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 Q12311

Entry ID Method Resolution Chain Position Source
AF-Q12311-F1 Predicted AlphaFoldDB

16 variants for Q12311

Variant ID(s) Position Change Description Diseaes Association Provenance
s16-631524 5 S>A No SGRP
s16-631628 39 E>D No SGRP
s16-631828 106 N>S No SGRP
s16-631839 110 V>I No SGRP
s16-631855 115 S>T No SGRP
s16-631941 144 A>T No SGRP
s16-631983 158 I>V No SGRP
s16-632142 211 I>V No SGRP
s16-632941 477 T>K No SGRP
s16-632954 481 F>L No SGRP
s16-633135 542 F>V No SGRP
s16-633254 581 K>N No SGRP
s16-633262 584 Q>R No SGRP
s16-633513 668 G>S No SGRP
s16-633642 711 I>V No SGRP
s16-633667 719 P>L No SGRP

No associated diseases with Q12311

3 regional properties for Q12311

Type Name Position InterPro Accession
domain B3 DNA binding domain 21 - 118 IPR003340-1
domain B3 DNA binding domain 140 - 236 IPR003340-2
domain B3 DNA binding domain 320 - 427 IPR003340-3

Functions

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

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
MOZ/MORF histone acetyltransferase complex A histone acetyltransferase complex that has histone H3 acetyltransferase and coactivator activities. Subunits of the human complex include MYST3/MOZ, MYST4/MORF, ING5, EAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.
NuA3 histone acetyltransferase complex A Gcn5-independent multisubunit complex that catalyzes the acetylation of histone H3. The budding yeast complex includes Sas3p, Taf30p, and Yng1p.
NuA3a histone acetyltransferase complex A NuA3 complex that catalyzes the acetylation of Histone H3. In S. cerevisiae, this complex consists of Eaf6p, Nto1p, Sas3p, Taf14p, Yng1p and associates with H3K4me3 using Yng1p.
NuA3b histone acetyltransferase complex A NuA3 complex that catalyzes the acetylation of Histone H3. In S. cerevisiae, this complex consists of Eaf6p, Nto1p, Sas3p, Taf14p, Pdp3 and associates with H3K4me3 via Pdp3p.
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.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
methylated histone binding Binding to a histone in which a residue has been modified by methylation.

3 GO annotations of biological process

Name Definition
DNA-templated transcription The synthesis of an RNA transcript from a DNA template.
histone acetylation The modification of a histone by the addition of an acetyl group.
regulation of transcription by RNA polymerase II Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O95696 BRD1 Bromodomain-containing protein 1 Homo sapiens (Human) PR
10 20 30 40 50 60
MNRGSLDDGP KLREEKHFQD FYPDLNADTL LPFIVPLVET KDNSTDTDSD DISNRNNREI
70 80 90 100 110 120
GSVKSVQTKE LIFKGRVTTE PLVLKKNEVE FQKCKITTNE LKGKKNPYCV RFNESFISRY
130 140 150 160 170 180
YHINKVRNRK SYKQQQKEFD GVEAPYFTKF SSKEAPNITI STSTKSAIQK FASISPNLVN
190 200 210 220 230 240
FKPQYDMDEQ DELYLHYLNK RYFKDQMSHE IFEILMTTLE TEWFHIEKHI PSTNSLIARH
250 260 270 280 290 300
NILRDCKNYE LYGSDDGTGL SMDQACAVCL GTDSDNLNTI VFCDGCDIAV HQECYGIIFI
310 320 330 340 350 360
PEGKWLCRRC MISKNNFATC LMCPSHTGAF KQTDTGSWVH NICALWLPEL YFSNLHYMEP
370 380 390 400 410 420
IEGVQNVSVS RWKLNCYICK KKMGACIQCF QRNCFTAYHV TCARRAGLYM SKGKCTIQEL
430 440 450 460 470 480
ASNQFSQKYS VESFCHKHAP RGWQTSIEGI NKARKYFSLL STLQTETPQH NEANDRTNSK
490 500 510 520 530 540
FNKTIWKTPN QTPVAPHVFA EILQKVVDFF GLANPPAGAF DICKYWSMKR ELTGGTPLTA
550 560 570 580 590 600
CFENNSLGSL TEEQVQTRID FANDQLEDLY RLKELTTLVK KRTQASNSLS RSRKKVFDIV
610 620 630 640 650 660
KSPQKYLLKI NVLDIFIKSE QFKALERLVT EPKLLVILEK CKHCDFDTVQ IFKEEIMHFF
670 680 690 700 710 720
EVLETLPGAS RILQTVSSKA KEQVTNLIGL IEHVDIKKLL SRDFIINDDK IEERPWSGPV
730 740
IMEEEGLSDA EELSAGEHRM LKLILNSG