Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Dihydrolipoyl dehydrogenase, mitochondrial  

UniProtKB / Swiss-Prot ID :  DLDH_HUMAN

Gene Name (Synonyms) : 
DLD, GCSL, LAD, PHE3  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Mitochondrion matrix. 

Protein Function :  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. 

Protein Sequence MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCI...
Predicted Secondary Structure CCCEEECCEEHHHHHCCCCCHHHHHHCCCCCCCCCCCCCCCCEEEEECCCHHHHHHHHHHHHCCCCEEEE...
Protein Variant
LocationDescription
72K -> E (in DLD deficiency). VAR_006907
104K -> T (in dbSNP:rs1130477). VAR_031922
229G -> C (in DLD deficiency; carrier rateamong Askenazi Jewish 1:94).
331L -> V (in dbSNP:rs17624). VAR_014555
488P -> L (in DLD deficiency). VAR_006908
495R -> G (in DLD deficiency; loss of enzymeactivity).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MAHGKDFAS
HHHCCCCCC
39.54Phosphositeplus
Link
132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)STAVKALTG
HHHHHHHHH
34.90Phosphositeplus
Link
143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AHLFKQNKV
HHHHCCCCE
60.36Phosphositeplus
Link
143N6-acetyllysineAHLFKQNKV
HHHHCCCCE
60.36HPRD
Link
143N6-acetyllysineAHLFKQNKV
HHHHCCCCE
60.36Phosphositeplus
Link
143N6-acetyllysine.AHLFKQNKV
HHHHCCCCE
60.36UniProtKB
Link
166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VTATKADGG
EEEEECCCC
41.85Phosphositeplus
Link
267N6-acetyllysineRILQKQGFK
HHHHHCCCE
49.28HPRD
Link
267N6-acetyllysineRILQKQGFK
HHHHHCCCE
49.28Phosphositeplus
Link
267N6-acetyllysine.RILQKQGFK
HHHHHCCCE
49.28UniProtKB
Link
276PhosphothreonineFKLNTKVTG
EEECCEEEE
37.01HPRD
Link
276PhosphothreonineFKLNTKVTG
EEECCEEEE
37.01Phosphositeplus
Link
297PhosphoserineIEAASGGKA
EEECCCCCE
55.94Phosphositeplus
Link
320Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RPFTKNLGL
EECCCCCCC
51.02Phosphositeplus
Link
320N6-acetyllysineRPFTKNLGL
EECCCCCCC
51.02HPRD
Link
320N6-acetyllysineRPFTKNLGL
EECCCCCCC
51.02Phosphositeplus
Link
320N6-acetyllysine.RPFTKNLGL
EECCCCCCC
51.02UniProtKB
Link
341PhosphothreonineIPVNTRFQT
EEECCCCCC
32.85HPRD
Link
346Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RFQTKIPNI
CCCCCCCCE
45.44Phosphositeplus
Link
410Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEQLKEEGI
HHHHHHCCC
54.11Phosphositeplus
Link
410N6-acetyllysineEEQLKEEGI
HHHHHHCCC
54.11HPRD
Link
410N6-acetyllysineEEQLKEEGI
HHHHHHCCC
54.11Phosphositeplus
Link
410N6-acetyllysine.EEQLKEEGI
HHHHHHCCC
54.11UniProtKB
Link
417N6-acetyllysineGIEYKVGKF
CCCEEEEEE
31.55HPRD
Link
417N6-acetyllysineGIEYKVGKF
CCCEEEEEE
31.55Phosphositeplus
Link
417N6-acetyllysine.GIEYKVGKF
CCCEEEEEE
31.55UniProtKB
Link
420N6-acetyllysineYKVGKFPFA
EEEEEEEEC
53.50HPRD
Link
420N6-acetyllysineYKVGKFPFA
EEEEEEEEC
53.50Phosphositeplus
Link
420N6-acetyllysine.YKVGKFPFA
EEEEEEEEC
53.50UniProtKB
Link
440Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DGMVKILGQ
CEEEEEEEE
24.26Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
DLDH_HUMANdirect interactionEBI-966791
intact16263718
ODPX_HUMANdirect interactionEBI-966791
intact16263718
DLDH_HUMANin vivoHPRD:02006HPRD15576032
ODO1_HUMANENSP00000205402STRING
ODO1_HUMANENSP00000205402STRING
LDHA_HUMANENSP00000205402STRING
ODPX_HUMANENSP00000205402STRING
LDHB_HUMANENSP00000205402STRING
AGT2_HUMANENSP00000205402STRING
THIL_HUMANENSP00000205402STRING
ODBA_HUMANENSP00000205402STRING
KPYR_HUMANENSP00000205402STRING
GCST_HUMANENSP00000205402STRING
ODP2_HUMANENSP00000205402STRING
LDHC_HUMANENSP00000205402STRING
LDH6A_HUMANENSP00000205402STRING
ODPAT_HUMANENSP00000205402STRING
ODPAT_HUMANENSP00000205402STRING
ODPAT_HUMANENSP00000205402STRING
LDHD_HUMANENSP00000205402STRING
LDH6B_HUMANENSP00000205402STRING
SPYA_HUMANENSP00000205402STRING
ACO12_HUMANENSP00000205402STRING
ODPB_HUMANENSP00000205402STRING
CACP_HUMANENSP00000205402STRING
ACS2L_HUMANENSP00000205402STRING
ODBB_HUMANENSP00000205402STRING
MAOM_HUMANENSP00000205402STRING
KPYM_HUMANENSP00000205402STRING
KPYM_HUMANENSP00000205402STRING
ODO2_HUMANENSP00000205402STRING
ACACA_HUMANENSP00000205402STRING
ALAT2_HUMANENSP00000205402STRING
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Disease Reference
Kegg disease
OMIM disease
246900Dihydrolipoamide dehydrogenase deficiency (DLDD)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143; LYS-267; LYS-320;LYS-410; LYS-417 AND LYS-420, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures