Skip Header

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

P09622

- DLDH_HUMAN

UniProt

P09622 - DLDH_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

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

DLD

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

Functioni

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactori

Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FAD
Binding sitei154 – 1541FAD; via amide nitrogen and carbonyl oxygen
Binding sitei243 – 2431NAD
Binding sitei278 – 2781NAD; via amide nitrogen and carbonyl oxygen
Binding sitei314 – 3141NAD; via amide nitrogen
Binding sitei355 – 3551FAD
Active sitei487 – 4871Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 8010FAD
Nucleotide bindingi183 – 1853FAD
Nucleotide bindingi220 – 2278NAD
Nucleotide bindingi361 – 3644FAD

GO - Molecular functioni

  1. dihydrolipoyl dehydrogenase activity Source: ProtInc
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: Reactome
  2. cell redox homeostasis Source: InterPro
  3. cellular metabolic process Source: Reactome
  4. cellular nitrogen compound metabolic process Source: Reactome
  5. gastrulation Source: Ensembl
  6. lysine catabolic process Source: Reactome
  7. mitochondrial electron transport, NADH to ubiquinone Source: Ensembl
  8. proteolysis Source: Ensembl
  9. pyruvate metabolic process Source: Reactome
  10. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
  11. regulation of membrane potential Source: Ensembl
  12. small molecule metabolic process Source: Reactome
  13. sperm capacitation Source: Ensembl
  14. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS01727-MONOMER.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).
REACT_197. Branched-chain amino acid catabolism.
REACT_2071. Pyruvate metabolism.
SABIO-RKP09622.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Glycine cleavage system L protein
Gene namesi
Name:DLD
Synonyms:GCSL, LAD, PHE3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2898. DLD.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal matrix Source: Ensembl
  2. cilium Source: Ensembl
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: UniProt
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Dihydrolipoamide dehydrogenase deficiency (DLDD) [MIM:246900]: An autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721K → E in DLDD. 1 Publication
VAR_006907
Natural varianti229 – 2291G → C in DLDD. 1 Publication
VAR_015820
Natural varianti488 – 4881P → L in DLDD. 1 Publication
VAR_006908
Natural varianti495 – 4951R → G in DLDD; loss of enzyme activity. 1 Publication
VAR_015821

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi246900. phenotype.
Orphaneti2394. Pyruvate dehydrogenase E3 deficiency.
PharmGKBiPA27352.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionAdd
BLAST
Chaini36 – 509474Dihydrolipoyl dehydrogenase, mitochondrialPRO_0000030295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
Disulfide bondi80 ↔ 85Redox-active
Modified residuei104 – 1041N6-acetyllysine; alternateBy similarity
Modified residuei104 – 1041N6-succinyllysine; alternateBy similarity
Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
Modified residuei132 – 1321N6-acetyllysine; alternateBy similarity
Modified residuei132 – 1321N6-succinyllysine; alternateBy similarity
Modified residuei143 – 1431N6-acetyllysine; alternate1 Publication
Modified residuei143 – 1431N6-succinyllysine; alternateBy similarity
Modified residuei159 – 1591N6-succinyllysineBy similarity
Modified residuei166 – 1661N6-succinyllysineBy similarity
Modified residuei273 – 2731N6-succinyllysineBy similarity
Modified residuei277 – 2771N6-succinyllysineBy similarity
Modified residuei346 – 3461N6-acetyllysineBy similarity
Modified residuei410 – 4101N6-acetyllysine; alternate1 Publication
Modified residuei410 – 4101N6-succinyllysine; alternateBy similarity
Modified residuei417 – 4171N6-acetyllysine1 Publication
Modified residuei420 – 4201N6-acetyllysineBy similarity
Modified residuei430 – 4301N6-succinyllysineBy similarity
Modified residuei505 – 5051N6-acetyllysine; alternateBy similarity
Modified residuei505 – 5051N6-succinyllysine; alternateBy similarity

Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP09622.
PaxDbiP09622.
PRIDEiP09622.

2D gel databases

REPRODUCTION-2DPAGEIPI00015911.
UCD-2DPAGEP09622.

PTM databases

PhosphoSiteiP09622.

Expressioni

Gene expression databases

BgeeiP09622.
CleanExiHS_DLD.
ExpressionAtlasiP09622. baseline and differential.
GenevestigatoriP09622.

Organism-specific databases

HPAiHPA044849.

Interactioni

Subunit structurei

Homodimer. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds.2 Publications

Protein-protein interaction databases

BioGridi108082. 56 interactions.
DIPiDIP-29027N.
IntActiP09622. 7 interactions.
MINTiMINT-3007138.
STRINGi9606.ENSP00000205402.

Structurei

Secondary structure

1
509
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 478
Helixi51 – 6212
Beta strandi67 – 715
Beta strandi73 – 775
Helixi78 – 836
Helixi85 – 10218
Helixi105 – 1084
Beta strandi111 – 1144
Beta strandi116 – 1183
Helixi120 – 14425
Beta strandi148 – 15811
Beta strandi161 – 1655
Beta strandi171 – 18111
Beta strandi185 – 1873
Beta strandi197 – 2015
Helixi203 – 2064
Beta strandi214 – 2196
Helixi223 – 23412
Beta strandi238 – 2425
Beta strandi244 – 2496
Helixi255 – 26713
Beta strandi271 – 2733
Beta strandi275 – 2839
Beta strandi289 – 2957
Beta strandi302 – 31110
Beta strandi315 – 3173
Helixi324 – 3274
Beta strandi350 – 3523
Helixi354 – 3563
Beta strandi357 – 3593
Helixi363 – 37715
Helixi386 – 3883
Beta strandi391 – 3933
Beta strandi395 – 4039
Helixi406 – 4127
Beta strandi416 – 4227
Helixi423 – 4253
Helixi427 – 4315
Beta strandi438 – 4447
Turni445 – 4473
Beta strandi449 – 4579
Helixi460 – 47314
Helixi477 – 4826
Helixi491 – 50313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZMCX-ray2.53A/B/C/D/E/F/G/H36-509[»]
1ZMDX-ray2.08A/B/C/D/E/F/G/H36-509[»]
1ZY8X-ray2.59A/B/C/D/E/F/G/H/I/J36-509[»]
2F5ZX-ray2.18A/B/C/D/E/F/G/H/I/J36-509[»]
3RNMX-ray2.40A/B/C/D36-509[»]
ProteinModelPortaliP09622.
SMRiP09622. Positions 37-509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09622.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
HOVERGENiHBG002290.
InParanoidiP09622.
KOiK00382.
OMAiENLNLDM.
OrthoDBiEOG77126S.
PhylomeDBiP09622.
TreeFamiTF300414.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 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: P09622-1) [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
MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQPI DADVTVIGSG
60 70 80 90 100
PGGYVAAIKA AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM
110 120 130 140 150
AHGKDFASRG IEMSEVRLNL DKMMEQKSTA VKALTGGIAH LFKQNKVVHV
160 170 180 190 200
NGYGKITGKN QVTATKADGG TQVIDTKNIL IATGSEVTPF PGITIDEDTI
210 220 230 240 250
VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG
260 270 280 290 300
VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK
310 320 330 340 350
AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI
360 370 380 390 400
YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA
410 420 430 440 450
WVGKSEEQLK EEGIEYKVGK FPFAANSRAK TNADTDGMVK ILGQKSTDRV
460 470 480 490 500
LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA

ASFGKSINF
Length:509
Mass (Da):54,177
Last modified:November 24, 2009 - v2
Checksum:i7613492C516F3835
GO
Isoform 2 (identifier: P09622-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.

Note: No experimental confirmation available.

Show »
Length:410
Mass (Da):43,587
Checksum:i4FB4B37B7A801353
GO
Isoform 3 (identifier: P09622-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-194: Missing.

Note: No experimental confirmation available.

Show »
Length:461
Mass (Da):49,283
Checksum:iE9BB766499627F76
GO

Sequence cautioni

The sequence BAD92940.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541G → R in AAA35764. (PubMed:3278312)Curated
Sequence conflicti209 – 2091L → F in BAD92940. 1 PublicationCurated
Sequence conflicti493 – 4931A → AEA in AAB01381. (PubMed:8406489)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721K → E in DLDD. 1 Publication
VAR_006907
Natural varianti104 – 1041K → T.2 Publications
Corresponds to variant rs1130477 [ dbSNP | Ensembl ].
VAR_031922
Natural varianti229 – 2291G → C in DLDD. 1 Publication
VAR_015820
Natural varianti331 – 3311L → V.
Corresponds to variant rs17624 [ dbSNP | Ensembl ].
VAR_014555
Natural varianti488 – 4881P → L in DLDD. 1 Publication
VAR_006908
Natural varianti495 – 4951R → G in DLDD; loss of enzyme activity. 1 Publication
VAR_015821

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9999Missing in isoform 2. 1 PublicationVSP_055855Add
BLAST
Alternative sequencei147 – 19448Missing in isoform 3. 1 PublicationVSP_055856Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03490 mRNA. Translation: AAA59527.1.
J03620 mRNA. Translation: AAA35764.1.
L13761
, L13749, L13750, L13751, L13752, L13753, L13754, L13748, L13755, L13759, L13760, L13756, L13757, L13758 Genomic DNA. Translation: AAB01381.1.
AK295080 mRNA. Translation: BAG58122.1.
AK300077 mRNA. Translation: BAG61881.1.
AK312346 mRNA. Translation: BAG35267.1.
AB209703 mRNA. Translation: BAD92940.1. Different initiation.
AC005046 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24389.1.
CH471070 Genomic DNA. Translation: EAW83421.1.
BC018648 mRNA. Translation: AAH18648.1.
BC018696 mRNA. Translation: AAH18696.1.
M99384 Genomic DNA. Translation: AAA35759.1.
CCDSiCCDS5749.1. [P09622-1]
PIRiA92622. DEHULP.
RefSeqiNP_000099.2. NM_000108.4. [P09622-1]
NP_001276679.1. NM_001289750.1. [P09622-2]
NP_001276680.1. NM_001289751.1.
NP_001276681.1. NM_001289752.1. [P09622-3]
UniGeneiHs.131711.

Genome annotation databases

EnsembliENST00000205402; ENSP00000205402; ENSG00000091140. [P09622-1]
ENST00000417551; ENSP00000390667; ENSG00000091140. [P09622-1]
ENST00000437604; ENSP00000387542; ENSG00000091140. [P09622-3]
GeneIDi1738.
KEGGihsa:1738.
UCSCiuc003vet.3. human. [P09622-1]

Polymorphism databases

DMDMi269849557.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03490 mRNA. Translation: AAA59527.1 .
J03620 mRNA. Translation: AAA35764.1 .
L13761
, L13749 , L13750 , L13751 , L13752 , L13753 , L13754 , L13748 , L13755 , L13759 , L13760 , L13756 , L13757 , L13758 Genomic DNA. Translation: AAB01381.1 .
AK295080 mRNA. Translation: BAG58122.1 .
AK300077 mRNA. Translation: BAG61881.1 .
AK312346 mRNA. Translation: BAG35267.1 .
AB209703 mRNA. Translation: BAD92940.1 . Different initiation.
AC005046 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24389.1 .
CH471070 Genomic DNA. Translation: EAW83421.1 .
BC018648 mRNA. Translation: AAH18648.1 .
BC018696 mRNA. Translation: AAH18696.1 .
M99384 Genomic DNA. Translation: AAA35759.1 .
CCDSi CCDS5749.1. [P09622-1 ]
PIRi A92622. DEHULP.
RefSeqi NP_000099.2. NM_000108.4. [P09622-1 ]
NP_001276679.1. NM_001289750.1. [P09622-2 ]
NP_001276680.1. NM_001289751.1.
NP_001276681.1. NM_001289752.1. [P09622-3 ]
UniGenei Hs.131711.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZMC X-ray 2.53 A/B/C/D/E/F/G/H 36-509 [» ]
1ZMD X-ray 2.08 A/B/C/D/E/F/G/H 36-509 [» ]
1ZY8 X-ray 2.59 A/B/C/D/E/F/G/H/I/J 36-509 [» ]
2F5Z X-ray 2.18 A/B/C/D/E/F/G/H/I/J 36-509 [» ]
3RNM X-ray 2.40 A/B/C/D 36-509 [» ]
ProteinModelPortali P09622.
SMRi P09622. Positions 37-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108082. 56 interactions.
DIPi DIP-29027N.
IntActi P09622. 7 interactions.
MINTi MINT-3007138.
STRINGi 9606.ENSP00000205402.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSitei P09622.

Polymorphism databases

DMDMi 269849557.

2D gel databases

REPRODUCTION-2DPAGE IPI00015911.
UCD-2DPAGE P09622.

Proteomic databases

MaxQBi P09622.
PaxDbi P09622.
PRIDEi P09622.

Protocols and materials databases

DNASUi 1738.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000205402 ; ENSP00000205402 ; ENSG00000091140 . [P09622-1 ]
ENST00000417551 ; ENSP00000390667 ; ENSG00000091140 . [P09622-1 ]
ENST00000437604 ; ENSP00000387542 ; ENSG00000091140 . [P09622-3 ]
GeneIDi 1738.
KEGGi hsa:1738.
UCSCi uc003vet.3. human. [P09622-1 ]

Organism-specific databases

CTDi 1738.
GeneCardsi GC07P107531.
H-InvDB HIX0006994.
HGNCi HGNC:2898. DLD.
HPAi HPA044849.
MIMi 238331. gene.
246900. phenotype.
neXtProti NX_P09622.
Orphaneti 2394. Pyruvate dehydrogenase E3 deficiency.
PharmGKBi PA27352.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1249.
GeneTreei ENSGT00550000074844.
HOGENOMi HOG000276708.
HOVERGENi HBG002290.
InParanoidi P09622.
KOi K00382.
OMAi ENLNLDM.
OrthoDBi EOG77126S.
PhylomeDBi P09622.
TreeFami TF300414.

Enzyme and pathway databases

BioCyci MetaCyc:HS01727-MONOMER.
Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_1298. Lysine catabolism.
REACT_1785. Citric acid cycle (TCA cycle).
REACT_197. Branched-chain amino acid catabolism.
REACT_2071. Pyruvate metabolism.
SABIO-RK P09622.

Miscellaneous databases

EvolutionaryTracei P09622.
GeneWikii Dihydrolipoamide_dehydrogenase.
GenomeRNAii 1738.
NextBioi 35472004.
PROi P09622.
SOURCEi Search...

Gene expression databases

Bgeei P09622.
CleanExi HS_DLD.
ExpressionAtlasi P09622. baseline and differential.
Genevestigatori P09622.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01350. lipoamide_DH. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases."
    Otulakowski G., Robinson B.H.
    J. Biol. Chem. 262:17313-17318(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-104.
  2. "Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes."
    Pons G., Raefsky-Estrin C., Carothers D.J., Pepin R.A., Javed A.A., Jesse B.W., Ganapathi M.K., Samols D., Patel M.S.
    Proc. Natl. Acad. Sci. U.S.A. 85:1422-1426(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements."
    Feigenbaum A.S., Robinson B.H.
    Genomics 17:376-381(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-104.
    Tissue: Liver.
  4. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Brain, Brain cortex and Pericardium.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Ovary.
  10. "Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene."
    Johanning G.L., Morris J.I., Madhusudhan K.T., Samols D., Patel M.S.
    Proc. Natl. Acad. Sci. U.S.A. 89:10964-10968(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
  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-143; LYS-410 AND LYS-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations."
    Brautigam C.A., Chuang J.L., Tomchick D.R., Machius M., Chuang D.T.
    J. Mol. Biol. 350:543-552(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 36-509 IN COMPLEXES WITH NAD AND FAD, SUBUNIT.
  14. "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 36-509.
  15. "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 (2.18 ANGSTROMS) OF 36-509 IN COMPLEX WITH PDHX, CHARACTERIZATION OF VARIANT DLDD GLY-495.
  16. "Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient."
    Liu T.-C., Kim H., Arizmendi C., Kitano A., Patel M.S.
    Proc. Natl. Acad. Sci. U.S.A. 90:5186-5190(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DLDD GLU-72 AND LEU-488.
  17. "Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency."
    Hong Y.S., Kerr D.S., Craigen W.J., Tan J., Pan Y., Lusk M., Patel M.S.
    Hum. Mol. Genet. 5:1925-1930(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DLDD GLY-495.
  18. "Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews."
    Shaag A., Saada A., Berger I., Mandel H., Joseph A., Feigenbaum A., Elpeleg O.N.
    Am. J. Med. Genet. 82:177-182(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DLDD CYS-229.

Entry informationi

Entry nameiDLDH_HUMAN
AccessioniPrimary (citable) accession number: P09622
Secondary accession number(s): B2R5X0
, B4DHG0, B4DT69, Q14131, Q14167, Q59EV8, Q8WTS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 24, 2009
Last modified: October 29, 2014
This is version 186 of the entry and version 2 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

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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