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 Q569Z5

Entry ID Method Resolution Chain Position Source
AF-Q569Z5-F1 Predicted AlphaFoldDB

37 variants for Q569Z5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389301846 18 S>C No EVA
rs222476673 41 R>W No EVA
rs3389284692 134 K>N No EVA
rs3413055857 148 A>V No EVA
rs3403978879 164 K>N No EVA
rs3389282612 194 Q>H No EVA
rs3389286716 221 E>K No EVA
rs3389286786 222 D>H No EVA
rs3389278263 241 K>R No EVA
rs3389286775 243 N>D No EVA
rs3389278203 247 V>M No EVA
rs3389293804 266 T>N No EVA
rs3389282571 281 K>T No EVA
rs3389284522 294 Y>* No EVA
rs3389301841 338 E>* No EVA
rs3389287682 338 E>V No EVA
rs3404188393 372 K>* No EVA
rs3389293743 396 T>K No EVA
rs3389301902 400 T>I No EVA
rs3389244325 414 G>S No EVA
rs3389284542 424 I>N No EVA
rs3404273203 575 L>R No EVA
rs3389268849 625 F>C No EVA
rs3389287869 640 M>L No EVA
rs3389301876 739 E>* No EVA
rs3389301909 752 L>R No EVA
rs3389296554 761 K>I No EVA
rs3403766097 764 G>A No EVA
rs3389296571 874 M>I No EVA
rs3389215108 884 G>C No EVA
rs3389215109 884 G>D No EVA
rs3389287727 912 V>M No EVA
rs3389268806 925 G>R No EVA
rs3389260534 965 A>T No EVA
rs3389268866 973 Y>N No EVA
rs3389215132 979 E>K No EVA
rs3389282579 989 L>M No EVA

No associated diseases with Q569Z5

3 regional properties for Q569Z5

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 11 - 18 IPR018181-1
conserved_site Heat shock protein 70, conserved site 202 - 215 IPR018181-2
conserved_site Heat shock protein 70, conserved site 339 - 353 IPR018181-3

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus speckle
  • Nucleus, Cajal body
  • Present in Cajal bodies (CBs) and nuclear speckles
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.
fibrillar center A structure found most metazoan nucleoli, but not usually found in lower eukaryotes; surrounded by the dense fibrillar component; the zone of transcription from multiple copies of the pre-rRNA genes is in the border region between these two structures.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

1 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.

16 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P21372 PRP5 Pre-mRNA-processing ATP-dependent RNA helicase PRP5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) EV
Q9VNP5 BoYb Putative ATP-dependent RNA helicase BoYb Drosophila melanogaster (Fruit fly) PR
Q9VL52 SoYb Putative ATP-dependent RNA helicase SoYb Drosophila melanogaster (Fruit fly) PR
Q7L014 DDX46 Probable ATP-dependent RNA helicase DDX46 Homo sapiens (Human) PR
Q6ZPL9 Ddx55 ATP-dependent RNA helicase DDX55 Mus musculus (Mouse) PR
P60843 Eif4a1 Eukaryotic initiation factor 4A-I Mus musculus (Mouse) PR
P10630 Eif4a2 Eukaryotic initiation factor 4A-II Mus musculus (Mouse) PR
Q4FZF3 Ddx49 Probable ATP-dependent RNA helicase DDX49 Mus musculus (Mouse) PR
Q8K363 Ddx18 ATP-dependent RNA helicase DDX18 Mus musculus (Mouse) PR
Q9CWX9 Ddx47 Probable ATP-dependent RNA helicase DDX47 Mus musculus (Mouse) PR
Q8K4L0 Ddx54 ATP-dependent RNA helicase DDX54 Mus musculus (Mouse) PR
Q9ESV0 Ddx24 ATP-dependent RNA helicase DDX24 Mus musculus (Mouse) PR
Q91VR5 Ddx1 ATP-dependent RNA helicase DDX1 Mus musculus (Mouse) PR
Q9CWT6 Ddx28 Probable ATP-dependent RNA helicase DDX28 Mus musculus (Mouse) PR
Q62780 Ddx46 Probable ATP-dependent RNA helicase DDX46 Rattus norvegicus (Rat) PR
Q8H0U8 RH42 DEAD-box ATP-dependent RNA helicase 42 Arabidopsis thaliana (Mouse-ear cress) SS
10 20 30 40 50 60
MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS
70 80 90 100 110 120
RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGSK TKKTENRSRS
130 140 150 160 170 180
KEKAEGGDSS KEKKKDKDDK EDEKEKDAGN FDQNKLEEEM RKRKERVEKW REEQRKKAME
190 200 210 220 230 240
NIGELKKEIE EMKQGKKWSL EDDDDDEDDP AEAEKEGTEM EDEELDPLDA YMEEVKEEVK
250 260 270 280 290 300
KFNMRSVKGG AGNEKKSGPT VTKVVTVVTT KKAVVDADKK KGELMENDQD AMEYSSEEEE
310 320 330 340 350 360
VDLQTALTGY QTKQRKLLEP VDHGKIEYEP FRKNFYVEVP ELAKMSQEEV NVFRLEMEGI
370 380 390 400 410 420
TVKGKGCPKP IKSWVQCGIS MKILNSLKKH GYEKPTPIQT QAIPAIMSGR DLIGIAKTGS
430 440 450 460 470 480
GKTIAFLLPM FRHIMDQRSL EEGEGPIAVI MTPTRELALQ ITKECKKFSK TLGLRVVCVY
490 500 510 520 530 540
GGTGISEQIA ELKRGAEIIV CTPGRMIDML AANSGRVTNL RRVTYVVLDE ADRMFDMGFE
550 560 570 580 590 600
PQVMRIVDNV RPDRQTVMFS ATFPRAMEAL ARRILSKPIE VQVGGRSVVC SDVEQQVIVI
610 620 630 640 650 660
EEEKKFLKLL ELLGHYQESG SVIIFVDKQE HADGLLKDLM RASYPCMSLH GGIDQYDRDS
670 680 690 700 710 720
IINDFKNGTC KLLVATSVAA RGLDVKHLIL VVNYSCPNHY EDYVHRAGRT GRAGNKGYAY
730 740 750 760 770 780
TFITEDQARY AGDIIKALEL SGTAVPPDLE KLWSDFKDQQ KAEGKIIKKS SGFSGKGFKF
790 800 810 820 830 840
DETEQALANE RKKLQKAALG LQDSDDEDAA VDIDEQIESM FNSKKRVKDM AAPGTSSVPA
850 860 870 880 890 900
PTAGNAEKLE IAKRLALRIN AQKNLGIESQ VDVMQQATNA ILRGGTILAP TVSAKTIAEQ
910 920 930 940 950 960
LAEKINAKLN YVPLEKQEEE RQEGGQSESF KRYEEELEIN DFPQTARWKV TSKEALQRIS
970 980 990 1000 1010 1020
EYSEAAITIR GTYFPPGKEP KEGERKIYLA IESANELAVQ KAKAEITRLI KEELIRLQNS
1030
YQPTNKGRYK VL