LETM1_HUMAN - dbPTM
LETM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LETM1_HUMAN
UniProt AC O95202
Protein Name Mitochondrial proton/calcium exchanger protein {ECO:0000305}
Gene Name LETM1 {ECO:0000312|HGNC:HGNC:6556}
Organism Homo sapiens (Human).
Sequence Length 739
Subcellular Localization Mitochondrion inner membrane
Single-pass membrane protein .
Protein Description Mitochondrial proton/calcium antiporter that mediates proton-dependent calcium efflux from mitochondrion. [PubMed: 19797662 Crucial for the maintenance of mitochondrial tubular networks and for the assembly of the supercomplexes of the respiratory chain]
Protein Sequence MASILLRSCRGRAPARLPPPPRYTVPRGSPGDPAHLSCASTLGLRNCLNVPFGCCTPIHPVYTSSRGDHLGCWALRPECLRIVSRAPWTSTSVGFVAVGPQCLPVRGWHSSRPVRDDSVVEKSLKSLKDKNKKLEEGGPVYSPPAEVVVKKSLGQRVLDELKHYYHGFRLLWIDTKIAARMLWRILNGHSLTRRERRQFLRICADLFRLVPFLVFVVVPFMEFLLPVAVKLFPNMLPSTFETQSLKEERLKKELRVKLELAKFLQDTIEEMALKNKAAKGSATKDFSVFFQKIRETGERPSNEEIMRFSKLFEDELTLDNLTRPQLVALCKLLELQSIGTNNFLRFQLTMRLRSIKADDKLIAEEGVDSLNVKELQAACRARGMRALGVTEDRLRGQLKQWLDLHLHQEIPTSLLILSRAMYLPDTLSPADQLKSTLQTLPEIVAKEAQVKVAEVEGEQVDNKAKLEATLQEEAAIQQEHREKELQKRSEVAKDFEPERVVAAPQRPGTEPQPEMPDTVLQSETLKDTAPVLEGLKEEEITKEEIDILSDACSKLQEQKKSLTKEKEELELLKEDVQDYSEDLQEIKKELSKTGEEKYVEESKASKRLTKRVQQMIGQIDGLISQLEMDQQAGKLAPANGMPTGENVISVAELINAMKQVKHIPESKLTSLAAALDENKDGKVNIDDLVKVIELVDKEDVHISTSQVAEIVATLEKEEKVEEKEKAKEKAEKEVAEVKS
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
3Phosphorylation-----MASILLRSCR
-----CCHHHHHHCC		16.69-
8PhosphorylationMASILLRSCRGRAPA
CCHHHHHHCCCCCCC		14.24-
112UbiquitinationVRGWHSSRPVRDDSV
CCCCCCCCCCCCCHH		36.4321890473
118PhosphorylationSRPVRDDSVVEKSLK
CCCCCCCHHHHHHHH		32.1426074081
123PhosphorylationDDSVVEKSLKSLKDK
CCHHHHHHHHHHHHH		27.7626074081
126PhosphorylationVVEKSLKSLKDKNKK
HHHHHHHHHHHHCCC		46.0426074081
141PhosphorylationLEEGGPVYSPPAEVV
HHCCCCCCCCCHHHE		20.7025884760
142PhosphorylationEEGGPVYSPPAEVVV
HCCCCCCCCCHHHEE		25.3320068231
1502-HydroxyisobutyrylationPPAEVVVKKSLGQRV
CCHHHEEECHHHHHH		25.65-
1622-HydroxyisobutyrylationQRVLDELKHYYHGFR
HHHHHHHHHHHHHCE		27.75-
162AcetylationQRVLDELKHYYHGFR
HHHHHHHHHHHHHCE		27.7527452117
164PhosphorylationVLDELKHYYHGFRLL
HHHHHHHHHHHCEEE		8.79-
175PhosphorylationFRLLWIDTKIAARML
CEEEEEHHHHHHHHH		18.4120068231
1762-HydroxyisobutyrylationRLLWIDTKIAARMLW
EEEEEHHHHHHHHHH		26.97-
180UbiquitinationIDTKIAARMLWRILN
EHHHHHHHHHHHHHC		16.2324816145
190PhosphorylationWRILNGHSLTRRERR
HHHHCCCCCCHHHHH		32.6030108239
192PhosphorylationILNGHSLTRRERRQF
HHCCCCCCHHHHHHH		30.6030108239
238PhosphorylationLFPNMLPSTFETQSL
HCCCCCCCCCCCCCC		41.5920068231
239PhosphorylationFPNMLPSTFETQSLK
CCCCCCCCCCCCCCC		24.4520068231
242PhosphorylationMLPSTFETQSLKEER
CCCCCCCCCCCCHHH		21.1920068231
244PhosphorylationPSTFETQSLKEERLK
CCCCCCCCCCHHHHH		49.1520068231
252UbiquitinationLKEERLKKELRVKLE
CCHHHHHHHHHHHHH		67.58-
257AcetylationLKKELRVKLELAKFL
HHHHHHHHHHHHHHH		29.7927452117
257UbiquitinationLKKELRVKLELAKFL
HHHHHHHHHHHHHHH		29.7929967540
271SulfoxidationLQDTIEEMALKNKAA
HHHHHHHHHHHCCCC		3.2521406390
284AcetylationAAKGSATKDFSVFFQ
CCCCCCCCCHHHHHH		57.39164295
284UbiquitinationAAKGSATKDFSVFFQ
CCCCCCCCCHHHHHH		57.39-
287PhosphorylationGSATKDFSVFFQKIR
CCCCCCHHHHHHHHH		28.3121712546
292 (in isoform 1)Ubiquitination-38.2821890473
292UbiquitinationDFSVFFQKIRETGER
CHHHHHHHHHHHCCC		38.2823000965
306SulfoxidationRPSNEEIMRFSKLFE
CCCHHHHHHHHHHHC		3.9121406390
307MethylationPSNEEIMRFSKLFED
CCHHHHHHHHHHHCC		38.05115482059
310UbiquitinationEEIMRFSKLFEDELT
HHHHHHHHHHCCCCC		55.26-
313UbiquitinationMRFSKLFEDELTLDN
HHHHHHHCCCCCCCC		62.1024816145
330GlutathionylationRPQLVALCKLLELQS
HHHHHHHHHHHHHHH		1.7922555962
360UbiquitinationRSIKADDKLIAEEGV
HHCCCCCCHHHHCCC		42.2024816145
373SuccinylationGVDSLNVKELQAACR
CCCCCCHHHHHHHHH		52.1927452117
373MalonylationGVDSLNVKELQAACR
CCCCCCHHHHHHHHH		52.1926320211
3732-HydroxyisobutyrylationGVDSLNVKELQAACR
CCCCCCHHHHHHHHH		52.19-
373UbiquitinationGVDSLNVKELQAACR
CCCCCCHHHHHHHHH		52.1929967540
393MethylationALGVTEDRLRGQLKQ
HCCCCHHHHHHHHHH		21.76115482051
421SulfoxidationLLILSRAMYLPDTLS
HHHHHHHHCCCCCCC		3.2521406390
422PhosphorylationLILSRAMYLPDTLSP
HHHHHHHCCCCCCCH		17.6920068231
426PhosphorylationRAMYLPDTLSPADQL
HHHCCCCCCCHHHHH		27.4820068231
428PhosphorylationMYLPDTLSPADQLKS
HCCCCCCCHHHHHHH		21.8220068231
435PhosphorylationSPADQLKSTLQTLPE
CHHHHHHHHHHHHHH		42.8320068231
436PhosphorylationPADQLKSTLQTLPEI
HHHHHHHHHHHHHHH		22.6920068231
439PhosphorylationQLKSTLQTLPEIVAK
HHHHHHHHHHHHHHH		47.6022210691
463AcetylationEGEQVDNKAKLEATL
CCCCCCCHHHHHHHH		42.2925953088
493UbiquitinationQKRSEVAKDFEPERV
HHHHHHHHHCCHHHE		69.0324816145
541PhosphorylationGLKEEEITKEEIDIL
CCCHHHCCHHHHHHH		35.3729523821
549PhosphorylationKEEIDILSDACSKLQ
HHHHHHHHHHHHHHH		24.4026074081
553PhosphorylationDILSDACSKLQEQKK
HHHHHHHHHHHHHHH		37.8126074081
561PhosphorylationKLQEQKKSLTKEKEE
HHHHHHHHCHHHHHH		48.5926074081
563PhosphorylationQEQKKSLTKEKEELE
HHHHHHCHHHHHHHH		44.2226074081
5662-HydroxyisobutyrylationKKSLTKEKEELELLK
HHHCHHHHHHHHHHH		59.03-
579PhosphorylationLKEDVQDYSEDLQEI
HHHHHHHHHHHHHHH		9.25-
580PhosphorylationKEDVQDYSEDLQEIK
HHHHHHHHHHHHHHH		32.68-
597AcetylationLSKTGEEKYVEESKA
HHHHCCHHHHHHHHH		50.7419608861
602PhosphorylationEEKYVEESKASKRLT
CHHHHHHHHHHHHHH		21.73-
643PhosphorylationAPANGMPTGENVISV
CCCCCCCCCCHHHCH		48.51-
649PhosphorylationPTGENVISVAELINA
CCCCHHHCHHHHHHH		15.82-
666PhosphorylationQVKHIPESKLTSLAA
HHCCCCHHHHHHHHH		27.8422817900
6792-HydroxyisobutyrylationAAALDENKDGKVNID
HHHHCCCCCCCCCHH		66.85-
682UbiquitinationLDENKDGKVNIDDLV
HCCCCCCCCCHHHHH		42.0929967540
713PhosphorylationQVAEIVATLEKEEKV
HHHHHHHHHHHHHHH		25.2624719451
739PhosphorylationKEVAEVKS-------
HHHHHHCC-------		51.1027251275
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
192TPhosphorylationKinasePINK1Q9BXM7
PSP
192TPhosphorylationKinasePINK1Q99MQ3
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LETM1_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 LETM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSA3_HUMANPSMA3physical
25416956
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 LETM1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-597, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-666, AND MASSSPECTROMETRY.

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