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Protein

Trimethyllysine dioxygenase, mitochondrial

Gene

TMLHE

Organism
Homo sapiens (Human)
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

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

  1. iron ion binding Source: InterPro
  2. L-ascorbic acid binding Source: InterPro
  3. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: Ensembl
  4. trimethyllysine dioxygenase activity Source: BHF-UCL

GO - Biological processi

  1. carnitine biosynthetic process Source: BHF-UCL
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. negative regulation of oxidoreductase activity Source: BHF-UCL
  4. oxidation-reduction process Source: GOC
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Carnitine biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08089-MONOMER.
BRENDAi1.14.11.8. 2681.
ReactomeiREACT_2125. 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
Epsilon-trimethyllysine hydroxylase
TML hydroxylase
TML-alpha-ketoglutarate dioxygenase
Short name:
TML dioxygenase
Short name:
TMLD
Gene namesi
Name:TMLHE
Synonyms:TMLH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:18308. TMLHE.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Epsilon-trimethyllysine hydroxylase deficiency1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn inborn error of carnitine biosynthesis associated with an increased risk for developing autistic behavior. Autism is a complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.

See also OMIM:300872

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi389 – 3891H → L: No catalytic activity. 1 Publication

Organism-specific databases

MIMi300872. phenotype.
Orphaneti106. Autism.
PharmGKBiPA38311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1515Mitochondrion1 PublicationAdd
BLAST
Chaini16 – 421406Trimethyllysine dioxygenase, mitochondrialPRO_0000002795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysineBy similarity
Modified residuei236 – 2361N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NVH6.
PaxDbiQ9NVH6.
PRIDEiQ9NVH6.

PTM databases

PhosphoSiteiQ9NVH6.

Expressioni

Tissue specificityi

All isoforms, but isoform 8, are widely expressed in adult and fetal tissues. Isoform 8 is restricted to heart and skeletal muscle.2 Publications

Gene expression databases

BgeeiQ9NVH6.
CleanExiHS_TMLHE.
GenevestigatoriQ9NVH6.

Organism-specific databases

HPAiHPA034589.
HPA040331.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi120513. 4 interactions.
IntActiQ9NVH6. 6 interactions.
MINTiMINT-3074990.
STRINGi9606.ENSP00000335261.

Structurei

3D structure databases

ProteinModelPortaliQ9NVH6.
SMRiQ9NVH6. Positions 74-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the gamma-BBH/TMLD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2175.
GeneTreeiENSGT00530000063582.
HOGENOMiHOG000210004.
HOVERGENiHBG035650.
InParanoidiQ9NVH6.
KOiK00474.
OMAiHPRILWN.
OrthoDBiEOG7XPZ5P.
PhylomeDBiQ9NVH6.
TreeFamiTF313805.

Family and domain databases

InterProiIPR010376. DUF971.
IPR003819. Taurine_dOase.
IPR012776. Trimethyllysine_dOase.
[Graphical view]
PfamiPF06155. DUF971. 1 hit.
PF02668. TauD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02410. carnitine_TMLD. 1 hit.

Sequences (8)i

Sequence statusi: Complete.

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

This entry describes 8 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1 (identifier: Q9NVH6-1) [UniParc]FASTAAdd to Basket

Also known as: TMLHa, TMLH1a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT
60 70 80 90 100
CAWQQHEDHF ELKYANTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV
110 120 130 140 150
DLCIKPKTIR LDETTLFFTW PDGHVTKYDL NWLVKNSYEG QKQKVIQPRI
160 170 180 190 200
LWNAEIYQQA QVPSVDCQSF LETNEGLKKF LQNFLLYGIA FVENVPPTQE
210 220 230 240 250
HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD RHTDTTYFQE
260 270 280 290 300
PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE
310 320 330 340 350
YIEDVGECHN HMIGIGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH
360 370 380 390 400
RWYTAHRTLT IELRRPENEF WVKLKPGRVL FIDNWRVLHG RECFTGYRQL
410 420
CGCYLTRDDV LNTARLLGLQ A
Length:421
Mass (Da):49,518
Last modified:October 1, 2000 - v1
Checksum:i4E55DF349B866B43
GO
Isoform 2 (identifier: Q9NVH6-3) [UniParc]FASTAAdd to Basket

Also known as: TMLHb

The sequence of this isoform differs from the canonical sequence as follows:
     333-421: YNNYDRAVIN...NTARLLGLQA → VLRSWCSTRT...PWLSGVFYTI

Note: Produced by alternative splicing. Lacks enzymatic activity.

Show »
Length:399
Mass (Da):46,590
Checksum:i73A092B32CB15DF1
GO
Isoform 3 (identifier: Q9NVH6-4) [UniParc]FASTAAdd to Basket

Also known as: TMLHc

The sequence of this isoform differs from the canonical sequence as follows:
     333-421: Missing.

Note: Produced by alternative splicing. Lacks enzymatic activity.

Show »
Length:332
Mass (Da):38,864
Checksum:i864FB6A12712C1D3
GO
Isoform 4 (identifier: Q9NVH6-2) [UniParc]FASTAAdd to Basket

Also known as: TMLHd

The sequence of this isoform differs from the canonical sequence as follows:
     333-421: YNNYDRAVIN...NTARLLGLQA → LFKEKQNTVN...TSIEHRGSLI

Note: Produced by alternative splicing. Lacks enzymatic activity.

Show »
Length:376
Mass (Da):44,049
Checksum:iAB6D7A1DC57D6FCF
GO
Isoform 5 (identifier: Q9NVH6-5) [UniParc]FASTAAdd to Basket

Also known as: TMLHe

The sequence of this isoform differs from the canonical sequence as follows:
     380-383: LFID → GPN
     384-421: Missing.

Note: Produced by alternative splicing. Lacks enzymatic activity.

Show »
Length:382
Mass (Da):44,902
Checksum:i634B62F65E00F528
GO
Isoform 6 (identifier: Q9NVH6-6) [UniParc]FASTAAdd to Basket

Also known as: TMLHf

The sequence of this isoform differs from the canonical sequence as follows:
     61-120: ELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTW → G

Note: Produced by alternative splicing. Lacks the mitochondrial transit signal.

Show »
Length:362
Mass (Da):42,416
Checksum:i36F27DC4C85AC9B5
GO
Isoform 7 (identifier: Q9NVH6-7) [UniParc]FASTAAdd to Basket

Also known as: TMLHg

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.

Note: Produced by alternative splicing.

Show »
Length:353
Mass (Da):41,537
Checksum:iE7CDDCCF3D91E4E9
GO
Isoform 8 (identifier: Q9NVH6-8) [UniParc]FASTAAdd to Basket

Also known as: TMLH1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKIDSFLPILRM

Note: Produced by alternative promoter usage. Although the expression of the alternative 5' exon has been detected by PCR in heart and skeletal muscle, the identification of the alternative promoter leading to this form remains elusive (PubMed:17408883).1 Publication

Show »
Length:432
Mass (Da):50,832
Checksum:i47019D752A5E120A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661N → D in CAG33546. 1 PublicationCurated
Sequence conflicti170 – 1701F → S in BAF84383. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6868Missing in isoform 7. 1 PublicationVSP_042275Add
BLAST
Alternative sequencei1 – 11M → MKIDSFLPILRM in isoform 8. CuratedVSP_042276
Alternative sequencei61 – 12060ELKYA…LFFTW → G in isoform 6. CuratedVSP_042277Add
BLAST
Alternative sequencei333 – 42189YNNYD…LGLQA → VLRSWCSTRTIEATSKEIKL YIVCRYSYFGETLFPRSKET VTSLPHMCAYKAAATNRPWL SGVFYTI in isoform 2. CuratedVSP_042278Add
BLAST
Alternative sequencei333 – 42189Missing in isoform 3. 1 PublicationVSP_042279Add
BLAST
Alternative sequencei333 – 42189YNNYD…LGLQA → LFKEKQNTVNRQWNSSLQCD IPERILTYRHFVSGTSIEHR GSLI in isoform 4. 2 PublicationsVSP_021579Add
BLAST
Alternative sequencei380 – 3834LFID → GPN in isoform 5. CuratedVSP_042280
Alternative sequencei384 – 42138Missing in isoform 5. CuratedVSP_042281Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF373407 mRNA. Translation: AAL01871.1.
AK001589 mRNA. Translation: BAA91775.1.
AK291694 mRNA. Translation: BAF84383.1.
AK304830 mRNA. Translation: BAG65575.1.
AK310667 mRNA. No translation available.
CR457265 mRNA. Translation: CAG33546.1.
AM393196 mRNA. Translation: CAL38074.1.
BX276110 Genomic DNA. Translation: CAH71441.1.
BX276110 Genomic DNA. Translation: CAH71442.1.
BC025269 mRNA. Translation: AAH25269.1.
CCDSiCCDS14768.1. [Q9NVH6-1]
CCDS55547.1. [Q9NVH6-2]
RefSeqiNP_001171726.1. NM_001184797.1. [Q9NVH6-2]
NP_060666.1. NM_018196.3. [Q9NVH6-1]
UniGeneiHs.133321.

Genome annotation databases

EnsembliENST00000334398; ENSP00000335261; ENSG00000185973. [Q9NVH6-1]
ENST00000369439; ENSP00000358447; ENSG00000185973. [Q9NVH6-2]
GeneIDi55217.
KEGGihsa:55217.
UCSCiuc004fnn.3. human. [Q9NVH6-1]
uc004fnp.4. human. [Q9NVH6-2]

Polymorphism databases

DMDMi21542295.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF373407 mRNA. Translation: AAL01871.1.
AK001589 mRNA. Translation: BAA91775.1.
AK291694 mRNA. Translation: BAF84383.1.
AK304830 mRNA. Translation: BAG65575.1.
AK310667 mRNA. No translation available.
CR457265 mRNA. Translation: CAG33546.1.
AM393196 mRNA. Translation: CAL38074.1.
BX276110 Genomic DNA. Translation: CAH71441.1.
BX276110 Genomic DNA. Translation: CAH71442.1.
BC025269 mRNA. Translation: AAH25269.1.
CCDSiCCDS14768.1. [Q9NVH6-1]
CCDS55547.1. [Q9NVH6-2]
RefSeqiNP_001171726.1. NM_001184797.1. [Q9NVH6-2]
NP_060666.1. NM_018196.3. [Q9NVH6-1]
UniGeneiHs.133321.

3D structure databases

ProteinModelPortaliQ9NVH6.
SMRiQ9NVH6. Positions 74-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120513. 4 interactions.
IntActiQ9NVH6. 6 interactions.
MINTiMINT-3074990.
STRINGi9606.ENSP00000335261.

Chemistry

DrugBankiDB00139. Succinic acid.
DB00126. Vitamin C.

PTM databases

PhosphoSiteiQ9NVH6.

Polymorphism databases

DMDMi21542295.

Proteomic databases

MaxQBiQ9NVH6.
PaxDbiQ9NVH6.
PRIDEiQ9NVH6.

Protocols and materials databases

DNASUi55217.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334398; ENSP00000335261; ENSG00000185973. [Q9NVH6-1]
ENST00000369439; ENSP00000358447; ENSG00000185973. [Q9NVH6-2]
GeneIDi55217.
KEGGihsa:55217.
UCSCiuc004fnn.3. human. [Q9NVH6-1]
uc004fnp.4. human. [Q9NVH6-2]

Organism-specific databases

CTDi55217.
GeneCardsiGC0XM154719.
HGNCiHGNC:18308. TMLHE.
HPAiHPA034589.
HPA040331.
MIMi300777. gene.
300872. phenotype.
neXtProtiNX_Q9NVH6.
Orphaneti106. Autism.
PharmGKBiPA38311.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2175.
GeneTreeiENSGT00530000063582.
HOGENOMiHOG000210004.
HOVERGENiHBG035650.
InParanoidiQ9NVH6.
KOiK00474.
OMAiHPRILWN.
OrthoDBiEOG7XPZ5P.
PhylomeDBiQ9NVH6.
TreeFamiTF313805.

Enzyme and pathway databases

UniPathwayiUPA00118.
BioCyciMetaCyc:HS08089-MONOMER.
BRENDAi1.14.11.8. 2681.
ReactomeiREACT_2125. Carnitine synthesis.

Miscellaneous databases

GeneWikiiTMLHE.
GenomeRNAii55217.
NextBioi59184.
PROiQ9NVH6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NVH6.
CleanExiHS_TMLHE.
GenevestigatoriQ9NVH6.

Family and domain databases

InterProiIPR010376. DUF971.
IPR003819. Taurine_dOase.
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. "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] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 66-332 (ISOFORM 3).
    Tissue: Placenta, Teratocarcinoma, Thymus and Uterus.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. Bechtel S., Schupp I., Duda A., Wellenreuther R., Mehrle A., Ruschke V., Poustka A., Wiemann S.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 4).
    Tissue: Pancreas.
  7. "Functional analysis of TMLH variants and definition of domains required for catalytic activity and mitochondrial targeting."
    Monfregola J., Cevenini A., Terracciano A., van Vlies N., Arbucci S., Wanders R.J., D'Urso M., Vaz F.M., Ursini M.V.
    J. Cell. Physiol. 204:839-847(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, TRANSIT PEPTIDE CLEAVAGE SITE, MUTAGENESIS OF HIS-389, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  8. "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: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: INVOLVEMENT IN TMLHED.

Entry informationi

Entry nameiTMLH_HUMAN
AccessioniPrimary (citable) accession number: Q9NVH6
Secondary accession number(s): A8K6M9
, B4E3R3, Q5TZB5, Q6IA90, Q8TBT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.