IDH3B_HUMAN - dbPTM
IDH3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IDH3B_HUMAN
UniProt AC O43837
Protein Name Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
Gene Name IDH3B
Organism Homo sapiens (Human).
Sequence Length 385
Subcellular Localization Mitochondrion.
Protein Description Plays a structural role to facilitate the assembly and ensure the full activity of the enzyme catalyzing 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 MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRTRDMGGYSTTTDFIKSVIGHLQTKGS
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
5Phosphorylation---MAALSGVRWLTR
---CCHHHHHHHHHH		30.4324719451
11PhosphorylationLSGVRWLTRALVSAG
HHHHHHHHHHHHHCC		13.6124719451
29PhosphorylationAWRGLSTSAAAHAAS
HHHCCCHHHHHHHHH		16.7225599653
36PhosphorylationSAAAHAASRSQAEDV
HHHHHHHHHHHCCCC		32.9925599653
47UbiquitinationAEDVRVEGSFPVTML
CCCCEEECEECCEEC		31.5621890473
47 (in isoform 3)Acetylation-31.56-
68AcetylationPELMHAVKEVFKAAA
HHHHHHHHHHHHHCC		49.2825038526
96 (in isoform 2)Acetylation-53.96-
96UbiquitinationQNMASEEKLEQVLSS
HHHCCHHHHHHHHHH		53.9619608861
96AcetylationQNMASEEKLEQVLSS
HHHCCHHHHHHHHHH		53.9623954790
102PhosphorylationEKLEQVLSSMKENKV
HHHHHHHHHHHHCCE		29.5422210691
103PhosphorylationKLEQVLSSMKENKVA
HHHHHHHHHHHCCEE		29.7022210691
105SuccinylationEQVLSSMKENKVAII
HHHHHHHHHCCEEEE		61.1527452117
105AcetylationEQVLSSMKENKVAII
HHHHHHHHHCCEEEE		61.1525038526
105 (in isoform 2)Ubiquitination-61.1521890473
105UbiquitinationEQVLSSMKENKVAII
HHHHHHHHHCCEEEE		61.15-
113 (in isoform 1)Ubiquitination-19.4221890473
114AcetylationNKVAIIGKIHTPMEY
CCEEEEEEECCCCHH		22.3925953088
117PhosphorylationAIIGKIHTPMEYKGE
EEEEEECCCCHHCCC		28.0124719451
121PhosphorylationKIHTPMEYKGELASY
EECCCCHHCCCHHCH		20.3124719451
122AcetylationIHTPMEYKGELASYD
ECCCCHHCCCHHCHH		32.3825953088
135MalonylationYDMRLRRKLDLFANV
HHHHHHHHHHHHCCE		39.6626320211
135UbiquitinationYDMRLRRKLDLFANV
HHHHHHHHHHHHCCE		39.66-
135AcetylationYDMRLRRKLDLFANV
HHHHHHHHHHHHCCE		39.6625953088
146 (in isoform 2)Acetylation-31.25-
146AcetylationFANVVHVKSLPGYMT
HCCEEEHHHCCCCHH		31.2523236377
147PhosphorylationANVVHVKSLPGYMTR
CCEEEHHHCCCCHHC		38.4127135362
167PhosphorylationLVIIREQTEGEYSSL
EEEEEECCCCCCCCC		41.0021406692
171PhosphorylationREQTEGEYSSLEHES
EECCCCCCCCCCHHH		17.8921406692
172PhosphorylationEQTEGEYSSLEHESA
ECCCCCCCCCCHHHH		24.9321406692
173PhosphorylationQTEGEYSSLEHESAR
CCCCCCCCCCHHHHH		36.5521406692
178PhosphorylationYSSLEHESARGVIEC
CCCCCHHHHHHHHHH		25.7721406692
199AcetylationAKSQRIAKFAFDYAT
HHHHHHHHHHHHHHC		34.5519608861
199UbiquitinationAKSQRIAKFAFDYAT
HHHHHHHHHHHHHHC		34.5521890473
199 (in isoform 2)Ubiquitination-34.5521890473
199 (in isoform 2)Acetylation-34.55-
207SuccinylationFAFDYATKKGRGKVT
HHHHHHCCCCCCCEE		45.0923954790
207 (in isoform 1)Ubiquitination-45.0921890473
207UbiquitinationFAFDYATKKGRGKVT
HHHHHHCCCCCCCEE		45.09-
207AcetylationFAFDYATKKGRGKVT
HHHHHHCCCCCCCEE		45.0923236377
212UbiquitinationATKKGRGKVTAVHKA
HCCCCCCCEEEEEEC		34.74-
218UbiquitinationGKVTAVHKANIMKLG
CCEEEEEECCCEECC		36.21-
218AcetylationGKVTAVHKANIMKLG
CCEEEEEECCCEECC		36.2125825284
222 (in isoform 3)Acetylation-2.69-
242UbiquitinationEVAELYPKIKFETMI
HHHHHCCCCCCEEEE		45.00-
242AcetylationEVAELYPKIKFETMI
HHHHHCCCCCCEEEE		45.0025953088
323PhosphorylationGRNIANPTAMLLSAS
CCCCCCHHHHHHHHH		25.2220068231
330PhosphorylationTAMLLSASNMLRHLN
HHHHHHHHHHHHHCC		21.28-
350AcetylationSMIADAVKKVIKVGK
HHHHHHHHHHHHCCC		42.9425953088
360 (in isoform 2)Phosphorylation-33.73-
363SulfoxidationGKVRTRDMGGYSTTT
CCEECCCCCCCCCHH		3.9628183972
366PhosphorylationRTRDMGGYSTTTDFI
ECCCCCCCCCHHHHH		9.3422817900
367PhosphorylationTRDMGGYSTTTDFIK
CCCCCCCCCHHHHHH		23.6624043423
368PhosphorylationRDMGGYSTTTDFIKS
CCCCCCCCHHHHHHH		25.8224043423
369PhosphorylationDMGGYSTTTDFIKSV
CCCCCCCHHHHHHHH		20.5924043423
370PhosphorylationMGGYSTTTDFIKSVI
CCCCCCHHHHHHHHH		29.0624043423
374AcetylationSTTTDFIKSVIGHLQ
CCHHHHHHHHHHHHH		38.3723954790
375PhosphorylationTTTDFIKSVIGHLQT
CHHHHHHHHHHHHHC		17.72-
383UbiquitinationVIGHLQTKGS-----
HHHHHHCCCC-----		44.17-
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 IDH3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IDH3B_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 IDH3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IDH3G_HUMANIDH3Gphysical
26186194
ODB2_HUMANDBTphysical
26186194
CASP3_HUMANCASP3physical
26344197
IDHC_HUMANIDH1physical
26344197
IDH3G_HUMANIDH3Gphysical
28514442
ODB2_HUMANDBTphysical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
612572Retinitis pigmentosa 46 (RP46)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IDH3B_HUMAN

loading...

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-146; LYS-199 AND LYS-374,AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory