LONM_YEAST - dbPTM
LONM_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LONM_YEAST
UniProt AC P36775
Protein Name Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120}
Gene Name PIM1 {ECO:0000255|HAMAP-Rule:MF_03120}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1133
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. [PubMed: 15870080]
Protein Sequence MLRTRTTKTLSTVARTTRAIQYYRSIAKTAAVSQRRFASTLTVRDVENIKPSHIIKSPTWQEFQHQLKDPRYMEHFAQLDAQFARHFMATNSGKSILAKDDSTSQKKDEDVKIVPDEKDTDNDVEPTRDDEIVNKDQEGEASKNSRSSASGGGQSSSSRSDSGDGSSKQKPPKDVPEVYPQMLALPIARRPLFPGFYKAVVISDERVMKAIKEMLDRQQPYIGAFMLKNSEEDTDVITDKNDVYDVGVLAQITSAFPSKDEKTGTETMTALLYPHRRIKIDELFPPNEEKEKSKEQAKDTDTETTVVEDANNPEDQESTSPATPKLEDIVVERIPDSELQHHKRVEATEEESEELDDIQEGEDINPTEFLKNYNVSLVNVLNLEDEPFDRKSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEDELQDILSSLNIEHRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQREYYLMEQLKGIKRELGIDDGRDKLIDTYKERIKSLKLPDSVQKIFDDEITKLSTLETSMSEFGVIRNYLDWLTSIPWGKHSKEQYSIPRAKKILDEDHYGMVDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSIARALNRKFFRFSVGGMTDVAEIKGHRRTYIGALPGRVVQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEDKVKIAEQYLVPSAKKSAGLENSHVDMTEDAITALMKYYCRESGVRNLKKHIEKIYRKAALQVVKKLSIEDSPTSSADSKPKESVSSEEKAENNAKSSSEKTKDNNSEKTSDDIEALKTSEKINVSISQKNLKDYVGPPVYTTDRLYETTPPGVVMGLAWTNMGGCSLYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFAKMYLAQKFPENRFFEKASIHLHCPEGATPKDGPSAGVTMATSFLSLALNKSIDPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGLEPLAADWYNDIFQKLFKDVNTKEGNSVWKAEFEILDAKKEKD
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
90PhosphorylationFARHFMATNSGKSIL
HHHHHHHHCCCCEEE		20.3727017623
102PhosphorylationSILAKDDSTSQKKDE
EEECCCCCCCCCCCC		39.8429136822
103PhosphorylationILAKDDSTSQKKDED
EECCCCCCCCCCCCC		42.0229136822
104PhosphorylationLAKDDSTSQKKDEDV
ECCCCCCCCCCCCCC		43.9129136822
120PhosphorylationIVPDEKDTDNDVEPT
ECCCCCCCCCCCCCC		48.0120377248
148PhosphorylationASKNSRSSASGGGQS
CCCCCCCCCCCCCCC		25.9127017623
150PhosphorylationKNSRSSASGGGQSSS
CCCCCCCCCCCCCCC		39.6627017623
155PhosphorylationSASGGGQSSSSRSDS
CCCCCCCCCCCCCCC		35.1527017623
156PhosphorylationASGGGQSSSSRSDSG
CCCCCCCCCCCCCCC		25.1719779198
157PhosphorylationSGGGQSSSSRSDSGD
CCCCCCCCCCCCCCC		34.7130377154
162PhosphorylationSSSSRSDSGDGSSKQ
CCCCCCCCCCCCCCC		39.7830377154
166PhosphorylationRSDSGDGSSKQKPPK
CCCCCCCCCCCCCCC		38.8219779198
167PhosphorylationSDSGDGSSKQKPPKD
CCCCCCCCCCCCCCC		44.6430377154
230PhosphorylationGAFMLKNSEEDTDVI
EEEEECCCCCCCCCC		40.5527017623
234PhosphorylationLKNSEEDTDVITDKN
ECCCCCCCCCCCCCC		35.1327017623
238PhosphorylationEEDTDVITDKNDVYD
CCCCCCCCCCCCCEE		40.5527017623
300PhosphorylationSKEQAKDTDTETTVV
HHHHHCCCCCCCEEE		44.0820377248
391UbiquitinationEDEPFDRKSPVINAL
CCCCCCCCCHHHHHH		62.0424961812
471AcetylationNIEHRLEKSLLVLKK
CHHHHHHHHHHHHHH		51.5024489116
525AcetylationGIDDGRDKLIDTYKE
CCCCCHHHHHHHHHH		46.0824489116
538AcetylationKERIKSLKLPDSVQK
HHHHHHCCCCHHHHH		66.1322865919
545AcetylationKLPDSVQKIFDDEIT
CCCHHHHHHCCCHHH		43.0924489116
584AcetylationIPWGKHSKEQYSIPR
CCCCCCCHHHHCCCH		48.8622865919
607AcetylationHYGMVDVKDRILEFI
CCCCCCHHHHHHHHH		36.5024489116
622AcetylationAVGKLLGKVDGKIIC
HHHHHHCEECCEEEE		36.8025381059
787PhosphorylationAEQYLVPSAKKSAGL
HHHHCCCCHHHCCCC		45.2821126336
846PhosphorylationKKLSIEDSPTSSADS
HHCCCCCCCCCCCCC		19.7921440633
883UbiquitinationTKDNNSEKTSDDIEA
CCCCCCCCCHHHHHH		53.8219722269
892AcetylationSDDIEALKTSEKINV
HHHHHHHHHHCCCCE		57.9924489116
900PhosphorylationTSEKINVSISQKNLK
HHCCCCEEECCCCHH		16.4322369663
902PhosphorylationEKINVSISQKNLKDY
CCCCEEECCCCHHHC		27.8222369663
904AcetylationINVSISQKNLKDYVG
CCEEECCCCHHHCCC		58.4122865919
907AcetylationSISQKNLKDYVGPPV
EECCCCHHHCCCCCE		57.3024489116
988AcetylationAKMYLAQKFPENRFF
HHHHHHHHCCCCCCC		58.2324489116
1129AcetylationEFEILDAKKEKD---
EEEEEHHHHHCC---		62.2224489116
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 LONM_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LONM_YEAST !!
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 LONM_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IDH2_YEASTIDH2physical
11805826
METK1_YEASTSAM1physical
11805826
RLA0_YEASTRPP0physical
16429126
SC61G_YEASTSSS1genetic
9585511
PHB1_YEASTPHB1physical
20150421
PHB2_YEASTPHB2physical
20150421
ATP7_YEASTATP7physical
20150421
CRD1_YEASTCRD1genetic
21825164
PHB1_YEASTPHB1genetic
21825164
PHB2_YEASTPHB2genetic
21825164
LONM_YEASTPIM1physical
22940862
HS104_YEASTHSP104genetic
23220263
PER1_YEASTPER1genetic
27708008
IDH1_YEASTIDH1genetic
27708008
AGP2_YEASTAGP2genetic
27708008
RGD1_YEASTRGD1genetic
27708008
CRD1_YEASTCRD1genetic
27708008
WDR59_YEASTMTC5genetic
27708008
YHH7_YEASTYSC83genetic
27708008
EAF7_YEASTEAF7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LONM_YEAST

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Related Literatures of Post-Translational Modification

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