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 Q0VD24

Entry ID Method Resolution Chain Position Source
AF-Q0VD24-F1 Predicted AlphaFoldDB

27 variants for Q0VD24

Variant ID(s) Position Change Description Diseaes Association Provenance
rs453816009 2 A>E No EVA
rs471618573 7 V>G No EVA
rs437905711 11 L>S No EVA
rs469086474 13 G>A No EVA
rs449230925 20 G>V No EVA
rs435569342 21 L>I No EVA
rs466900695 21 L>P No EVA
rs446941713 22 E>Q No EVA
rs458385631 24 L>R No EVA
rs451112701 25 P>H No EVA
rs482550980 32 G>R No EVA
rs442316472 34 E>D No EVA
rs460060264 39 Q>H No EVA
rs473833237 39 Q>K No EVA
rs448098726 50 A>E No EVA
rs133874747 52 A>T No EVA
rs445841352 53 D>E No EVA
rs801039369 78 R>H No EVA
rs443516218 88 C>* No EVA
rs463668535 88 C>S No EVA
rs517089473 92 I>T No EVA
rs135249241 99 T>A No EVA
rs876269878 119 V>G No EVA
rs876162327 122 W>G No EVA
rs441332037 159 V>A No EVA
rs447508360 227 M>I No EVA
rs382744157 300 T>M No EVA

No associated diseases with Q0VD24

3 regional properties for Q0VD24

Type Name Position InterPro Accession
domain SET domain 126 - 256 IPR001214
domain Post-SET domain 270 - 286 IPR003616
domain Pre-SET domain 14 - 123 IPR007728

Functions

Description
EC Number 2.1.1.357 Methyltransferases
Subcellular Localization
  • Nucleus
  • Chromosome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
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.

5 GO annotations of molecular function

Name Definition
double-stranded DNA binding Binding to double-stranded DNA.
histone methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue.
histone methyltransferase activity (H3-K36 specific) Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 36) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 36). This reaction is the addition of a methyl group onto lysine at position 36 of the histone H3 protein.
histone methyltransferase activity (H3-K4 specific) Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 4) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 4). This reaction is the addition of a methyl group onto lysine at position 4 of the histone H3 protein.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
chromatin organization The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA.
histone H3-K36 methylation The modification of histone H3 by addition of one or more methyl groups to lysine at position 36 of the histone.
histone H3-K4 methylation The modification of histone H3 by addition of one or more methyl groups to lysine at position 4 of the histone.
histone methylation The modification of histones by addition of methyl groups.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9C5P0 SUVH8 Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH8 Arabidopsis thaliana (Mouse-ear cress) PR
Q9T0G7 SUVH9 Histone-lysine N-methyltransferase family member SUVH9 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MATCEEVPEA LKGQLDVARG LENLPVSAWP PGAEPEPFQY TPDHVAGPGA DADPSQITFP
70 80 90 100 110 120
GCACLKTPCL PGTCSCLRHE NNYDDRSCLR DIGSEAKCTE PVFECNVLCQ CSERCRNRVV
130 140 150 160 170 180
QWGLQFHLQV FKTDHKGWGL RTLDFIPKGR FVCEYAGEVL GISEVQRRVQ LQTIHDSNYI
190 200 210 220 230 240
IAIREHVYNG QVMETFVDPA SIGNIGRFLN HSCEPNLLMI PVRIDSMVPK LALFAARDIL
250 260 270 280 290 300
PEEELSYDYS GRFLNLMHSE DKERLDNGKL RKPCYCGARS CAAFLPYDSS LYCPTEKPDT
SEEGRA