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Q8BMF4

- ODP2_MOUSE

UniProt

Q8BMF4 - ODP2_MOUSE

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

Dlat

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

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.By similarity

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei615 – 6151Sequence Analysis
Active sitei619 – 6191Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: MGI

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: MGI
  2. glucose metabolic process Source: UniProtKB-KW
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name:
PDC-E2
Short name:
PDCE2
Gene namesi
Name:Dlat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:2385311. Dlat.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial pyruvate dehydrogenase complex Source: MGI
  2. mitochondrion Source: MGI
  3. pyruvate dehydrogenase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8585MitochondrionBy similarityAdd
BLAST
Chaini86 – 642557Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000285717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei258 – 2581N6-lipoyllysineBy similarity
Modified residuei461 – 4611N6-acetyllysineBy similarity
Modified residuei468 – 4681N6-succinyllysine1 Publication
Modified residuei542 – 5421N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BMF4.
PaxDbiQ8BMF4.
PRIDEiQ8BMF4.

2D gel databases

REPRODUCTION-2DPAGEIPI00153660.
UCD-2DPAGEQ8BMF4.

PTM databases

PhosphoSiteiQ8BMF4.

Expressioni

Gene expression databases

BgeeiQ8BMF4.
GenevestigatoriQ8BMF4.

Interactioni

Subunit structurei

Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi231646. 2 interactions.
IntActiQ8BMF4. 7 interactions.
MINTiMINT-135876.

Structurei

3D structure databases

ProteinModelPortaliQ8BMF4.
SMRiQ8BMF4. Positions 91-181, 217-294, 349-388, 404-642.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 16575Lipoyl-binding 1Add
BLAST
Domaini218 – 29275Lipoyl-binding 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni353 – 38432E3- and/or E1-component binding domainSequence AnalysisAdd
BLAST
Regioni466 – 642177CatalyticBy similarityAdd
BLAST
Regioni610 – 62112CoA-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 2 lipoyl-binding domains.Curated

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00760000119281.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiQ8BMF4.
KOiK00627.
OMAiPISNIRK.
OrthoDBiEOG7K3TKW.
PhylomeDBiQ8BMF4.
TreeFamiTF106145.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BMF4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWRVCARRAR SAVPRDGFRA RWAALKEGPG APCGSPRIGP AAVRCGSGIP
60 70 80 90 100
RYGVRSLCGW SSGSGTVPRN RLLRQLLGSP SRRSYSLPPH QKVPLPSLSP
110 120 130 140 150
TMQAGTIARW EKKEGEKISE GDLIAEVETD KATVGFESLE ECYMAKILVP
160 170 180 190 200
EGTRDVPVGS IICITVEKPQ DIEAFKNYTL DLAAAAAPQA APAAAPAPAA
210 220 230 240 250
APAAPSASAP GSSYPTHMQI VLPALSPTMT MGTVQRWEKK VGEKLSEGDL
260 270 280 290 300
LAEIETDKAT IGFEVQEEGY LAKILVPEGT RDVPLGAPLC IIVEKQEDIA
310 320 330 340 350
AFADYRPTEV TSLKPQAAPP APPPVAAVPP TPQPVAPTPS AAPAGPKGRV
360 370 380 390 400
FVSPLAKKLA AEKGIDLTQV KGTGPEGRII KKDIDSFVPS KAAPAAAAAM
410 420 430 440 450
APPGPRVAPA PAGVFTDIPI SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG
460 470 480 490 500
EVLLVRKELN KMLEGKGKIS VNDFIIKASA LACLKVPEAN SSWMDTVIRQ
510 520 530 540 550
NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA SKAREGKLQP
560 570 580 590 600
HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG
610 620 630 640
FDVASVMSVT LSCDHRVVDG AVGAQWLAEF KKYLEKPITM LL
Length:642
Mass (Da):67,942
Last modified:May 1, 2007 - v2
Checksum:i1294FAC4857FC29C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841S → Y in AAL02400. (PubMed:12108679)Curated
Sequence conflicti198 – 1981P → T in BAC27715. (PubMed:16141072)Curated
Sequence conflicti225 – 2251L → P in AAL02400. (PubMed:12108679)Curated
Sequence conflicti393 – 3931A → V in AAH31495. (PubMed:15489334)Curated
Sequence conflicti604 – 6041A → V in AAH31495. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK032124 mRNA. Translation: BAC27715.1.
BC026680 mRNA. Translation: AAH26680.1.
BC031495 mRNA. Translation: AAH31495.1.
BC069862 mRNA. Translation: AAH69862.1.
AY044265 mRNA. Translation: AAL02400.1.
CCDSiCCDS23168.1.
RefSeqiNP_663589.3. NM_145614.4.
UniGeneiMm.285076.
Mm.471144.

Genome annotation databases

EnsembliENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168.
GeneIDi235339.
KEGGimmu:235339.
UCSCiuc009pka.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK032124 mRNA. Translation: BAC27715.1 .
BC026680 mRNA. Translation: AAH26680.1 .
BC031495 mRNA. Translation: AAH31495.1 .
BC069862 mRNA. Translation: AAH69862.1 .
AY044265 mRNA. Translation: AAL02400.1 .
CCDSi CCDS23168.1.
RefSeqi NP_663589.3. NM_145614.4.
UniGenei Mm.285076.
Mm.471144.

3D structure databases

ProteinModelPortali Q8BMF4.
SMRi Q8BMF4. Positions 91-181, 217-294, 349-388, 404-642.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 231646. 2 interactions.
IntActi Q8BMF4. 7 interactions.
MINTi MINT-135876.

PTM databases

PhosphoSitei Q8BMF4.

2D gel databases

REPRODUCTION-2DPAGE IPI00153660.
UCD-2DPAGE Q8BMF4.

Proteomic databases

MaxQBi Q8BMF4.
PaxDbi Q8BMF4.
PRIDEi Q8BMF4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034567 ; ENSMUSP00000034567 ; ENSMUSG00000000168 .
GeneIDi 235339.
KEGGi mmu:235339.
UCSCi uc009pka.2. mouse.

Organism-specific databases

CTDi 1737.
MGIi MGI:2385311. Dlat.

Phylogenomic databases

eggNOGi COG0508.
GeneTreei ENSGT00760000119281.
HOGENOMi HOG000281566.
HOVERGENi HBG005063.
InParanoidi Q8BMF4.
KOi K00627.
OMAi PISNIRK.
OrthoDBi EOG7K3TKW.
PhylomeDBi Q8BMF4.
TreeFami TF106145.

Enzyme and pathway databases

Reactomei REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

ChiTaRSi DLAT. mouse.
NextBioi 382617.
PROi Q8BMF4.
SOURCEi Search...

Gene expression databases

Bgeei Q8BMF4.
Genevestigatori Q8BMF4.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  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].
    Strain: Czech II, FVB/N-3 and NMRI.
    Tissue: Mammary tumor.
  3. "Molecular cloning, and characterization and expression of dihydrolipoamide acetyltransferase component of murine pyruvate dehydrogenase complex in bile duct cancer cells."
    Wang L., Kaneko S., Kagaya M., Ohno H., Honda M., Kobayashi K.
    J. Gastroenterol. 37:449-454(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-642.
    Tissue: Hepatoma.
  4. Lubec G., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 93-109; 147-176; 282-295; 383-424; 469-477; 486-499; 528-542; 548-569; 600-631 AND 633-642, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "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-468 AND LYS-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiODP2_MOUSE
AccessioniPrimary (citable) accession number: Q8BMF4
Secondary accession number(s): Q8K2G8, Q8R339, Q91ZB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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