Q96HY7 (DHTK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial
EC=1.2.4.2

Alternative name(s):
Dehydrogenase E1 and transketolase domain-containing protein 1

Gene names

Name:	DHTKD1
Synonyms:	KIAA1630

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

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate By similarity.
Subcellular location	Mitochondrion Potential.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.
Sequence caution	The sequence BAB13456.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB13456.1 differs from that shown. Reason: Chimeric cDNA. C-terminal exons are derived from the neighboring gene.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 919		Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial		PRO_0000307936
Natural variations
	Natural variant	20	1	F → L. Ref.2 Ref.3 Corresponds to variant rs1279138 [ dbSNP | Ensembl ].		VAR_036715
	Natural variant	272	1	Y → D. Ref.2 Ref.3 Corresponds to variant rs3740015 [ dbSNP | Ensembl ].		VAR_036716
	Natural variant	308	1	R → L. Ref.2 Corresponds to variant rs17849603 [ dbSNP | Ensembl ].		VAR_036717
	Natural variant	350	1	N → D. Corresponds to variant rs34716552 [ dbSNP | Ensembl ].		VAR_036718
	Natural variant	607	1	I → M. Ref.2 Ref.3 Ref.4 Corresponds to variant rs2062988 [ dbSNP | Ensembl ].		VAR_036719

Sequences

	Sequence		Length	Mass (Da)
	Q96HY7 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: CD1E437F919324B6	FASTA	919	103,077
	10 20 30 40 50 60 MASATAAAAR RGLGRALPLF WRGYQTERGV YGYRPRKPES REPQGALERP PVDHGLARLV 70 80 90 100 110 120 TVYCEHGHKA AKINPLFTGQ ALLENVPEIQ ALVQTLQGPF HTAGLLNMGK EEASLEEVLV 130 140 150 160 170 180 YLNQIYCGQI SIETSQLQSQ DEKDWFAKRF EELQKETFTT EERKHLSKLM LESQEFDHFL 190 200 210 220 230 240 ATKFSTVKRY GGEGAESMMG FFHELLKMSA YSGITDVIIG MPHRGRLNLL TGLLQFPPEL 250 260 270 280 290 300 MFRKMRGLSE FPENFSATGD VLSHLTSSVD LYFGAHHPLH VTMLPNPSHL EAVNPVAVGK 310 320 330 340 350 360 TRGRQQSRQD GDYSPDNSAQ PGDRVICLQV HGDASFCGQG IVPETFTLSN LPHFRIGGSV 370 380 390 400 410 420 HLIVNNQLGY TTPAERGRSS LYCSDIGKLV GCAIIHVNGD SPEEVVRATR LAFEYQRQFR 430 440 450 460 470 480 KDVIIDLLCY RQWGHNELDE PFYTNPIMYK IIRARKSIPD TYAEHLIAGG LMTQEEVSEI 490 500 510 520 530 540 KSSYYAKLND HLNNMAHYRP PALNLQAHWQ GLAQPEAQIT TWSTGVPLDL LRFVGMKSVE 550 560 570 580 590 600 VPRELQMHSH LLKTHVQSRM EKMMDGIKLD WATAEALALG SLLAQGFNVR LSGQDVGRGT 610 620 630 640 650 660 FSQRHAIVVC QETDDTYIPL NHMDPNQKGF LEVSNSPLSE EAVLGFEYGM SIESPKLLPL 670 680 690 700 710 720 WEAQFGDFFN GAQIIFDTFI SGGEAKWLLQ SGIVILLPHG YDGAGPDHSS CRIERFLQMC 730 740 750 760 770 780 DSAEEGVDGD TVNMFVVHPT TPAQYFHLLR RQMVRNFRKP LIVASPKMLL RLPAAVSTLQ 790 800 810 820 830 840 EMAPGTTFNP VIGDSSVDPK KVKTLVFCSG KHFYSLVKQR ESLGAKKHDF AIIRVEELCP 850 860 870 880 890 900 FPLDSLQQEM SKYKHVKDHI WSQEEPQNMG PWSFVSPRFE KQLACKLRLV GRPPLPVPAV 910 GIGTVHLHQH EDILAKTFA

References

[1]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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], VARIANTS LEU-20; ASP-272; LEU-308 AND MET-607. Tissue: Kidney and Uterus.
[3]	"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O. DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-886, VARIANTS LEU-20; ASP-272 AND MET-607. Tissue: Brain.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 380-919, VARIANT MET-607. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC073160 Genomic DNA. No translation available. BC002477 mRNA. Translation: AAH02477.1. BC007955 mRNA. Translation: AAH07955.1. AB046850 mRNA. Translation: BAB13456.1. Sequence problems. CR749726 mRNA. Translation: CAH18489.1.
IPI	IPI00063408.
PIR	T50617.
RefSeq	NP_061176.3. NM_018706.5.
UniGene	Hs.104980. Hs.711138.
3D structure databases
ProteinModelPortal	Q96HY7.
SMR	Q96HY7. Positions 58-914.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000263035.
PTM databases
PhosphoSite	Q96HY7.
Polymorphism databases
DMDM	296434477.
Proteomic databases
PaxDb	Q96HY7.
PRIDE	Q96HY7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263035; ENSP00000263035; ENSG00000181192.
GeneID	55526.
KEGG	hsa:55526.
UCSC	uc001ild.4. human.
Organism-specific databases
CTD	55526.
GeneCards	GC10P012028.
HGNC	HGNC:23537. DHTKD1.
HPA	HPA037950.
MIM	614984. gene.
neXtProt	NX_Q96HY7.
PharmGKB	PA134962952.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0567.
HOGENOM	HOG000259586.
HOVERGEN	HBG001892.
InParanoid	Q96HY7.
KO	K15791.
OMA	WGHNEMD.
OrthoDB	EOG4F7NJB.
PhylomeDB	Q96HY7.
Gene expression databases
ArrayExpress	Q96HY7.
Bgee	Q96HY7.
CleanEx	HS_DHTKD1.
Genevestigator	Q96HY7.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. PTHR23152. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	DHTKD1. human.
GenomeRNAi	55526.
NextBio	59950.
SOURCE	Search...

Entry information

Entry name

DHTK1_HUMAN

Accession

Primary (citable) accession number: Q96HY7
Secondary accession number(s): Q68CU5, Q9BUM8, Q9HCE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 82 of the entry and version 2 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.