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 Q8K2I3

Entry ID Method Resolution Chain Position Source
AF-Q8K2I3-F1 Predicted AlphaFoldDB

26 variants for Q8K2I3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388506697 2 A>T No EVA
rs3410929130 43 F>I No EVA
rs3390856823 89 E>K No EVA
rs3390829106 94 F>L No EVA
rs3388506743 112 S>C No EVA
rs3388511558 135 E>D No EVA
rs3388509963 205 K>M No EVA
rs3388509827 210 V>M No EVA
rs226699669 251 V>I No EVA
rs235924735 259 Q>H No EVA
rs3388512478 314 E>V No EVA
rs3388508377 318 V>L No EVA
rs3413053070 322 V>L No EVA
rs3388511943 344 K>E No EVA
rs3388512093 346 E>D No EVA
rs3388512681 398 S>R No EVA
rs37258889 403 T>M No EVA
rs264514213 412 R>K No EVA
rs244094298 418 N>D No EVA
rs3388512474 423 S>G No EVA
rs3388510605 433 V>I No EVA
rs3388514406 461 V>L No EVA
rs3388508229 500 K>R No EVA
rs3388510347 515 L>M No EVA
rs3388508383 522 L>F No EVA
rs3388512017 529 F>L No EVA

No associated diseases with Q8K2I3

No regional properties for Q8K2I3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8K2I3

Functions

Description
EC Number
Subcellular Localization
  • Microsome membrane ; Single-pass membrane protein
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

4 GO annotations of molecular function

Name Definition
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.
monooxygenase activity Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water.
N,N-dimethylaniline monooxygenase activity Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

8 GO annotations of biological process

Name Definition
energy homeostasis Any process involved in the balance between food intake (energy input) and energy expenditure.
NADP metabolic process The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
NADPH oxidation A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADPH, to the oxidized form, NADP.
negative regulation of fatty acid oxidation Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid oxidation.
organic acid metabolic process The chemical reactions and pathways involving organic acids, any acidic compound containing carbon in covalent linkage.
oxygen metabolic process The chemical reactions and pathways involving diatomic oxygen (O2).
toxin metabolic process The chemical reactions and pathways involving a toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism.
xenobiotic metabolic process The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P49326 FMO5 Flavin-containing monooxygenase 5 Homo sapiens (Human) PR
P31512 FMO4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Homo sapiens (Human) PR
P97501 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 Mus musculus (Mouse) PR
P97872 Fmo5 Flavin-containing monooxygenase 5 Mus musculus (Mouse) PR
Q8VHG0 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Mus musculus (Mouse) PR
Q8K4B7 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Rattus norvegicus (Rat) PR
Q9EQ76 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 Rattus norvegicus (Rat) PR
Q8K4C0 Fmo5 Flavin-containing monooxygenase 5 Rattus norvegicus (Rat) PR
Q6IRI9 Fmo2 Dimethylaniline monooxygenase [N-oxide-forming] 2 Rattus norvegicus (Rat) PR
Q9SVU0 YUC8 Probable indole-3-pyruvate monooxygenase YUCCA8 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SXD9 At1g62580 Flavin-containing monooxygenase FMO GS-OX-like 7 Arabidopsis thaliana (Mouse-ear cress) PR
Q9C8T8 At1g63340 Putative flavin-containing monooxygenase FMO GS-OX-like 10 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAKKVVVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYRSVIT
70 80 90 100 110 120
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV ISVKKRPDFA
130 140 150 160 170 180
SSGQWEVYTQ SNGKEQRTVF DAVMVCSGHH IQPHLPLKSF PGIERFRGQY FHSREYKHPV
190 200 210 220 230 240
GFEGKRILVV GIGNSAADIA SELSKTAAQV FVSTRHGSWV MSRISEDGYP WDMVFHTRFS
250 260 270 280 290 300
SMLRNVLPRT VVKWMMEQQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK
310 320 330 340 350 360
TRVKELTETA VVFEDGTVEE DVDIIVFATG YTFSFSFLED SLVKVEDNRV SLYKAMFPPH
370 380 390 400 410 420
LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGLCSLP SETTMMADIV ERNEKRVNLF
430 440 450 460 470 480
GKSQSQILQT NYVDYLDELA LEIGAKPDFV SLFFKDPKLA VKLYFGPCNS YQYRLVGPGQ
490 500 510 520 530
WEGARNAILT QKQRILKPLK TRTLQSSDSA PVSFLLKILG LLAVVLAFFF QLQGF