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A2ATU0

- DHTK1_MOUSE

UniProt

A2ATU0 - DHTK1_MOUSE

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Protein

Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial

Gene

Dhtkd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactori

Thiamine pyrophosphate.By similarity

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
  2. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. generation of precursor metabolites and energy Source: UniProtKB
  2. glycolytic process Source: UniProtKB-KW
  3. hematopoietic progenitor cell differentiation Source: MGI
  4. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
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 namesi
Name:Dhtkd1
Synonyms:Kiaa1630
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2445096. Dhtkd1.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 921Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrialPRO_0000307937
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841N6-succinyllysine1 Publication
Modified residuei189 – 1891N6-succinyllysine1 Publication
Modified residuei801 – 8011N6-succinyllysine1 Publication
Modified residuei819 – 8191N6-succinyllysine1 Publication

Proteomic databases

MaxQBiA2ATU0.
PaxDbiA2ATU0.
PRIDEiA2ATU0.

PTM databases

PhosphoSiteiA2ATU0.

Expressioni

Gene expression databases

BgeeiA2ATU0.
GenevestigatoriA2ATU0.

Interactioni

Protein-protein interaction databases

IntActiA2ATU0. 2 interactions.
MINTiMINT-1839549.

Structurei

3D structure databases

ProteinModelPortaliA2ATU0.
SMRiA2ATU0. Positions 60-919.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0567.
GeneTreeiENSGT00530000063092.
HOGENOMiHOG000259586.
HOVERGENiHBG001892.
InParanoidiA2ATU0.
KOiK15791.
OMAiLCSGKHY.
OrthoDBiEOG7CZK4Z.
PhylomeDBiA2ATU0.
TreeFamiTF314198.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2ATU0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASAATVAAA GRALRRAVLL LRRGYQTERG VYGYRPRKAK SGEPRGDRAR
60 70 80 90 100
PSVDHGLARL VTVYCEHGHK AAQINPLFPG QALLDTVPEI QALVRTLQGP
110 120 130 140 150
FTTTGLLNLG KEAASLEEVL AYLNHIYCGP ISIETAQLQS QEERDWFARR
160 170 180 190 200
FEELKKETFT TEERKYLSKL LLESQEFDHF LATKFATVKR YGGEGAESMM
210 220 230 240 250
GFFHELLKLS AYGGITDIII GMPHRGRLNL LTGLLQLPPE LMFRKMRGLS
260 270 280 290 300
EFPENVATIG DVLSHLTSSV DLDFGAHQPL HVTMLPNPSH LEAVNPVAVG
310 320 330 340 350
KTRGRQQSRE DGDYSPNGSA QPGDKVICLQ VHGDASFCGQ GIVLETFTLS
360 370 380 390 400
NLPHFRIGGS IHLIVNNQLG YTTPAERGRS SLYSSDIGKL VGCAIIHVNG
410 420 430 440 450
DSPEEVVRAT RLAFEYQRQF RKDVIVDLLC YRQWGHNELD EPFFTNPVMY
460 470 480 490 500
KIIRARKSIP DTYAEHLIAS GLMTQEEVSD IKTSYYTKLN DHLANVAHYS
510 520 530 540 550
PPATNLQARW QGLVQPEACV TTWDTGVPLE LLRFIGVKSV EVPEELQVHS
560 570 580 590 600
HLLKMYVQSR MEKVKNGSGL DWATAETLAL GSLLAQGFNV RLSGQDVGRG
610 620 630 640 650
TFSQRHAMVV CQDTDDAYIP LNHMDPNQKG FLEVSNSPLS EEAVLGFEYG
660 670 680 690 700
MSIESPTLLP LWEAQFGDFF NGAQIIFDTF ISGGEAKWLL QSGLVILLPH
710 720 730 740 750
GYDGAGPEHS SCRIERFLQM CDSAEEGVDS DTVNMFVVHP TTPAQYFHLL
760 770 780 790 800
RRQMIRNFRK PLIVASPKML LRYPAAVSTL EEMAPGTAFK PVIGDSSVDP
810 820 830 840 850
KNVKTLIFCS GKHFYALLKQ RESLGTKKHD FAIIRLEELC PFPLDALQQE
860 870 880 890 900
MSKYKHVRDV IWSQEEPQNM GPWSFVSPRF EKQLACRLRL VSRPPLPAPA
910 920
VGIGTVHQQQ HEDILSKTFT Q
Length:921
Mass (Da):102,793
Last modified:February 20, 2007 - v1
Checksum:iE40170D7D26EED65
GO

Sequence cautioni

The sequence BAD32501.1 differs from that shown. Reason: Intron retention.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241G → S in AAI17995. (PubMed:15489334)Curated
Sequence conflicti436 – 4361H → R in AAI17995. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL928924 Genomic DNA. Translation: CAM20352.1.
BC117994 mRNA. Translation: AAI17995.1.
AK173223 mRNA. Translation: BAD32501.1. Sequence problems.
AK050057 mRNA. Translation: BAC34055.1.
CCDSiCCDS38040.1.
RefSeqiNP_001074600.1. NM_001081131.2.
UniGeneiMm.222517.

Genome annotation databases

EnsembliENSMUST00000026924; ENSMUSP00000026924; ENSMUSG00000025815.
ENSMUST00000095147; ENSMUSP00000092769; ENSMUSG00000025815.
ENSMUST00000169865; ENSMUSP00000129194; ENSMUSG00000025815.
GeneIDi209692.
KEGGimmu:209692.
UCSCiuc008iga.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL928924 Genomic DNA. Translation: CAM20352.1 .
BC117994 mRNA. Translation: AAI17995.1 .
AK173223 mRNA. Translation: BAD32501.1 . Sequence problems.
AK050057 mRNA. Translation: BAC34055.1 .
CCDSi CCDS38040.1.
RefSeqi NP_001074600.1. NM_001081131.2.
UniGenei Mm.222517.

3D structure databases

ProteinModelPortali A2ATU0.
SMRi A2ATU0. Positions 60-919.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi A2ATU0. 2 interactions.
MINTi MINT-1839549.

PTM databases

PhosphoSitei A2ATU0.

Proteomic databases

MaxQBi A2ATU0.
PaxDbi A2ATU0.
PRIDEi A2ATU0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026924 ; ENSMUSP00000026924 ; ENSMUSG00000025815 .
ENSMUST00000095147 ; ENSMUSP00000092769 ; ENSMUSG00000025815 .
ENSMUST00000169865 ; ENSMUSP00000129194 ; ENSMUSG00000025815 .
GeneIDi 209692.
KEGGi mmu:209692.
UCSCi uc008iga.1. mouse.

Organism-specific databases

CTDi 55526.
MGIi MGI:2445096. Dhtkd1.
Rougei Search...

Phylogenomic databases

eggNOGi COG0567.
GeneTreei ENSGT00530000063092.
HOGENOMi HOG000259586.
HOVERGENi HBG001892.
InParanoidi A2ATU0.
KOi K15791.
OMAi LCSGKHY.
OrthoDBi EOG7CZK4Z.
PhylomeDBi A2ATU0.
TreeFami TF314198.

Miscellaneous databases

ChiTaRSi DHTKD1. mouse.
NextBioi 372765.
PROi A2ATU0.
SOURCEi Search...

Gene expression databases

Bgeei A2ATU0.
Genevestigatori A2ATU0.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 330-587.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 525-921.
    Strain: C57BL/6J.
    Tissue: Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-184; LYS-189; LYS-801 AND LYS-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDHTK1_MOUSE
AccessioniPrimary (citable) accession number: A2ATU0
Secondary accession number(s): Q0VFY3, Q69ZE3, Q8BWT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: February 20, 2007
Last modified: October 1, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3