEMIQRYLSDAEER
HHHHHHHHHHHHHHH
8.3229449344
633PhosphorylationEMIQRYLSDAEERFL
HHHHHHHHHHHHHHH
26.3228857561
644UbiquitinationERFLAEQKQKEAERK
HHHHHHHHHHHHHHH
55.6421906983
646UbiquitinationFLAEQKQKEAERKIM
HHHHHHHHHHHHHHH
66.9622817900
651UbiquitinationKQKEAERKIMNGGIG
HHHHHHHHHHCCCCC
37.5022817900
653UbiquitinationKEAERKIMNGGIGGG
HHHHHHHHCCCCCCC
4.2322817900
655UbiquitinationAERKIMNGGIGGGPP
HHHHHHCCCCCCCCC
16.2422817900
660UbiquitinationMNGGIGGGPPPAKKP
HCCCCCCCCCCCCCC
26.7422817900
665UbiquitinationGGGPPPAKKPEPDAR
CCCCCCCCCCCCCCC
74.7122817900
666UbiquitinationGGPPPAKKPEPDARE
CCCCCCCCCCCCCCC
57.6321906983
674UbiquitinationPEPDAREEQPTGPPA
CCCCCCCCCCCCCCH
57.2022817900
675UbiquitinationEPDAREEQPTGPPAE
CCCCCCCCCCCCCHH
35.7822817900
677PhosphorylationDAREEQPTGPPAESR
CCCCCCCCCCCHHHH
63.1123090842
683PhosphorylationPTGPPAESRAMAFST
CCCCCHHHHHCCCCC
27.6923090842
700MethylationPGDFTIPRPSGGGVH
CCCCCCCCCCCCCCC
33.88-
702PhosphorylationDFTIPRPSGGGVHCQ
CCCCCCCCCCCCCCC
51.8828555341
727PhosphorylationCVGGLPPYATFPRQC
CCCCCCCCCCCCCCC
19.1427642862
729PhosphorylationGGLPPYATFPRQCPP
CCCCCCCCCCCCCCC
28.4728348404
740PhosphorylationQCPPGRPYPHQDSIP
CCCCCCCCCCCCCCC
16.4027080861
745PhosphorylationRPYPHQDSIPSLEPG
CCCCCCCCCCCCCCC
29.8123312004
748PhosphorylationPHQDSIPSLEPGSHS
CCCCCCCCCCCCCCC
43.6323312004
753PhosphorylationIPSLEPGSHSKDGLH
CCCCCCCCCCCCCCC
34.9928555341
769PhosphorylationGALLPPPYRVADSYS
CCCCCCCCEECCCCC
24.4028674419
775PhosphorylationPYRVADSYSNGYREP
CCEECCCCCCCCCCC
13.5027642862
779PhosphorylationADSYSNGYREPPEPD
CCCCCCCCCCCCCCC
18.9622817900
808PhosphorylationKCKQPNCSFYGHPET
CCCCCCCCCCCCCCC
28.3022210691
810PhosphorylationKQPNCSFYGHPETNN
CCCCCCCCCCCCCCC
9.7622210691
823PhosphorylationNNFCSCCYREELRRR
CCCCHHHHHHHHHHH
25.9522210691

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 OTU7B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OTU7B_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 OTU7B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHRF2_HUMANSLC9A3R2physical
19615732
NU155_HUMANNUP155physical
19615732
ACAD9_HUMANACAD9physical
19615732
HIF1N_HUMANHIF1ANphysical
19615732
PARK7_HUMANPARK7physical
21097510
EGFR_HUMANEGFRphysical
22179831
UBC_HUMANUBCphysical
20622874
UBE2S_HUMANUBE2Sphysical
20622874
XPO1_HUMANXPO1physical
21888622
UBC_HUMANUBCphysical
23827681
P55G_HUMANPIK3R3physical
25814554
UBC_HUMANUBCphysical
25752577
UBC_HUMANUBCphysical
25723849
AURKA_HUMANAURKAphysical
26446837
UBC_HUMANUBCphysical
26876099
UBC_HUMANUBCphysical
27732584

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 OTU7B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-467, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND MASSSPECTROMETRY.

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