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Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) (E2K)

 ODO2_HUMAN              Reviewed;         453 AA.
P36957; B7Z5W8; E7ESY5; Q7LDY7; Q9BQ32;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
27-SEP-2017, entry version 192.
RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
EC=2.3.1.61;
AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
Short=OGDC-E2;
AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
AltName: Full=E2K;
Flags: Precursor;
Name=DLST; Synonyms=DLTS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-213.
PubMed=8268217; DOI=10.1016/0167-4781(93)90002-U;
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], AND VARIANT ALA-213.
TISSUE=Peripheral blood;
PubMed=8076640; DOI=10.1111/j.1432-1033.1994.tb20010.x;
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] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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].
PubMed=12508121; DOI=10.1038/nature01348;
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].
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] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 68-89.
TISSUE=Leukemic T-cell;
PubMed=19892738; DOI=10.1073/pnas.0908958106;
Xu G., Shin S.B., Jaffrey S.R.;
"Global profiling of protease cleavage sites by chemoselective
labeling of protein N-termini.";
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
contains multiple copies of 3 enzymatic components: 2-oxoglutarate
dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
lipoamide dehydrogenase (E3).
-!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
succinyldihydrolipoyl)lysine.
-!- COFACTOR:
Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
Note=Binds 1 lipoyl cofactor covalently.;
-!- PATHWAY: Amino-acid degradation; L-lysine degradation via
saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
-!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
symmetry.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P36957-1; Sequence=Displayed;
Name=2;
IsoId=P36957-2; Sequence=VSP_056439, VSP_056440;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
{ECO:0000305}.
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EMBL; D16373; BAA03871.1; -; mRNA.
EMBL; D26535; BAA05536.1; -; Genomic_DNA.
EMBL; L37418; AAB59629.1; -; mRNA.
EMBL; AK289414; BAF82103.1; -; mRNA.
EMBL; AK299505; BAH13054.1; -; mRNA.
EMBL; AC006530; AAD30181.1; -; Genomic_DNA.
EMBL; CH471061; EAW81199.1; -; Genomic_DNA.
EMBL; BC000302; AAH00302.1; -; mRNA.
EMBL; BC001922; AAH01922.1; -; mRNA.
CCDS; CCDS9833.1; -. [P36957-1]
PIR; S39786; PN0673.
RefSeq; NP_001924.2; NM_001933.4. [P36957-1]
UniGene; Hs.525459; -.
ProteinModelPortal; P36957; -.
SMR; P36957; -.
BioGrid; 108087; 34.
IntAct; P36957; 29.
MINT; MINT-3014449; -.
STRING; 9606.ENSP00000335304; -.
iPTMnet; P36957; -.
PhosphoSitePlus; P36957; -.
SwissPalm; P36957; -.
BioMuta; DLST; -.
DMDM; 317373578; -.
OGP; P36957; -.
UCD-2DPAGE; P36957; -.
EPD; P36957; -.
MaxQB; P36957; -.
PaxDb; P36957; -.
PeptideAtlas; P36957; -.
PRIDE; P36957; -.
TopDownProteomics; P36957-1; -. [P36957-1]
DNASU; 1743; -.
Ensembl; ENST00000334220; ENSP00000335304; ENSG00000119689. [P36957-1]
GeneID; 1743; -.
KEGG; hsa:1743; -.
UCSC; uc001xqv.3; human. [P36957-1]
CTD; 1743; -.
DisGeNET; 1743; -.
EuPathDB; HostDB:ENSG00000119689.14; -.
GeneCards; DLST; -.
H-InvDB; HIX0131240; -.
HGNC; HGNC:2911; DLST.
HPA; HPA003010; -.
MIM; 126063; gene.
neXtProt; NX_P36957; -.
OpenTargets; ENSG00000119689; -.
PharmGKB; PA27367; -.
eggNOG; KOG0559; Eukaryota.
eggNOG; COG0508; LUCA.
GeneTree; ENSGT00890000139479; -.
HOGENOM; HOG000281563; -.
HOVERGEN; HBG000268; -.
InParanoid; P36957; -.
KO; K00658; -.
OMA; MKVPSPG; -.
OrthoDB; EOG091G08FX; -.
PhylomeDB; P36957; -.
TreeFam; TF314164; -.
BioCyc; MetaCyc:HS04324-MONOMER; -.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-71064; Lysine catabolism.
Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
UniPathway; UPA00868; UER00840.
ChiTaRS; DLST; human.
GeneWiki; DLST; -.
GenomeRNAi; 1743; -.
PRO; PR:P36957; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000119689; -.
CleanEx; HS_DLST; -.
ExpressionAtlas; P36957; baseline and differential.
Genevisible; P36957; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR011053; Single_hybrid_motif.
InterPro; IPR006255; SucB.
Pfam; PF00198; 2-oxoacid_dh; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
SUPFAM; SSF51230; SSF51230; 1.
TIGRFAMs; TIGR01347; sucB; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS00189; LIPOYL; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Alternative splicing; Complete proteome;
Direct protein sequencing; Lipoyl; Mitochondrion; Phosphoprotein;
Polymorphism; Reference proteome; Transferase; Transit peptide;
Tricarboxylic acid cycle.
TRANSIT 1 67 Mitochondrion.
{ECO:0000269|PubMed:19892738}.
CHAIN 68 453 Dihydrolipoyllysine-residue
succinyltransferase component of 2-
oxoglutarate dehydrogenase complex,
mitochondrial.
/FTId=PRO_0000020472.
DOMAIN 70 144 Lipoyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
ACT_SITE 424 424 {ECO:0000255}.
ACT_SITE 428 428 {ECO:0000255}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D2G2}.
MOD_RES 110 110 N6-lipoyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D2G2}.
MOD_RES 267 267 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D2G2}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D2G2}.
MOD_RES 273 273 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D2G2}.
MOD_RES 277 277 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D2G2}.
MOD_RES 307 307 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D2G2}.
VAR_SEQ 1 23 MLSRSRCVSRAFSRSLSAFQKGN -> MTWLQSKPQRLQNL
SQREMSGGR (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056439.
VAR_SEQ 24 109 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056440.
VARIANT 213 213 P -> A. {ECO:0000269|PubMed:8076640,
ECO:0000269|PubMed:8268217}.
/FTId=VAR_004976.
VARIANT 384 384 P -> T.
/FTId=VAR_004977.
CONFLICT 14 15 RS -> AP (in Ref. 1; BAA03871, 2;
BAA05536 and 3; AAB59629). {ECO:0000305}.
CONFLICT 132 132 G -> T (in Ref. 1; BAA03871).
{ECO:0000305}.
CONFLICT 212 212 E -> D (in Ref. 1; BAA03871 and 2;
BAA05536). {ECO:0000305}.
CONFLICT 312 312 R -> T (in Ref. 2; BAA05536).
{ECO:0000305}.
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


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