CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018603
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Trimethyllysine dioxygenase, mitochondrial 
Protein Synonyms/Alias
 Epsilon-trimethyllysine 2-oxoglutarate dioxygenase; TML hydroxylase; TML-alpha-ketoglutarate dioxygenase; TML dioxygenase; TMLD 
Gene Name
 Tmlhe 
Gene Synonyms/Alias
 Tmlh 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
135YDLDWLVKNSYEGQKacetylation[1]
142KNSYEGQKQKVIQPRacetylation[2, 3]
179ETNEGLKKFLQNFLLacetylation[4]
294EEFELLSKVPLKHEYacetylation[1]
378WVKLKPGKVLFIDNWacetylation[2]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753] 
Functional Description
 Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML). 
Sequence Annotation
 METAL 242 242 Iron; catalytic (By similarity).
 METAL 244 244 Iron; catalytic (By similarity).
 METAL 389 389 Iron; catalytic (By similarity).
 MOD_RES 236 236 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Carnitine biosynthesis; Complete proteome; Dioxygenase; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 421 AA 
Protein Sequence
MWYHKLLHQQ SRLRNLMKRG NIAQGLHLSN FKSLFSSSIH WCHTTSKSVN CTWHQHEDHL 60
ELQYAGTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTVH LDETMLFFTW 120
PDGHVTRYDL DWLVKNSYEG QKQKVIQPRI LWNSKLYQQA QVPSVDFQCF LETNEGLKKF 180
LQNFLLYGIA FVENVPPTEE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 240
RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAQQ VLQKAPEEFE LLSKVPLKHE 300
YIENVGQCHN HMIGVGPILN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT 360
TELRRPENEL WVKLKPGKVL FIDNWRVLHG RESFTGYRQL CGCYLTRDDV LNTARLLGLH 420
A 421 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:MGI.
 GO:0050353; F:trimethyllysine dioxygenase activity; IEA:EC.
 GO:0045329; P:carnitine biosynthetic process; IDA:MGI.
 GO:0051354; P:negative regulation of oxidoreductase activity; IEA:Compara. 
Interpro
 IPR010376; DUF971.
 IPR003819; Taurine_dOase.
 IPR012776; Trimethyllysine_dOase. 
Pfam
 PF06155; DUF971
 PF02668; TauD 
SMART
  
PROSITE
  
PRINTS