LONM1_ARATH - dbPTM
LONM1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LONM1_ARATH
UniProt AC P93655
Protein Name Lon protease homolog 1, mitochondrial
Gene Name LON1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 940
Subcellular Localization Mitochondrion matrix .
Protein Description ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner..
Protein Sequence MLKLFTSSASRVHHLTPVSRVVGSSPVESPLFKALSQITGWNRRSTSLGHRAFFCSEPTNGEAAAEAETKAVESDSEVSDSKSSSAIVPTNPRPEDCLTVLALPVPHRPLFPGFYMPIYVKDPKVLAALQESRRRQAPYAGAFLLKDDPSADSSSSTDAEKNINELKGKELLNRLHEVGTLAQISSIQGDQVILVGHRRLRIKEMVSEEPLTVKVDHLKDNPFDMDDDVVKATSFEVISTLRDVLKTSSLWRDHVQTYTQHIGDFTYPRLADFGAAICGANRHQAQEVLEELDVHKRLRLTLELMKKEMEISKIQETIAKAIEEKISGEQRRYLLNEQLKAIKKELGVETDDKSALSAKFKERIEPNKEKIPAHVLQVIEEELTKLQLLEASSSEFNVTRNYLDWLTILPWGNYSNENFDVARAQTILDEDHYGLSDVKERILEFIAVGRLRGTSQGKIICLSGPPGVGKTSIGRSIARALNRKFFRFSVGGLADVAEIKGHRRTYVGAMPGKMVQCLKSVGTANPLVLIDEIDKLGRGHAGDPASALLELLDPEQNANFLDHYLDVTIDLSKVLFVCTANVIDMIPNPLLDRMEVISIAGYITDEKVHIARDYLEKTARGDCGVKPEQVEVSDAALLSLIENYCREAGVRNLQKQIEKIYRKIALKLVREGAVPEEPAVASDPEEAEIVADVGESIENHTVEENTVSSAEEPKEEAQTEKIAIETVMIDESNLADYVGKPVFHAEKLYEQTPVGVVMGLAWTSMGGSTLYIETTVVEEGEGKGGLNITGQLGDVMKESAQIAHTVARKIMLEKEPENQFFANSKLHLHVPAGATPKDGPSAGCTMITSLLSLATKKPVRKDLAMTGEVTLTGRILPIGGVKEKTIAARRSQIKTIIFPEANRRDFDELAENVKEGLNVHFVDDYGKIFELAFGYDKQED
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
36PhosphorylationSPLFKALSQITGWNR
CHHHHHHHHHHCCCC
25.1323111157
47PhosphorylationGWNRRSTSLGHRAFF
CCCCCCCCCCCCEEE
33.3323111157
74PhosphorylationAETKAVESDSEVSDS
HHHHHHHCCCCCCCC
39.5819880383
76PhosphorylationTKAVESDSEVSDSKS
HHHHHCCCCCCCCCC
49.5323776212
79PhosphorylationVESDSEVSDSKSSSA
HHCCCCCCCCCCCCC
31.9219376835
81PhosphorylationSDSEVSDSKSSSAIV
CCCCCCCCCCCCCCC
27.2519376835
214AcetylationSEEPLTVKVDHLKDN
CCCCCEEEEEHHCCC
36.3924727099
682PhosphorylationPEEPAVASDPEEAEI
CCCCCCCCCHHHCEE
47.2830291188

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 LONM1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LONM1_ARATH !!

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 LONM1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LONM1_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LONM1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.

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