OPTN_MOUSE - dbPTM
OPTN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OPTN_MOUSE
UniProt AC Q8K3K8
Protein Name Optineurin
Gene Name Optn
Organism Mus musculus (Mouse).
Sequence Length 584
Subcellular Localization Cytoplasm, perinuclear region . Golgi apparatus . Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle. Recycling endosome. Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes
Protein Description Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation. In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. May constitute a cellular target for adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby affecting cell death..
Protein Sequence MSHQPLSCLTEKGDSPCETPGNGPSNMVHPSLDTFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEKSEKPLEDLTGGYRYPRALEEEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGETEGAMKEMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQCRHGARTSDSDQQTYLFQRGAEDRSWQHGQQPRSIPIHSCPKCGEVLPDIDTLQIHVMDCII
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
7Phosphorylation-MSHQPLSCLTEKGD
-CCCCCCCCCCCCCC		17.4828066266
10PhosphorylationHQPLSCLTEKGDSPC
CCCCCCCCCCCCCCC		39.7228066266
172PhosphorylationADLLGIVSELQLKLN
HHHHHHHHHEEHHHC		30.5718779572
180PhosphorylationELQLKLNSGGSSEDS
HEEHHHCCCCCCCCC		55.7726239621
183PhosphorylationLKLNSGGSSEDSFVE
HHHCCCCCCCCCCEE		33.8026239621
184PhosphorylationKLNSGGSSEDSFVEI
HHCCCCCCCCCCEEE		49.0127742792
187PhosphorylationSGGSSEDSFVEIRMT
CCCCCCCCCEEEEEC		27.4325521595
210PhosphorylationKEMKNCPTPTRTDPI
HHHCCCCCCCCCCCC		39.2225521595
212PhosphorylationMKNCPTPTRTDPISL
HCCCCCCCCCCCCCC		48.9924453211
214PhosphorylationNCPTPTRTDPISLSN
CCCCCCCCCCCCCCC		48.9125263469
218PhosphorylationPTRTDPISLSNCTED
CCCCCCCCCCCCCCC		31.0025521595
220PhosphorylationRTDPISLSNCTEDAR
CCCCCCCCCCCCCHH		24.0624453211
223PhosphorylationPISLSNCTEDARSCA
CCCCCCCCCCHHHCH		40.9427742792
250UbiquitinationCLREGNQKVERLEVA
HHHHCCHHHHHHHHH		50.4927667366
294UbiquitinationDREKEDKGQESVGSE
HHHHHHHCCCCCHHH		49.1327667366
297PhosphorylationKEDKGQESVGSEVET
HHHHCCCCCHHHHHH		24.7230352176
345PhosphorylationQALERKNSATPSELN
HHHHHCCCCCHHHHH		36.2327742792
347PhosphorylationLERKNSATPSELNEK
HHHCCCCCHHHHHHH		27.4522324799
349PhosphorylationRKNSATPSELNEKQE
HCCCCCHHHHHHHHH		50.8118846507
443UbiquitinationAEQALASKQLQMDEM
HHHHHHHHHHCHHHH		49.7922790023
451UbiquitinationQLQMDEMKQTLAKQE
HHCHHHHHHHHHHHH		37.7822790023
504UbiquitinationLQLAILLKENNDIEE
HHHHHHHHHCCCCCC		55.75-
514PhosphorylationNDIEEGGSRQSLMEM
CCCCCCCCHHHHHHH		37.6923684622
517PhosphorylationEEGGSRQSLMEMQCR
CCCCCHHHHHHHHCC		28.68-
529PhosphorylationQCRHGARTSDSDQQT
HCCCCCCCCCHHHHH		36.0327742792
530PhosphorylationCRHGARTSDSDQQTY
CCCCCCCCCHHHHHH		29.5727087446
532PhosphorylationHGARTSDSDQQTYLF
CCCCCCCHHHHHHHH		36.7726745281
536PhosphorylationTSDSDQQTYLFQRGA
CCCHHHHHHHHHCCC		19.2923984901
547PhosphorylationQRGAEDRSWQHGQQP
HCCCCCCCCCCCCCC		43.3329899451
556PhosphorylationQHGQQPRSIPIHSCP
CCCCCCCCCCCCCCC		39.1223684622
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
187SPhosphorylationKinaseTBK1Q9UHD2
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OPTN_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 OPTN_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OPTN_MOUSEOptnphysical
24983867
HACE1_MOUSEHace1physical
25026213
SQSTM_MOUSESqstm1physical
25026213
SEM4A_MOUSESema4aphysical
22465952
RB11A_MOUSERab11aphysical
22465952
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OPTN_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-345, AND MASSSPECTROMETRY.
"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-187; THR-210 ANDSER-218, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory