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Q9NVH6

- TMLH_HUMAN

UniProt

Q9NVH6 - TMLH_HUMAN

Protein

Trimethyllysine dioxygenase, mitochondrial

Gene

TMLHE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    Binds 1 Fe2+ ion per subunit.By similarity
    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

    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

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Epsilon-trimethyllysine hydroxylase deficiency (TMLHED) [MIM:300872]: An 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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.
    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

    MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT    50
    CAWQQHEDHF ELKYANTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV 100
    DLCIKPKTIR LDETTLFFTW PDGHVTKYDL NWLVKNSYEG QKQKVIQPRI 150
    LWNAEIYQQA QVPSVDCQSF LETNEGLKKF LQNFLLYGIA FVENVPPTQE 200
    HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD RHTDTTYFQE 250
    PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 300
    YIEDVGECHN HMIGIGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH 350
    RWYTAHRTLT IELRRPENEF WVKLKPGRVL FIDNWRVLHG RECFTGYRQL 400
    CGCYLTRDDV LNTARLLGLQ A 421
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14768.1. [Q9NVH6-1 ]
    CCDS55547.1. [Q9NVH6-2 ]
    RefSeqi NP_001171726.1. NM_001184797.1. [Q9NVH6-2 ]
    NP_060666.1. NM_018196.3. [Q9NVH6-1 ]
    UniGenei Hs.133321.

    3D structure databases

    ProteinModelPortali Q9NVH6.
    SMRi Q9NVH6. Positions 74-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120513. 4 interactions.
    IntActi Q9NVH6. 6 interactions.
    MINTi MINT-3074990.
    STRINGi 9606.ENSP00000335261.

    Chemistry

    DrugBanki DB00139. Succinic acid.
    DB00126. Vitamin C.

    PTM databases

    PhosphoSitei Q9NVH6.

    Polymorphism databases

    DMDMi 21542295.

    Proteomic databases

    MaxQBi Q9NVH6.
    PaxDbi Q9NVH6.
    PRIDEi Q9NVH6.

    Protocols and materials databases

    DNASUi 55217.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334398 ; ENSP00000335261 ; ENSG00000185973 . [Q9NVH6-1 ]
    ENST00000369439 ; ENSP00000358447 ; ENSG00000185973 . [Q9NVH6-2 ]
    GeneIDi 55217.
    KEGGi hsa:55217.
    UCSCi uc004fnn.3. human. [Q9NVH6-1 ]
    uc004fnp.4. human. [Q9NVH6-2 ]

    Organism-specific databases

    CTDi 55217.
    GeneCardsi GC0XM154719.
    HGNCi HGNC:18308. TMLHE.
    HPAi HPA034589.
    HPA040331.
    MIMi 300777. gene.
    300872. phenotype.
    neXtProti NX_Q9NVH6.
    Orphaneti 106. Autism.
    PharmGKBi PA38311.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2175.
    HOGENOMi HOG000210004.
    HOVERGENi HBG035650.
    InParanoidi Q9NVH6.
    KOi K00474.
    OMAi HPRILWN.
    OrthoDBi EOG7XPZ5P.
    PhylomeDBi Q9NVH6.
    TreeFami TF313805.

    Enzyme and pathway databases

    UniPathwayi UPA00118 .
    BioCyci MetaCyc:HS08089-MONOMER.
    BRENDAi 1.14.11.8. 2681.
    Reactomei REACT_2125. Carnitine synthesis.

    Miscellaneous databases

    GeneWikii TMLHE.
    GenomeRNAii 55217.
    NextBioi 59184.
    PROi Q9NVH6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NVH6.
    CleanExi HS_TMLHE.
    Genevestigatori Q9NVH6.

    Family and domain databases

    InterProi IPR010376. DUF971.
    IPR003819. Taurine_dOase.
    IPR012776. Trimethyllysine_dOase.
    [Graphical view ]
    Pfami PF06155. DUF971. 1 hit.
    PF02668. TauD. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02410. carnitine_TMLD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 119 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