ODO1_YEAST - dbPTM
ODO1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ODO1_YEAST
UniProt AC P20967
Protein Name 2-oxoglutarate dehydrogenase, mitochondrial
Gene Name KGD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1014
Subcellular Localization Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid.
Protein Description The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3)..
Protein Sequence MLRFVSSQTCRYSSRGLLKTSLLKNASTVKIVGRGLATTGTDNFLSTSNATYIDEMYQAWQKDPSSVHVSWDAYFKNMSNPKIPATKAFQAPPSISNFPQGTEAAPLGTAMTGSVDENVSIHLKVQLLCRAYQVRGHLKAHIDPLGISFGSNKNNPVPPELTLDYYGFSKHDLDKEINLGPGILPRFARDGKSKMSLKEIVDHLEKLYCSSYGVQYTHIPSKQKCDWLRERIEIPEPYQYTVDQKRQILDRLTWATSFESFLSTKFPNDKRFGLEGLESVVPGIKTLVDRSVELGVEDIVLGMAHRGRLNVLSNVVRKPNESIFSEFKGSSARDDIEGSGDVKYHLGMNYQRPTTSGKYVNLSLVANPSHLESQDPVVLGRTRALLHAKNDLKEKTKALGVLLHGDAAFAGQGVVYETMGFLTLPEYSTGGTIHVITNNQIGFTTDPRFARSTPYPSDLAKAIDAPIFHVNANDVEAVTFIFNLAAEWRHKFHTDAIIDVVGWRKHGHNETDQPSFTQPLMYKKIAKQKSVIDVYTEKLISEGTFSKKDIDEHKKWVWNLFEDAFEKAKDYVPSQREWLTAAWEGFKSPKELATEILPHEPTNVPESTLKELGKVLSSWPEGFEVHKNLKRILKNRGKSIETGEGIDWATGEALAFGTLVLDGQNVRVSGEDVERGTFSQRHAVLHDQQSEAIYTPLSTLNNEKADFTIANSSLSEYGVMGFEYGYSLTSPDYLVMWEAQFGDFANTAQVIIDQFIAGGEQKWKQRSGLVLSLPHGYDGQGPEHSSGRLERFLQLANEDPRYFPSEEKLQRQHQDCNFQVVYPTTPANLFHILRRQQHRQFRKPLALFFSKQLLRHPLARSSLSEFTEGGFQWIIEDIEHGKSIGTKEETKRLVLLSGQVYTALHKRRESLGDKTTAFLKIEQLHPFPFAQLRDSLNSYPNLEEIVWCQEEPLNMGSWAYTEPRLHTTLKETDKYKDFKVRYCGRNPSGAVAAGSKSLHLAEEDAFLKDVFQQS
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
27PhosphorylationTSLLKNASTVKIVGR
HHHHCCCCEEEEECC		43.0321440633
51PhosphorylationFLSTSNATYIDEMYQ
CCCCCCCCCHHHHHH		25.8417330950
79PhosphorylationDAYFKNMSNPKIPAT
HHHHCCCCCCCCCCC		60.4121126336
86PhosphorylationSNPKIPATKAFQAPP
CCCCCCCCCCCCCCC		19.9728889911
170AcetylationLDYYGFSKHDLDKEI
EEECCCCHHHCCCCC		38.5924489116
175AcetylationFSKHDLDKEINLGPG
CCHHHCCCCCCCCCC		68.7224489116
198AcetylationGKSKMSLKEIVDHLE
CCCCCCHHHHHHHHH		37.7824489116
256PhosphorylationLDRLTWATSFESFLS
HHHHHHHHHHHHHHC		26.0522369663
257PhosphorylationDRLTWATSFESFLST
HHHHHHHHHHHHHCC		21.1922369663
260PhosphorylationTWATSFESFLSTKFP
HHHHHHHHHHCCCCC		29.4922369663
263PhosphorylationTSFESFLSTKFPNDK
HHHHHHHCCCCCCCC		27.7822369663
264PhosphorylationSFESFLSTKFPNDKR
HHHHHHCCCCCCCCC		38.5622369663
270UbiquitinationSTKFPNDKRFGLEGL
CCCCCCCCCCCCCHH		57.1617644757
285UbiquitinationESVVPGIKTLVDRSV
HHHCCCHHHHHHHHH		41.5417644757
328AcetylationESIFSEFKGSSARDD
HHHHHHCCCCCCCCC		54.5624489116
331PhosphorylationFSEFKGSSARDDIEG
HHHCCCCCCCCCCCC		35.6721440633
358UbiquitinationQRPTTSGKYVNLSLV
CCCCCCCCEEEEEEE		45.8817644757
453PhosphorylationDPRFARSTPYPSDLA
CCHHCCCCCCCHHHH		22.6827214570
530PhosphorylationKKIAKQKSVIDVYTE
HHHHHCCCCHHHHHH		23.0829734811
547AcetylationISEGTFSKKDIDEHK
HHCCCCCHHHHHHHH		50.7222865919
547SuccinylationISEGTFSKKDIDEHK
HHCCCCCHHHHHHHH		50.7223954790
548AcetylationSEGTFSKKDIDEHKK
HCCCCCHHHHHHHHH		59.7324489116
590UbiquitinationWEGFKSPKELATEIL
HHCCCCHHHHHHHHC		72.8915699485
610UbiquitinationNVPESTLKELGKVLS
CCCHHHHHHHHHHHH		51.4815699485
614AcetylationSTLKELGKVLSSWPE
HHHHHHHHHHHCCCC		53.2624489116
627AcetylationPEGFEVHKNLKRILK
CCCHHHHHHHHHHHH		69.9724489116
630AcetylationFEVHKNLKRILKNRG
HHHHHHHHHHHHHCC		46.9524489116
808AcetylationRYFPSEEKLQRQHQD
CCCCCHHHHHHHHCC		45.9624489116
901PhosphorylationVLLSGQVYTALHKRR
EEHHHHHHHHHHHHH		4.3828889911
910PhosphorylationALHKRRESLGDKTTA
HHHHHHHHCCCCCEE		35.5219795423
914AcetylationRRESLGDKTTAFLKI
HHHHCCCCCEEEEEH		46.0724489116
988PhosphorylationRYCGRNPSGAVAAGS
EECCCCCCCCCCCCC		42.8227214570
995PhosphorylationSGAVAAGSKSLHLAE
CCCCCCCCCCEEHHH		17.8427214570
996SuccinylationGAVAAGSKSLHLAEE
CCCCCCCCCEEHHHH		57.0023954790
997PhosphorylationAVAAGSKSLHLAEED
CCCCCCCCEEHHHHH		23.7922369663
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 ODO1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ODO1_YEAST !!
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 ODO1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ODO2_YEASTKGD2physical
11805826
RU2A_YEASTLEA1physical
11805826
DLDH_YEASTLPD1physical
11805826
RT31_YEASTYMR31physical
11805826
ODO2_YEASTKGD2physical
16429126
DLDH_YEASTLPD1physical
16429126
RL15B_YEASTRPL15Bphysical
16429126
RL16B_YEASTRPL16Bphysical
16429126
RL27A_YEASTRPL27Aphysical
16429126
RL30_YEASTRPL30physical
16429126
RL7A_YEASTRPL7Aphysical
16429126
RS18A_YEASTRPS18Aphysical
16429126
RS18B_YEASTRPS18Aphysical
16429126
RS3A2_YEASTRPS1Bphysical
16429126
RS24A_YEASTRPS24Bphysical
16429126
RS24B_YEASTRPS24Bphysical
16429126
RT31_YEASTYMR31physical
16429126
LYS12_YEASTLYS12genetic
16941010
HOSC_YEASTLYS20genetic
16941010
LYS4_YEASTLYS4genetic
16941010
ODO1_YEASTKGD1physical
22940862
VAM3_YEASTVAM3genetic
27708008
CDC24_YEASTCDC24genetic
27708008
SYIC_YEASTILS1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
TECR_YEASTTSC13genetic
27708008
ARP2_YEASTARP2genetic
27708008
DPOD_YEASTPOL3genetic
27708008
COPA_YEASTCOP1genetic
27708008
UBC3_YEASTCDC34genetic
27708008
SEC7_YEASTSEC7genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
SRPR_YEASTSRP101genetic
27708008
PANK_YEASTCAB1genetic
27708008
ACT_YEASTACT1genetic
27708008
SWC4_YEASTSWC4genetic
27708008
MED6_YEASTMED6genetic
27708008
RRN3_YEASTRRN3genetic
27708008
COFI_YEASTCOF1genetic
27708008
SEC13_YEASTSEC13genetic
27708008
SEC22_YEASTSEC22genetic
27708008
LST8_YEASTLST8genetic
27708008
CAP_YEASTSRV2genetic
27708008
APC5_YEASTAPC5genetic
27708008
SLA1_YEASTSLA1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
CSG2_YEASTCSG2genetic
27708008
ODPB_YEASTPDB1genetic
27708008
CLPX_YEASTMCX1genetic
27708008
PEX19_YEASTPEX19genetic
27708008
PAA1_YEASTPAA1genetic
27708008
ARO1_YEASTARO1genetic
27708008
SAS4_YEASTSAS4genetic
27708008
METK2_YEASTSAM2genetic
27708008
IRC4_YEASTIRC4genetic
27708008
ODPA_YEASTPDA1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
CHO2_YEASTCHO2genetic
27708008
YHI2_YEASTYHR022Cgenetic
27708008
KEL1_YEASTKEL1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
MNN11_YEASTMNN11genetic
27708008
BLI1_YEASTBLI1genetic
27708008
MGR3L_YEASTYKL133Cgenetic
27708008
DOA1_YEASTDOA1genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
ERG3_YEASTERG3genetic
27708008
PEX13_YEASTPEX13genetic
27708008
VPS71_YEASTVPS71genetic
27708008
VPS9_YEASTVPS9genetic
27708008
YNF0_YEASTYNL050Cgenetic
27708008
ODP2_YEASTLAT1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
SIN3_YEASTSIN3genetic
27708008
VPS17_YEASTVPS17genetic
27708008
SFL1_YEASTSFL1genetic
27708008
CARP_YEASTPEP4genetic
27708008
BRR1_YEASTBRR1genetic
27708008
ODO2_YEASTKGD2physical
25165143
DLDH_YEASTLPD1physical
25165143
RT31_YEASTYMR31physical
25165143
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ODO1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-901, AND MASSSPECTROMETRY.

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