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O00330

- ODPX_HUMAN

UniProt

O00330 - ODPX_HUMAN

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Protein

Pyruvate dehydrogenase protein X component, mitochondrial

Gene

PDHX

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

Functioni

Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.

GO - Molecular functioni

  1. transferase activity, transferring acyl groups Source: InterPro

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. pyruvate metabolic process Source: Reactome
  3. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000110435-MONOMER.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase protein X component, mitochondrial
Alternative name(s):
Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
E3-binding protein
Short name:
E3BP
Lipoyl-containing pyruvate dehydrogenase complex component X
proX
Gene namesi
Name:PDHX
Synonyms:PDX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:21350. PDHX.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:245349]: A metabolic disorder characterized by decreased activity of the pyruvate dehydrogenase complex without observable reduction in the activities of enzymes E1, E2, or E3. Clinical features include hypotonia and psychomotor retardation.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi183 – 1831R → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi185 – 1851S → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi186 – 1861P → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi187 – 1871A → M: Strongly decreased DLD binding. 1 Publication
Mutagenesisi189 – 1891R → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi190 – 1901N → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi193 – 1931E → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi208 – 2081R → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi210 – 2101I → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi213 – 2131K → A: Strongly decreased DLD binding. 1 Publication
Mutagenesisi214 – 2141E → A: Strongly decreased DLD binding. 1 Publication

Organism-specific databases

MIMi245349. phenotype.
Orphaneti255182. Pyruvate dehydrogenase E3-binding protein deficiency.
PharmGKBiPA134976445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionBy similarityAdd
BLAST
Chaini54 – 501448Pyruvate dehydrogenase protein X component, mitochondrialPRO_0000020484Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971N6-lipoyllysineBy similarityPROSITE-ProRule annotation
Modified residuei194 – 1941N6-acetyllysine1 Publication
Modified residuei394 – 3941N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO00330.
PaxDbiO00330.
PeptideAtlasiO00330.
PRIDEiO00330.

PTM databases

PhosphoSiteiO00330.

Expressioni

Gene expression databases

BgeeiO00330.
CleanExiHS_PDHX.
HS_PDX1.
ExpressionAtlasiO00330. baseline and differential.
GenevestigatoriO00330.

Organism-specific databases

HPAiHPA038484.
HPA038485.

Interactioni

Subunit structurei

Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules. This core binds multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3).3 Publications

Protein-protein interaction databases

BioGridi113737. 16 interactions.
DIPiDIP-29026N.
IntActiO00330. 5 interactions.
MINTiMINT-1482590.
STRINGi9606.ENSP00000227868.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 604Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 786Combined sources
Beta strandi88 – 947Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi127 – 1326Combined sources
Helixi180 – 1834Combined sources
Helixi186 – 1949Combined sources
Helixi199 – 2013Combined sources
Helixi207 – 2093Combined sources
Helixi213 – 22816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZY8X-ray2.59K/L/M/N/O54-274[»]
2DNCNMR-A57-141[»]
2F5ZX-ray2.18K/L/M/N/O173-228[»]
2F60X-ray1.55K173-228[»]
ProteinModelPortaliO00330.
SMRiO00330. Positions 57-144, 183-225, 266-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00330.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13277Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 21432Interaction with DLDAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi149 – 17022Pro-richAdd
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.
GeneTreeiENSGT00760000119281.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiO00330.
KOiK13997.
OMAiSWRLGCD.
PhylomeDBiO00330.
TreeFamiTF332256.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00330-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASWRLGCD PRLLRYLVGF PGRRSVGLVK GALGWSVSRG ANWRWFHSTQ
60 70 80 90 100
WLRGDPIKIL MPSLSPTMEE GNIVKWLKKE GEAVSAGDAL CEIETDKAVV
110 120 130 140 150
TLDASDDGIL AKIVVEEGSK NIRLGSLIGL IVEEGEDWKH VEIPKDVGPP
160 170 180 190 200
PPVSKPSEPR PSPEPQISIP VKKEHIPGTL RFRLSPAARN ILEKHSLDAS
210 220 230 240 250
QGTATGPRGI FTKEDALKLV QLKQTGKITE SRPTPAPTAT PTAPSPLQAT
260 270 280 290 300
AGPSYPRPVI PPVSTPGQPN AVGTFTEIPA SNIRRVIAKR LTESKSTVPH
310 320 330 340 350
AYATADCDLG AVLKVRQDLV KDDIKVSVND FIIKAAAVTL KQMPDVNVSW
360 370 380 390 400
DGEGPKQLPF IDISVAVATD KGLLTPIIKD AAAKGIQEIA DSVKALSKKA
410 420 430 440 450
RDGKLLPEEY QGGSFSISNL GMFGIDEFTA VINPPQACIL AVGRFRPVLK
460 470 480 490 500
LTEDEEGNAK LQQRQLITVT MSSDSRVVDD ELATRFLKSF KANLENPIRL

A
Length:501
Mass (Da):54,122
Last modified:January 24, 2001 - v3
Checksum:i9CF0C1DAE9E12EF9
GO
Isoform 2 (identifier: O00330-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-341: Missing.

Note: No experimental confirmation available.

Show »
Length:274
Mass (Da):29,906
Checksum:i7657F43CA5F9B61D
GO
Isoform 3 (identifier: O00330-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-53: AASWRLGCDP...RWFHSTQWLR → QSGGAEGSPG...ISSGAPDFPG

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:486
Mass (Da):51,460
Checksum:iC0682D60CAC5BDF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411A → R in AAC39661. (PubMed:9467010)Curated
Sequence conflicti251 – 2511A → S in AAB66315. (PubMed:9242632)Curated
Sequence conflicti251 – 2511A → S in CAA73606. (PubMed:9399911)Curated
Sequence conflicti344 – 3441P → S in BAG62924. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231R → C.1 Publication
Corresponds to variant rs1049306 [ dbSNP | Ensembl ].
VAR_046619
Natural varianti101 – 1011T → A.
Corresponds to variant rs11539202 [ dbSNP | Ensembl ].
VAR_046620
Natural varianti370 – 3701D → V.1 Publication
Corresponds to variant rs17850649 [ dbSNP | Ensembl ].
VAR_046621

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 5352AASWR…TQWLR → QSGGAEGSPGAGRTGRGPGS GKAPPAEISSGAPDFPG in isoform 3. CuratedVSP_053817Add
BLAST
Alternative sequencei115 – 341227Missing in isoform 2. CuratedVSP_045271Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001437 mRNA. Translation: AAB66315.1.
Y13145 mRNA. Translation: CAA73606.1.
U82328 mRNA. Translation: AAC39661.1.
AJ298105 Genomic DNA. Translation: CAC18649.1.
AK301384 mRNA. Translation: BAG62924.1.
AC107928 Genomic DNA. No translation available.
AL138810 Genomic DNA. No translation available.
AL356215 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68158.1.
CH471064 Genomic DNA. Translation: EAW68160.1.
BC010389 mRNA. Translation: AAH10389.1.
U79296 mRNA. Translation: AAB50223.1.
CCDSiCCDS44569.1. [O00330-3]
CCDS53616.1. [O00330-2]
CCDS7896.1. [O00330-1]
RefSeqiNP_001128496.1. NM_001135024.1. [O00330-3]
NP_001159630.1. NM_001166158.1. [O00330-2]
NP_003468.2. NM_003477.2. [O00330-1]
UniGeneiHs.502315.

Genome annotation databases

EnsembliENST00000227868; ENSP00000227868; ENSG00000110435. [O00330-1]
ENST00000430469; ENSP00000415695; ENSG00000110435. [O00330-2]
ENST00000448838; ENSP00000389404; ENSG00000110435. [O00330-3]
GeneIDi8050.
KEGGihsa:8050.
UCSCiuc001mvt.3. human. [O00330-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001437 mRNA. Translation: AAB66315.1 .
Y13145 mRNA. Translation: CAA73606.1 .
U82328 mRNA. Translation: AAC39661.1 .
AJ298105 Genomic DNA. Translation: CAC18649.1 .
AK301384 mRNA. Translation: BAG62924.1 .
AC107928 Genomic DNA. No translation available.
AL138810 Genomic DNA. No translation available.
AL356215 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68158.1 .
CH471064 Genomic DNA. Translation: EAW68160.1 .
BC010389 mRNA. Translation: AAH10389.1 .
U79296 mRNA. Translation: AAB50223.1 .
CCDSi CCDS44569.1. [O00330-3 ]
CCDS53616.1. [O00330-2 ]
CCDS7896.1. [O00330-1 ]
RefSeqi NP_001128496.1. NM_001135024.1. [O00330-3 ]
NP_001159630.1. NM_001166158.1. [O00330-2 ]
NP_003468.2. NM_003477.2. [O00330-1 ]
UniGenei Hs.502315.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZY8 X-ray 2.59 K/L/M/N/O 54-274 [» ]
2DNC NMR - A 57-141 [» ]
2F5Z X-ray 2.18 K/L/M/N/O 173-228 [» ]
2F60 X-ray 1.55 K 173-228 [» ]
ProteinModelPortali O00330.
SMRi O00330. Positions 57-144, 183-225, 266-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113737. 16 interactions.
DIPi DIP-29026N.
IntActi O00330. 5 interactions.
MINTi MINT-1482590.
STRINGi 9606.ENSP00000227868.

PTM databases

PhosphoSitei O00330.

Proteomic databases

MaxQBi O00330.
PaxDbi O00330.
PeptideAtlasi O00330.
PRIDEi O00330.

Protocols and materials databases

DNASUi 8050.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000227868 ; ENSP00000227868 ; ENSG00000110435 . [O00330-1 ]
ENST00000430469 ; ENSP00000415695 ; ENSG00000110435 . [O00330-2 ]
ENST00000448838 ; ENSP00000389404 ; ENSG00000110435 . [O00330-3 ]
GeneIDi 8050.
KEGGi hsa:8050.
UCSCi uc001mvt.3. human. [O00330-1 ]

Organism-specific databases

CTDi 8050.
GeneCardsi GC11P034894.
HGNCi HGNC:21350. PDHX.
HPAi HPA038484.
HPA038485.
MIMi 245349. phenotype.
608769. gene.
neXtProti NX_O00330.
Orphaneti 255182. Pyruvate dehydrogenase E3-binding protein deficiency.
PharmGKBi PA134976445.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0508.
GeneTreei ENSGT00760000119281.
HOGENOMi HOG000281566.
HOVERGENi HBG005063.
InParanoidi O00330.
KOi K13997.
OMAi SWRLGCD.
PhylomeDBi O00330.
TreeFami TF332256.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000110435-MONOMER.
Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.

Miscellaneous databases

ChiTaRSi PDHX. human.
EvolutionaryTracei O00330.
GeneWikii E3_binding_protein.
GenomeRNAii 8050.
NextBioi 30644.
PROi O00330.
SOURCEi Search...

Gene expression databases

Bgeei O00330.
CleanExi HS_PDHX.
HS_PDX1.
ExpressionAtlasi O00330. baseline and differential.
Genevestigatori O00330.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
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. "Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex."
    Harris R.A., Bowker-Kinley M.M., Wu P., Jeng J., Popov K.M.
    J. Biol. Chem. 272:19746-19751(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-23.
  2. "Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis."
    Aral B., Benelli C., Ait-Ghezala G., Amessou M., Fouque F., Maunoury C., Creau N., Kamoun P., Marsac C.
    Am. J. Hum. Genet. 61:1318-1326(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN PDHXD.
    Tissue: Liver.
  3. "Detection of a homozygous four base pair deletion in the protein X gene in a case of pyruvate dehydrogenase complex deficiency."
    Ling M., McEachern G., Seyda A., Mackay N., Scherer S.W., Bratinova S., Beatty B., Giovannucci-Uzielli M.L., Robinson B.H.
    Hum. Mol. Genet. 7:501-505(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Human gene sequence for PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase complex."
    Aral B., Dey R., Marsac C.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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: Synovium.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1), VARIANT VAL-370.
    Tissue: Brain.
  9. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-501 (ISOFORM 1).
    Tissue: Brain.
  10. "Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."
    Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.
    J. Biol. Chem. 279:6921-6933(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. "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-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex."
    Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K., Korotchkina L.G., Patel M.S.
    J. Biol. Chem. 281:648-655(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 54-274 IN COMPLEX WITH DLD.
  14. "Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex."
    Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R., Chuang D.T.
    Structure 14:611-621(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 174-230 IN COMPLEX WITH DLD, MUTAGENESIS OF ARG-183; SER-185; PRO-186; ALA-187; ARG-189; ASN-190; GLU-193; ARG-208; ILE-210; LYS-213 AND GLU-214.
  15. "Solution structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid dehydrogenase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 57-141.

Entry informationi

Entry nameiODPX_HUMAN
AccessioniPrimary (citable) accession number: O00330
Secondary accession number(s): B4DW62
, D3DR11, E9PB14, E9PBP7, O60221, Q96FV8, Q99783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 24, 2001
Last modified: November 26, 2014
This is version 148 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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