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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

DLD

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

Functioni

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).By similarity7 Publications

Miscellaneous

The active site is a redox-active disulfide bond.By similarity

Catalytic activityi

Protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH.6 Publications

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Activity regulationi

Disruption of native heterodimer state inhibits primary dihydrolipoamide dehydrogenase activity and induces serine protease activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei89FAD1 Publication1
Binding sitei154FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei243NAD1 Publication1
Binding sitei278NAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei314NAD; via amide nitrogen1 Publication1
Binding sitei355FAD1 Publication1
Sitei448Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex1 Publication1
Sitei473Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex1 Publication1
Active sitei487Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi71 – 80FAD1 Publication10
Nucleotide bindingi183 – 185FAD1 Publication3
Nucleotide bindingi220 – 227NAD1 Publication8
Nucleotide bindingi361 – 364FAD1 Publication4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS01727-MONOMER
BRENDAi1.8.1.4 2681
ReactomeiR-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-HSA-389661 Glyoxylate metabolism and glycine degradation
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-6783984 Glycine degradation
R-HSA-70268 Pyruvate metabolism
R-HSA-70895 Branched-chain amino acid catabolism
R-HSA-71064 Lysine catabolism
R-HSA-71403 Citric acid cycle (TCA cycle)
SABIO-RKiP09622

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.46 Publications)
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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000091140.12
HGNCiHGNC:2898 DLD
MIMi238331 gene
neXtProtiNX_P09622

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasmic vesicle, Flagellum, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Dihydrolipoamide dehydrogenase deficiency (DLDD)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:246900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07698547I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs397514651EnsemblClinVar.1
Natural variantiVAR_00690772K → E in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964987EnsemblClinVar.1
Natural variantiVAR_076986136Missing in DLDD. 1 Publication1
Natural variantiVAR_015820229G → C in DLDD. 2 PublicationsCorresponds to variant dbSNP:rs121964990EnsemblClinVar.1
Natural variantiVAR_076987361M → V in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964993EnsemblClinVar.1
Natural variantiVAR_076988375E → K in DLDD; loss of enzyme activity; abolished interaction with PDHX. 4 PublicationsCorresponds to variant dbSNP:rs121964992EnsemblClinVar.1
Natural variantiVAR_076989393I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964991EnsemblClinVar.1
Natural variantiVAR_076990479D → V in DLDD; reduced dehydrogenase activity; increased proteolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs397514649EnsemblClinVar.1
Natural variantiVAR_076991482R → G in DLDD; reduced enzyme activity. Corresponds to variant dbSNP:rs397514650EnsemblClinVar.1
Natural variantiVAR_006908488P → L in DLDD; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964988EnsemblClinVar.1
Natural variantiVAR_015821495R → G in DLDD; loss of enzyme activity; reduced interaction with PDHX. 3 PublicationsCorresponds to variant dbSNP:rs121964989EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi89K → E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. 1 Publication1
Mutagenesisi383H → A: Reduces dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi383H → L: Reduces dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi448D → A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi448D → N: Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi466E → A: Decreases dehydrogenase activity. Loss of proteolytic activity. 1 Publication1
Mutagenesisi473Y → A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi473Y → F: Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi473Y → H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi482R → A: Does not affect dihydrolipoyl dehydrogenase activity. 1 Publication1
Mutagenesisi482R → M: Does not affect interaction with PDHX. 1 Publication1
Mutagenesisi485H → A: Loss of dehydrogenase activity. Increases proteolytic activity. 1 Publication1
Mutagenesisi491S → A: Loss of proteolytic activity. Does not affect dehydrogenase activity. 1 Publication1
Mutagenesisi492E → Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. 1 Publication1
Mutagenesisi505K → M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1738
MalaCardsiDLD
MIMi246900 phenotype
OpenTargetsiENSG00000091140
Orphaneti2394 Pyruvate dehydrogenase E3 deficiency
PharmGKBiPA27352

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide
DB00157 NADH

Polymorphism and mutation databases

BioMutaiDLD
DMDMi269849557

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 35MitochondrionCombined sourcesAdd BLAST35
ChainiPRO_000003029536 – 509Dihydrolipoyl dehydrogenase, mitochondrialAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-acetyllysine; alternateBy similarity1
Modified residuei66N6-succinyllysine; alternateBy similarity1
Disulfide bondi80 ↔ 85Redox-activeBy similarity
Modified residuei104N6-acetyllysine; alternateBy similarity1
Modified residuei104N6-succinyllysine; alternateBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1
Modified residuei132N6-acetyllysine; alternateBy similarity1
Modified residuei132N6-succinyllysine; alternateBy similarity1
Modified residuei143N6-acetyllysine; alternateCombined sources1
Modified residuei143N6-succinyllysine; alternateBy similarity1
Modified residuei159N6-succinyllysineBy similarity1
Modified residuei166N6-succinyllysineBy similarity1
Modified residuei273N6-succinyllysineBy similarity1
Modified residuei277N6-succinyllysineBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei297PhosphoserineBy similarity1
Modified residuei346N6-acetyllysineBy similarity1
Modified residuei410N6-acetyllysine; alternateCombined sources1
Modified residuei410N6-succinyllysine; alternateBy similarity1
Modified residuei417N6-acetyllysineCombined sources1
Modified residuei420N6-acetyllysineBy similarity1
Modified residuei430N6-succinyllysineBy similarity1
Modified residuei502PhosphoserineCombined sources1
Modified residuei505N6-acetyllysine; alternateBy similarity1
Modified residuei505N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP09622
MaxQBiP09622
PaxDbiP09622
PeptideAtlasiP09622
PRIDEiP09622
ProteomicsDBi52254

2D gel databases

REPRODUCTION-2DPAGEiIPI00015911
UCD-2DPAGEiP09622

PTM databases

iPTMnetiP09622
PhosphoSitePlusiP09622
SwissPalmiP09622

Expressioni

Gene expression databases

BgeeiENSG00000091140 Expressed in 234 organ(s), highest expression level in heart right ventricle
CleanExiHS_DLD
ExpressionAtlasiP09622 baseline and differential
GenevisibleiP09622 HS

Organism-specific databases

HPAiHPA044849

Interactioni

Subunit structurei

Homodimer (PubMed:15946682). Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDHA (PDHA1 or PDHA2) and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (PubMed:14638692). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds) (PubMed:14638692, PubMed:20361979). The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A (PubMed:29211711). Interacts with PDHX (PubMed:20385101, PubMed:16442803, PubMed:20160912, PubMed:20361979).7 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi108082, 375 interactors
CORUMiP09622
DIPiDIP-29027N
IntActiP09622, 319 interactors
MINTiP09622
STRINGi9606.ENSP00000205402

Structurei

Secondary structure

1509
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP09622
SMRiP09622
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09622

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG1335 Eukaryota
COG1249 LUCA
GeneTreeiENSGT00550000074844
HOGENOMiHOG000276708
HOVERGENiHBG002290
InParanoidiP09622
KOiK00382
OMAiTMSEAVM
OrthoDBiEOG091G05AA
PhylomeDBiP09622
TreeFamiTF300414

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006258 Lipoamide_DH
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit
PIRSFiPIRSF000350 Mercury_reductase_MerA, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit
TIGRFAMsiTIGR01350 lipoamide_DH, 1 hit
PROSITEiView protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 1 hit

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. AlignAdd to basket

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PEX6E9PEX6_HUMAN
Dihydrolipoyl dehydrogenase
DLD
486Annotation score:
F2Z2E3F2Z2E3_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
115Annotation score:
F8WDM5F8WDM5_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
114Annotation score:
A0A1W2PR83A0A1W2PR83_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
114Annotation score:
F8WDY5F8WDY5_HUMAN
Dihydrolipoyl dehydrogenase, mitoch...
DLD
58Annotation score:

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti154G → R in AAA35764 (PubMed:3278312).Curated1
Sequence conflicti209L → F in BAD92940 (Ref. 5) Curated1
Sequence conflicti493A → AEA in AAB01381 (PubMed:8406489).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07698547I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs397514651EnsemblClinVar.1
Natural variantiVAR_00690772K → E in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964987EnsemblClinVar.1
Natural variantiVAR_031922104K → T2 PublicationsCorresponds to variant dbSNP:rs1130477Ensembl.1
Natural variantiVAR_076986136Missing in DLDD. 1 Publication1
Natural variantiVAR_015820229G → C in DLDD. 2 PublicationsCorresponds to variant dbSNP:rs121964990EnsemblClinVar.1
Natural variantiVAR_014555331L → V. Corresponds to variant dbSNP:rs17624Ensembl.1
Natural variantiVAR_076987361M → V in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964993EnsemblClinVar.1
Natural variantiVAR_076988375E → K in DLDD; loss of enzyme activity; abolished interaction with PDHX. 4 PublicationsCorresponds to variant dbSNP:rs121964992EnsemblClinVar.1
Natural variantiVAR_076989393I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964991EnsemblClinVar.1
Natural variantiVAR_076990479D → V in DLDD; reduced dehydrogenase activity; increased proteolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs397514649EnsemblClinVar.1
Natural variantiVAR_076991482R → G in DLDD; reduced enzyme activity. Corresponds to variant dbSNP:rs397514650EnsemblClinVar.1
Natural variantiVAR_006908488P → L in DLDD; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964988EnsemblClinVar.1
Natural variantiVAR_015821495R → G in DLDD; loss of enzyme activity; reduced interaction with PDHX. 3 PublicationsCorresponds to variant dbSNP:rs121964989EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0558551 – 99Missing in isoform 2. 1 PublicationAdd BLAST99
Alternative sequenceiVSP_055856147 – 194Missing in isoform 3. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS78268.1 [P09622-3]
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.5 human [P09622-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS78268.1 [P09622-3]
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5J5ZX-ray1.84A/B36-509[»]
5NHGX-ray2.27A/B/C/D/E/F/G/H36-509[»]
ProteinModelPortaliP09622
SMRiP09622
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108082, 375 interactors
CORUMiP09622
DIPiDIP-29027N
IntActiP09622, 319 interactors
MINTiP09622
STRINGi9606.ENSP00000205402

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide
DB00157 NADH

PTM databases

iPTMnetiP09622
PhosphoSitePlusiP09622
SwissPalmiP09622

Polymorphism and mutation databases

BioMutaiDLD
DMDMi269849557

2D gel databases

REPRODUCTION-2DPAGEiIPI00015911
UCD-2DPAGEiP09622

Proteomic databases

EPDiP09622
MaxQBiP09622
PaxDbiP09622
PeptideAtlasiP09622
PRIDEiP09622
ProteomicsDBi52254

Protocols and materials databases

DNASUi1738
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000205402; ENSP00000205402; ENSG00000091140 [P09622-1]
ENST00000417551; ENSP00000390667; ENSG00000091140 [P09622-1]
ENST00000437604; ENSP00000387542; ENSG00000091140 [P09622-3]
GeneIDi1738
KEGGihsa:1738
UCSCiuc003vet.5 human [P09622-1]

Organism-specific databases

CTDi1738
DisGeNETi1738
EuPathDBiHostDB:ENSG00000091140.12
GeneCardsiDLD
H-InvDBiHIX0006994
HGNCiHGNC:2898 DLD
HPAiHPA044849
MalaCardsiDLD
MIMi238331 gene
246900 phenotype
neXtProtiNX_P09622
OpenTargetsiENSG00000091140
Orphaneti2394 Pyruvate dehydrogenase E3 deficiency
PharmGKBiPA27352
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1335 Eukaryota
COG1249 LUCA
GeneTreeiENSGT00550000074844
HOGENOMiHOG000276708
HOVERGENiHBG002290
InParanoidiP09622
KOiK00382
OMAiTMSEAVM
OrthoDBiEOG091G05AA
PhylomeDBiP09622
TreeFamiTF300414

Enzyme and pathway databases

BioCyciMetaCyc:HS01727-MONOMER
BRENDAi1.8.1.4 2681
ReactomeiR-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-HSA-389661 Glyoxylate metabolism and glycine degradation
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-6783984 Glycine degradation
R-HSA-70268 Pyruvate metabolism
R-HSA-70895 Branched-chain amino acid catabolism
R-HSA-71064 Lysine catabolism
R-HSA-71403 Citric acid cycle (TCA cycle)
SABIO-RKiP09622

Miscellaneous databases

ChiTaRSiDLD human
EvolutionaryTraceiP09622
GeneWikiiDihydrolipoamide_dehydrogenase
GenomeRNAii1738
PROiPR:P09622
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000091140 Expressed in 234 organ(s), highest expression level in heart right ventricle
CleanExiHS_DLD
ExpressionAtlasiP09622 baseline and differential
GenevisibleiP09622 HS

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006258 Lipoamide_DH
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit
PIRSFiPIRSF000350 Mercury_reductase_MerA, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit
TIGRFAMsiTIGR01350 lipoamide_DH, 1 hit
PROSITEiView protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDLDH_HUMAN
AccessioniPrimary (citable) accession number: P09622
Secondary accession number(s): B2R5X0
, B4DHG0, B4DT69, Q14131, Q14167, Q59EV8, Q8WTS4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 24, 2009
Last modified: November 7, 2018
This is version 227 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
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