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P36957

- ODO2_HUMAN

UniProt

P36957 - ODO2_HUMAN

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Protein

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

Gene
DLST, DLTS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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).

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei424 – 4241 Reviewed prediction
Active sitei428 – 4281 Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. generation of precursor metabolites and energy Source: ProtInc
  4. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  5. lysine catabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciMetaCyc:HS04324-MONOMER.
ReactomeiREACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).
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
Synonyms:DLTS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:2911. DLST.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial matrix Source: Reactome
  3. nucleus Source: UniProt
  4. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6767Mitochondrion1 PublicationAdd
BLAST
Chaini68 – 453386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-lipoyllysine Reviewed prediction
Modified residuei154 – 1541N6-acetyllysine By similarity
Modified residuei267 – 2671N6-acetyllysine By similarity
Modified residuei272 – 2721N6-acetyllysine By similarity
Modified residuei273 – 2731N6-acetyllysine By similarity
Modified residuei277 – 2771N6-acetyllysine By similarity
Modified residuei307 – 3071N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP36957.
PaxDbiP36957.
PRIDEiP36957.

2D gel databases

OGPiP36957.
UCD-2DPAGEP36957.

PTM databases

PhosphoSiteiP36957.

Expressioni

Gene expression databases

ArrayExpressiP36957.
BgeeiP36957.
CleanExiHS_DLST.
GenevestigatoriP36957.

Organism-specific databases

HPAiHPA003010.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

BioGridi108087. 26 interactions.
IntActiP36957. 19 interactions.
MINTiMINT-3014449.
STRINGi9606.ENSP00000335304.

Structurei

3D structure databases

ProteinModelPortaliP36957.
SMRiP36957. Positions 73-140, 220-453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 14373Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiP36957.
KOiK00658.
OMAiQIFRNIF.
PhylomeDBiP36957.
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]

Sequencei

Sequence statusi: Complete.

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

P36957-1 [UniParc]FASTAAdd to Basket

« Hide

MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI    50
NNSVFSVRFF RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED 100
EVVCEIETDK TSVQVPSPAN GVIEALLVPD GGKVEGGTPL FTLRKTGAAP 150
AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI PTQMPPVPSP SQPPSGKPVS 200
AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE AQNTCAMLTT 250
FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA 300
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL 350
GEKARKNELA IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF 400
DRPVAIGGKV EVRPMMYVAL TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL 450
LDL 453
Length:453
Mass (Da):48,755
Last modified:January 11, 2011 - v4
Checksum:iA30E8CC959106B8F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti213 – 2131P → A.2 Publications
Corresponds to variant rs2853769 [ dbSNP | Ensembl ].
VAR_004976
Natural varianti384 – 3841P → T.
VAR_004977

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152RS → AP in BAA03871. 1 Publication
Sequence conflicti14 – 152RS → AP in BAA05536. 1 Publication
Sequence conflicti14 – 152RS → AP in AAB59629. 1 Publication
Sequence conflicti132 – 1321G → T in BAA03871. 1 Publication
Sequence conflicti212 – 2121E → D in BAA03871. 1 Publication
Sequence conflicti212 – 2121E → D in BAA05536. 1 Publication
Sequence conflicti312 – 3121R → T in BAA05536. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16373 mRNA. Translation: BAA03871.1.
D26535 Genomic DNA. Translation: BAA05536.1.
L37418 mRNA. Translation: AAB59629.1.
AK289414 mRNA. Translation: BAF82103.1.
AC006530 Genomic DNA. Translation: AAD30181.1.
CH471061 Genomic DNA. Translation: EAW81199.1.
BC000302 mRNA. Translation: AAH00302.1.
BC001922 mRNA. Translation: AAH01922.1.
CCDSiCCDS9833.1.
PIRiS39786. PN0673.
RefSeqiNP_001924.2. NM_001933.4.
UniGeneiHs.525459.

Genome annotation databases

EnsembliENST00000334220; ENSP00000335304; ENSG00000119689.
GeneIDi1743.
KEGGihsa:1743.
UCSCiuc001xqs.3. human.

Polymorphism databases

DMDMi317373578.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16373 mRNA. Translation: BAA03871.1 .
D26535 Genomic DNA. Translation: BAA05536.1 .
L37418 mRNA. Translation: AAB59629.1 .
AK289414 mRNA. Translation: BAF82103.1 .
AC006530 Genomic DNA. Translation: AAD30181.1 .
CH471061 Genomic DNA. Translation: EAW81199.1 .
BC000302 mRNA. Translation: AAH00302.1 .
BC001922 mRNA. Translation: AAH01922.1 .
CCDSi CCDS9833.1.
PIRi S39786. PN0673.
RefSeqi NP_001924.2. NM_001933.4.
UniGenei Hs.525459.

3D structure databases

ProteinModelPortali P36957.
SMRi P36957. Positions 73-140, 220-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108087. 26 interactions.
IntActi P36957. 19 interactions.
MINTi MINT-3014449.
STRINGi 9606.ENSP00000335304.

PTM databases

PhosphoSitei P36957.

Polymorphism databases

DMDMi 317373578.

2D gel databases

OGPi P36957.
UCD-2DPAGE P36957.

Proteomic databases

MaxQBi P36957.
PaxDbi P36957.
PRIDEi P36957.

Protocols and materials databases

DNASUi 1743.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334220 ; ENSP00000335304 ; ENSG00000119689 .
GeneIDi 1743.
KEGGi hsa:1743.
UCSCi uc001xqs.3. human.

Organism-specific databases

CTDi 1743.
GeneCardsi GC14P075348.
H-InvDB HIX0131240.
HGNCi HGNC:2911. DLST.
HPAi HPA003010.
MIMi 126063. gene.
neXtProti NX_P36957.
PharmGKBi PA27367.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281563.
HOVERGENi HBG000268.
InParanoidi P36957.
KOi K00658.
OMAi QIFRNIF.
PhylomeDBi P36957.
TreeFami TF314164.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .
BioCyci MetaCyc:HS04324-MONOMER.
Reactomei REACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi DLST. human.
GeneWikii DLST.
GenomeRNAii 1743.
NextBioi 7071.
PROi P36957.
SOURCEi Search...

Gene expression databases

ArrayExpressi P36957.
Bgeei P36957.
CleanExi HS_DLST.
Genevestigatori P36957.

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. "Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3."
    Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S., Ariyama T., Inazawa J., Abe T., Miyata T.
    Biochim. Biophys. Acta 1216:360-368(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-213.
  2. "Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex."
    Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S., Matuda S.
    Eur. J. Biochem. 224:179-189(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-213.
    Tissue: Peripheral blood.
  3. "Physical mapping and nucleotide sequence analysis of the human dihydrolipoamide succinyltransferase gene."
    Keryanov S., Liang Y., Rogaev E.I., Sherrington R., Tsuda T., Rogaeva E., Chi H., Crapper-Mclachlan D., Chumakov Y., Rommens J.M., St George-Hyslop P.H.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Lung.
  8. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
    Xu G., Shin S.B., Jaffrey S.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89.
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiODO2_HUMAN
AccessioniPrimary (citable) accession number: P36957
Secondary accession number(s): Q7LDY7, Q9BQ32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 160 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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