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Q9NVH6

- TMLH_HUMAN

UniProt

Q9NVH6 - TMLH_HUMAN

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Protein

Trimethyllysine dioxygenase, mitochondrial

Gene
TMLHE, TMLH
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 Fe2+ ion per subunit By similarity.
Ascorbate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi242 – 2421Iron; catalytic By similarity
Metal bindingi244 – 2441Iron; catalytic By similarity
Metal bindingi389 – 3891Iron; catalytic By 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 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 – 1515MitochondrionAdd
BLAST
Chaini16 – 421406Trimethyllysine dioxygenase, mitochondrialPRO_0000002795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysine By 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the gamma-BBH/TMLD family.

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).

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6868Missing in isoform 7. VSP_042275Add
BLAST
Alternative sequencei1 – 11M → MKIDSFLPILRM in isoform 8. VSP_042276
Alternative sequencei61 – 12060ELKYA…LFFTW → G in isoform 6. VSP_042277Add
BLAST
Alternative sequencei333 – 42189YNNYD…LGLQA → VLRSWCSTRTIEATSKEIKL YIVCRYSYFGETLFPRSKET VTSLPHMCAYKAAATNRPWL SGVFYTI in isoform 2. VSP_042278Add
BLAST
Alternative sequencei333 – 42189Missing in isoform 3. VSP_042279Add
BLAST
Alternative sequencei333 – 42189YNNYD…LGLQA → LFKEKQNTVNRQWNSSLQCD IPERILTYRHFVSGTSIEHR GSLI in isoform 4. VSP_021579Add
BLAST
Alternative sequencei380 – 3834LFID → GPN in isoform 5. VSP_042280
Alternative sequencei384 – 42138Missing in isoform 5. VSP_042281Add
BLAST

Sequence conflict

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

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]
ENST00000596345; ENSP00000469021; ENSG00000267946. [Q9NVH6-2]
ENST00000597729; ENSP00000470860; ENSG00000267946. [Q9NVH6-1]
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 ]
ENST00000596345 ; ENSP00000469021 ; ENSG00000267946 . [Q9NVH6-2 ]
ENST00000597729 ; ENSP00000470860 ; ENSG00000267946 . [Q9NVH6-1 ]
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

« 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: September 3, 2014
This is version 118 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

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