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Protein

Trimethyllysine dioxygenase, mitochondrial

Gene

Tmlhe

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).

Catalytic activityi

N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity
  • L-ascorbate

Pathwayi: carnitine biosynthesis

This protein is involved in the pathway carnitine biosynthesis, which is part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the pathway carnitine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi242 – 2421Iron; catalyticBy similarity
Metal bindingi244 – 2441Iron; catalyticBy similarity
Metal bindingi389 – 3891Iron; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Carnitine biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.11.8. 3474.
ReactomeiR-MMU-71262. Carnitine synthesis.
UniPathwayiUPA00118.

Names & Taxonomyi

Protein namesi
Recommended name:
Trimethyllysine dioxygenase, mitochondrial (EC:1.14.11.8)
Alternative name(s):
Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
TML hydroxylase
TML-alpha-ketoglutarate dioxygenase
Short name:
TML dioxygenase
Short name:
TMLD
Gene namesi
Name:Tmlhe
Synonyms:Tmlh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2180203. Tmlhe.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1515MitochondrionBy similarityAdd
BLAST
Chaini16 – 421406Trimethyllysine dioxygenase, mitochondrialPRO_0000002796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysineCombined sources
Modified residuei236 – 2361N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ91ZE0.
MaxQBiQ91ZE0.
PaxDbiQ91ZE0.
PRIDEiQ91ZE0.

PTM databases

iPTMnetiQ91ZE0.
PhosphoSiteiQ91ZE0.
SwissPalmiQ91ZE0.

Expressioni

Developmental stagei

Present already at 9.0 dpc. At 10.5 dpc, expressed throughout the embryo. At 12.5 dpc, higher levels in the developing lung, liver and brain compared to other tissues. In the postnatal day 7 brain, high levels in the Purkinje cell layer of the cerebellum and in the hyppocampal areas of the dentate gyrus and CA1, CA2 and CA3 pyramidal cells.1 Publication

Gene expression databases

BgeeiQ91ZE0.
CleanExiMM_TMLHE.
GenevisibleiQ91ZE0. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ91ZE0. 1 interaction.
MINTiMINT-4138064.
STRINGi10090.ENSMUSP00000111624.

Structurei

3D structure databases

ProteinModelPortaliQ91ZE0.
SMRiQ91ZE0. Positions 53-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the gamma-BBH/TMLD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3889. Eukaryota.
COG2175. LUCA.
GeneTreeiENSGT00530000063582.
HOGENOMiHOG000210004.
HOVERGENiHBG035650.
InParanoidiQ91ZE0.
KOiK00474.
OMAiIEINEFW.
OrthoDBiEOG7XPZ5P.
PhylomeDBiQ91ZE0.
TreeFamiTF313805.

Family and domain databases

InterProiIPR010376. DUF971.
IPR003819. TauD/TfdA-like.
IPR012776. Trimethyllysine_dOase.
[Graphical view]
PfamiPF06155. DUF971. 1 hit.
PF02668. TauD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02410. carnitine_TMLD. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91ZE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWYHKLLHQQ SRLRNLMKRG NIAQGLHLSN FKSLFSSSIH WCHTTSKSVN
60 70 80 90 100
CTWHQHEDHL ELQYAGTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV
110 120 130 140 150
DLCIKPKTVH LDETMLFFTW PDGHVTRYDL DWLVKNSYEG QKQKVIQPRI
160 170 180 190 200
LWNSKLYQQA QVPSVDFQCF LETNEGLKKF LQNFLLYGIA FVENVPPTEE
210 220 230 240 250
HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD RHTDTTYFQE
260 270 280 290 300
PCGIQVFHCL KHEGTGGRTL LVDGFYAAQQ VLQKAPEEFE LLSKVPLKHE
310 320 330 340 350
YIENVGQCHN HMIGVGPILN IYPWNKELYL IRYNNYDRAV INTVPYDVVH
360 370 380 390 400
RWYTAHRTLT TELRRPENEL WVKLKPGKVL FIDNWRVLHG RESFTGYRQL
410 420
CGCYLTRDDV LNTARLLGLH A
Length:421
Mass (Da):49,610
Last modified:June 20, 2002 - v2
Checksum:i1474AD5742E88F43
GO

Sequence cautioni

The sequence AAK54387.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81H → Q in BAE36549 (PubMed:16141072).Curated
Sequence conflicti188 – 1881G → K in BAE36549 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK144627 mRNA. Translation: BAE25977.1.
AK161724 mRNA. Translation: BAE36549.1.
CAAA01137825 Genomic DNA. No translation available.
CAAA01183048 Genomic DNA. No translation available.
CAAA01120074 Genomic DNA. No translation available.
CAAA01019119 Genomic DNA. No translation available.
CH466822 Genomic DNA. Translation: EDL07804.1.
BC010495 mRNA. Translation: AAH10495.1.
BC115365 mRNA. Translation: AAI15366.1.
AY033513 mRNA. Translation: AAK54387.1. Different initiation.
RefSeqiNP_620097.1. NM_138758.1.
UniGeneiMm.394228.

Genome annotation databases

EnsembliENSMUST00000115964; ENSMUSP00000111624; ENSMUSG00000079834.
GeneIDi192289.
KEGGimmu:192289.
UCSCiuc009uyo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK144627 mRNA. Translation: BAE25977.1.
AK161724 mRNA. Translation: BAE36549.1.
CAAA01137825 Genomic DNA. No translation available.
CAAA01183048 Genomic DNA. No translation available.
CAAA01120074 Genomic DNA. No translation available.
CAAA01019119 Genomic DNA. No translation available.
CH466822 Genomic DNA. Translation: EDL07804.1.
BC010495 mRNA. Translation: AAH10495.1.
BC115365 mRNA. Translation: AAI15366.1.
AY033513 mRNA. Translation: AAK54387.1. Different initiation.
RefSeqiNP_620097.1. NM_138758.1.
UniGeneiMm.394228.

3D structure databases

ProteinModelPortaliQ91ZE0.
SMRiQ91ZE0. Positions 53-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91ZE0. 1 interaction.
MINTiMINT-4138064.
STRINGi10090.ENSMUSP00000111624.

PTM databases

iPTMnetiQ91ZE0.
PhosphoSiteiQ91ZE0.
SwissPalmiQ91ZE0.

Proteomic databases

EPDiQ91ZE0.
MaxQBiQ91ZE0.
PaxDbiQ91ZE0.
PRIDEiQ91ZE0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115964; ENSMUSP00000111624; ENSMUSG00000079834.
GeneIDi192289.
KEGGimmu:192289.
UCSCiuc009uyo.1. mouse.

Organism-specific databases

CTDi55217.
MGIiMGI:2180203. Tmlhe.

Phylogenomic databases

eggNOGiKOG3889. Eukaryota.
COG2175. LUCA.
GeneTreeiENSGT00530000063582.
HOGENOMiHOG000210004.
HOVERGENiHBG035650.
InParanoidiQ91ZE0.
KOiK00474.
OMAiIEINEFW.
OrthoDBiEOG7XPZ5P.
PhylomeDBiQ91ZE0.
TreeFamiTF313805.

Enzyme and pathway databases

UniPathwayiUPA00118.
BRENDAi1.14.11.8. 3474.
ReactomeiR-MMU-71262. Carnitine synthesis.

Miscellaneous databases

NextBioi371290.
PROiQ91ZE0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZE0.
CleanExiMM_TMLHE.
GenevisibleiQ91ZE0. MM.

Family and domain databases

InterProiIPR010376. DUF971.
IPR003819. TauD/TfdA-like.
IPR012776. Trimethyllysine_dOase.
[Graphical view]
PfamiPF06155. DUF971. 1 hit.
PF02668. TauD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02410. carnitine_TMLD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  5. "Molecular and biochemical characterization of rat epsilon-N-trimethyllysine hydroxylase, the first enzyme of carnitine biosynthesis."
    Vaz F.M., Ofman R., Westinga K., Back J.W., Wanders R.J.A.
    J. Biol. Chem. 276:33512-33517(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-421.
    Strain: FVB/N.
  6. "Functional characterization of the TMLH gene: promoter analysis, in situ hybridization, identification and mapping of alternative splicing variants."
    Monfregola J., Napolitano G., Conte I., Cevenini A., Migliaccio C., D'Urso M., Ursini M.V.
    Gene 395:86-97(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Pancreas and Testis.
  8. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTMLH_MOUSE
AccessioniPrimary (citable) accession number: Q91ZE0
Secondary accession number(s): Q3TSX6, Q3UMX1, Q91XH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 20, 2002
Last modified: March 16, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.