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Q9D2G2

- ODO2_MOUSE

UniProt

Q9D2G2 - ODO2_MOUSE

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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

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.

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 – 4251 Reviewed prediction
Active sitei429 – 4291 Reviewed prediction

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6868Mitochondrion By similarity
Add
BLAST
Chaini69 – 454386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
PRO_0000020473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-lipoyllysine Reviewed prediction
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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 253253Missing in isoform 2.
VSP_025015Add
BLAST
Alternative sequencei254 – 2574EVDM → MTSL in isoform 2.
VSP_025016

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti276 – 2761N → S in BAE29011. 1 Publication

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...

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

« 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] (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: July 9, 2014
This is version 116 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

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