ODBA_HUMAN - dbPTM
ODBA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ODBA_HUMAN
UniProt AC P12694
Protein Name 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Gene Name BCKDHA
Organism Homo sapiens (Human).
Sequence Length 445
Subcellular Localization Mitochondrion matrix.
Protein Description The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3)..
Protein Sequence MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQLRKQQESLARHLQTYGEHYPLDHFDK
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
46PhosphorylationPRQQQQFSSLDDKPQ
HHHHHCCCCCCCCCC		26.1730108239
47PhosphorylationRQQQQFSSLDDKPQF
HHHHCCCCCCCCCCC		36.7926657352
85UbiquitinationIYRVMDRQGQIINPS
EEEEECCCCCCCCCC		43.83-
106PhosphorylationKEKVLKLYKSMTLLN
HHHHHHHHHHHHHHH		10.22-
107AcetylationEKVLKLYKSMTLLNT
HHHHHHHHHHHHHHH		44.1625953088
107MalonylationEKVLKLYKSMTLLNT
HHHHHHHHHHHHHHH		44.1626320211
107UbiquitinationEKVLKLYKSMTLLNT
HHHHHHHHHHHHHHH		44.16-
114PhosphorylationKSMTLLNTMDRILYE
HHHHHHHHHHHHHHH		22.03-
117MethylationTLLNTMDRILYESQR
HHHHHHHHHHHHHHH		15.25-
166PhosphorylationREAGVLMYRDYPLEL
CEECEEEECCCCHHH		9.0022468782
169PhosphorylationGVLMYRDYPLELFMA
CEEEECCCCHHHHHH		10.7522468782
202UbiquitinationYGCKERHFVTISSPL
CCCCCCCEEEECCCH		6.94-
206PhosphorylationERHFVTISSPLATQI
CCCEEEECCCHHHHH		19.28-
207PhosphorylationRHFVTISSPLATQIP
CCEEEECCCHHHHHH		21.78-
224UbiquitinationVGAAYAAKRANANRV
HHHHHHHHHHCCCCE		43.82-
289UbiquitinationDGIAARGPGYGIMSI
CCCCCCCCCCCEEEE		27.55-
295PhosphorylationGPGYGIMSIRVDGND
CCCCCEEEEEECCCE		12.8112812918
307PhosphorylationGNDVFAVYNATKEAR
CCEEEEEEECCHHHH		8.82-
311AcetylationFAVYNATKEARRRAV
EEEEECCHHHHHHHH		47.1425038526
311UbiquitinationFAVYNATKEARRRAV
EEEEECCHHHHHHHH		47.14-
337PhosphorylationTYRIGHHSTSDDSSA
EEECCCCCCCCCCHH		24.7529255136
338PhosphorylationYRIGHHSTSDDSSAY
EECCCCCCCCCCHHC		31.6429255136
339PhosphorylationRIGHHSTSDDSSAYR
ECCCCCCCCCCHHCC		42.3022167270
342PhosphorylationHHSTSDDSSAYRSVD
CCCCCCCCHHCCCHH		23.1222167270
343PhosphorylationHSTSDDSSAYRSVDE
CCCCCCCHHCCCHHC		35.9923401153
345PhosphorylationTSDDSSAYRSVDEVN
CCCCCHHCCCHHCCC		12.8423401153
347PhosphorylationDDSSAYRSVDEVNYW
CCCHHCCCHHCCCCC		22.6519664994
353PhosphorylationRSVDEVNYWDKQDHP
CCHHCCCCCCCCCCH		21.8423927012
356UbiquitinationDEVNYWDKQDHPISR
HCCCCCCCCCCHHHH		43.40-
356AcetylationDEVNYWDKQDHPISR
HCCCCCCCCCCHHHH		43.4025038526
356SuccinylationDEVNYWDKQDHPISR
HCCCCCCCCCCHHHH		43.40-
356SuccinylationDEVNYWDKQDHPISR
HCCCCCCCCCCHHHH		43.40-
359AcetylationNYWDKQDHPISRLRH
CCCCCCCCHHHHHHH		21.06-
359UbiquitinationNYWDKQDHPISRLRH
CCCCCCCCHHHHHHH		21.06-
362PhosphorylationDKQDHPISRLRHYLL
CCCCCHHHHHHHHHH		29.7024702127
380AcetylationWWDEEQEKAWRKQSR
CCCHHHHHHHHHHHH		53.6025038526
380SuccinylationWWDEEQEKAWRKQSR
CCCHHHHHHHHHHHH		53.60-
380SuccinylationWWDEEQEKAWRKQSR
CCCHHHHHHHHHHHH		53.60-
389MalonylationWRKQSRRKVMEAFEQ
HHHHHHHHHHHHHHH		44.8426320211
389SuccinylationWRKQSRRKVMEAFEQ
HHHHHHHHHHHHHHH		44.8427452117
445AcetylationYPLDHFDK-------
CCCCCCCC-------		62.382374953
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
337SPhosphorylationKinaseBCKDKQ00972
PSP
347SPhosphorylationKinaseBCKDKQ00972
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ODBA_HUMAN !!
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 ODBA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPOLL_HUMANPOLLphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
248600Maple syrup urine disease 1A (MSUD1A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ODBA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-347, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; TYR-345 ANDSER-347, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-347, ANDMASS SPECTROMETRY.

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