Q9NVH6 (TMLH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TMLHE
Synonyms:	TMLH

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
Catalytic activity	N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2.
Cofactor	Binds 1 Fe2+ ion per subunit By similarity. Ascorbate.
Pathway	Amine and polyamine biosynthesis; carnitine biosynthesis.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix Ref.7.
Tissue specificity	All isoforms, but isoform 8, are widely expressed in adult and fetal tissues. Isoform 8 is restricted to heart and skeletal muscle. Ref.7 Ref.8
Involvement in disease	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. Ref.10
Sequence similarities	Belongs to the gamma-BBH/TMLD family.

Ontologies

Keywords
Biological process	Carnitine biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative promoter usage Alternative splicing
Domain	Transit peptide
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carnitine biosynthetic process Inferred from direct assay Ref.7. Source: BHF-UCL negative regulation of oxidoreductase activity Inferred from direct assay Ref.7. Source: BHF-UCL
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome mitochondrion Inferred from direct assay Ref.7. Source: BHF-UCL
Molecular_function	L-ascorbic acid binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW trimethyllysine dioxygenase activity Inferred from direct assay Ref.7. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NVH6-1)

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.

Isoform 2 (identifier: Q9NVH6-3)

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.

Isoform 3 (identifier: Q9NVH6-4)

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.

Isoform 4 (identifier: Q9NVH6-2)

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.

Isoform 5 (identifier: Q9NVH6-5)

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.

Isoform 6 (identifier: Q9NVH6-6)

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.

Isoform 7 (identifier: Q9NVH6-7)

Also known as: TMLHg;

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

Note: Produced by alternative splicing.

Isoform 8 (identifier: Q9NVH6-8)

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).

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 15	15	Mitochondrion
	Chain	16 – 421	406	Trimethyllysine dioxygenase, mitochondrial		PRO_0000002795
Sites
	Metal binding	242	1	Iron; catalytic By similarity
	Metal binding	244	1	Iron; catalytic By similarity
	Metal binding	389	1	Iron; catalytic By similarity
Amino acid modifications
	Modified residue	236	1	N6-acetyllysine Ref.9
Natural variations
	Alternative sequence	1 – 68	68	Missing in isoform 7.		VSP_042275
	Alternative sequence	1	1	M → MKIDSFLPILRM in isoform 8.		VSP_042276
	Alternative sequence	61 – 120	60	ELKYA…LFFTW → G in isoform 6.		VSP_042277
	Alternative sequence	333 – 421	89	YNNYD…LGLQA → VLRSWCSTRTIEATSKEIKL YIVCRYSYFGETLFPRSKET VTSLPHMCAYKAAATNRPWL SGVFYTI in isoform 2.		VSP_042278
	Alternative sequence	333 – 421	89	Missing in isoform 3.		VSP_042279
	Alternative sequence	333 – 421	89	YNNYD…LGLQA → LFKEKQNTVNRQWNSSLQCD IPERILTYRHFVSGTSIEHR GSLI in isoform 4.		VSP_021579
	Alternative sequence	380 – 383	4	LFID → GPN in isoform 5.		VSP_042280
	Alternative sequence	384 – 421	38	Missing in isoform 5.		VSP_042281
Experimental info
	Mutagenesis	389	1	H → L: No catalytic activity. Ref.7
	Sequence conflict	66	1	N → D in CAG33546. Ref.3
	Sequence conflict	170	1	F → S in BAF84383. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TMLHa) (TMLH1a) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4E55DF349B866B43	FASTA	421	49,518
	10 20 30 40 50 60 MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT CAWQQHEDHF 70 80 90 100 110 120 ELKYANTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTIR LDETTLFFTW 130 140 150 160 170 180 PDGHVTKYDL NWLVKNSYEG QKQKVIQPRI LWNAEIYQQA QVPSVDCQSF LETNEGLKKF 190 200 210 220 230 240 LQNFLLYGIA FVENVPPTQE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 250 260 270 280 290 300 RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 310 320 330 340 350 360 YIEDVGECHN HMIGIGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT 370 380 390 400 410 420 IELRRPENEF WVKLKPGRVL FIDNWRVLHG RECFTGYRQL CGCYLTRDDV LNTARLLGLQ A
	Isoform 2 (TMLHb) [UniParc]. Checksum: 73A092B32CB15DF1	FASTA	399	46,590
	10 20 30 40 50 60 MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT CAWQQHEDHF 70 80 90 100 110 120 ELKYANTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTIR LDETTLFFTW 130 140 150 160 170 180 PDGHVTKYDL NWLVKNSYEG QKQKVIQPRI LWNAEIYQQA QVPSVDCQSF LETNEGLKKF 190 200 210 220 230 240 LQNFLLYGIA FVENVPPTQE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 250 260 270 280 290 300 RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 310 320 330 340 350 360 YIEDVGECHN HMIGIGPVLN IYPWNKELYL IRVLRSWCST RTIEATSKEI KLYIVCRYSY 370 380 390 FGETLFPRSK ETVTSLPHMC AYKAAATNRP WLSGVFYTI
	Isoform 3 (TMLHc) [UniParc]. Checksum: 864FB6A12712C1D3	FASTA	332	38,864
	10 20 30 40 50 60 MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT CAWQQHEDHF 70 80 90 100 110 120 ELKYANTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTIR LDETTLFFTW 130 140 150 160 170 180 PDGHVTKYDL NWLVKNSYEG QKQKVIQPRI LWNAEIYQQA QVPSVDCQSF LETNEGLKKF 190 200 210 220 230 240 LQNFLLYGIA FVENVPPTQE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 250 260 270 280 290 300 RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 310 320 330 YIEDVGECHN HMIGIGPVLN IYPWNKELYL IR
	Isoform 4 (TMLHd) [UniParc]. Checksum: AB6D7A1DC57D6FCF	FASTA	376	44,049
	10 20 30 40 50 60 MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT CAWQQHEDHF 70 80 90 100 110 120 ELKYANTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTIR LDETTLFFTW 130 140 150 160 170 180 PDGHVTKYDL NWLVKNSYEG QKQKVIQPRI LWNAEIYQQA QVPSVDCQSF LETNEGLKKF 190 200 210 220 230 240 LQNFLLYGIA FVENVPPTQE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 250 260 270 280 290 300 RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 310 320 330 340 350 360 YIEDVGECHN HMIGIGPVLN IYPWNKELYL IRLFKEKQNT VNRQWNSSLQ CDIPERILTY 370 RHFVSGTSIE HRGSLI
	Isoform 5 (TMLHe) [UniParc]. Checksum: 634B62F65E00F528	FASTA	382	44,902
	10 20 30 40 50 60 MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT CAWQQHEDHF 70 80 90 100 110 120 ELKYANTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTIR LDETTLFFTW 130 140 150 160 170 180 PDGHVTKYDL NWLVKNSYEG QKQKVIQPRI LWNAEIYQQA QVPSVDCQSF LETNEGLKKF 190 200 210 220 230 240 LQNFLLYGIA FVENVPPTQE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 250 260 270 280 290 300 RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 310 320 330 340 350 360 YIEDVGECHN HMIGIGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT 370 380 IELRRPENEF WVKLKPGRVG PN
	Isoform 6 (TMLHf) [UniParc]. Checksum: 36F27DC4C85AC9B5	FASTA	362	42,416
	10 20 30 40 50 60 MWYHRLSHLH SRLQDLLKGG VIYPALPQPN FKSLLPLAVH WHHTASKSLT CAWQQHEDHF 70 80 90 100 110 120 GPDGHVTKYD LNWLVKNSYE GQKQKVIQPR ILWNAEIYQQ AQVPSVDCQS FLETNEGLKK 130 140 150 160 170 180 FLQNFLLYGI AFVENVPPTQ EHTEKLAERI SLIRETIYGR MWYFTSDFSR GDTAYTKLAL 190 200 210 220 230 240 DRHTDTTYFQ EPCGIQVFHC LKHEGTGGRT LLVDGFYAAE QVLQKAPEEF ELLSKVPLKH 250 260 270 280 290 300 EYIEDVGECH NHMIGIGPVL NIYPWNKELY LIRYNNYDRA VINTVPYDVV HRWYTAHRTL 310 320 330 340 350 360 TIELRRPENE FWVKLKPGRV LFIDNWRVLH GRECFTGYRQ LCGCYLTRDD VLNTARLLGL QA
	Isoform 7 (TMLHg) [UniParc]. Checksum: E7CDDCCF3D91E4E9	FASTA	353	41,537
	10 20 30 40 50 60 MRFDYVWLRD HCRSASCYNS KTHQRSLDTA SVDLCIKPKT IRLDETTLFF TWPDGHVTKY 70 80 90 100 110 120 DLNWLVKNSY EGQKQKVIQP RILWNAEIYQ QAQVPSVDCQ SFLETNEGLK KFLQNFLLYG 130 140 150 160 170 180 IAFVENVPPT QEHTEKLAER ISLIRETIYG RMWYFTSDFS RGDTAYTKLA LDRHTDTTYF 190 200 210 220 230 240 QEPCGIQVFH CLKHEGTGGR TLLVDGFYAA EQVLQKAPEE FELLSKVPLK HEYIEDVGEC 250 260 270 280 290 300 HNHMIGIGPV LNIYPWNKEL YLIRYNNYDR AVINTVPYDV VHRWYTAHRT LTIELRRPEN 310 320 330 340 350 EFWVKLKPGR VLFIDNWRVL HGRECFTGYR QLCGCYLTRD DVLNTARLLG LQA
	Isoform 8 (TMLH1b) [UniParc]. Checksum: 47019D752A5E120A	FASTA	432	50,832
	10 20 30 40 50 60 MKIDSFLPIL RMWYHRLSHL HSRLQDLLKG GVIYPALPQP NFKSLLPLAV HWHHTASKSL 70 80 90 100 110 120 TCAWQQHEDH FELKYANTVM RFDYVWLRDH CRSASCYNSK THQRSLDTAS VDLCIKPKTI 130 140 150 160 170 180 RLDETTLFFT WPDGHVTKYD LNWLVKNSYE GQKQKVIQPR ILWNAEIYQQ AQVPSVDCQS 190 200 210 220 230 240 FLETNEGLKK FLQNFLLYGI AFVENVPPTQ EHTEKLAERI SLIRETIYGR MWYFTSDFSR 250 260 270 280 290 300 GDTAYTKLAL DRHTDTTYFQ EPCGIQVFHC LKHEGTGGRT LLVDGFYAAE QVLQKAPEEF 310 320 330 340 350 360 ELLSKVPLKH EYIEDVGECH NHMIGIGPVL NIYPWNKELY LIRYNNYDRA VINTVPYDVV 370 380 390 400 410 420 HRWYTAHRTL TIELRRPENE FWVKLKPGRV LFIDNWRVLH GRECFTGYRQ LCGCYLTRDD 430 VLNTARLLGL QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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, MASS SPECTROMETRY.
[10]	"Use of array CGH to detect exonic copy number variants throughout the genome in autism families detects a novel deletion in TMLHE." Celestino-Soper P.B., Shaw C.A., Sanders S.J., Li J., Murtha M.T., Ercan-Sencicek A.G., Davis L., Thomson S., Gambin T., Chinault A.C., Ou Z., German J.R., Milosavljevic A., Sutcliffe J.S., Cook E.H. Jr., Stankiewicz P., State M.W., Beaudet A.L. Hum. Mol. Genet. 20:4360-4370(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN TMLHED.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00301224. IPI00382858.
RefSeq	NP_001171726.1. NM_001184797.1. NP_060666.1. NM_018196.3.
UniGene	Hs.133321.
3D structure databases
ProteinModelPortal	Q9NVH6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NVH6. 5 interactions.
STRING	9606.ENSP00000335261.
PTM databases
PhosphoSite	Q9NVH6.
Polymorphism databases
DMDM	21542295.
Proteomic databases
PaxDb	Q9NVH6.
PRIDE	Q9NVH6.
Protocols and materials databases
DNASU	55217.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000334398; ENSP00000335261; ENSG00000185973. ENST00000369439; ENSP00000358447; ENSG00000185973. ENST00000596345; ENSP00000469021; ENSG00000267946. ENST00000597729; ENSP00000470860; ENSG00000267946.
GeneID	55217.
KEGG	hsa:55217.
UCSC	uc004fnn.3. human. uc004fnp.4. human.
Organism-specific databases
CTD	55217.
GeneCards	GC0XM154719.
HGNC	HGNC:18308. TMLHE.
HPA	HPA034589.
MIM	300777. gene. 300872. phenotype.
neXtProt	NX_Q9NVH6.
PharmGKB	PA38311.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2175.
HOGENOM	HOG000210004.
HOVERGEN	HBG035650.
InParanoid	Q9NVH6.
KO	K00474.
OMA	LCGCYLT.
OrthoDB	EOG4QRH4C.
PhylomeDB	Q9NVH6.
Enzyme and pathway databases
BRENDA	1.14.11.8. 2681.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00118.
Gene expression databases
Bgee	Q9NVH6.
CleanEx	HS_TMLHE.
Genevestigator	Q9NVH6.
GermOnline	ENSG00000185973. Homo sapiens.
Family and domain databases
InterPro	IPR010376. DUF971. IPR003819. Taurine_dOase. IPR012776. Trimethyllysine_dOase. [Graphical view]
PANTHER	PTHR10696:SF2. PTHR10696:SF2. 1 hit.
Pfam	PF06155. DUF971. 1 hit. PF02668. TauD. 1 hit. [Graphical view]
TIGRFAMs	TIGR02410. carnitine_TMLD. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00139. Succinic acid. DB00126. Vitamin C.
GenomeRNAi	55217.
NextBio	59184.
SOURCE	Search...

Entry information

Entry name

TMLH_HUMAN

Accession

Primary (citable) accession number: Q9NVH6
Secondary accession number(s): A8K6M9 , B4E3R3, Q5TZB5, Q6IA90, Q8TBT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.