IDH3B
entrez
3420
canonical
uniprot
O43837
canonical
ensembl
ENSG00000101365
resolver
ensp
ENSP00000370223
resolver
ensp
ENSP00000370232
resolver
ensp
ENSP00000482773
resolver
ensp
ENSP00000484922
resolver
enst
ENST00000474315
resolver
enst
ENST00000613370
resolver
genesymbol
IDH3B
resolver
hgnc
HGNC:5385
resolver
uniprot
A0A087WZN1
resolver
uniprot
A0A087X2E5
resolver
uniprot
B2RDR1
resolver
uniprot
D3DVX2
resolver
uniprot
D3DVX3
resolver
uniprot
O95106
resolver
uniprot
Q5JXS8
resolver
uniprot
Q9NQ06
resolver
uniprot
Q9NQ07
resolver
uniprot
Q9NUZ0
resolver
uniprot
Q9UEX0
resolver
uniprot
Q9UG99
resolver
uniprot_entry
A0A087WZN1_HUMAN
resolver
uniprot_entry
A0A087X2E5_HUMAN
resolver
uniprot_entry
IDH3B_HUMAN
resolver
uniprot_sec
B2RDR1
resolver
uniprot_sec
D3DVX2
resolver
uniprot_sec
D3DVX3
resolver
uniprot_sec
O95106
resolver
uniprot_sec
Q5JXS8
resolver
uniprot_sec
Q9NQ06
resolver
uniprot_sec
Q9NQ07
resolver
uniprot_sec
Q9NUZ0
resolver
uniprot_sec
Q9UEX0
resolver
uniprot_sec
Q9UG99
resolver
activity_regulation
ACTIVITY REGULATION: The heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits can be allosterically activated by citrate (CIT) or/and ADP, and the two activators can act independently or synergistically. The heterodimer composed of IDH3A and IDH3B subunits cannot be allosterically regulated and the allosteric regulation of the heterotetramer is through the IDH3G subunit and not the IDH3B subunit. The IDH3G subunit contains the allosteric site which consists of a CIT-binding site and an ADP-binding site, and the binding of CIT and ADP causes conformational changes at the allosteric site which are transmitted to the active site in the catalytic subunit (IDH3A) through a cascade of conformational changes at the heterodimer interface, leading to stabilization of the isocitrate-binding at the active site and thus activation of the enzyme. ATP can activate the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits at low concentrations but inhibits their activities at high concentrations, whereas ATP exhibits only inhibitory effect on the heterodimer composed of IDH3A and IDH3B subunits. {ECO:0000269|PubMed:28098230, ECO:0000269|PubMed:28139779}.
uniprot
proteins
amino_acid_sequence
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRTRDMGGYSTTTDFIKSVIGHLQTKGS
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 46 (RP46) [MIM:612572]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:18806796}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:28139779}.
uniprot
proteins
mass_dalton
42184
uniprot
proteins
protein_family
Isocitrate and isopropylmalate dehydrogenases family
uniprot
proteins
pubmed
10601238
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18806796
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28098230
uniprot
proteins
pubmed
28139779
uniprot
proteins
sequence_length
385
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion.
uniprot
proteins