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UniProtKB/Swiss-Prot entry P36957


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODO2_HUMAN
Primary accession number P36957
Secondary accession numbers Q7LDY7 Q9BQ32
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on September 23, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 99)
Name and origin of the protein
Protein name Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial [Precursor]
Synonyms EC 2.3.1.61
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2
E2K
Gene name
Name: DLST
Synonyms: DLTS
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0167-4781(93)90002-U; PubMed=8268217 [NCBI, ExPASy, EBI, Israel, Japan]
Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S., Ariyama T., Inazawa J., Abe T., Miyata T.;
"Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3.";
Biochim. Biophys. Acta 1216:360-368(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Peripheral blood;
PubMed=8076640 [NCBI, ExPASy, EBI, Israel, Japan]
Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S., Matuda S.;
"Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex.";
Eur. J. Biochem. 224:179-189(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-213.
TISSUE=Fetal brain;
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.;
"Physical mapping and nucleotide sequence analysis of the human dihydrolipoamide succinyltransferase gene.";
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-213.
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-213.
DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-213.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-213.
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D16373; BAA03871.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D26535; BAA05536.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L37418; AAB59629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK289414; BAF82103.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006530; AAD30181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471061; EAW81199.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000302; AAH00302.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001922; AAH01922.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S39786; PN0673.
UniGene Hs.525459
3D structure databases
HSSP P07016; 1C4T. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P36957.
Protein-protein interaction databases
IntAct P36957; -.
PTM databases
PhosphoSite P36957; -.
Enzyme and pathway databases
Reactome REACT_1046; Pyruvate metabolism and TCA cycle.
REACT_13; Metabolism of amino acids.
2D gel databases
OGP P36957; -.
Organism-specific databases
HGNC HGNC:2911; DLST.
GenAtlas DLST.
HPA HPA003010; -.
MIM 126063; gene. [NCBI / EBI]
PharmGKB PA27367; -.
GeneCards P36957.
Gene expression databases
CleanEx HS_DLST; -.
GermOnline ENSG00000119689; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from experiment from Reactome).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0045252; Cellular component: oxoglutarate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004149; Molecular function: dihydrolipoyllysine-residue succinyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031405; Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR000089; Biotin_lipoyl.
IPR006255; SucB.
Graphical view of domain structure.
Pfam PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
Pfam graphical view of domain structure.
ProDom PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01347; sucB; 1.
PROSITE PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P36957.
Genome annotation databases
Ensembl ENSG00000119689; Homo sapiens. [Contig view]
Phylogenomic databases
HOGENOM P36957; -.
HOVERGEN P36957; -.
Other
LinkHub P36957; -.
SOURCE DLST; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Lipoyl; Mitochondrion; Polymorphism; Transferase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    67  67     Mitochondrion (By similarity). 
CHAIN   68   453  386     Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial. PRO_0000020472
DOMAIN   71   143  73     Lipoyl-binding. 
ACT_SITE   424   424        Potential. 
ACT_SITE   428   428        Potential. 
BINDING   110   110        Lipoyl (covalent) (Potential). 
VARIANT   213   213  1     A -> P. VAR_004976 
VARIANT   384   384  1     P -> T. VAR_004977 
CONFLICT   14    15        RS -> AP (in Ref. 1; BAA03871, 2; BAA05536 and 3; AAB59629). 
CONFLICT   132   132        G -> T (in Ref. 1; BAA03871). 
CONFLICT   212   212        E -> D (in Ref. 1; BAA03871 and 2; BAA05536). 
CONFLICT   312   312        R -> T (in Ref. 2; BAA05536). 
Sequence information
Length: 453 AA [This is the length of the unprocessed precursor] Molecular weight: 48729 Da [This is the MW of the unprocessed precursor] CRC64: F40857A4E37DDD54 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI NNSVFSVRFF 

        70         80         90        100        110        120 
RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED EVVCEIETDK TSVQVPSPAN 

       130        140        150        160        170        180 
GVIEALLVPD GGKVEGGTPL FTLRKTGAAP AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI 

       190        200        210        220        230        240 
PTQMPPVPSP SQPPSGKPVS AVKPTVAPPL AEAGAGKGLR SEHREKMNRM RQRIAQRLKE 

       250        260        270        280        290        300 
AQNTCAMLTT FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA 

       310        320        330        340        350        360 
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL GEKARKNELA 

       370        380        390        400        410        420 
IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF DRPVAIGGKV EVRPMMYVAL 

       430        440        450 
TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL LDL 

P36957 in FASTA format

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