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 P75824

Entry ID Method Resolution Chain Position Source
AF-P75824-F1 Predicted AlphaFoldDB

No variants for P75824

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P75824

No associated diseases with P75824

1 regional properties for P75824

Type Name Position InterPro Accession
domain Myc-type, basic helix-loop-helix (bHLH) domain 92 - 150 IPR011598

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTMPTNQCPW RMQVHHITQE TPDVWTISLI CHDYYPYRAG QYALVSVRNS AETLRAYTIS
70 80 90 100 110 120
STPGVSEYIT LTVRRIDDGV GSQWLTRDVK RGDYLWLSDA MGEFTCDDKA EDKFLLLAAG
130 140 150 160 170 180
CGVTPIMSMR RWLAKNRPQA DVRVIYNVRT PQDVIFADEW RNYPVTLVAE NNVTEGFIAG
190 200 210 220 230 240
RLTRELLAGV PDLASRTVMT CGPAPYMDWV EQEVKALGVT RFFKEKFFTP VAEAATSGLK
250 260 270 280 290 300
FTKLQPAREF YAPVGTTLLE ALESNNVPVV AACRAGVCGC CKTKVVSGEY TVSSTMTLTD
310 320
AEIAEGYVLA CSCHPQGDLV LA