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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

DLD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). In monomeric form has 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 similarity1 Publication

Miscellaneous

The active site is a redox-active disulfide bond.

Catalytic activityi

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

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Enzyme 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
Binding sitei154FAD; via amide nitrogen and carbonyl oxygen1
Binding sitei243NAD1
Binding sitei278NAD; via amide nitrogen and carbonyl oxygen1
Binding sitei314NAD; via amide nitrogen1
Binding sitei355FAD1
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 – 80FAD10
Nucleotide bindingi183 – 185FAD3
Nucleotide bindingi220 – 227NAD8
Nucleotide bindingi361 – 364FAD4

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

HGNCiHGNC:2898. DLD.

Subcellular locationi

  • Mitochondrion matrix 1 Publication
  • Cytoplasmic vesiclesecretory vesicleacrosome 1 Publication
  • Cell projectionciliumflagellum By similarity

GO - Cellular componenti

  • acrosomal matrix Source: Ensembl
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
  • motile cilium Source: UniProtKB-KW
  • myelin sheath Source: Ensembl
  • nucleoplasm Source: HPA
  • oxoglutarate dehydrogenase complex Source: Ensembl
  • pyruvate dehydrogenase complex Source: MGI

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasmic vesicle, Flagellum, Mitochondrion

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:rs397514651Ensembl.1
Natural variantiVAR_00690772K → E in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964987Ensembl.1
Natural variantiVAR_076986136Missing in DLDD. 1 Publication1
Natural variantiVAR_015820229G → C in DLDD. 2 PublicationsCorresponds to variant dbSNP:rs121964990Ensembl.1
Natural variantiVAR_076987361M → V in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964993Ensembl.1
Natural variantiVAR_076988375E → K in DLDD; loss of enzyme activity; abolished interaction with PDHX. 4 PublicationsCorresponds to variant dbSNP:rs121964992Ensembl.1
Natural variantiVAR_076989393I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964991Ensembl.1
Natural variantiVAR_076990479D → V in DLDD; reduced dehydrogenase activity; increased proteolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs397514649Ensembl.1
Natural variantiVAR_076991482R → G in DLDD; reduced enzyme activity. Corresponds to variant dbSNP:rs397514650Ensembl.1
Natural variantiVAR_006908488P → L in DLDD; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964988Ensembl.1
Natural variantiVAR_015821495R → G in DLDD; loss of enzyme activity; reduced interaction with PDHX. 3 PublicationsCorresponds to variant dbSNP:rs121964989Ensembl.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-active
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.

2D gel databases

REPRODUCTION-2DPAGEiIPI00015911.
UCD-2DPAGEiP09622.

PTM databases

iPTMnetiP09622.
PhosphoSitePlusiP09622.
SwissPalmiP09622.

Expressioni

Gene expression databases

BgeeiENSG00000091140.
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 PDH1A 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). Interacts with PDHX (PubMed:20385101, PubMed:16442803, PubMed:20160912, PubMed:20361979).6 Publications

Protein-protein interaction databases

BioGridi108082. 82 interactors.
DIPiDIP-29027N.
IntActiP09622. 15 interactors.
MINTiMINT-3007138.
STRINGi9606.ENSP00000205402.

Structurei

Secondary structure

1509
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 47Combined sources8
Helixi51 – 62Combined sources12
Beta strandi67 – 71Combined sources5
Beta strandi73 – 77Combined sources5
Helixi78 – 83Combined sources6
Helixi85 – 102Combined sources18
Helixi105 – 108Combined sources4
Beta strandi111 – 114Combined sources4
Beta strandi116 – 118Combined sources3
Helixi120 – 144Combined sources25
Beta strandi148 – 158Combined sources11
Beta strandi161 – 165Combined sources5
Beta strandi171 – 181Combined sources11
Beta strandi185 – 187Combined sources3
Beta strandi197 – 201Combined sources5
Helixi203 – 206Combined sources4
Beta strandi214 – 219Combined sources6
Helixi223 – 234Combined sources12
Beta strandi238 – 242Combined sources5
Beta strandi244 – 249Combined sources6
Helixi255 – 267Combined sources13
Beta strandi271 – 273Combined sources3
Beta strandi275 – 283Combined sources9
Beta strandi289 – 295Combined sources7
Beta strandi302 – 311Combined sources10
Beta strandi315 – 317Combined sources3
Helixi324 – 327Combined sources4
Beta strandi350 – 352Combined sources3
Helixi354 – 356Combined sources3
Beta strandi357 – 359Combined sources3
Helixi363 – 377Combined sources15
Helixi386 – 388Combined sources3
Beta strandi391 – 393Combined sources3
Beta strandi395 – 403Combined sources9
Helixi406 – 412Combined sources7
Beta strandi416 – 422Combined sources7
Helixi423 – 425Combined sources3
Helixi427 – 431Combined sources5
Beta strandi438 – 444Combined sources7
Turni445 – 447Combined sources3
Beta strandi449 – 457Combined sources9
Helixi460 – 473Combined sources14
Helixi477 – 482Combined sources6
Helixi491 – 503Combined sources13

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[»]
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. 1 hit.
InterProiView protein in InterPro
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
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.
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

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 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:rs397514651Ensembl.1
Natural variantiVAR_00690772K → E in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964987Ensembl.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:rs121964990Ensembl.1
Natural variantiVAR_014555331L → V. Corresponds to variant dbSNP:rs17624Ensembl.1
Natural variantiVAR_076987361M → V in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964993Ensembl.1
Natural variantiVAR_076988375E → K in DLDD; loss of enzyme activity; abolished interaction with PDHX. 4 PublicationsCorresponds to variant dbSNP:rs121964992Ensembl.1
Natural variantiVAR_076989393I → T in DLDD. 1 PublicationCorresponds to variant dbSNP:rs121964991Ensembl.1
Natural variantiVAR_076990479D → V in DLDD; reduced dehydrogenase activity; increased proteolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs397514649Ensembl.1
Natural variantiVAR_076991482R → G in DLDD; reduced enzyme activity. Corresponds to variant dbSNP:rs397514650Ensembl.1
Natural variantiVAR_006908488P → L in DLDD; no effect on interaction with PDHX. 2 PublicationsCorresponds to variant dbSNP:rs121964988Ensembl.1
Natural variantiVAR_015821495R → G in DLDD; loss of enzyme activity; reduced interaction with PDHX. 3 PublicationsCorresponds to variant dbSNP:rs121964989Ensembl.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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

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: July 5, 2017
This is version 215 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. 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