IDH3A_HUMAN - dbPTM
IDH3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IDH3A_HUMAN
UniProt AC P50213
Protein Name Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Gene Name IDH3A
Organism Homo sapiens (Human).
Sequence Length 366
Subcellular Localization Mitochondrion.
Protein Description Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers..
Protein Sequence MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD
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
8PhosphorylationMAGPAWISKVSRLLG
CCCHHHHHHHHHHHH		19.1229449344
11PhosphorylationPAWISKVSRLLGAFH
HHHHHHHHHHHHHCC		22.4329449344
22 (in isoform 2)Ubiquitination-42.9721890473
58UbiquitinationMKIFDAAKAPIQWEE
HHHHHHHCCCCCEEC		57.3121890473
58 (in isoform 1)Ubiquitination-57.3121890473
58AcetylationMKIFDAAKAPIQWEE
HHHHHHHCCCCCEEC		57.3125953088
58MalonylationMKIFDAAKAPIQWEE
HHHHHHHCCCCCEEC		57.3126320211
66MethylationAPIQWEERNVTAIQG
CCCCEECCCEEEEEC		31.25115480155
69O-linked_GlycosylationQWEERNVTAIQGPGG
CEECCCEEEEECCCC		22.9229351928
69PhosphorylationQWEERNVTAIQGPGG
CEECCCEEEEECCCC		22.92-
77 (in isoform 1)Ubiquitination-39.2321890473
77AcetylationAIQGPGGKWMIPSEA
EEECCCCCEECCHHH		39.2323954790
77SuccinylationAIQGPGGKWMIPSEA
EEECCCCCEECCHHH		39.23-
77SuccinylationAIQGPGGKWMIPSEA
EEECCCCCEECCHHH		39.23-
77MalonylationAIQGPGGKWMIPSEA
EEECCCCCEECCHHH		39.2326320211
77UbiquitinationAIQGPGGKWMIPSEA
EEECCCCCEECCHHH		39.2321890473
82PhosphorylationGGKWMIPSEAKESMD
CCCEECCHHHHHHHC		38.98-
85AcetylationWMIPSEAKESMDKNK
EECCHHHHHHHCCCC		46.3926822725
87PhosphorylationIPSEAKESMDKNKMG
CCHHHHHHHCCCCCC		31.41-
90AcetylationEAKESMDKNKMGLKG
HHHHHHCCCCCCCCC		50.2312439119
100UbiquitinationMGLKGPLKTPIAAGH
CCCCCCCCCCCCCCC		56.2221890473
100 (in isoform 1)Ubiquitination-56.2221890473
100AcetylationMGLKGPLKTPIAAGH
CCCCCCCCCCCCCCC		56.2225953088
100MalonylationMGLKGPLKTPIAAGH
CCCCCCCCCCCCCCC		56.2226320211
101PhosphorylationGLKGPLKTPIAAGHP
CCCCCCCCCCCCCCC		27.84-
109PhosphorylationPIAAGHPSMNLLLRK
CCCCCCCCHHHHHHH		18.0323312004
116UbiquitinationSMNLLLRKTFDLYAN
CHHHHHHHHHHHHCC		54.21-
117PhosphorylationMNLLLRKTFDLYANV
HHHHHHHHHHHHCCC		18.8928152594
121PhosphorylationLRKTFDLYANVRPCV
HHHHHHHHCCCCCCE		9.6628152594
129PhosphorylationANVRPCVSIEGYKTP
CCCCCCEEECCCCCC		22.9528152594
133PhosphorylationPCVSIEGYKTPYTDV
CCEEECCCCCCCCCE		10.0120068231
135PhosphorylationVSIEGYKTPYTDVNI
EEECCCCCCCCCEEE		17.0328152594
137PhosphorylationIEGYKTPYTDVNIVT
ECCCCCCCCCEEEEE		22.3228152594
138PhosphorylationEGYKTPYTDVNIVTI
CCCCCCCCCEEEEEE		34.3728152594
154PhosphorylationENTEGEYSGIEHVIV
CCCCCCCCCCCEEEE		29.06-
167PhosphorylationIVDGVVQSIKLITEG
EECCHHHHEEHHHCC		15.3024719451
172PhosphorylationVQSIKLITEGASKRI
HHHEEHHHCCHHHHH		38.5120860994
177AcetylationLITEGASKRIAEFAF
HHHCCHHHHHHHHHH		47.4925953088
177UbiquitinationLITEGASKRIAEFAF
HHHCCHHHHHHHHHH		47.49-
186PhosphorylationIAEFAFEYARNNHRS
HHHHHHHHHHHCCCC		12.3828152594
193PhosphorylationYARNNHRSNVTAVHK
HHHHCCCCCCHHHHH		28.2721406692
196PhosphorylationNNHRSNVTAVHKANI
HCCCCCCHHHHHHHH		27.4921406692
200AcetylationSNVTAVHKANIMRMS
CCCHHHHHHHHHHHC		36.2125953088
200UbiquitinationSNVTAVHKANIMRMS
CCCHHHHHHHHHHHC		36.21-
206SulfoxidationHKANIMRMSDGLFLQ
HHHHHHHHCCCCHHH		2.0721406390
207PhosphorylationKANIMRMSDGLFLQK
HHHHHHHCCCCHHHH		20.4021712546
214AcetylationSDGLFLQKCREVAES
CCCCHHHHHHHHHHH		37.0926822725
214UbiquitinationSDGLFLQKCREVAES
CCCCHHHHHHHHHHH		37.09-
223AcetylationREVAESCKDIKFNEM
HHHHHHCCCCCCCHH		72.3025953088
223UbiquitinationREVAESCKDIKFNEM
HHHHHHCCCCCCCHH		72.30-
331GlutathionylationAARIEAACFATIKDG
HHHHHHHEEEEECCC		2.8422555962
334PhosphorylationIEAACFATIKDGKSL
HHHHEEEEECCCCCC		14.3328060719
336UbiquitinationAACFATIKDGKSLTK
HHEEEEECCCCCCCC		56.95-
336AcetylationAACFATIKDGKSLTK
HHEEEEECCCCCCCC		56.9525953088
336SuccinylationAACFATIKDGKSLTK
HHEEEEECCCCCCCC		56.9527452117
343SuccinylationKDGKSLTKDLGGNAK
CCCCCCCCCCCCCCC		57.1427452117
343UbiquitinationKDGKSLTKDLGGNAK
CCCCCCCCCCCCCCC		57.1419608861
343SuccinylationKDGKSLTKDLGGNAK
CCCCCCCCCCCCCCC		57.14-
343AcetylationKDGKSLTKDLGGNAK
CCCCCCCCCCCCCCC		57.1419608861
350SuccinylationKDLGGNAKCSDFTEE
CCCCCCCCCCHHHHH		37.97-
350UbiquitinationKDLGGNAKCSDFTEE
CCCCCCCCCCHHHHH		37.97-
350MalonylationKDLGGNAKCSDFTEE
CCCCCCCCCCHHHHH		37.9726320211
350AcetylationKDLGGNAKCSDFTEE
CCCCCCCCCCHHHHH		37.9725953088
350SuccinylationKDLGGNAKCSDFTEE
CCCCCCCCCCHHHHH		37.97-
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 IDH3A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IDH3A_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 IDH3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
S10AG_HUMANS100A16physical
22939629
SUCB1_HUMANSUCLA2physical
22939629
MBNL1_HUMANMBNL1physical
21988832
RAB4A_HUMANRAB4Aphysical
21988832
IDH3B_HUMANIDH3Bphysical
26186194
RDH13_HUMANRDH13physical
26186194
IDH3G_HUMANIDH3Gphysical
26186194
MRP1_HUMANABCC1physical
26344197
MRP3_HUMANABCC3physical
26344197
ACON_HUMANACO2physical
26344197
ACTN4_HUMANACTN4physical
26344197
AT2B1_HUMANATP2B1physical
26344197
TCPQ_HUMANCCT8physical
26344197
HDHD1_HUMANHDHD1physical
26344197
IDHC_HUMANIDH1physical
26344197
IPO9_HUMANIPO9physical
26344197
PSMD2_HUMANPSMD2physical
26344197
SUCB1_HUMANSUCLA2physical
26344197
UBE2N_HUMANUBE2Nphysical
26344197
QCR2_HUMANUQCRC2physical
26344197
IDH3G_HUMANIDH3Gphysical
28514442
IDH3B_HUMANIDH3Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IDH3A_HUMAN

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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-343, AND MASS SPECTROMETRY.

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