DLDH_MOUSE - dbPTM
DLDH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLDH_MOUSE
UniProt AC O08749
Protein Name Dihydrolipoyl dehydrogenase, mitochondrial
Gene Name Dld
Organism Mus musculus (Mouse).
Sequence Length 509
Subcellular Localization Mitochondrion matrix . Nucleus . Cell projection, cilium, flagellum . Cytoplasmic vesicle, secretory vesicle, acrosome . Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex
Protein Description 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) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). 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 (By similarity). 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]
Protein Sequence MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAFGKPINF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
8PhosphorylationMQSWSRVYRSLAKKG
CCHHHHHHHHHHHCC		8.0628576409
66SuccinylationKSAQLGFKTVCIEKN
HCCCCCCEEEEEECC		37.9523806337
66AcetylationKSAQLGFKTVCIEKN
HCCCCCCEEEEEECC		37.9523806337
66GlutarylationKSAQLGFKTVCIEKN
HCCCCCCEEEEEECC		37.9524703693
66SuccinylationKSAQLGFKTVCIEKN
HCCCCCCEEEEEECC		37.95-
69S-nitrosylationQLGFKTVCIEKNETL
CCCCEEEEEECCCCC		3.9424895380
72AcetylationFKTVCIEKNETLGGT
CEEEEEECCCCCCCE		39.9223864654
80S-nitrosylationNETLGGTCLNVGCIP
CCCCCCEEEECCEEC		2.6924895380
80S-palmitoylationNETLGGTCLNVGCIP
CCCCCCEEEECCEEC		2.6928526873
85S-palmitoylationGTCLNVGCIPSKALL
CEEEECCEECCHHHH		3.4428526873
85S-nitrosylationGTCLNVGCIPSKALL
CEEEECCEECCHHHH		3.4424895380
104AcetylationYYHMAHGKDFASRGI
CHHHHCCCCHHHCCC		39.5423576753
104SuccinylationYYHMAHGKDFASRGI
CHHHHCCCCHHHCCC		39.54-
104SuccinylationYYHMAHGKDFASRGI
CHHHHCCCCHHHCCC		39.5423806337
122SuccinylationEVRLNLEKMMEQKHS
HHHHCHHHHHHHHHH		46.8723806337
122GlutarylationEVRLNLEKMMEQKHS
HHHHCHHHHHHHHHH		46.8724703693
122AcetylationEVRLNLEKMMEQKHS
HHHHCHHHHHHHHHH		46.8723576753
122SuccinylationEVRLNLEKMMEQKHS
HHHHCHHHHHHHHHH		46.87-
127AcetylationLEKMMEQKHSAVKAL
HHHHHHHHHHHHHHH		26.6523864654
132GlutarylationEQKHSAVKALTGGIA
HHHHHHHHHHHHHHH		37.0824703693
132SuccinylationEQKHSAVKALTGGIA
HHHHHHHHHHHHHHH		37.0823806337
132AcetylationEQKHSAVKALTGGIA
HHHHHHHHHHHHHHH		37.0823576753
132SuccinylationEQKHSAVKALTGGIA
HHHHHHHHHHHHHHH		37.08-
135PhosphorylationHSAVKALTGGIAHLF
HHHHHHHHHHHHHHH		37.9220531401
143MalonylationGGIAHLFKQNKVVHV
HHHHHHHHCCCEEEE		60.3626320211
143UbiquitinationGGIAHLFKQNKVVHV
HHHHHHHHCCCEEEE		60.36-
143GlutarylationGGIAHLFKQNKVVHV
HHHHHHHHCCCEEEE		60.3624703693
143AcetylationGGIAHLFKQNKVVHV
HHHHHHHHCCCEEEE		60.3623576753
143SuccinylationGGIAHLFKQNKVVHV
HHHHHHHHCCCEEEE		60.3623806337
143SuccinylationGGIAHLFKQNKVVHV
HHHHHHHHCCCEEEE		60.36-
146SuccinylationAHLFKQNKVVHVNGF
HHHHHCCCEEEECCC		43.0424315375
146AcetylationAHLFKQNKVVHVNGF
HHHHHCCCEEEECCC		43.0423864654
155SuccinylationVHVNGFGKITGKNQV
EEECCCCCCCCCCCE		34.5323806337
155AcetylationVHVNGFGKITGKNQV
EEECCCCCCCCCCCE		34.5323864654
159MalonylationGFGKITGKNQVTATK
CCCCCCCCCCEEEEE		35.2426320211
159GlutarylationGFGKITGKNQVTATK
CCCCCCCCCCEEEEE		35.2424703693
159SuccinylationGFGKITGKNQVTATK
CCCCCCCCCCEEEEE		35.24-
159AcetylationGFGKITGKNQVTATK
CCCCCCCCCCEEEEE		35.2424062335
159SuccinylationGFGKITGKNQVTATK
CCCCCCCCCCEEEEE		35.2423806337
159UbiquitinationGFGKITGKNQVTATK
CCCCCCCCCCEEEEE		35.2427667366
166SuccinylationKNQVTATKADGSTQV
CCCEEEEECCCCEEE		41.8523806337
166UbiquitinationKNQVTATKADGSTQV
CCCEEEEECCCCEEE		41.8527667366
166AcetylationKNQVTATKADGSTQV
CCCEEEEECCCCEEE		41.8523806337
166GlutarylationKNQVTATKADGSTQV
CCCEEEEECCCCEEE		41.8524703693
166SuccinylationKNQVTATKADGSTQV
CCCEEEEECCCCEEE		41.85-
170PhosphorylationTATKADGSTQVIDTK
EEEECCCCEEEEECC		19.0625521595
259SuccinylationGIDMEISKNFQRILQ
CCCHHHHHHHHHHHH		68.4026388266
271SuccinylationILQRQGFKFKLNTKV
HHHHCCCEEEEECEE		48.7026388266
271AcetylationILQRQGFKFKLNTKV
HHHHCCCEEEEECEE		48.7023864654
273AcetylationQRQGFKFKLNTKVTG
HHCCCEEEEECEEEC		41.2223864654
273SuccinylationQRQGFKFKLNTKVTG
HHCCCEEEEECEEEC		41.22-
273SuccinylationQRQGFKFKLNTKVTG
HHCCCEEEEECEEEC		41.2223806337
277GlutarylationFKFKLNTKVTGATKK
CEEEEECEEECCEEC		36.4024703693
277MalonylationFKFKLNTKVTGATKK
CEEEEECEEECCEEC		36.4026320211
277AcetylationFKFKLNTKVTGATKK
CEEEEECEEECCEEC		36.4021728379
277SuccinylationFKFKLNTKVTGATKK
CEEEEECEEECCEEC		36.40-
277SuccinylationFKFKLNTKVTGATKK
CEEEEECEEECCEEC		36.4023806337
282PhosphorylationNTKVTGATKKSDGKI
ECEEECCEECCCCCE		40.1129899451
284SuccinylationKVTGATKKSDGKIDV
EEECCEECCCCCEEE		49.8023954790
284AcetylationKVTGATKKSDGKIDV
EEECCEECCCCCEEE		49.8024062335
285PhosphorylationVTGATKKSDGKIDVS
EECCEECCCCCEEEE		53.8320495213
288AcetylationATKKSDGKIDVSVEA
CEECCCCCEEEEEEE		40.5023201123
288SuccinylationATKKSDGKIDVSVEA
CEECCCCCEEEEEEE		40.5023954790
292PhosphorylationSDGKIDVSVEAASGG
CCCCEEEEEEECCCC		15.5329899451
297PhosphorylationDVSVEAASGGKAEVI
EEEEEECCCCCEEEE		55.9427180971
334SuccinylationLGIELDPKGRIPVNN
HCCCCCCCCCCCCCC		61.56-
334UbiquitinationLGIELDPKGRIPVNN
HCCCCCCCCCCCCCC		61.56-
334SuccinylationLGIELDPKGRIPVNN
HCCCCCCCCCCCCCC		61.5623806337
334AcetylationLGIELDPKGRIPVNN
HCCCCCCCCCCCCCC		61.5623576753
346AcetylationVNNRFQTKIPNIYAI
CCCCCCCCCCCEEEE		45.4423576753
410SuccinylationGKSEEQLKEEGIEFK
CCCHHHHHHCCCEEE		54.11-
410SuccinylationGKSEEQLKEEGIEFK
CCCHHHHHHCCCEEE		54.1123806337
410GlutarylationGKSEEQLKEEGIEFK
CCCHHHHHHCCCEEE		54.1124703693
410AcetylationGKSEEQLKEEGIEFK
CCCHHHHHHCCCEEE		54.1123806337
417AcetylationKEEGIEFKIGKFPFA
HHCCCEEEEECCCCC		37.45-
420AcetylationGIEFKIGKFPFAANS
CCEEEEECCCCCCCC		54.0223576753
420SuccinylationGIEFKIGKFPFAANS
CCEEEEECCCCCCCC		54.0223806337
420UbiquitinationGIEFKIGKFPFAANS
CCEEEEECCCCCCCC		54.0227667366
430UbiquitinationFAANSRAKTNADTDG
CCCCCCCCCCCCCCC		41.0027667366
430SuccinylationFAANSRAKTNADTDG
CCCCCCCCCCCCCCC		41.0023806337
430SuccinylationFAANSRAKTNADTDG
CCCCCCCCCCCCCCC		41.00-
430AcetylationFAANSRAKTNADTDG
CCCCCCCCCCCCCCC		41.0023806337
430GlutarylationFAANSRAKTNADTDG
CCCCCCCCCCCCCCC		41.0024703693
445AcetylationMVKILGHKSTDRVLG
CEEECCCCCCCCEEE		53.9323806337
445SuccinylationMVKILGHKSTDRVLG
CEEECCCCCCCCEEE		53.9323806337
476PhosphorylationLALEYGASCEDIARV
HHHHHCCCHHHHHHH		17.4223567750
477S-nitrosylationALEYGASCEDIARVC
HHHHCCCHHHHHHHH		5.5921278135
477GlutathionylationALEYGASCEDIARVC
HHHHCCCHHHHHHHH		5.5924333276
477S-nitrosocysteineALEYGASCEDIARVC
HHHHCCCHHHHHHHH		5.59-
484S-nitrosylationCEDIARVCHAHPTLS
HHHHHHHHHHCCCHH		1.6322178444
484S-palmitoylationCEDIARVCHAHPTLS
HHHHHHHHHHCCCHH		1.6328526873
484S-nitrosocysteineCEDIARVCHAHPTLS
HHHHHHHHHHCCCHH		1.63-
505SuccinylationNLAAAFGKPINF---
HHHHHHCCCCCC---		35.9523806337
505UbiquitinationNLAAAFGKPINF---
HHHHHHCCCCCC---		35.95-
505SuccinylationNLAAAFGKPINF---
HHHHHHCCCCCC---		35.95-
505AcetylationNLAAAFGKPINF---
HHHHHHCCCCCC---		35.9523576753
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DLDH_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLDH_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DLDH_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DLDH_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLDH_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, AND MASS SPECTROMETRY.

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