Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NVH6 (TMLH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1515Mitochondrion
Chain16 – 421406Trimethyllysine dioxygenase, mitochondrial
PRO_0000002795

Sites

Metal binding2421Iron; catalytic By similarity
Metal binding2441Iron; catalytic By similarity
Metal binding3891Iron; catalytic By similarity

Amino acid modifications

Modified residue1791N6-acetyllysine By similarity
Modified residue2361N6-acetyllysine Ref.9

Natural variations

Alternative sequence1 – 6868Missing in isoform 7.
VSP_042275
Alternative sequence11M → MKIDSFLPILRM in isoform 8.
VSP_042276
Alternative sequence61 – 12060ELKYA…LFFTW → G in isoform 6.
VSP_042277
Alternative sequence333 – 42189YNNYD…LGLQA → VLRSWCSTRTIEATSKEIKL YIVCRYSYFGETLFPRSKET VTSLPHMCAYKAAATNRPWL SGVFYTI in isoform 2.
VSP_042278
Alternative sequence333 – 42189Missing in isoform 3.
VSP_042279
Alternative sequence333 – 42189YNNYD…LGLQA → LFKEKQNTVNRQWNSSLQCD IPERILTYRHFVSGTSIEHR GSLI in isoform 4.
VSP_021579
Alternative sequence380 – 3834LFID → GPN in isoform 5.
VSP_042280
Alternative sequence384 – 42138Missing in isoform 5.
VSP_042281

Experimental info

Mutagenesis3891H → L: No catalytic activity. Ref.7
Sequence conflict661N → D in CAG33546. Ref.3
Sequence conflict1701F → S in BAF84383. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TMLHa) (TMLH1a) [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4E55DF349B866B43

FASTA42149,518
        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 

« Hide

Isoform 2 (TMLHb) [UniParc].

Checksum: 73A092B32CB15DF1
Show »

FASTA39946,590
Isoform 3 (TMLHc) [UniParc].

Checksum: 864FB6A12712C1D3
Show »

FASTA33238,864
Isoform 4 (TMLHd) [UniParc].

Checksum: AB6D7A1DC57D6FCF
Show »

FASTA37644,049
Isoform 5 (TMLHe) [UniParc].

Checksum: 634B62F65E00F528
Show »

FASTA38244,902
Isoform 6 (TMLHf) [UniParc].

Checksum: 36F27DC4C85AC9B5
Show »

FASTA36242,416
Isoform 7 (TMLHg) [UniParc].

Checksum: E7CDDCCF3D91E4E9
Show »

FASTA35341,537
Isoform 8 (TMLH1b) [UniParc].

Checksum: 47019D752A5E120A
Show »

FASTA43250,832

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
CCDSCCDS14768.1. [Q9NVH6-1]
CCDS55547.1. [Q9NVH6-2]
RefSeqNP_001171726.1. NM_001184797.1. [Q9NVH6-2]
NP_060666.1. NM_018196.3. [Q9NVH6-1]
UniGeneHs.133321.

3D structure databases

ProteinModelPortalQ9NVH6.
SMRQ9NVH6. Positions 74-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120513. 2 interactions.
IntActQ9NVH6. 6 interactions.
MINTMINT-3074990.
STRING9606.ENSP00000335261.

Chemistry

DrugBankDB00139. Succinic acid.
DB00126. Vitamin C.

PTM databases

PhosphoSiteQ9NVH6.

Polymorphism databases

DMDM21542295.

Proteomic databases

MaxQBQ9NVH6.
PaxDbQ9NVH6.
PRIDEQ9NVH6.

Protocols and materials databases

DNASU55217.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334398; ENSP00000335261; ENSG00000185973. [Q9NVH6-1]
ENST00000369439; ENSP00000358447; ENSG00000185973. [Q9NVH6-2]
ENST00000596345; ENSP00000469021; ENSG00000267946. [Q9NVH6-2]
ENST00000597729; ENSP00000470860; ENSG00000267946. [Q9NVH6-1]
GeneID55217.
KEGGhsa:55217.
UCSCuc004fnn.3. human. [Q9NVH6-1]
uc004fnp.4. human. [Q9NVH6-2]

Organism-specific databases

CTD55217.
GeneCardsGC0XM154719.
HGNCHGNC:18308. TMLHE.
HPAHPA034589.
HPA040331.
MIM300777. gene.
300872. phenotype.
neXtProtNX_Q9NVH6.
Orphanet106. Autism.
PharmGKBPA38311.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2175.
HOGENOMHOG000210004.
HOVERGENHBG035650.
InParanoidQ9NVH6.
KOK00474.
OMAHPRILWN.
OrthoDBEOG7XPZ5P.
PhylomeDBQ9NVH6.
TreeFamTF313805.

Enzyme and pathway databases

BioCycMetaCyc:HS08089-MONOMER.
BRENDA1.14.11.8. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00118.

Gene expression databases

BgeeQ9NVH6.
CleanExHS_TMLHE.
GenevestigatorQ9NVH6.

Family and domain databases

InterProIPR010376. DUF971.
IPR003819. Taurine_dOase.
IPR012776. Trimethyllysine_dOase.
[Graphical view]
PfamPF06155. DUF971. 1 hit.
PF02668. TauD. 1 hit.
[Graphical view]
TIGRFAMsTIGR02410. carnitine_TMLD. 1 hit.
ProtoNetSearch...

Other

GeneWikiTMLHE.
GenomeRNAi55217.
NextBio59184.
PROQ9NVH6.
SOURCESearch...

Entry information

Entry nameTMLH_HUMAN
AccessionPrimary (citable) accession number: Q9NVH6
Secondary accession number(s): A8K6M9 expand/collapse secondary AC list , B4E3R3, Q5TZB5, Q6IA90, Q8TBT0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM