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Database: UniProt
Entry: P36957
LinkDB: P36957
Original site: P36957 
ID   ODO2_HUMAN              Reviewed;         453 AA.
AC   P36957; B7Z5W8; E7ESY5; Q7LDY7; Q9BQ32;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 4.
DT   01-OCT-2014, entry version 161.
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] (ISOFORM 1), 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] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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] (ISOFORM 1).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P36957-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P36957-2; Sequence=VSP_056439, VSP_056440;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 lipoyl-binding domain. {ECO:0000305}.
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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; AK299505; BAH13054.1; -; 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   CCDS; CCDS9833.1; -.
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   BioGrid; 108087; 26.
DR   IntAct; P36957; 19.
DR   MINT; MINT-3014449; -.
DR   STRING; 9606.ENSP00000335304; -.
DR   PhosphoSite; P36957; -.
DR   DMDM; 317373578; -.
DR   OGP; P36957; -.
DR   UCD-2DPAGE; P36957; -.
DR   MaxQB; P36957; -.
DR   PaxDb; P36957; -.
DR   PRIDE; P36957; -.
DR   DNASU; 1743; -.
DR   Ensembl; ENST00000334212; ENSP00000335465; ENSG00000119689.
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; QIFRNIF; -.
DR   PhylomeDB; P36957; -.
DR   TreeFam; TF314164; -.
DR   BioCyc; MetaCyc:HS04324-MONOMER; -.
DR   Reactome; REACT_1298; Lysine catabolism.
DR   Reactome; REACT_1785; Citric acid cycle (TCA cycle).
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:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProt.
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:0044237; P:cellular metabolic process; TAS:Reactome.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
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:0044281; P:small molecule metabolic 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; Alternative splicing; 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                                {ECO:0000269|PubMed:19892738}.
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       {ECO:0000255}.
FT   ACT_SITE    428    428       {ECO:0000255}.
FT   MOD_RES     110    110       N6-lipoyllysine. {ECO:0000255}.
FT   MOD_RES     154    154       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     267    267       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     272    272       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     273    273       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     277    277       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     307    307       N6-acetyllysine. {ECO:0000250}.
FT   VAR_SEQ       1     23       MLSRSRCVSRAFSRSLSAFQKGN -> MTWLQSKPQRLQNL
FT                                SQREMSGGR (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056439.
FT   VAR_SEQ      24    109       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056440.
FT   VARIANT     213    213       P -> A (in dbSNP:rs2853769).
FT                                {ECO:0000269|PubMed:8076640,
FT                                ECO:0000269|PubMed:8268217}.
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). {ECO:0000305}.
FT   CONFLICT    132    132       G -> T (in Ref. 1; BAA03871).
FT                                {ECO:0000305}.
FT   CONFLICT    212    212       E -> D (in Ref. 1; BAA03871 and 2;
FT                                BAA05536). {ECO:0000305}.
FT   CONFLICT    312    312       R -> T (in Ref. 2; BAA05536).
FT                                {ECO:0000305}.
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
//
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