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 Q66JG8

Entry ID Method Resolution Chain Position Source
AF-Q66JG8-F1 Predicted AlphaFoldDB

No variants for Q66JG8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q66JG8

No associated diseases with Q66JG8

2 regional properties for Q66JG8

Type Name Position InterPro Accession
domain Zinc finger, RING-type 375 - 413 IPR001841
conserved_site Zinc finger, RING-type, conserved site 390 - 399 IPR017907

Functions

Description
EC Number 1.14.11.53 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Subcellular Localization
  • Nucleus speckle
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
nuclear speck A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
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.

4 GO annotations of molecular function

Name Definition
2-oxoglutarate-dependent dioxygenase activity Catalysis of the reaction: A + 2-oxoglutarate + O2 = B + succinate + CO2. This is an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from 2-oxoglutarate and one other donor, and one atom of oxygen is incorporated into each donor.
metal ion binding Binding to a metal ion.
mRNA N6-methyladenosine dioxygenase activity Catalysis of the oxidative demethylation of N6-methyladenosine RNA, with concomitant decarboxylation of 2-oxoglutarate and releases oxidized methyl group on N6-methyladenosine as formaldehyde.
oxidative RNA demethylase activity Catalysis of the removal of a methyl group from one or more nucleosides within a RNA molecule involving the oxidation (i.e. electron loss) of one or more atoms.

5 GO annotations of biological process

Name Definition
mRNA export from nucleus The directed movement of mRNA from the nucleus to the cytoplasm.
mRNA processing Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
oxidative single-stranded RNA demethylation Removal of the methyl group from one or more nucleotides within a single-stranded RNA molecule involving the oxidation (i.e. electron loss) of one or more atoms.
response to hypoxia Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
spermatogenesis The developmental process by which male germ line stem cells self renew or give rise to successive cell types resulting in the development of a spermatozoa.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
E1BH29 ALKBH5 RNA demethylase ALKBH5 Bos taurus (Bovine) PR
Q6P6C2 ALKBH5 RNA demethylase ALKBH5 Homo sapiens (Human) PR
Q3TSG4 Alkbh5 RNA demethylase ALKBH5 Mus musculus (Mouse) PR
10 20 30 40 50 60
MSATYTDLRE KLQSLYRDSP KEVRKRKQPT SDTEEEEAAS EPEEEEEARK VRSGIRQVRL
70 80 90 100 110 120
FSPDECARIE AKIDEVVSRA EKGLYREHTV DRAPLRNKYF FGEGYTYGAQ LQRRGPGQER
130 140 150 160 170 180
LYPKGEVDEI PAWVNELVIR RLVEHRVIPE GFVNSAVIND YQPGGCIVSH VDPIHIFERP
190 200 210 220 230 240
IVSVSFFSDS ALCFGCKFQF KPIRVSEPVF FLPVQRGSVT VLSGYAADEI THCIRPQDIK
250 260 270 280 290 300
ERRAVVILRK TRTEAPRLEM KSLSSSYQPE RLQGSNRQHI LKPKRSHRKA DPDAAHRPRI
310 320 330 340 350
LEMDKEENRR SVLLPKQRRR SHFSSENYWR RSHDYVDTYT ETGEDDGSPV RKVKMRRH