Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

3 structures for Q60597

Entry ID Method Resolution Chain Position Source
3E2H X-ray 380 A Q 932-940 PDB
3TF7 X-ray 275 A B/F 932-940 PDB
AF-Q60597-F1 Predicted AlphaFoldDB

41 variants for Q60597

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389141089 15 T>I No EVA
rs3389114311 36 Q>H No EVA
rs3389139601 73 H>L No EVA
rs3401794294 183 D>V No EVA
rs3401911637 191 T>N No EVA
rs3389141090 298 S>G No EVA
rs3389081212 330 F>L No EVA
rs3389118534 342 E>Q No EVA
rs3389140888 346 D>Y No EVA
rs3389140910 378 E>D No EVA
rs3389147391 436 G>D No EVA
rs3389081260 440 V>M No EVA
rs3389138392 448 F>S No EVA
rs3389118555 462 T>I No EVA
rs3389114404 464 V>M No EVA
rs3389134926 467 V>L No EVA
rs3389151646 474 H>Y No EVA
rs3401960033 483 V>I* No EVA
rs3401817408 484 M>I No EVA
rs3389140907 484 M>L No EVA
rs3389138387 523 Q>H No EVA
rs3389143558 556 E>K No EVA
rs3389140846 592 F>L No EVA
rs3389140858 604 C>R No EVA
rs3389153178 621 A>V No EVA
rs3389138407 624 V>I No EVA
rs3401812039 641 T>I No EVA
rs3389130573 645 L>F No EVA
rs3389139597 670 H>N No EVA
rs3389114352 680 R>Q No EVA
rs3389147350 681 G>D No EVA
rs3389147389 682 T>S No EVA
rs3389138411 698 R>G No EVA
rs3389144772 741 V>A No EVA
rs3389138423 859 P>H No EVA
rs3389141465 908 V>M No EVA
rs3389153225 945 A>P No EVA
rs3389141078 946 Q>* No EVA
rs3389118548 972 R>* No EVA
rs260357355 980 A>V No EVA
rs3389130625 1002 H>L No EVA

No associated diseases with Q60597

4 regional properties for Q60597

Type Name Position InterPro Accession
domain Dehydrogenase, E1 component 257 - 581 IPR001017
domain Transketolase-like, pyrimidine-binding domain 650 - 866 IPR005475
domain Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal 870 - 1014 IPR031717
domain 2-oxoglutarate dehydrogenase E1 component, N-terminal domain 48 - 86 IPR032106

Functions

Description
EC Number 1.2.4.2 With a disulfide as acceptor
Subcellular Localization
  • Mitochondrion
  • Nucleus
  • Mainly localizes in the mitochondrion
  • A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
oxoglutarate dehydrogenase complex A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) (E1), dihydrolipoamide S-succinyltransferase (E2) and dihydrolipoamide dehydrogenase (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2).

6 GO annotations of molecular function

Name Definition
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
heat shock protein binding Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.
metal ion binding Binding to a metal ion.
oxoglutarate dehydrogenase (NAD+) activity Catalysis of the reaction: 2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH.
oxoglutarate dehydrogenase (succinyl-transferring) activity Catalysis of the reaction: 2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2.
thiamine pyrophosphate binding Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.

14 GO annotations of biological process

Name Definition
2-oxoglutarate metabolic process The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
cerebellar cortex development The process whose specific outcome is the progression of the cerebellar cortex over time, from its formation to the mature structure. The cerebellar cortex is a thin mantle of gray matter that covers the surface of each cerebral hemisphere. It has a characteristic morphology with convolutions (gyri) and crevices (sulci) that have specific functions. Six layers of nerve cells and the nerve pathways that connect them comprise the cerebellar cortex. Together, these regions are responsible for the processes of conscious thought, perception, emotion and memory as well as advanced motor function.
generation of precursor metabolites and energy The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances.
glycolytic process The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
hippocampus development The progression of the hippocampus over time from its initial formation until its mature state.
histone succinylation The modification of a histone by the addition of an succinyl group.
NADH metabolic process The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
olfactory bulb mitral cell layer development The progression of the olfactory bulb mitral cell layer over time from its initial formation until its mature state. The mitral cell layer is composed of pyramidal neurons whose cell bodies are located between the granule cell layer and the plexiform layer.
pyramidal neuron development The progression of a pyramidal neuron from its initial formation to its mature state.
striatum development The progression of the striatum over time from its initial formation until its mature state. The striatum is a region of the forebrain consisting of the caudate nucleus, putamen and fundus striati.
succinyl-CoA metabolic process The chemical reactions and pathways involving succinyl-CoA, a compound composed of the monovalent acyl group 3-carboxypropanoyl, derived from succinic acid by loss of one OH group, linked to coenzyme A.
tangential migration from the subventricular zone to the olfactory bulb The migration of cells in the telencephalon from the subventricular zone to the olfactory bulb in which cells move orthogonally to the direction of radial migration and do not use radial glial cell processes as substrates for migration.
thalamus development The process in which the thalamus changes over time, from its initial formation to its mature state.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE
70 80 90 100 110 120
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV
130 140 150 160 170 180
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES
190 200 210 220 230 240
DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
250 260 270 280 290 300
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN
310 320 330 340 350 360
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR
370 380 390 400 410 420
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
430 440 450 460 470 480
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
490 500 510 520 530 540
EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
550 560 570 580 590 600
AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR
610 620 630 640 650 660
SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA
670 680 690 700 710 720
FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
730 740 750 760 770 780
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP
790 800 810 820 830 840
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH
850 860 870 880 890 900
VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR
910 920 930 940 950 960
LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH
970 980 990 1000 1010 1020
KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK
KFS