OTUD5_HUMAN - dbPTM
OTUD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTUD5_HUMAN
UniProt AC Q96G74
Protein Name OTU domain-containing protein 5
Gene Name OTUD5
Organism Homo sapiens (Human).
Sequence Length 571
Subcellular Localization
Protein Description Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro)..
Protein Sequence MTILPKKKPPPPDADPANEPPPPGPMPPAPRRGGGVGVGGGGTGVGGGDRDRDSGVVGARPRASPPPQGPLPGPPGALHRWALAVPPGAVAGPRPQQASPPPCGGPGGPGGGPGDALGAAAAGVGAAGVVVGVGGAVGVGGCCSGPGHSKRRRQAPGVGAVGGGSPEREEVGAGYNSEDEYEAAAARIEAMDPATVEQQEHWFEKALRDKKGFIIKQMKEDGACLFRAVADQVYGDQDMHEVVRKHCMDYLMKNADYFSNYVTEDFTTYINRKRKNNCHGNHIEMQAMAEMYNRPVEVYQYSTGTSAVEPINTFHGIHQNEDEPIRVSYHRNIHYNSVVNPNKATIGVGLGLPSFKPGFAEQSLMKNAIKTSEESWIEQQMLEDKKRATDWEATNEAIEEQVARESYLQWLRDQEKQARQVRGPSQPRKASATCSSATAAASSGLEEWTSRSPRQRSSASSPEHPELHAELGMKPPSPGTVLALAKPPSPCAPGTSSQFSAGADRATSPLVSLYPALECRALIQQMSPSAFGLNDWDDDEILASVLAVSQQEYLDSMKKNKVHRDPPPDKS
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
32MethylationPMPPAPRRGGGVGVG
CCCCCCCCCCCCCCC		47.23115368531
54PhosphorylationGGDRDRDSGVVGARP
CCCCCCCCCCCCCCC		34.0928464451
64PhosphorylationVGARPRASPPPQGPL
CCCCCCCCCCCCCCC		38.9429255136
121UbiquitinationGDALGAAAAGVGAAG
HHHHHHHHHCCCCCE		12.2921890473
134UbiquitinationAGVVVGVGGAVGVGG
CEEEEECCCCCCCCC		16.6521890473
165PhosphorylationVGAVGGGSPEREEVG
CCCCCCCCCCHHHCC		27.1919664994
175PhosphorylationREEVGAGYNSEDEYE
HHHCCCCCCCHHHHH		18.2523927012
177PhosphorylationEVGAGYNSEDEYEAA
HCCCCCCCHHHHHHH		37.6323927012
181PhosphorylationGYNSEDEYEAAAARI
CCCCHHHHHHHHHHH		24.1623927012
181 (in isoform 2)Ubiquitination-24.1621890473
205 (in isoform 1)Ubiquitination-43.1621890473
205 (in isoform 3)Ubiquitination-43.1621890473
205UbiquitinationQQEHWFEKALRDKKG
HHHHHHHHHHHCCCC		43.16-
205UbiquitinationQQEHWFEKALRDKKG
HHHHHHHHHHHCCCC		43.1621890473
219UbiquitinationGFIIKQMKEDGACLF
CEEEEEECHHCCHHH		50.59-
219UbiquitinationGFIIKQMKEDGACLF
CEEEEEECHHCCHHH		50.59-
245UbiquitinationDMHEVVRKHCMDYLM
CHHHHHHHHHHHHHH		29.55-
245UbiquitinationDMHEVVRKHCMDYLM
CHHHHHHHHHHHHHH		29.55-
253UbiquitinationHCMDYLMKNADYFSN
HHHHHHHHCCCHHHH		46.5220972266
253UbiquitinationHCMDYLMKNADYFSN
HHHHHHHHCCCHHHH		46.52-
314 (in isoform 2)Ubiquitination-4.2521890473
327 (in isoform 2)Ubiquitination-7.4421890473
338 (in isoform 3)Ubiquitination-4.2521890473
338UbiquitinationRNIHYNSVVNPNKAT
CCCCCCCCCCCCCCE		4.25-
341 (in isoform 2)Ubiquitination-31.8921890473
343UbiquitinationNSVVNPNKATIGVGL
CCCCCCCCCEEEEEC		48.4321890473
343 (in isoform 1)Ubiquitination-48.4321890473
351 (in isoform 3)Ubiquitination-29.6121890473
351UbiquitinationATIGVGLGLPSFKPG
CEEEEECCCCCCCCC		29.61-
354PhosphorylationGVGLGLPSFKPGFAE
EEECCCCCCCCCHHH		51.4424719451
356AcetylationGLGLPSFKPGFAEQS
ECCCCCCCCCHHHHH		48.8726051181
356UbiquitinationGLGLPSFKPGFAEQS
ECCCCCCCCCHHHHH		48.8721906983
356 (in isoform 1)Ubiquitination-48.8721890473
356 (in isoform 2)Ubiquitination-48.8721890473
357 (in isoform 2)Ubiquitination-40.92-
365 (in isoform 3)Ubiquitination-3.6821890473
365UbiquitinationGFAEQSLMKNAIKTS
CHHHHHHHHHHHHHC		3.68-
366UbiquitinationFAEQSLMKNAIKTSE
HHHHHHHHHHHHHCH		48.82-
370UbiquitinationSLMKNAIKTSEESWI
HHHHHHHHHCHHHHH		43.5221906983
370 (in isoform 1)Ubiquitination-43.5221890473
375PhosphorylationAIKTSEESWIEQQML
HHHHCHHHHHHHHHH		29.3321712546
380 (in isoform 3)Ubiquitination-26.1521890473
380UbiquitinationEESWIEQQMLEDKKR
HHHHHHHHHHHHHHH		26.15-
381UbiquitinationESWIEQQMLEDKKRA
HHHHHHHHHHHHHHC		4.41-
385 (in isoform 1)Ubiquitination-34.4821890473
385UbiquitinationEQQMLEDKKRATDWE
HHHHHHHHHHCCCHH		34.4821906983
386UbiquitinationQQMLEDKKRATDWEA
HHHHHHHHHCCCHHH		60.63-
394PhosphorylationRATDWEATNEAIEEQ
HCCCHHHHHHHHHHH		23.2930576142
429UbiquitinationRGPSQPRKASATCSS
CCCCCCCCCCCCCHH		54.07-
431PhosphorylationPSQPRKASATCSSAT
CCCCCCCCCCCHHHH		27.4423927012
433PhosphorylationQPRKASATCSSATAA
CCCCCCCCCHHHHHH		15.4929978859
435PhosphorylationRKASATCSSATAAAS
CCCCCCCHHHHHHHH		20.7523927012
436PhosphorylationKASATCSSATAAASS
CCCCCCHHHHHHHHH		31.6123927012
438PhosphorylationSATCSSATAAASSGL
CCCCHHHHHHHHHCH		20.8323927012
442PhosphorylationSSATAAASSGLEEWT
HHHHHHHHHCHHHHH		21.8823927012
443PhosphorylationSATAAASSGLEEWTS
HHHHHHHHCHHHHHH		42.5423927012
449PhosphorylationSSGLEEWTSRSPRQR
HHCHHHHHHCCHHHH		19.9723927012
450PhosphorylationSGLEEWTSRSPRQRS
HCHHHHHHCCHHHHC		31.6625159151
452PhosphorylationLEEWTSRSPRQRSSA
HHHHHHCCHHHHCCC		24.9723401153
457PhosphorylationSRSPRQRSSASSPEH
HCCHHHHCCCCCCCC		23.1722817900
458PhosphorylationRSPRQRSSASSPEHP
CCHHHHCCCCCCCCH		34.0730576142
460PhosphorylationPRQRSSASSPEHPEL
HHHHCCCCCCCCHHH		48.6629209046
461PhosphorylationRQRSSASSPEHPELH
HHHCCCCCCCCHHHH		33.7422817900
477PhosphorylationELGMKPPSPGTVLAL
HHCCCCCCCCCEEEE		44.4828464451
480PhosphorylationMKPPSPGTVLALAKP
CCCCCCCCEEEECCC		18.7426074081
489PhosphorylationLALAKPPSPCAPGTS
EEECCCCCCCCCCCC		40.9326657352
496PhosphorylationSPCAPGTSSQFSAGA
CCCCCCCCCCCCCCC		28.2330576142
500PhosphorylationPGTSSQFSAGADRAT
CCCCCCCCCCCCCCC		20.3926074081
507PhosphorylationSAGADRATSPLVSLY
CCCCCCCCCCHHHHH		31.6025159151
508PhosphorylationAGADRATSPLVSLYP
CCCCCCCCCHHHHHH		18.4323927012
512PhosphorylationRATSPLVSLYPALEC
CCCCCHHHHHHHHHH		29.8423927012
514PhosphorylationTSPLVSLYPALECRA
CCCHHHHHHHHHHHH		4.4823927012
519GlutathionylationSLYPALECRALIQQM
HHHHHHHHHHHHHHH		2.9922555962
527PhosphorylationRALIQQMSPSAFGLN
HHHHHHHCHHHHCCC		16.0322199227
529PhosphorylationLIQQMSPSAFGLNDW
HHHHHCHHHHCCCCC		28.9928464451
544PhosphorylationDDDEILASVLAVSQQ
CHHHHHHHHHHHHHH		17.7628464451
549PhosphorylationLASVLAVSQQEYLDS
HHHHHHHHHHHHHHH		22.1228348404
556PhosphorylationSQQEYLDSMKKNKVH
HHHHHHHHHHHCCCC		29.8828348404
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
177SPhosphorylationKinaseCK2A1P68400
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
177SPhosphorylation

18669648
177Subiquitylation

18669648
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 OTUD5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF3_HUMANTRAF3physical
17991829
UBC_HUMANUBCphysical
17991829
FLNA_HUMANFLNAphysical
19615732
GPX4_HUMANGPX4physical
19615732
GRB2_HUMANGRB2physical
19615732
GYS1_HUMANGYS1physical
19615732
KPYR_HUMANPKLRphysical
19615732
SET_HUMANSETphysical
19615732
P53_HUMANTP53physical
19615732
SYVC_HUMANVARSphysical
19615732
UBP11_HUMANUSP11physical
19615732
CYBP_HUMANCACYBPphysical
19615732
LANC2_HUMANLANCL2physical
19615732
PYRG2_HUMANCTPS2physical
19615732
LONF2_HUMANLONRF2physical
19615732
UBC_HUMANUBCphysical
22245969
P53_HUMANTP53physical
24143256
TRAF3_HUMANTRAF3physical
24763515
UBC_HUMANUBCphysical
23827681
PDCD5_HUMANPDCD5physical
25499082
P53_HUMANTP53physical
25499082
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 OTUD5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation-dependent activity of the deubiquitinase DUBA.";
Huang O.W., Ma X., Yin J., Flinders J., Maurer T., Kayagaki N.,Phung Q., Bosanac I., Arnott D., Dixit V.M., Hymowitz S.G.,Starovasnik M.A., Cochran A.G.;
Nat. Struct. Mol. Biol. 19:171-175(2012).
Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 172-351 IN COMPLEX WITHUBIQUITIN, CATALYTIC ACTIVITY, FUNCTION, INDUCTION, PHOSPHORYLATION ATSER-64; SER-165; TYR-175; SER-177 AND THR-507, MUTAGENESIS OF SER-177AND CYS-224, ACTIVE SITE, AND MASS SPECTROMETRY.
"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-165 AND SER-177, ANDMASS SPECTROMETRY.
"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-165; TYR-175; THR-507AND SER-508, AND MASS 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-64; SER-165; SER-177 ANDSER-452, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.

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