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Q9D2G2

- ODO2_MOUSE

UniProt

Q9D2G2 - ODO2_MOUSE

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

Dlst

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei425 – 4251Sequence Analysis
    Active sitei429 – 4291Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    2. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2
    Short name:
    OGDC-E2
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    E2K
    Gene namesi
    Name:Dlst
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1926170. Dlst.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. nucleus Source: Ensembl
    3. oxoglutarate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6868MitochondrionBy similarityAdd
    BLAST
    Chaini69 – 454386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020473Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111N6-lipoyllysineSequence Analysis
    Modified residuei155 – 1551N6-acetyllysine1 Publication
    Modified residuei268 – 2681N6-acetyllysine1 Publication
    Modified residuei273 – 2731N6-acetyllysine1 Publication
    Modified residuei274 – 2741N6-acetyllysine1 Publication
    Modified residuei278 – 2781N6-acetyllysine1 Publication
    Modified residuei308 – 3081N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9D2G2.
    PaxDbiQ9D2G2.
    PRIDEiQ9D2G2.

    2D gel databases

    REPRODUCTION-2DPAGEQ9D2G2.
    UCD-2DPAGEQ9D2G2.

    PTM databases

    PhosphoSiteiQ9D2G2.

    Expressioni

    Gene expression databases

    BgeeiQ9D2G2.
    GenevestigatoriQ9D2G2.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

    Protein-protein interaction databases

    BioGridi219707. 1 interaction.
    IntActiQ9D2G2. 5 interactions.
    MINTiMINT-1860129.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D2G2.
    SMRiQ9D2G2. Positions 72-146, 221-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 14473Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115255.
    HOGENOMiHOG000281563.
    HOVERGENiHBG000268.
    InParanoidiQ9D2G2.
    KOiK00658.
    OMAiVRTYADQ.
    OrthoDBiEOG78PV93.
    PhylomeDBiQ9D2G2.
    TreeFamiTF314164.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01347. sucB. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9D2G2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCRGP GYPDNRKMVI    50
    NSGSVFRVRF FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE 100
    DEVVCEIETD KTSVQVPSPA NGIIEALLVP DGGKVEGGTP LFTLRKTGAA 150
    PAKAKPAETP APAHKAEPAA PAAPPPPAAP VLTQMPPVPS PSQPPSSKPV 200
    SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK EAQNTCAMLT 250
    TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN 300
    AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE 350
    LGEKARKNEL AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHAI 400
    FDRPVAVGGK VEVRPMMYVA LTYDHRLIDG REAVTFLRKI KAAVEDPRVL 450
    LLDL 454
    Length:454
    Mass (Da):48,995
    Last modified:June 1, 2001 - v1
    Checksum:i9CB31698D185442A
    GO
    Isoform 2 (identifier: Q9D2G2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-253: Missing.
         254-257: EVDM → MTSL

    Note: No experimental confirmation available.

    Show »
    Length:201
    Mass (Da):22,230
    Checksum:iD999AAE99C49D3D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti276 – 2761N → S in BAE29011. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 253253Missing in isoform 2. 1 PublicationVSP_025015Add
    BLAST
    Alternative sequencei254 – 2574EVDM → MTSL in isoform 2. 1 PublicationVSP_025016

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK019713 mRNA. Translation: BAB31840.1.
    AK054053 mRNA. Translation: BAC35637.1.
    AK149664 mRNA. Translation: BAE29011.1.
    AK158877 mRNA. Translation: BAE34709.1.
    AK168570 mRNA. Translation: BAE40440.1.
    AK169943 mRNA. Translation: BAE41472.1.
    CT010197 mRNA. Translation: CAJ18405.1.
    BC006702 mRNA. Translation: AAH06702.1.
    BC024066 mRNA. Translation: AAH24066.1.
    CCDSiCCDS26052.1. [Q9D2G2-1]
    RefSeqiNP_084501.1. NM_030225.4. [Q9D2G2-1]
    UniGeneiMm.296221.

    Genome annotation databases

    EnsembliENSMUST00000053811; ENSMUSP00000060346; ENSMUSG00000004789. [Q9D2G2-1]
    GeneIDi78920.
    KEGGimmu:78920.
    UCSCiuc007ogj.2. mouse. [Q9D2G2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK019713 mRNA. Translation: BAB31840.1 .
    AK054053 mRNA. Translation: BAC35637.1 .
    AK149664 mRNA. Translation: BAE29011.1 .
    AK158877 mRNA. Translation: BAE34709.1 .
    AK168570 mRNA. Translation: BAE40440.1 .
    AK169943 mRNA. Translation: BAE41472.1 .
    CT010197 mRNA. Translation: CAJ18405.1 .
    BC006702 mRNA. Translation: AAH06702.1 .
    BC024066 mRNA. Translation: AAH24066.1 .
    CCDSi CCDS26052.1. [Q9D2G2-1 ]
    RefSeqi NP_084501.1. NM_030225.4. [Q9D2G2-1 ]
    UniGenei Mm.296221.

    3D structure databases

    ProteinModelPortali Q9D2G2.
    SMRi Q9D2G2. Positions 72-146, 221-454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 219707. 1 interaction.
    IntActi Q9D2G2. 5 interactions.
    MINTi MINT-1860129.

    Chemistry

    ChEMBLi CHEMBL2176822.

    PTM databases

    PhosphoSitei Q9D2G2.

    2D gel databases

    REPRODUCTION-2DPAGE Q9D2G2.
    UCD-2DPAGE Q9D2G2.

    Proteomic databases

    MaxQBi Q9D2G2.
    PaxDbi Q9D2G2.
    PRIDEi Q9D2G2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000053811 ; ENSMUSP00000060346 ; ENSMUSG00000004789 . [Q9D2G2-1 ]
    GeneIDi 78920.
    KEGGi mmu:78920.
    UCSCi uc007ogj.2. mouse. [Q9D2G2-1 ]

    Organism-specific databases

    CTDi 1743.
    MGIi MGI:1926170. Dlst.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115255.
    HOGENOMi HOG000281563.
    HOVERGENi HBG000268.
    InParanoidi Q9D2G2.
    KOi K00658.
    OMAi VRTYADQ.
    OrthoDBi EOG78PV93.
    PhylomeDBi Q9D2G2.
    TreeFami TF314164.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .

    Miscellaneous databases

    NextBioi 349758.
    PROi Q9D2G2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D2G2.
    Genevestigatori Q9D2G2.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    TIGRFAMsi TIGR01347. sucB. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Heart, Oviduct, Testis and Visual cortex.
    2. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
      Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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] (ISOFORMS 1 AND 2).
      Strain: Czech II and FVB/N.
      Tissue: Mammary tumor.
    4. Lubec G., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 69-89; 288-308; 314-334 AND 355-346, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155; LYS-268; LYS-273; LYS-274; LYS-278 AND LYS-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiODO2_MOUSE
    AccessioniPrimary (citable) accession number: Q9D2G2
    Secondary accession number(s): Q3UEA0, Q4FK55, Q8CIE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 117 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3