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 Q5REG1

Entry ID Method Resolution Chain Position Source
AF-Q5REG1-F1 Predicted AlphaFoldDB

No variants for Q5REG1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5REG1

No associated diseases with Q5REG1

12 regional properties for Q5REG1

Type Name Position InterPro Accession
domain RNA recognition motif domain 722 - 800 IPR000504-1
domain RNA recognition motif domain 819 - 896 IPR000504-2
repeat HAT (Half-A-TPR) repeat 126 - 158 IPR003107-1
repeat HAT (Half-A-TPR) repeat 164 - 195 IPR003107-2
repeat HAT (Half-A-TPR) repeat 201 - 237 IPR003107-3
repeat HAT (Half-A-TPR) repeat 342 - 374 IPR003107-4
repeat HAT (Half-A-TPR) repeat 377 - 409 IPR003107-5
repeat HAT (Half-A-TPR) repeat 412 - 448 IPR003107-6
repeat HAT (Half-A-TPR) repeat 505 - 538 IPR003107-7
domain LSM-interacting domain 962 - 980 IPR008669
domain SART3, RNA recognition motif 1 723 - 796 IPR034217
domain SART3, RNA recognition motif 2 817 - 897 IPR034218

Functions

Description
EC Number
Subcellular Localization
  • Nucleus, nucleoplasm
  • Nucleus, Cajal body
  • Nucleus speckle
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
Cajal body A class of nuclear body, first seen after silver staining by Ramon y Cajal in 1903, enriched in small nuclear ribonucleoproteins, and certain general RNA polymerase II transcription factors; ultrastructurally, they appear as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter; involved in aspects of snRNP biogenesis; the protein coilin serves as a marker for Cajal bodies. Some argue that Cajal bodies are the sites for preassembly of transcriptosomes, unitary particles involved in transcription and processing of RNA.
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.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.

3 GO annotations of molecular function

Name Definition
histone binding Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription.
U6 snRNA binding Binding to a U6 small nuclear RNA (U6 snRNA).
U6atac snRNA binding Binding to a U6atac small nuclear RNA (U6atac snRNA).

5 GO annotations of biological process

Name Definition
mRNA splicing, via spliceosome The joining together of exons from one or more primary transcripts of messenger RNA (mRNA) and the excision of intron sequences, via a spliceosomal mechanism, so that mRNA consisting only of the joined exons is produced.
nucleosome assembly The aggregation, arrangement and bonding together of a nucleosome, the beadlike structural units of eukaryotic chromatin composed of histones and DNA.
positive regulation of histone deubiquitination Any process that activates or increases the frequency, rate or extent of histone deubiquitination.
spliceosomal snRNP assembly The aggregation, arrangement and bonding together of one or more snRNA and multiple protein components to form a ribonucleoprotein complex that is involved in formation of the spliceosome.
spliceosomal tri-snRNP complex assembly The formation of a tri-snRNP complex containing U4 and U6 (or U4atac and U6atac) snRNAs and U5 snRNAs and associated proteins. This includes reannealing of U4 and U6 (or U4atac and U6atac) snRNAs released from previous rounds of splicing to reform the U4/U6 snRNP (or U4atac/U6atac snRNP) as well as the subsequent association of the U5 snRNP with the U4/U6 snRNP (or U4atac/U6atac snRNP) to form a tri-snRNP that is ready to reassemble into another spliceosome complex.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MATAAATSAS EPEAESKAGP KADGEEDEVK AARTRRKVLS RAVAAATYKT MGPGWDQQEE
70 80 90 100 110 120
GVSESDGDEY AMASSAESSP GEYEWEYDEE EEKNQLEIER LEEQLSINVY DYNCHVDLIR
130 140 150 160 170 180
LLRLEGELTK VRMARQKMSE IFPLTEELWL EWLHDEISMA QDGLDREHVY DLFEKAVKDY
190 200 210 220 230 240
ICPNIWLEYG QYSVGGIGQK GGLEKVRSVF ERALSSVGLH MTKGLALWEA YREFESAIVE
250 260 270 280 290 300
AARPVAGFLS PFDREQTFDS QLEKVHSLFR RQLAIPLYDM EATFAEYEEW SEDPIPESVI
310 320 330 340 350 360
QNYNKALQQL EKYKPYEEAL LQAEAPRLAE YQAYIDFEMK IGDPARIQLI FERALVENCL
370 380 390 400 410 420
VPDLWIRYSQ YLDRQLKVKD LVLSVHNRAI RNCPWTVALW SRYLLAMERH GVDHQVISVT
430 440 450 460 470 480
FEKALNAGFI QATDYVEIWQ AYLDYLRRRV DFKQDSSKEL EELRAAFTRA LEYLKQEVEE
490 500 510 520 530 540
RFNESGDPSC VIMQNWARIE ARLCNNMQKA RELWDSIMTR GNAKYANMWL EYYNLERAHG
550 560 570 580 590 600
DTQHCRKALH RAVQCTSDYP EHVCEVLLTM ERTEGSLEDW DIAVQKTETR LARVNEQRMK
610 620 630 640 650 660
AAEKEAALVQ QEEEKAEQRK RARAEKKALK KKKKIRGPEK RGADEDDEKE WGDDEEEQPS
670 680 690 700 710 720
KRRRVENSIP AAGETQNVEV APGPAGKCAA VDVEPPSKQK EKAASLKRDM PKVLHDSSKD
730 740 750 760 770 780
SITVFVSNLP YSMQEPDAKL RPLFEACGEV VQIRPIFSNR GDFRGYRYVE FKEEKSALQA
790 800 810 820 830 840
LEMDRKSVEG RPMFVSPCVD KSKNPDFKVF RYSTSLEKHK LFISGLPFSC TKEELEEICK
850 860 870 880 890 900
AHGTVKDLRL VTNRAGKPKG LAYVEYENES QASQAVMKMD GMTIKENVIK VAISNPPQRK
910 920 930 940 950 960
VPEKPETRKA PGGPTLLPQT YGARGKGRTQ LSLLPRALQR PGAAAPQAEN GPAAAPAVAA
970 980
PAATEAPKMS NADFAKLFLR K