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 Q9WTK2

Entry ID Method Resolution Chain Position Source
AF-Q9WTK2-F1 Predicted AlphaFoldDB

30 variants for Q9WTK2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389278730 16 C>S No EVA
rs222023544 26 T>N No EVA
rs3404149135 31 C>W No EVA
rs232989039 47 A>V No EVA
rs3389269212 49 P>S No EVA
rs3389236652 90 P>L No EVA
rs3389275134 95 V>E No EVA
rs3389280031 102 H>Q No EVA
rs236790074 148 L>P No EVA
rs260584802 150 V>I No EVA
rs864296075 187 S>P No EVA
rs3389273137 191 I>T No EVA
rs3404363742 244 A>P No EVA
rs3389252345 291 N>H No EVA
rs3389278273 305 A>V No EVA
rs3389269254 310 F>I No EVA
rs3389285106 326 S>N No EVA
rs3389207844 335 R>I No EVA
rs3389269256 423 R>* No EVA
rs3389262791 428 T>I No EVA
rs3389252362 438 V>E No EVA
rs3404166856 443 P>R No EVA
rs3404060421 443 P>S No EVA
rs3389273150 445 I>V No EVA
rs3404060420 449 A>T No EVA
rs3389285134 453 P>H No EVA
rs1132017997 573 W>* No EVA
rs1134306915 576 A>T No EVA
rs3389252365 590 I>M No EVA
rs3404112235 594 F>W No EVA

No associated diseases with Q9WTK2

3 regional properties for Q9WTK2

Type Name Position InterPro Accession
domain Chromo/chromo shadow domain 55 - 116 IPR000953
conserved_site Chromo domain, conserved site 74 - 94 IPR023779
domain Chromo domain 57 - 107 IPR023780

Functions

Description
EC Number 2.3.1.48 Transferring groups other than amino-acyl groups
Subcellular Localization
  • [Isoform 2]: Nucleus
  • Chromosome
  • Recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) on chromatin (PubMed:24144980)
  • Multimerization is required for chromatin-binding (By similarity)
  • Recruited to Xist RNA-coated X chromosome (PubMed:24144980)
  • Recruited to sites of DNA double strand breaks in a PARP1-dependent fashion (PubMed:29177481)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 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.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.

7 GO annotations of molecular function

Name Definition
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
crotonyl-CoA hydratase activity Catalysis of the reaction: Acetyl-CoA + -N(6)-acetyl-L-lysine.
histone acetyltransferase activity Catalysis of the reaction: acetyl-CoA + histone = CoA + acetyl-histone.
identical protein binding Binding to an identical protein or proteins.
methylated histone binding Binding to a histone in which a residue has been modified by methylation.
protein-macromolecule adaptor activity The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid.
transcription corepressor activity A transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators.

3 GO annotations of biological process

Name Definition
negative regulation of peptidyl-lysine crotonylation Any process that stops or reduces the rate of crotonylation of a lysine residue in a protein.
random inactivation of X chromosome Compensating for the two-fold variation in X-chromosome:autosome ratios between sexes by a global inactivation of all, or most of, the genes on either the paternal or maternal X-chromosome in the XX sex.
spermatid development The process whose specific outcome is the progression of a spermatid over time, from its formation to the mature structure.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q99549 MPHOSPH8 M-phase phosphoprotein 8 Homo sapiens (Human) PR
P83916 CBX1 Chromobox protein homolog 1 Homo sapiens (Human) PR
Q8N8U2 CDYL2 Chromodomain Y-like protein 2 Homo sapiens (Human) PR
Q9Y232 CDYL Chromodomain Y-like protein Homo sapiens (Human) PR
P83917 Cbx1 Chromobox protein homolog 1 Mus musculus (Mouse) PR
Q9D5D8 Cdyl2 Chromodomain Y-like protein 2 Mus musculus (Mouse) PR
Q6AYK9 Cdyl Chromodomain Y-like protein Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MGIGNSQPNS QEAQLCTLPE KAEQPTDDNT CQQNNVVPAT VSEPDQASPA IQDAETQVES
70 80 90 100 110 120
IVDKRKNKKG KTEYLVRWKG YDSEDDTWEP EQHLVNCEEY IHDFNRRHNE RQKEGSLARA
130 140 150 160 170 180
SRASPSNARK QISRSTHSTL SKTNSKALVV GKDHESKSSQ LLAASQKFRK NPAPSLANRK
190 200 210 220 230 240
NMDLAKSGIK ILVPKSPVKG RTSVDGFQGE SPEKLDPVDQ GAEDTVAPEV TAEKPTGALL
250 260 270 280 290 300
GPGAERARMG SRPRIHPLVP QVSGPVTAAM ATGLAVNGKG TSPFMDALAA NGTVTIQTSV
310 320 330 340 350 360
TGVTAGKRKF IDDRRDQPFD KRLRFSVRQT ESAYRYRDIV VRKQDGFTHI LLSTKSSENN
370 380 390 400 410 420
SLNPEVMKEV QSALSTAAAD DSKLVLLSAV GSVFCCGLDF IYFIRRLTDD RKRESTKMAD
430 440 450 460 470 480
AIRNFVNTFI QFKKPIIVAV NGPAIGLGAS ILPLCDVVWA NEKAWFQTPY TTFGQSPDGC
490 500 510 520 530 540
STVMFPKIMG GASANEMLFS GRKLTAQEAC GKGLVSQVFW PGTFTQEVMV RIKELASCNP
550 560 570 580 590
VVLEESKALV RCNMKMELEQ ANERECEVLK KIWGSAQGMD SMLKYLQRKI DEF