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 O16102

Entry ID Method Resolution Chain Position Source
AF-O16102-F1 Predicted AlphaFoldDB

No variants for O16102

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O16102

No associated diseases with O16102

12 regional properties for O16102

Type Name Position InterPro Accession
domain SNF2, N-terminal 288 - 560 IPR000330
domain Chromo/chromo shadow domain 82 - 156 IPR000953-1
domain Chromo/chromo shadow domain 177 - 240 IPR000953-2
domain Helicase, C-terminal 587 - 739 IPR001650
domain Zinc finger, PHD-type 37 - 80 IPR001965
conserved_site DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site 404 - 413 IPR002464
domain Domain of unknown function DUF1087 819 - 875 IPR009463
domain Helicase superfamily 1/2, ATP-binding domain 263 - 466 IPR014001
conserved_site Zinc finger, PHD-type, conserved site 38 - 79 IPR019786
domain Zinc finger, PHD-finger 35 - 82 IPR019787
domain Chromo domain 102 - 147 IPR023780-1
domain Chromo domain 181 - 230 IPR023780-2

Functions

Description
EC Number 3.6.4.12 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus
  • Chromosome
  • During embryogenesis, detected in nuclei before and after their migration to the membrane of the preblastoderm embryo (PubMed:18250149)
  • Remains associated with condensed chromosomes in mitotic nuclei
  • Not detected in nuclei postgastrulation (PubMed:18250149)
  • In polytene chromosomes of third instar larvae, weakly expressed at the chromocenter and fourth chromosome localizing mainly to the interbands (PubMed:18250149)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
euchromatin A dispersed and relatively uncompacted form of chromatin that is in a transcription-competent conformation.
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.
ATP-dependent chromatin remodeler activity An activity, driven by ATP hydrolysis, that modulates the contacts between histones and DNA, resulting in a change in chromosome architecture within the nucleosomal array, leading to chromatin remodeling.
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.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA helicase activity Unwinding of a DNA helix, driven by ATP hydrolysis.
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.
metal ion binding Binding to a metal ion.

4 GO annotations of biological process

Name Definition
chromatin organization The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA.
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 transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
nucleosome organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of one or more nucleosomes.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8TDI0 CHD5 Chromodomain-helicase-DNA-binding protein 5 Homo sapiens (Human) PR
Q12873 CHD3 Chromodomain-helicase-DNA-binding protein 3 Homo sapiens (Human) PR
Q14839 CHD4 Chromodomain-helicase-DNA-binding protein 4 Homo sapiens (Human) PR
A2A8L1 Chd5 Chromodomain-helicase-DNA-binding protein 5 Mus musculus (Mouse) PR
Q6PDQ2 Chd4 Chromodomain-helicase-DNA-binding protein 4 Mus musculus (Mouse) PR
D3ZD32 Chd5 Chromodomain-helicase-DNA-binding protein 5 Rattus norvegicus (Rat) PR
Q22516 chd-3 Chromodomain-helicase-DNA-binding protein 3 homolog Caenorhabditis elegans PR
10 20 30 40 50 60
MSSKRGADPD WKTPGKASKD KRPKTNAKKQ KFRDEEYCKV CSDGGDLLCC DSCPSVYHRT
70 80 90 100 110 120
CLSPPLKSIP KGDWICPRCI PLPGKAEKIL SWRWALDRSV ELRTSKGEKR REYFIKWHGM
130 140 150 160 170 180
SYWHCEWIPE GQMLLHHASM VASFQRRSDM EEPSLEELDD QDGNLHERFY RYGIKPEWLL
190 200 210 220 230 240
VQRVINHSEE PNGGTMYLVK WRELSYNDSS WERESDSIPG LNQAIALYKK LRSSNKGRQR
250 260 270 280 290 300
DRPAPTIDLN KKYEDQPVFL KEAGLKLHPF QIEGVSWLRY SWGQGIPTIL ADEMGLGKTI
310 320 330 340 350 360
QTVVFLYSLF KEGHCRGPFL ISVPLSTLTN WERELELWAP ELYCVTYVGG KTARAVIRKH
370 380 390 400 410 420
EISFEEVTTK TMRENQTQYK FNVMLTSYEF ISVDAAFLGC IDWAALVVDE AHRLRSNQSK
430 440 450 460 470 480
FFRILSKYRI GYKLLLTGTP LQNNLEELFH LLNFLSSGKF NDLQTFQAEF TDVSKEEQVK
490 500 510 520 530 540
RLHEILEPHM LRRLKADVLK SMPPKSEFIV RVELSSMQKK FYKHILTKNF KALNQKGGGR
550 560 570 580 590 600
VCSLLNIMMD LRKCCNHPYL FPSAAEEATI SPSGLYEMSS LTKASGKLDL LSKMLKQLKA
610 620 630 640 650 660
DNHRVLLFSQ MTKMLNVLEH FLEGEGYQYD RIDGSIKGDL RQKAIDRFND PVSEHFVFLL
670 680 690 700 710 720
STRAGGLGIN LATADTVIIF DSDWNPHNDV QAFSRAHRMG QKKKVMIYRF VTHNSVEERI
730 740 750 760 770 780
MQVAKHKMML THLVVRPGMG GMTTNFSKDE LEDILRFGTE DLFKDGKSEA IHYDDKAVAD
790 800 810 820 830 840
LLDRTNRGIE EKESWANEYL SSFKVASYAT KEDHEEHDDY NNDAENTDPF YWENLMGKSQ
850 860 870 880 890
PKLPKKQKKQ SQQSQVDVES IMGKGKRIRK EIDYSNQYPS PNRATPSSIV LM