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 Q69ZX6

Entry ID Method Resolution Chain Position Source
AF-Q69ZX6-F1 Predicted AlphaFoldDB

53 variants for Q69ZX6

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389125506 7 S>N No EVA
rs3389077389 31 G>D No EVA
rs3389138081 34 A>D No EVA
rs3389137870 90 R>K No EVA
rs3389140332 127 C>S No EVA
rs260009026 130 L>M No EVA
rs3389134059 131 S>Y No EVA
rs3389149659 134 F>I No EVA
rs3389125496 136 E>D No EVA
rs3389111223 167 I>F No EVA
rs3389077343 170 E>G No EVA
rs3389149733 185 M>V No EVA
rs3389148871 231 E>A No EVA
rs3389111301 235 P>T No EVA
rs3389140282 247 L>H No EVA
rs3389132035 266 R>G No EVA
rs3389132073 286 T>S No EVA
rs3389077405 332 L>M No EVA
rs3389136604 345 E>D No EVA
rs3389132013 400 Q>R No EVA
rs3389136847 457 A>G No EVA
rs3389140472 461 I>F No EVA
rs3401154557 481 S>C No EVA
rs3389136808 497 I>T No EVA
rs3389132005 509 P>L No EVA
rs3389132070 511 Q>H No EVA
rs3389114035 521 D>E No EVA
rs3401893164 521 D>N No EVA
rs3389077357 525 C>S No EVA
rs3401851740 541 Q>E No EVA
rs3401792505 550 L>F No EVA
rs3401774660 551 K>* No EVA
rs3401790381 553 D>A No EVA
rs3401893159 553 D>Y No EVA
rs3389136588 561 Q>* No EVA
rs3389140465 565 T>R No EVA
rs3389136865 577 A>T No EVA
rs258989344 637 S>T No EVA
rs3389150330 653 T>I No EVA
rs3389140463 654 T>I No EVA
rs3389114019 786 L>F No EVA
rs3389136835 791 K>E No EVA
rs3389144517 798 E>Q No EVA
rs3389131991 806 Y>F No EVA
rs3389114113 812 A>V No EVA
rs3389125442 836 R>K No EVA
rs3389140331 855 P>S No EVA
rs3401893187 901 P>L No EVA
rs3389140316 913 L>F No EVA
rs3389114044 922 P>H No EVA
rs3389111263 934 V>A No EVA
rs3389132012 1013 N>K No EVA
rs3389144463 1030 D>G No EVA

No associated diseases with Q69ZX6

2 regional properties for Q69ZX6

Type Name Position InterPro Accession
domain Zinc finger, CW-type 490 - 544 IPR011124
domain Morc, S5 domain 2-like 329 - 451 IPR041006

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Cytoplasm, cytosol
  • Chromosome
  • Nucleus matrix
  • Mainly located in the nucleus
  • Upon phosphorylation at Ser-737, recruited to damaged chromatin
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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
heterochromatin A compact and highly condensed form of chromatin that is refractory to transcription.
nuclear matrix The dense fibrillar network lying on the inner side of the nuclear membrane.
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.

8 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.
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.
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.
identical protein binding Binding to an identical protein or proteins.
magnesium ion binding Binding to a magnesium (Mg) ion.
protein homodimerization activity Binding to an identical protein to form a homodimer.
zinc ion binding Binding to a zinc ion (Zn).

5 GO annotations of biological process

Name Definition
cellular response to DNA damage stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
chromatin remodeling A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication.
negative regulation of gene expression, epigenetic An epigenetic process that silences gene expression at specific genomic regions through chromatin remodelling either by modifying higher order chromatin fiber structure, nucleosomal histones, or the DNA.
negative regulation of single stranded viral RNA replication via double stranded DNA intermediate Any process that stops, prevents, or reduces the frequency, rate or extent of single stranded viral RNA replication via double stranded DNA intermediate.
positive regulation of DNA methylation-dependent heterochromatin assembly Any process that increases the rate, frequency, or extent of DNA methylation-dependent heterochromatin formation.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14149 MORC3 MORC family CW-type zinc finger protein 3 Homo sapiens (Human) EV
Q8TE76 MORC4 MORC family CW-type zinc finger protein 4 Homo sapiens (Human) SS
Q9Y6X9 MORC2 ATPase MORC2 Homo sapiens (Human) PR
F7BJB9 Morc3 MORC family CW-type zinc finger protein 3 Mus musculus (Mouse) SS
Q8BMD7 Morc4 MORC family CW-type zinc finger protein 4 Mus musculus (Mouse) SS
Q8C5W4 Morc2b ATPase MORC2B Mus musculus (Mouse) PR
10 20 30 40 50 60
MAFTNYSSLN RAQLTFEYLH TNSTTHEFLF GALAELVDNA RDADATRIDI YAERREDLRG
70 80 90 100 110 120
GFMLCFLDDG AGMDPSDAAS VIQFGKSAKR TPESTQIGQY GNGLKSGSMR IGKDFILFTK
130 140 150 160 170 180
KEDTMTCLFL SRTFHEEEGI DEVIVPLPTW NARTREPITD NVEKFAIETE LVYKYSPFHT
190 200 210 220 230 240
EEQVMNQFMK IPGNSGTLVI IFNLKLMDNG EPELDIISNP KDIQMAETSP EGTKPERRSF
250 260 270 280 290 300
RAYAAVLYID PRMRIFIHGH KVQTKRLSCC LYKPRMYKYT SSRFKTRAEQ EVKKAEHVAR
310 320 330 340 350 360
IAEEKAREAE SKARTLEVRM GGDLTRDSRV MLRQVQNTAI TLRREADVKK RIKDAKQRAL
370 380 390 400 410 420
KEPKELNFVF GVNIEHRDLD GMFIYNCSRL IKMYEKVGPQ LEGGMACGGV VGVVDVPYLV
430 440 450 460 470 480
LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY WKDIAIAQRG IIKFWDEFGY LSANWNQPPS
490 500 510 520 530 540
SELRFKRRRA MEIPTTIQCD LCLKWRTLPF QLSSVETDYP DTWVCSMNPD PEQDRCEASE
550 560 570 580 590 600
QKQKVPLGTL KKDPKTQEEK QKQLTEKIRQ QQEKLEALQK TTPIRSQADL KKLPLEVTTR
610 620 630 640 650 660
PIEEPVRRPQ RPRSPPLPAV IKNAPSRPPS IQTPRPSTQL RKTSVISLPK PPTTAARGET
670 680 690 700 710 720
STSRLLQPTE APRKPANPPI KTVPRPTPPV HTPPLSLIPS SKSLREVPAQ KAIKTPVVKK
730 740 750 760 770 780
PEPPVKQSVA TSGRKRSLAV SDEEEAEEEA EKRRERCKRG KLAVKEEKKE ANELSDSAGE
790 800 810 820 830 840
DHPAELRKAQ KDKGLHVEVR VNREWYTGRV TAVEVGKNAV RWKVKFDYVP TDTTPRDRWV
850 860 870 880 890 900
EKGSEDVRLM KPPSPEHQSP DTQQEGGEEE EAMVARQAVA LPEPSTSDGL PIEPDTTATS
910 920 930 940 950 960
PSHETIDLLV QILRNCLRYF LPPSFPISKK ELSVMNSEEL ISFPLKEYFK QYEVGLQNLC
970 980 990 1000 1010 1020
HSYQSRADSR AKASEESLRT SEKKLRETEE KLQKLRTNIV ALLQKVQEDI DINTDDELDA
YIEDLITKGD