OTUD4_MOUSE - dbPTM
OTUD4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTUD4_MOUSE
UniProt AC B2RRE7
Protein Name OTU domain-containing protein 4 {ECO:0000250|UniProtKB:Q01804}
Gene Name Otud4 {ECO:0000312|EMBL:AAI38374.1, ECO:0000312|MGI:MGI:1098801}
Organism Mus musculus (Mouse).
Sequence Length 1107
Subcellular Localization Cytoplasm . Nucleus . Primarily cytoplasmic.
Protein Description Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. May negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Upon phosphorylation at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like receptor signaling pathway, specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. [PubMed: 29395066 Independently of the catalytic activity, acts as a scaffold for alternative deubiquitinases to assemble specific deubiquitinase-substrate complexes. Associates with USP7 and USP9X deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby promoting the repair of alkylated DNA lesions (By similarity]
Protein Sequence MEAAVGAPDGVDQGGVGPLEDETPMDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYPITYKDSSAMCQSLLYELLYEKVFKTDVSKIMMGLEASEVAEESNSEISDSEDDSCKSKSTAATDVNGFKPSGSENPKNNGNSADLPLSRKVLKSLNPAVYRNVEYEIWLKSKQAQQKRDYSIAAGLQYEVGDKCHQVRLDHNGKLSNADIHGVHSENGLVLSEELGKKHTPKNLKPPPPESWNTVSGKKMKKPNSGQNFHSDTDYRGPKNLNKPIKAPSALPPRLQHPSSGVRQHAFSSHSTGSQSQKSSSEHKNLSRMPSQITRKPDRERAEDFDHVSRESYYFGLSPEERREKQAIEESRLLYEIQNRDEQAFPALSSSSVSQSPSQNSNACVPRKSSHARDRKGSMRRADAEERKDKDSLRGHTHVDKKPEPSTLEISDDKCTRVSSPSKSKKECPSPVEQKPAEHIPLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVPAQIPILSVTQTTGPDAAVSQAHLTPSPVPVSIQAVNQPLMPLPQTMSLYQDPLYPGFPCSEKGDRAIAPPYSLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYMAACRMYPKVPVPVYPQNTWFQEAPPAQSESDCPCTDAHYSLHPEASVNGQMPQAEMGPPAFASPLVIPPSQVSEGHGQLSYQPELESENPGQLLHAEYEESLSGKNMYPQQSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFVENPVMRQNIVLPPDDKGELDLPLENLDLSKECDSVSAVDEFPDARVEGAHSLSAASVSSKHEGRVEQSSQTRKADIDLASGSSAVEGKGHPPTQILNREREPGSAEPEPKRTIQSLKEKPEKVKDPKTAADVVSPGANSVDRLQRPKEESSEDENEVSNILRSGRSKQFYNQTYGSRKYKSDWGSSGRGGYQHVRGEESWKGQPNRSRDEGYQYHRHVRGRPYRGDRRRSGMGDGHRGQHT
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
1Acetylation-------MEAAVGAP
-------CCCCCCCC		36.30-
41UbiquitinationLYRKLVAKDGSCLFR
HHHHHHCCCCCHHHH		55.96-
120PhosphorylationYRKDFVIYQEPNVSP
HCCCEEEEECCCCCH		11.0925777480
126PhosphorylationIYQEPNVSPSHVTEN
EEECCCCCHHHCCCC		27.5926745281
128PhosphorylationQEPNVSPSHVTENNF
ECCCCCHHHCCCCCC		24.0823984901
131PhosphorylationNVSPSHVTENNFPEK
CCCHHHCCCCCCCCE		27.8023984901
166PhosphorylationDSSAMCQSLLYELLY
CHHHHHHHHHHHHHH		18.53-
169PhosphorylationAMCQSLLYELLYEKV
HHHHHHHHHHHHHHH		15.15-
175UbiquitinationLYELLYEKVFKTDVS
HHHHHHHHHHCCCHH		39.14-
199PhosphorylationEVAEESNSEISDSED
HHHHHHCCCCCCCCC		45.66-
202PhosphorylationEESNSEISDSEDDSC
HHHCCCCCCCCCCCC		30.9129395066
204PhosphorylationSNSEISDSEDDSCKS
HCCCCCCCCCCCCCC		35.81-
247UbiquitinationPLSRKVLKSLNPAVY
CHHHHHHHHCCHHHH		56.75-
282PhosphorylationSIAAGLQYEVGDKCH
CHHHCCEEEECCCEE		20.0226239621
287UbiquitinationLQYEVGDKCHQVRLD
CEEEECCCEEEEEEC		27.9022790023
298UbiquitinationVRLDHNGKLSNADIH
EEECCCCCCCCCEEC		54.80-
329UbiquitinationKHTPKNLKPPPPESW
CCCCCCCCCCCCCCC		65.9422790023
340PhosphorylationPESWNTVSGKKMKKP
CCCCCCCCCCCCCCC		42.74-
342AcetylationSWNTVSGKKMKKPNS
CCCCCCCCCCCCCCC		42.03130119
373PhosphorylationNKPIKAPSALPPRLQ
CCCCCCCCCCCCCCC		47.5028066266
400PhosphorylationSHSTGSQSQKSSSEH
CCCCCCCCCCCHHHC		41.0729514104
415PhosphorylationKNLSRMPSQITRKPD
CCHHCCCHHHCCCCC		25.5228418008
418PhosphorylationSRMPSQITRKPDRER
HCCCHHHCCCCCHHH		25.6325367039
436PhosphorylationFDHVSRESYYFGLSP
CCCCCHHHHHCCCCH		24.8323984901
437PhosphorylationDHVSRESYYFGLSPE
CCCCHHHHHCCCCHH		9.69-
438PhosphorylationHVSRESYYFGLSPEE
CCCHHHHHCCCCHHH		10.6417947660
442PhosphorylationESYYFGLSPEERREK
HHHHCCCCHHHHHHH		30.5526824392
459PhosphorylationIEESRLLYEIQNRDE
HHHHHHHHHHHCCCC		18.6425159016
478PhosphorylationALSSSSVSQSPSQNS
CCCCCCCCCCCCCCC		27.2125619855
480PhosphorylationSSSSVSQSPSQNSNA
CCCCCCCCCCCCCCC		21.0025619855
482PhosphorylationSSVSQSPSQNSNACV
CCCCCCCCCCCCCCC		47.4425619855
485PhosphorylationSQSPSQNSNACVPRK
CCCCCCCCCCCCCCC		20.4025619855
493PhosphorylationNACVPRKSSHARDRK
CCCCCCCCHHHCCCC		28.7430387612
502PhosphorylationHARDRKGSMRRADAE
HHCCCCCCCCHHHHH		16.49-
544PhosphorylationDKCTRVSSPSKSKKE
CCCCCCCCCCCCCCC		30.2727149854
554PhosphorylationKSKKECPSPVEQKPA
CCCCCCCCCCCCCCH		53.9223375375
730PhosphorylationYMAACRMYPKVPVPV
HHHHHHCCCCCCCCC		4.7920531401
895PhosphorylationPLENLDLSKECDSVS
CHHHCCCCCCCCCCC		26.52-
900PhosphorylationDLSKECDSVSAVDEF
CCCCCCCCCCCCCCC		29.6325619855
902PhosphorylationSKECDSVSAVDEFPD
CCCCCCCCCCCCCCC		26.9025619855
917PhosphorylationARVEGAHSLSAASVS
HHHCCCHHCCCHHCC		24.4020531401
919PhosphorylationVEGAHSLSAASVSSK
HCCCHHCCCHHCCCC		25.4625338131
970PhosphorylationNREREPGSAEPEPKR
CCCCCCCCCCCCCHH		39.9327149854
981PhosphorylationEPKRTIQSLKEKPEK
CCHHHHHHHHHCCHH		37.2429176673
994PhosphorylationEKVKDPKTAADVVSP
HHCCCCCCHHHHHCC		32.2525619855
999PhosphorylationPKTAADVVSPGANSV
CCCHHHHHCCCCCHH		6.1824719451
1000PhosphorylationKTAADVVSPGANSVD
CCHHHHHCCCCCHHH		19.9125521595
1005PhosphorylationVVSPGANSVDRLQRP
HHCCCCCHHHHCCCC		25.5121082442
1015PhosphorylationRLQRPKEESSEDENE
HCCCCCCCCCCCHHH		66.7424719451
1016PhosphorylationLQRPKEESSEDENEV
CCCCCCCCCCCHHHH		39.8718388127
1017PhosphorylationQRPKEESSEDENEVS
CCCCCCCCCCHHHHH		52.9618388127
1024PhosphorylationSEDENEVSNILRSGR
CCCHHHHHHHHHHCC		16.3925619855
1040PhosphorylationKQFYNQTYGSRKYKS
HHHHHCCCCCEECCC		11.8828285833
1042PhosphorylationFYNQTYGSRKYKSDW
HHHCCCCCEECCCCC		18.3827566939
1054MethylationSDWGSSGRGGYQHVR
CCCCCCCCCCCCCCC		36.9930760015
1054DimethylationSDWGSSGRGGYQHVR
CCCCCCCCCCCCCCC		36.99-
1073PhosphorylationWKGQPNRSRDEGYQY
CCCCCCCCHHHCCCE		51.2029899451
1080PhosphorylationSRDEGYQYHRHVRGR
CHHHCCCEEHHHCCC		7.7329514104
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 OTUD4_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
63KPhosphorylation

29395066
63Kubiquitylation

29395066
202SPhosphorylation

29395066
202Subiquitylation

29395066
204SPhosphorylation

29395066
204Subiquitylation

29395066
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 OTUD4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of OTUD4_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OTUD4_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016 AND SER-1017, ANDMASS SPECTROMETRY.
"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-1016 AND SER-1017, ANDMASS 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-1000; SER-1005; SER-1016AND SER-1017, AND MASS SPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-438, AND MASSSPECTROMETRY.

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