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

1 structures for Q3TY86

Entry ID Method Resolution Chain Position Source
AF-Q3TY86-F1 Predicted AlphaFoldDB

27 variants for Q3TY86

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389418737 9 K>N No EVA
rs3389365289 46 A>S No EVA
rs3389401178 108 K>E No EVA
rs3389396310 118 K>* No EVA
rs3389413267 119 G>C No EVA
rs3389404494 203 G>D No EVA
rs3389404561 243 D>E No EVA
rs3389407298 253 P>L No EVA
rs3389400790 300 S>T No EVA
rs3389398547 324 N>D No EVA
rs3389395035 337 V>I No EVA
rs3389396328 342 F>Y No EVA
rs3389404558 375 R>C No EVA
rs3389384410 392 Y>N No EVA
rs3406552316 407 L>P No EVA
rs3406381964 409 E>D No EVA
rs3406131409 411 V>G No EVA
rs3389398514 415 S>N No EVA
rs3389407330 434 G>S No EVA
rs3389396311 454 M>I No EVA
rs32326670 480 K>R No EVA
rs3389400838 527 Y>F No EVA
rs3389413236 552 S>C No EVA
rs3389384406 557 A>V No EVA
rs3389420729 565 P>H No EVA
rs3389365224 570 V>L No EVA
rs3389409569 579 A>D No EVA

No associated diseases with Q3TY86

3 regional properties for Q3TY86

Type Name Position InterPro Accession
domain Rieske [2Fe-2S] iron-sulphur domain 70 - 165 IPR017941
domain FAD/NAD(P)-binding domain 196 - 493 IPR023753
domain Reductase, C-terminal 512 - 583 IPR028202

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
  • Does not translocate to the nucleus upon induction of apoptosis
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
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.

4 GO annotations of molecular function

Name Definition
2 iron, 2 sulfur cluster binding Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
metal ion binding Binding to a metal ion.
oxidoreductase activity, acting on NAD(P)H Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

1 GO annotations of biological process

Name Definition
execution phase of apoptosis A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O95831 AIFM1 Apoptosis-inducing factor 1, mitochondrial Homo sapiens (Human) PR
Q96NN9 AIFM3 Apoptosis-inducing factor 3 Homo sapiens (Human) PR
Q9Z0X1 Aifm1 Apoptosis-inducing factor 1, mitochondrial Mus musculus (Mouse) PR
Q9JM53 Aifm1 Apoptosis-inducing factor 1, mitochondrial Rattus norvegicus (Rat) PR
Q93WJ8 MDAR2 Monodehydroascorbate reductase 2 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SR59 MDAR3 Monodehydroascorbate reductase 3 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MGGCFSKPKP VELKIEVVLP EKERGKEELS ASGKGSPRGY QGNGTARHFH AEERLPTPQP
70 80 90 100 110 120
YPSPQDCVEA TVCHVKDLEN GQMREVELGW GKVLLVKDNG EFHALGHKCP HYGAPLVKGV
130 140 150 160 170 180
LSRGRVRCPW HGACFNISTG DLEDFPGLDS LHKFQVKIEK EKVTIRASKQ ALQLQRRTKV
190 200 210 220 230 240
MAKCISPSAG HSSSTNVLIV GAGAAGLVCA ETLRQEGFSD RIVLCTLDRH LPYDRAKLSK
250 260 270 280 290 300
SLDAQPEQLA LRPKEFFRAY GIEMLTEAQV VTVDVRNKKV VFKDGFKLEY SKLLLAPGSS
310 320 330 340 350 360
PKTLTCKGKD VENVFTIRTP EDANRVLRLA RGRNAVVVGA GFLGMEVAAY LTEKAHSVSV
370 380 390 400 410 420
VELEETPFRR FLGERVGRAL MKMFENNRVK FYMQTEVSEL RAQEGKLQEV VLKSSKVLRA
430 440 450 460 470 480
DVCVLGIGAV PATGFLRQSG IGLDSRGFIP VNKMMQTNVP GVFAAGDAVT FPLAWRNNRK
490 500 510 520 530 540
VNIPHWQMAH AQGRVAAQNM LAQEAEINTV PYLWTAMFGK SLRYAGYGEG FDDVIIQGDL
550 560 570 580 590 600
EELKFVAFYT KSDEVIAVAS MNYDPIVSKV AEVLASGRAI RKREVELFML HSKTGDMSWL
TGKGS