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 Q5EA24

Entry ID Method Resolution Chain Position Source
AF-Q5EA24-F1 Predicted AlphaFoldDB

No variants for Q5EA24

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5EA24

No associated diseases with Q5EA24

2 regional properties for Q5EA24

Type Name Position InterPro Accession
domain JmjC domain 136 - 271 IPR003347
domain ROXA-like, winged helix 331 - 425 IPR046799

Functions

Description
EC Number 1.14.11.79 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Subcellular Localization
  • Nucleus
  • Nucleus, nucleolus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.

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.
histone H3-methyl-lysine-36 demethylase activity Catalysis of the removal of a methyl group from a modified lysine residue at position 36 of the histone H3 protein. This is a dioxygenase reaction that is dependent on Fe(II) and 2-oxoglutarate.
histone H3-methyl-lysine-4 demethylase activity Catalysis of the removal of a methyl group from a modified lysine residue at position 4 of the histone H3 protein.
metal ion binding Binding to a metal ion.

3 GO annotations of biological process

Name Definition
histone H3-K36 demethylation The modification of histone H3 by the removal of a methyl group from lysine at position 36 of the histone.
histone H3-K4 demethylation The modification of histone H3 by the removal of a methyl group from lysine at position 4 of the histone.
ribosome biogenesis A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits; includes transport to the sites of protein synthesis.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q7K4H4 NO66 Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 Drosophila melanogaster (Fruit fly) PR
10 20 30 40 50 60
MPKKARPAGD GKEQGPAPKQ VKVEAACGPS SPLNFDSPSG LFESFISPIK TETFFKEFWE
70 80 90 100 110 120
QKPLLIQRDD PALATYYQSL FRLSDLKSLC SWGIYYGRDV NVCRCVHGKK KVLNKDGRVH
130 140 150 160 170 180
FLQLRQDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGAQGLPPHY
190 200 210 220 230 240
DDVEVFILQL EGEKHWRLYQ PTVPLAREYS VEAEDRIGRP THEFTLKPGD LLYFPRGTIH
250 260 270 280 290 300
QADTPEGLAH STHVTISTYQ SSSWGDFLLD TISGLVFDTA KADVALRAGI PRQLLLQAES
310 320 330 340 350 360
IAVATRLSGF LRMLADRLEG TKELPSADMK KDFAMNRLPP YYMGDRAKLV APGGQLPGLD
370 380 390 400 410 420
STVRLQFRDH VVLTVGPYQD PSDETRGEMV YVYHSLRNRR DTHMMGNETE SYGLRFPLSY
430 440 450 460
MDALKQIWNS SAISVKDLKL TTDEEKQNLV LSLWTECLIQ VV