OTU6B_HUMAN - dbPTM
OTU6B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTU6B_HUMAN
UniProt AC Q8N6M0
Protein Name Deubiquitinase OTUD6B {ECO:0000305}
Gene Name OTUD6B {ECO:0000312|HGNC:HGNC:24281}
Organism Homo sapiens (Human).
Sequence Length 293
Subcellular Localization
Protein Description Isoform 1: Deubiquitinating enzyme that may play a role in the ubiquitin-dependent regulation of protein synthesis, downstream of mTORC1. [PubMed: 21267069]
Protein Sequence MEAVLTEELDEEEQLLRRHRKEKKELQAKIQGMKNAVPKNDKKRRKQLTEDVAKLEKEMEQKHREELEQLKLTTKENKIDSVAVNISNLVLENQPPRISKAQKRREKKAALEKEREERIAEAEIENLTGARHMESEKLAQILAARQLEIKQIPSDGHCMYKAIEDQLKEKDCALTVVALRSQTAEYMQSHVEDFLPFLTNPNTGDMYTPEEFQKYCEDIVNTAAWGGQLELRALSHILQTPIEIIQADSPPIIVGEEYSKKPLILVYMRHAYGLGEHYNSVTRLVNIVTENCS
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-------MEAVLTEE
-------CCCCCCCC		7.2322814378
24UbiquitinationRRHRKEKKELQAKIQ
HHHHHHHHHHHHHHH		65.822097226
29AcetylationEKKELQAKIQGMKNA
HHHHHHHHHHHHHHC		23.7025953088
29UbiquitinationEKKELQAKIQGMKNA
HHHHHHHHHHHHHHC		23.70-
34UbiquitinationQAKIQGMKNAVPKND
HHHHHHHHHCCCCCH		48.88-
46UbiquitinationKNDKKRRKQLTEDVA
CCHHHHHHHHHHHHH		54.41-
54UbiquitinationQLTEDVAKLEKEMEQ
HHHHHHHHHHHHHHH		57.96-
57AcetylationEDVAKLEKEMEQKHR
HHHHHHHHHHHHHHH		73.1818530631
59UbiquitinationVAKLEKEMEQKHREE
HHHHHHHHHHHHHHH		11.08-
64UbiquitinationKEMEQKHREELEQLK
HHHHHHHHHHHHHHH		46.23-
76UbiquitinationQLKLTTKENKIDSVA
HHHCCCCCCCCCEEE		62.76-
81PhosphorylationTKENKIDSVAVNISN
CCCCCCCEEEEEHHH		18.5620068231
87PhosphorylationDSVAVNISNLVLENQ
CEEEEEHHHHHHCCC		20.9320068231
101UbiquitinationQPPRISKAQKRREKK
CCCCCCHHHHHHHHH		17.21-
113UbiquitinationEKKAALEKEREERIA
HHHHHHHHHHHHHHH		64.02-
117PhosphorylationALEKEREERIAEAEI
HHHHHHHHHHHHHHH		56.4620068231
128PhosphorylationEAEIENLTGARHMES
HHHHHHHHCCCCCCH		40.1428555341
137UbiquitinationARHMESEKLAQILAA
CCCCCHHHHHHHHHH		59.40-
143UbiquitinationEKLAQILAARQLEIK
HHHHHHHHHHHCCCE		11.39-
167UbiquitinationYKAIEDQLKEKDCAL
HHHHHHHHHHCCCHH		13.80-
183PhosphorylationVVALRSQTAEYMQSH
HHHHHHHHHHHHHHH		23.78-
189PhosphorylationQTAEYMQSHVEDFLP
HHHHHHHHHHHHHHH		16.99-
272PhosphorylationLVYMRHAYGLGEHYN
EEEHHHHCCCCHHHH		13.5228152594
280PhosphorylationGLGEHYNSVTRLVNI
CCCHHHHHHHHHHHH		20.0720873877
282PhosphorylationGEHYNSVTRLVNIVT
CHHHHHHHHHHHHHC		20.3620873877
293PhosphorylationNIVTENCS-------
HHHCCCCC-------		55.6328348404
302Phosphorylation----------------
----------------		-
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OTU6B_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 OTU6B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASCC3_HUMANASCC3physical
19615732
OTUB1_HUMANOTUB1physical
19615732
RPF2_HUMANRPF2physical
19615732
LYRIC_HUMANMTDHphysical
19615732
OTUB1_HUMANOTUB1physical
22939629
COR1B_HUMANCORO1Bphysical
22863883
MYH9_HUMANMYH9physical
22863883
PARVA_HUMANPARVAphysical
22863883
SPC24_HUMANSPC24physical
22863883
SWP70_HUMANSWAP70physical
22863883
MAP2_HUMANMETAP2physical
26186194
LIMC1_HUMANLIMCH1physical
26186194
GALC_HUMANGALCphysical
26186194
BTBD1_HUMANBTBD1physical
26186194
AP2M1_HUMANAP2M1physical
26344197
APEX1_HUMANAPEX1physical
26344197
BASP1_HUMANBASP1physical
26344197
CHD3_HUMANCHD3physical
26344197
HDDC2_HUMANHDDC2physical
26344197
MCTS1_HUMANMCTS1physical
26344197
OTUB1_HUMANOTUB1physical
26344197
FAK1_HUMANPTK2physical
26344197
GALC_HUMANGALCphysical
28514442
BTBD1_HUMANBTBD1physical
28514442
LIMC1_HUMANLIMCH1physical
28514442
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 OTU6B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-272, AND MASSSPECTROMETRY.

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