Full text data of DLST
DLST
(DLTS)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2.3.1.61 (2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2.3.1.61 (2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P36957
ID ODO2_HUMAN Reviewed; 453 AA.
AC P36957; Q7LDY7; Q9BQ32;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
DE EC=2.3.1.61;
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE Short=OGDC-E2;
DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE AltName: Full=E2K;
DE Flags: Precursor;
GN Name=DLST; Synonyms=DLTS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-213.
RX PubMed=8268217; DOI=10.1016/0167-4781(93)90002-U;
RA Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S.,
RA Ariyama T., Inazawa J., Abe T., Miyata T.;
RT "Human dihydrolipoamide succinyltransferase: cDNA cloning and
RT localization on chromosome 14q24.2-q24.3.";
RL Biochim. Biophys. Acta 1216:360-368(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-213.
RC TISSUE=Peripheral blood;
RX PubMed=8076640; DOI=10.1111/j.1432-1033.1994.tb20010.x;
RA Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S.,
RA Matuda S.;
RT "Isolation, characterization and structural organization of the gene
RT and pseudogene for the dihydrolipoamide succinyltransferase component
RT of the human 2-oxoglutarate dehydrogenase complex.";
RL Eur. J. Biochem. 224:179-189(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Keryanov S., Liang Y., Rogaev E.I., Sherrington R., Tsuda T.,
RA Rogaeva E., Chi H., Crapper-Mclachlan D., Chumakov Y., Rommens J.M.,
RA St George-Hyslop P.H.;
RT "Physical mapping and nucleotide sequence analysis of the human
RT dihydrolipoamide succinyltransferase gene.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
CC succinyldihydrolipoyl)lysine.
CC -!- COFACTOR: Binds 1 lipoyl cofactor covalently.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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DR EMBL; D16373; BAA03871.1; -; mRNA.
DR EMBL; D26535; BAA05536.1; -; Genomic_DNA.
DR EMBL; L37418; AAB59629.1; -; mRNA.
DR EMBL; AK289414; BAF82103.1; -; mRNA.
DR EMBL; AC006530; AAD30181.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81199.1; -; Genomic_DNA.
DR EMBL; BC000302; AAH00302.1; -; mRNA.
DR EMBL; BC001922; AAH01922.1; -; mRNA.
DR PIR; S39786; PN0673.
DR RefSeq; NP_001924.2; NM_001933.4.
DR UniGene; Hs.525459; -.
DR ProteinModelPortal; P36957; -.
DR SMR; P36957; 73-140, 220-453.
DR IntAct; P36957; 19.
DR MINT; MINT-3014449; -.
DR STRING; 9606.ENSP00000335304; -.
DR PhosphoSite; P36957; -.
DR DMDM; 206729909; -.
DR OGP; P36957; -.
DR UCD-2DPAGE; P36957; -.
DR PaxDb; P36957; -.
DR PRIDE; P36957; -.
DR DNASU; 1743; -.
DR Ensembl; ENST00000334220; ENSP00000335304; ENSG00000119689.
DR GeneID; 1743; -.
DR KEGG; hsa:1743; -.
DR UCSC; uc001xqs.3; human.
DR CTD; 1743; -.
DR GeneCards; GC14P075348; -.
DR H-InvDB; HIX0131240; -.
DR HGNC; HGNC:2911; DLST.
DR HPA; HPA003010; -.
DR MIM; 126063; gene.
DR neXtProt; NX_P36957; -.
DR PharmGKB; PA27367; -.
DR eggNOG; COG0508; -.
DR HOGENOM; HOG000281563; -.
DR HOVERGEN; HBG000268; -.
DR InParanoid; P36957; -.
DR KO; K00658; -.
DR OMA; IKFTCKV; -.
DR PhylomeDB; P36957; -.
DR BioCyc; MetaCyc:HS04324-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00868; UER00840.
DR ChiTaRS; DLST; human.
DR GeneWiki; DLST; -.
DR GenomeRNAi; 1743; -.
DR NextBio; 7071; -.
DR PRO; PR:P36957; -.
DR ArrayExpress; P36957; -.
DR Bgee; P36957; -.
DR CleanEx; HS_DLST; -.
DR Genevestigator; P36957; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR006255; SucB.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01347; sucB; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Complete proteome;
KW Direct protein sequencing; Lipoyl; Mitochondrion; Polymorphism;
KW Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1 67 Mitochondrion.
FT CHAIN 68 453 Dihydrolipoyllysine-residue
FT succinyltransferase component of 2-
FT oxoglutarate dehydrogenase complex,
FT mitochondrial.
FT /FTId=PRO_0000020472.
FT DOMAIN 71 143 Lipoyl-binding.
FT ACT_SITE 424 424 Potential.
FT ACT_SITE 428 428 Potential.
FT MOD_RES 110 110 N6-lipoyllysine (Potential).
FT MOD_RES 154 154 N6-acetyllysine (By similarity).
FT MOD_RES 267 267 N6-acetyllysine (By similarity).
FT MOD_RES 272 272 N6-acetyllysine (By similarity).
FT MOD_RES 273 273 N6-acetyllysine (By similarity).
FT MOD_RES 277 277 N6-acetyllysine (By similarity).
FT MOD_RES 307 307 N6-acetyllysine (By similarity).
FT VARIANT 213 213 P -> A (in dbSNP:rs2853769).
FT /FTId=VAR_004976.
FT VARIANT 384 384 P -> T.
FT /FTId=VAR_004977.
FT CONFLICT 14 15 RS -> AP (in Ref. 1; BAA03871, 2;
FT BAA05536 and 3; AAB59629).
FT CONFLICT 132 132 G -> T (in Ref. 1; BAA03871).
FT CONFLICT 212 212 E -> D (in Ref. 1; BAA03871 and 2;
FT BAA05536).
FT CONFLICT 312 312 R -> T (in Ref. 2; BAA05536).
SQ SEQUENCE 453 AA; 48755 MW; A30E8CC959106B8F CRC64;
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI NNSVFSVRFF
RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED EVVCEIETDK TSVQVPSPAN
GVIEALLVPD GGKVEGGTPL FTLRKTGAAP AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI
PTQMPPVPSP SQPPSGKPVS AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE
AQNTCAMLTT FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL GEKARKNELA
IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF DRPVAIGGKV EVRPMMYVAL
TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL LDL
//
ID ODO2_HUMAN Reviewed; 453 AA.
AC P36957; Q7LDY7; Q9BQ32;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
DE EC=2.3.1.61;
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE Short=OGDC-E2;
DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE AltName: Full=E2K;
DE Flags: Precursor;
GN Name=DLST; Synonyms=DLTS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-213.
RX PubMed=8268217; DOI=10.1016/0167-4781(93)90002-U;
RA Nakano K., Matsuda S., Sakamoto T., Takase C., Nakagawa S., Ohta S.,
RA Ariyama T., Inazawa J., Abe T., Miyata T.;
RT "Human dihydrolipoamide succinyltransferase: cDNA cloning and
RT localization on chromosome 14q24.2-q24.3.";
RL Biochim. Biophys. Acta 1216:360-368(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-213.
RC TISSUE=Peripheral blood;
RX PubMed=8076640; DOI=10.1111/j.1432-1033.1994.tb20010.x;
RA Nakano K., Takase C., Sakamoto T., Nakagawa S., Inazawa J., Ohta S.,
RA Matuda S.;
RT "Isolation, characterization and structural organization of the gene
RT and pseudogene for the dihydrolipoamide succinyltransferase component
RT of the human 2-oxoglutarate dehydrogenase complex.";
RL Eur. J. Biochem. 224:179-189(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Keryanov S., Liang Y., Rogaev E.I., Sherrington R., Tsuda T.,
RA Rogaeva E., Chi H., Crapper-Mclachlan D., Chumakov Y., Rommens J.M.,
RA St George-Hyslop P.H.;
RT "Physical mapping and nucleotide sequence analysis of the human
RT dihydrolipoamide succinyltransferase gene.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
CC succinyldihydrolipoyl)lysine.
CC -!- COFACTOR: Binds 1 lipoyl cofactor covalently.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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DR EMBL; D16373; BAA03871.1; -; mRNA.
DR EMBL; D26535; BAA05536.1; -; Genomic_DNA.
DR EMBL; L37418; AAB59629.1; -; mRNA.
DR EMBL; AK289414; BAF82103.1; -; mRNA.
DR EMBL; AC006530; AAD30181.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81199.1; -; Genomic_DNA.
DR EMBL; BC000302; AAH00302.1; -; mRNA.
DR EMBL; BC001922; AAH01922.1; -; mRNA.
DR PIR; S39786; PN0673.
DR RefSeq; NP_001924.2; NM_001933.4.
DR UniGene; Hs.525459; -.
DR ProteinModelPortal; P36957; -.
DR SMR; P36957; 73-140, 220-453.
DR IntAct; P36957; 19.
DR MINT; MINT-3014449; -.
DR STRING; 9606.ENSP00000335304; -.
DR PhosphoSite; P36957; -.
DR DMDM; 206729909; -.
DR OGP; P36957; -.
DR UCD-2DPAGE; P36957; -.
DR PaxDb; P36957; -.
DR PRIDE; P36957; -.
DR DNASU; 1743; -.
DR Ensembl; ENST00000334220; ENSP00000335304; ENSG00000119689.
DR GeneID; 1743; -.
DR KEGG; hsa:1743; -.
DR UCSC; uc001xqs.3; human.
DR CTD; 1743; -.
DR GeneCards; GC14P075348; -.
DR H-InvDB; HIX0131240; -.
DR HGNC; HGNC:2911; DLST.
DR HPA; HPA003010; -.
DR MIM; 126063; gene.
DR neXtProt; NX_P36957; -.
DR PharmGKB; PA27367; -.
DR eggNOG; COG0508; -.
DR HOGENOM; HOG000281563; -.
DR HOVERGEN; HBG000268; -.
DR InParanoid; P36957; -.
DR KO; K00658; -.
DR OMA; IKFTCKV; -.
DR PhylomeDB; P36957; -.
DR BioCyc; MetaCyc:HS04324-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00868; UER00840.
DR ChiTaRS; DLST; human.
DR GeneWiki; DLST; -.
DR GenomeRNAi; 1743; -.
DR NextBio; 7071; -.
DR PRO; PR:P36957; -.
DR ArrayExpress; P36957; -.
DR Bgee; P36957; -.
DR CleanEx; HS_DLST; -.
DR Genevestigator; P36957; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR006255; SucB.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01347; sucB; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Complete proteome;
KW Direct protein sequencing; Lipoyl; Mitochondrion; Polymorphism;
KW Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1 67 Mitochondrion.
FT CHAIN 68 453 Dihydrolipoyllysine-residue
FT succinyltransferase component of 2-
FT oxoglutarate dehydrogenase complex,
FT mitochondrial.
FT /FTId=PRO_0000020472.
FT DOMAIN 71 143 Lipoyl-binding.
FT ACT_SITE 424 424 Potential.
FT ACT_SITE 428 428 Potential.
FT MOD_RES 110 110 N6-lipoyllysine (Potential).
FT MOD_RES 154 154 N6-acetyllysine (By similarity).
FT MOD_RES 267 267 N6-acetyllysine (By similarity).
FT MOD_RES 272 272 N6-acetyllysine (By similarity).
FT MOD_RES 273 273 N6-acetyllysine (By similarity).
FT MOD_RES 277 277 N6-acetyllysine (By similarity).
FT MOD_RES 307 307 N6-acetyllysine (By similarity).
FT VARIANT 213 213 P -> A (in dbSNP:rs2853769).
FT /FTId=VAR_004976.
FT VARIANT 384 384 P -> T.
FT /FTId=VAR_004977.
FT CONFLICT 14 15 RS -> AP (in Ref. 1; BAA03871, 2;
FT BAA05536 and 3; AAB59629).
FT CONFLICT 132 132 G -> T (in Ref. 1; BAA03871).
FT CONFLICT 212 212 E -> D (in Ref. 1; BAA03871 and 2;
FT BAA05536).
FT CONFLICT 312 312 R -> T (in Ref. 2; BAA05536).
SQ SEQUENCE 453 AA; 48755 MW; A30E8CC959106B8F CRC64;
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI NNSVFSVRFF
RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED EVVCEIETDK TSVQVPSPAN
GVIEALLVPD GGKVEGGTPL FTLRKTGAAP AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI
PTQMPPVPSP SQPPSGKPVS AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE
AQNTCAMLTT FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL GEKARKNELA
IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF DRPVAIGGKV EVRPMMYVAL
TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL LDL
//
MIM
126063
*RECORD*
*FIELD* NO
126063
*FIELD* TI
*126063 DIHYDROLIPOAMIDE S-SUCCINYLTRANSFERASE; DLST
;;ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX, E2 COMPONENT OF
read more*FIELD* TX
CLONING
The alpha-keto acid dehydrogenase complexes (pyruvate dehydrogenase
complex, alpha-ketoglutarate dehydrogenase complex, and branched chain
alpha-keto acid dehydrogenase complex) are a family of multienzyme
complexes. They are localized in mitochondria and catalyze the oxidative
decarboxylation of alpha-keto acids. These 3 alpha-keto acid
dehydrogenase complexes are composed of 3 different enzymes: alpha-keto
acid dehydrogenase (E1; 300502), dihydrolipoamide acyltransferase (E2),
and dihydrolipoamide dehydrogenase (E3; 238331). Dihydrolipoamide
succinyltransferase, which is a component of the structural core of the
alpha-keto glutarate dehydrogenase complex, was studied by Nakano et al.
(1993), who isolated a cDNA from a human fibroblast cDNA library. Amino
acid sequence analysis supported their previous observation (Nakano et
al., 1993) that human dihydrolipoamide succinyltransferase lacks a
sequence motif for an E1 and/or E3 binding site. By Northern blot
analysis, Ali et al. (1994) detected ubiquitous expression of DLST in
peripheral tissues and brain.
GENE STRUCTURE
Nakano et al. (1993) found that the DLST gene contains 3 exons and 4
introns and that the nucleotide sequence at the 5-prime donor and
3-prime acceptor sites of all introns conformed to the gt-ag rule.
GENE FUNCTION
DLST is the E2 component of the alpha-ketoglutarate dehydrogenase
complex. In contrast to the E2 components of the other 2 alpha-keto acid
dehydrogenase complexes, the pyruvate dehydrogenase complex (see 300502)
and the branched-chain alpha-keto acid dehydrogenase complex (see
608348), the alpha-KGDC E2 has a unique structure consisting of 2
domains and lacking a sequence motif of an E3 and/or E1 binding site
(Patel and Harris, 1995).
MAPPING
By fluorescence in situ hybridization, Nakano et al. (1993) found that
the DLST gene is located on 14q24.2-q24.3 and that a related sequence is
located on 1p31. The gene for the dihydrolipoamide acyltransferase of
the branched chain alpha-keto acid dehydrogenase complex (DBT; 248610),
the site of the mutation in type 2 maple syrup urine disease (see
248600), is located on 1p31. Nakano et al. (1993) mentioned the
possibility that mutation of the DLST gene may be a cause of familial
Alzheimer disease that maps to 14q24.3 (AD3; 607822). Ali et al. (1994)
mapped the DLST gene (symbolized by them KGDHC) to 14q24.3 by isotopic
in situ hybridization. The cDNA they used also cross-hybridized to an
apparent E2k pseudogene on 1p31.
*FIELD* RF
1. Ali, G.; Wasco, W.; Cai, X.; Szabo, P.; Sheu, K.-F. R.; Cooper,
A. J. L.; Gaston, S. M.; Gusella, J. F.; Tanzi, R. E.; Blass, J. P.
: Isolation, characterization, and mapping of gene encoding dihydrolipoyl
succinyltransferase (E2k) of human alpha-ketoglutarate dehydrogenase
complex. Somat. Cell Molec. Genet. 20: 99-105, 1994.
2. Nakano, K.; Matuda, 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.
3. Nakano, K.; Takase, C.; Sakamoto, T.; Ohta, S.; Nakagawa, S.; Ariyama,
T.; Inazawa, J.; Abe, T.; Matuda, S.: An unspliced cDNA for human
dihydrolipoamide succinyltransferase: characterization and mapping
of the gene to chromosome 14q24.2-q24.3. Biochem. Biophys. Res. Commun. 196:
527-533, 1993.
4. Patel, M. S.; Harris, R. A.: Mammalian alpha-keto acid dehydrogenase
complexes: gene regulation and genetic defects. FASEB J. 9: 1164-1172,
1995.
*FIELD* CD
Victor A. McKusick: 9/21/1994
*FIELD* ED
alopez: 06/13/2005
ckniffin: 7/15/2004
ckniffin: 5/28/2003
mark: 11/1/1995
carol: 9/21/1994
*RECORD*
*FIELD* NO
126063
*FIELD* TI
*126063 DIHYDROLIPOAMIDE S-SUCCINYLTRANSFERASE; DLST
;;ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX, E2 COMPONENT OF
read more*FIELD* TX
CLONING
The alpha-keto acid dehydrogenase complexes (pyruvate dehydrogenase
complex, alpha-ketoglutarate dehydrogenase complex, and branched chain
alpha-keto acid dehydrogenase complex) are a family of multienzyme
complexes. They are localized in mitochondria and catalyze the oxidative
decarboxylation of alpha-keto acids. These 3 alpha-keto acid
dehydrogenase complexes are composed of 3 different enzymes: alpha-keto
acid dehydrogenase (E1; 300502), dihydrolipoamide acyltransferase (E2),
and dihydrolipoamide dehydrogenase (E3; 238331). Dihydrolipoamide
succinyltransferase, which is a component of the structural core of the
alpha-keto glutarate dehydrogenase complex, was studied by Nakano et al.
(1993), who isolated a cDNA from a human fibroblast cDNA library. Amino
acid sequence analysis supported their previous observation (Nakano et
al., 1993) that human dihydrolipoamide succinyltransferase lacks a
sequence motif for an E1 and/or E3 binding site. By Northern blot
analysis, Ali et al. (1994) detected ubiquitous expression of DLST in
peripheral tissues and brain.
GENE STRUCTURE
Nakano et al. (1993) found that the DLST gene contains 3 exons and 4
introns and that the nucleotide sequence at the 5-prime donor and
3-prime acceptor sites of all introns conformed to the gt-ag rule.
GENE FUNCTION
DLST is the E2 component of the alpha-ketoglutarate dehydrogenase
complex. In contrast to the E2 components of the other 2 alpha-keto acid
dehydrogenase complexes, the pyruvate dehydrogenase complex (see 300502)
and the branched-chain alpha-keto acid dehydrogenase complex (see
608348), the alpha-KGDC E2 has a unique structure consisting of 2
domains and lacking a sequence motif of an E3 and/or E1 binding site
(Patel and Harris, 1995).
MAPPING
By fluorescence in situ hybridization, Nakano et al. (1993) found that
the DLST gene is located on 14q24.2-q24.3 and that a related sequence is
located on 1p31. The gene for the dihydrolipoamide acyltransferase of
the branched chain alpha-keto acid dehydrogenase complex (DBT; 248610),
the site of the mutation in type 2 maple syrup urine disease (see
248600), is located on 1p31. Nakano et al. (1993) mentioned the
possibility that mutation of the DLST gene may be a cause of familial
Alzheimer disease that maps to 14q24.3 (AD3; 607822). Ali et al. (1994)
mapped the DLST gene (symbolized by them KGDHC) to 14q24.3 by isotopic
in situ hybridization. The cDNA they used also cross-hybridized to an
apparent E2k pseudogene on 1p31.
*FIELD* RF
1. Ali, G.; Wasco, W.; Cai, X.; Szabo, P.; Sheu, K.-F. R.; Cooper,
A. J. L.; Gaston, S. M.; Gusella, J. F.; Tanzi, R. E.; Blass, J. P.
: Isolation, characterization, and mapping of gene encoding dihydrolipoyl
succinyltransferase (E2k) of human alpha-ketoglutarate dehydrogenase
complex. Somat. Cell Molec. Genet. 20: 99-105, 1994.
2. Nakano, K.; Matuda, 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.
3. Nakano, K.; Takase, C.; Sakamoto, T.; Ohta, S.; Nakagawa, S.; Ariyama,
T.; Inazawa, J.; Abe, T.; Matuda, S.: An unspliced cDNA for human
dihydrolipoamide succinyltransferase: characterization and mapping
of the gene to chromosome 14q24.2-q24.3. Biochem. Biophys. Res. Commun. 196:
527-533, 1993.
4. Patel, M. S.; Harris, R. A.: Mammalian alpha-keto acid dehydrogenase
complexes: gene regulation and genetic defects. FASEB J. 9: 1164-1172,
1995.
*FIELD* CD
Victor A. McKusick: 9/21/1994
*FIELD* ED
alopez: 06/13/2005
ckniffin: 7/15/2004
ckniffin: 5/28/2003
mark: 11/1/1995
carol: 9/21/1994