Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11182

- ODB2_HUMAN

UniProt

P11182 - ODB2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

Gene

DBT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.

Catalytic activityi

2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei452 – 4521Sequence Analysis
Active sitei456 – 4561Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12007.
BRENDAi2.3.1.168. 2681.
ReactomeiREACT_197. Branched-chain amino acid catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC:2.3.1.168)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase complex component E2
Short name:
BCKAD-E2
Short name:
BCKADE2
Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
Dihydrolipoamide branched chain transacylase
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Gene namesi
Name:DBT
Synonyms:BCATE2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2698. DBT.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial alpha-ketoglutarate dehydrogenase complex Source: ProtInc
  2. mitochondrial matrix Source: Reactome
  3. mitochondrial nucleoid Source: BHF-UCL
  4. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Maple syrup urine disease 2 (MSUD2) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981I → M in MSUD2. 1 Publication
VAR_015099
Natural varianti276 – 2761F → C in MSUD2. 1 Publication
VAR_004978
Natural varianti384 – 3841G → S in MSUD2. 2 Publications
Corresponds to variant rs12021720 [ dbSNP | Ensembl ].
VAR_015100

Keywords - Diseasei

Disease mutation, Maple syrup urine disease

Organism-specific databases

MIMi248600. phenotype.
Orphaneti268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBiPA27167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6161MitochondrionSequence AnalysisAdd
BLAST
Chaini62 – 482421Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialPRO_0000020489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-lipoyllysineBy similarityPROSITE-ProRule annotation
Modified residuei133 – 1331N6-succinyllysineBy similarity
Modified residuei196 – 1961N6-acetyllysine; alternateBy similarity
Modified residuei196 – 1961N6-succinyllysine; alternateBy similarity
Modified residuei202 – 2021N6-acetyllysineBy similarity
Modified residuei243 – 2431N6-acetyllysineBy similarity
Modified residuei250 – 2501N6-acetyllysineBy similarity
Modified residuei261 – 2611N6-succinyllysineBy similarity
Modified residuei289 – 2891N6-acetyllysine; alternateBy similarity
Modified residuei289 – 2891N6-succinyllysine; alternateBy similarity
Modified residuei295 – 2951N6-acetyllysine1 Publication
Modified residuei304 – 3041N6-acetyllysineBy similarity
Modified residuei435 – 4351N6-acetyllysineBy similarity
Modified residuei440 – 4401N6-acetyllysine; alternateBy similarity
Modified residuei440 – 4401N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP11182.
PaxDbiP11182.
PRIDEiP11182.

PTM databases

PhosphoSiteiP11182.

Expressioni

Gene expression databases

BgeeiP11182.
CleanExiHS_DBT.
ExpressionAtlasiP11182. baseline and differential.
GenevestigatoriP11182.

Organism-specific databases

HPAiHPA026481.
HPA026485.
HPA026533.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

BioGridi107997. 19 interactions.
IntActiP11182. 6 interactions.
MINTiMINT-1161634.
STRINGi9606.ENSP00000359151.

Structurei

Secondary structure

1
482
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 684Combined sources
Beta strandi79 – 846Combined sources
Beta strandi94 – 963Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi116 – 1216Combined sources
Beta strandi125 – 1295Combined sources
Beta strandi133 – 1397Combined sources
Helixi175 – 1839Combined sources
Helixi188 – 1903Combined sources
Helixi196 – 1983Combined sources
Helixi202 – 21312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8MNMR-A62-145[»]
1K8ONMR-A62-145[»]
1ZWVNMR-A165-213[»]
2COONMR-A163-220[»]
3RNMX-ray2.40E/F165-213[»]
ProteinModelPortaliP11182.
SMRiP11182. Positions 62-147, 163-220, 249-482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11182.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 13976Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281564.
HOVERGENiHBG104085.
InParanoidiP11182.
KOiK09699.
OrthoDBiEOG7GFB4W.
PhylomeDBiP11182.
TreeFamiTF314182.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR015761. BCKDC_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR23151:SF46. PTHR23151:SF46. 1 hit.
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 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.

P11182-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVRMLRTW SRNAGKLICV RYFQTCGNVH VLKPNYVCFF GYPSFKYSHP
60 70 80 90 100
HHFLKTTAAL RGQVVQFKLS DIGEGIREVT VKEWYVKEGD TVSQFDSICE
110 120 130 140 150
VQSDKASVTI TSRYDGVIKK LYYNLDDIAY VGKPLVDIET EALKDSEEDV
160 170 180 190 200
VETPAVSHDE HTHQEIKGRK TLATPAVRRL AMENNIKLSE VVGSGKDGRI
210 220 230 240 250
LKEDILNYLE KQTGAILPPS PKVEIMPPPP KPKDMTVPIL VSKPPVFTGK
260 270 280 290 300
DKTEPIKGFQ KAMVKTMSAA LKIPHFGYCD EIDLTELVKL REELKPIAFA
310 320 330 340 350
RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT
360 370 380 390 400
EQGLIVPNVK NVQICSIFDI ATELNRLQKL GSVGQLSTTD LTGGTFTLSN
410 420 430 440 450
IGSIGGTFAK PVIMPPEVAI GALGSIKAIP RFNQKGEVYK AQIMNVSWSA
460 470 480
DHRVIDGATM SRFSNLWKSY LENPAFMLLD LK
Length:482
Mass (Da):53,487
Last modified:July 1, 1993 - v3
Checksum:iA7CA728C8F33D126
GO

Sequence cautioni

The sequence AAA35589.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA64512.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3211Q → P in AAA64512. (PubMed:2742576)Curated
Sequence conflicti354 – 3541L → V in AAA64512. (PubMed:2742576)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981I → M in MSUD2. 1 Publication
VAR_015099
Natural varianti276 – 2761F → C in MSUD2. 1 Publication
VAR_004978
Natural varianti384 – 3841G → S in MSUD2. 2 Publications
Corresponds to variant rs12021720 [ dbSNP | Ensembl ].
VAR_015100

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66785 mRNA. Translation: CAA47285.1.
J03208 mRNA. Translation: AAA35589.1. Different initiation.
M27093 mRNA. Translation: AAA64512.1. Different initiation.
BT007372 mRNA. Translation: AAP36036.1.
AL445928 Genomic DNA. Translation: CAH72257.1.
AK313191 mRNA. Translation: BAG36008.1.
CH471097 Genomic DNA. Translation: EAW72963.1.
BC016675 mRNA. Translation: AAH16675.1.
M19301 mRNA. Translation: AAA59200.1. Sequence problems.
X68104 Genomic DNA. Translation: CAA48225.1.
CCDSiCCDS767.1.
PIRiA32422.
RefSeqiNP_001909.3. NM_001918.3.
UniGeneiHs.709187.

Genome annotation databases

EnsembliENST00000370132; ENSP00000359151; ENSG00000137992.
GeneIDi1629.
KEGGihsa:1629.
UCSCiuc001dta.3. human.

Polymorphism databases

DMDMi400668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66785 mRNA. Translation: CAA47285.1 .
J03208 mRNA. Translation: AAA35589.1 . Different initiation.
M27093 mRNA. Translation: AAA64512.1 . Different initiation.
BT007372 mRNA. Translation: AAP36036.1 .
AL445928 Genomic DNA. Translation: CAH72257.1 .
AK313191 mRNA. Translation: BAG36008.1 .
CH471097 Genomic DNA. Translation: EAW72963.1 .
BC016675 mRNA. Translation: AAH16675.1 .
M19301 mRNA. Translation: AAA59200.1 . Sequence problems.
X68104 Genomic DNA. Translation: CAA48225.1 .
CCDSi CCDS767.1.
PIRi A32422.
RefSeqi NP_001909.3. NM_001918.3.
UniGenei Hs.709187.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K8M NMR - A 62-145 [» ]
1K8O NMR - A 62-145 [» ]
1ZWV NMR - A 165-213 [» ]
2COO NMR - A 163-220 [» ]
3RNM X-ray 2.40 E/F 165-213 [» ]
ProteinModelPortali P11182.
SMRi P11182. Positions 62-147, 163-220, 249-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107997. 19 interactions.
IntActi P11182. 6 interactions.
MINTi MINT-1161634.
STRINGi 9606.ENSP00000359151.

PTM databases

PhosphoSitei P11182.

Polymorphism databases

DMDMi 400668.

Proteomic databases

MaxQBi P11182.
PaxDbi P11182.
PRIDEi P11182.

Protocols and materials databases

DNASUi 1629.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370132 ; ENSP00000359151 ; ENSG00000137992 .
GeneIDi 1629.
KEGGi hsa:1629.
UCSCi uc001dta.3. human.

Organism-specific databases

CTDi 1629.
GeneCardsi GC01M100652.
GeneReviewsi DBT.
H-InvDB HIX0000815.
HGNCi HGNC:2698. DBT.
HPAi HPA026481.
HPA026485.
HPA026533.
MIMi 248600. phenotype.
248610. gene.
neXtProti NX_P11182.
Orphaneti 268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBi PA27167.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281564.
HOVERGENi HBG104085.
InParanoidi P11182.
KOi K09699.
OrthoDBi EOG7GFB4W.
PhylomeDBi P11182.
TreeFami TF314182.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-12007.
BRENDAi 2.3.1.168. 2681.
Reactomei REACT_197. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSi DBT. human.
EvolutionaryTracei P11182.
GeneWikii DBT_(gene).
GenomeRNAii 1629.
NextBioi 6684.
PROi P11182.
SOURCEi Search...

Gene expression databases

Bgeei P11182.
CleanExi HS_DBT.
ExpressionAtlasi P11182. baseline and differential.
Genevestigatori P11182.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR015761. BCKDC_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
PANTHERi PTHR23151:SF46. PTHR23151:SF46. 1 hit.
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex."
    Lau K.S., Chuang J.L., Herring W.J., Danner D.J., Cox R.P., Chuang D.T.
    Biochim. Biophys. Acta 1132:319-321(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure."
    Hummel K.B., Litwer S., Bradford A.P., Aitken A., Danner D.J., Yeaman S.J.
    J. Biol. Chem. 263:6165-6168(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase."
    Danner D.J., Litwer S., Herring W.J., Pruckler J.
    J. Biol. Chem. 264:7742-7746(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex."
    Nobukuni Y., Mitsubuchi H., Endo F., Matsuda I.
    Biochem. Biophys. Res. Commun. 161:1035-1041(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "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].
    Tissue: Kidney.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-384.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Skin.
  10. "Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs."
    Lau K.S., Griffin T.A., Hu C.-W.C., Chuang D.T.
    Biochemistry 27:1972-1981(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-313.
  11. "Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene."
    Lau K.S., Herring W.J., Chuang J.L., McKean M., Danner D.J., Cox R.P., Chuang D.T.
    J. Biol. Chem. 267:24090-24096(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
  12. "Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence."
    Wynn R.M., Kochi H., Cox R.P., Chuang D.T.
    Biochim. Biophys. Acta 1201:125-128(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-81.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex."
    Chang C.-F., Chou H.-T., Chuang J.L., Chuang D.T., Huang T.-H.
    J. Biol. Chem. 277:15865-15873(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 62-145.
  16. "Solution structure of the E3-binding domain of dihydrolipoamide branched chain transacylase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 163-220.
  17. "A 17-bp insertion and a Phe215-->Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34."
    Fisher C.W., Lau K.S., Fisher C.R., Wynn R.M., Cox R.P., Chuang D.T.
    Biochem. Biophys. Res. Commun. 174:804-809(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MSUD2 CYS-276.
  18. "Molecular basis of intermittent maple syrup urine disease: novel mutations in the E2 gene of the branched-chain alpha-keto acid dehydrogenase complex."
    Tsuruta M., Mitsubuchi H., Mardy S., Miura Y., Hayashida Y., Kinugasa A., Ishitsu T., Matsuda I., Indo Y.
    J. Hum. Genet. 43:91-100(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MSUD2 MET-98 AND SER-384.

Entry informationi

Entry nameiODB2_HUMAN
AccessioniPrimary (citable) accession number: P11182
Secondary accession number(s): B2R811, Q5VVL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1993
Last modified: November 26, 2014
This is version 187 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3