A2A8L1
PR
Gene name |
Chd5 (Kiaa0444) |
Protein name |
Chromodomain-helicase-DNA-binding protein 5 |
Names |
CHD-5, ATP-dependent helicase CHD5 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
|
EC number |
3.6.4.12: Acting on ATP; involved in cellular and subcellular movement |
Protein Class |
|
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 A2A8L1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2A8L1-F1 | Predicted | AlphaFoldDB |
72 variants for A2A8L1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs221822193 | 77 | D>E | No | EVA | |
| rs3388729633 | 172 | R>S | No | EVA | |
| rs3388743276 | 211 | A>T | No | EVA | |
| rs32857544 | 262 | A>V | No | EVA | |
| rs3388743265 | 306 | A>V | No | EVA | |
| rs3388732535 | 335 | D>Y | No | EVA | |
| rs3388727084 | 362 | T>I | No | EVA | |
| rs3388721027 | 371 | C>R | No | EVA | |
| rs3410922472 | 379 | A>V | No | EVA | |
| rs3394821613 | 392 | E>A | No | EVA | |
| rs3388711940 | 525 | C>S | No | EVA | |
| rs3388724674 | 560 | S>A | No | EVA | |
| rs3388740148 | 568 | E>G | No | EVA | |
| rs3388732634 | 575 | P>A | No | EVA | |
| rs3388729710 | 626 | W>R | No | EVA | |
| rs3388721052 | 638 | N>K | No | EVA | |
| rs3388740073 | 642 | A>D | No | EVA | |
| rs3388737194 | 687 | K>E | No | EVA | |
| rs3395113805 | 791 | V>E | No | EVA | |
| rs3395113800 | 791 | V>L | No | EVA | |
| rs3388730080 | 834 | D>N | No | EVA | |
| rs3388720966 | 850 | E>D | No | EVA | |
| rs3388740154 | 942 | M>K | No | EVA | |
| rs3388730068 | 976 | K>T | No | EVA | |
| rs3388743254 | 990 | D>G | No | EVA | |
| rs3388727078 | 1009 | P>S | No | EVA | |
| rs3388737221 | 1036 | K>M | No | EVA | |
| rs3388743281 | 1079 | G>S | No | EVA | |
| rs3388737220 | 1090 | A>V | No | EVA | |
| rs3388724684 | 1109 | I>T | No | EVA | |
| rs3388729650 | 1121 | D>E | No | EVA | |
| rs3388737049 | 1162 | Q>R | No | EVA | |
| rs3388736723 | 1163 | V>M | No | EVA | |
| rs3388721046 | 1228 | K>N | No | EVA | |
| rs3388724705 | 1238 | K>E | No | EVA | |
| rs3388721006 | 1242 | S>C | No | EVA | |
| rs3388730021 | 1282 | N>T | No | EVA | |
| rs3388736437 | 1294 | Q>* | No | EVA | |
| rs3388721043 | 1298 | R>L | No | EVA | |
| rs3388736409 | 1369 | D>H | No | EVA | |
| rs3388732559 | 1416 | R>W | No | EVA | |
| rs3388735047 | 1480 | P>S | No | EVA | |
| rs580342603 | 1533 | P>L | No | EVA | |
| rs251345389 | 1536 | A>P | No | EVA | |
| rs251345389 | 1536 | A>T | No | EVA | |
| rs3388737189 | 1554 | P>S | No | EVA | |
| rs233964946 | 1568 | T>P | No | EVA | |
| rs247143094 | 1575 | L>Q | No | EVA | |
| rs3388740072 | 1578 | T>R | No | EVA | |
| rs3388724730 | 1579 | D>N | No | EVA | |
| rs32857443 | 1588 | P>A | No | EVA | |
| rs3394559261 | 1591 | S>Y | No | EVA | |
| rs3395179347 | 1594 | I>F | No | EVA | |
| rs235035250 | 1594 | I>M | No | EVA | |
| rs3388724642 | 1627 | V>A | No | EVA | |
| rs260824017 | 1653 | P>L | No | EVA | |
| rs223220111 | 1658 | G>S | No | EVA | |
| rs3388729656 | 1664 | R>K | No | EVA | |
| rs3388724716 | 1677 | E>D | No | EVA | |
| rs3388736501 | 1691 | K>* | No | EVA | |
| rs3388729700 | 1705 | I>N | No | EVA | |
| rs3388712000 | 1725 | V>M | No | EVA | |
| rs3388730090 | 1728 | G>V | No | EVA | |
| rs3388730056 | 1737 | R>H | No | EVA | |
| rs3388724724 | 1767 | N>D | No | EVA | |
| rs3388740162 | 1821 | M>V | No | EVA | |
| rs3388720975 | 1824 | N>S | No | EVA | |
| rs32856840 | 1917 | R>P | No | EVA | |
| rs3394822031 | 1931 | P>A | No | EVA | |
| rs3394559239 | 1932 | S>N | No | EVA | |
| rs3394835994 | 1933 | H>Q | No | EVA | |
| rs3413068874 | 1941 | E>D | No | EVA |
No associated diseases with A2A8L1
6 regional properties for A2A8L1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Kinesin light chain repeat | 362 - 403 | IPR015792 |
| repeat | Tetratricopeptide repeat | 253 - 286 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 295 - 328 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 337 - 370 | IPR019734-3 |
| repeat | Tetratricopeptide repeat | 379 - 412 | IPR019734-4 |
| repeat | Tetratricopeptide repeat | 464 - 497 | IPR019734-5 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.4.12 | Acting on ATP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromatin | The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. |
| 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 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. |
| NuRD complex | An approximately 2 MDa multi-subunit complex that exhibits ATP-dependent chromatin remodeling activity in addition to histone deacetylase (HDAC) activity, and has been shown to establish transcriptional repression of a number of target genes in vertebrates, invertebrates and fungi. Amongst its subunits, the NuRD complex contains histone deacetylases, histone binding proteins and Mi-2-like proteins. |
10 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. |
| H3K27me3 modified histone binding | Binding to a histone H3 in which the lysine residue at position 27 has been modified by trimethylation. |
| 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. |
| histone deacetylase binding | Binding to histone deacetylase. |
| metal ion binding | Binding to a metal ion. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| cerebral cortex neuron differentiation | The process in which a relatively unspecialized cell acquires specialized features of a neuron residing in the cerebral cortex. |
| 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. |
| histone H3-K27 trimethylation | The modification of histone H3 by addition of three methyl groups to lysine at position 27 of the histone. |
| histone H4 acetylation | The modification of histone H4 by the addition of an acetyl group. |
| negative regulation of cell population proliferation | Any process that stops, prevents or reduces the rate or extent of cell proliferation. |
| 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. |
| positive regulation of signal transduction by p53 class mediator | Any process that activates or increases the frequency, rate or extent of signal transduction by p53 class mediator. |
| regulation of cell differentiation | Any process that modulates the frequency, rate or extent of cell differentiation, the process in which relatively unspecialized cells acquire specialized structural and functional features. |
| regulation of transcription by RNA polymerase II | Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| transcription by RNA polymerase II | The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs). |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O16102 | Chd3 | Chromodomain-helicase-DNA-binding protein 3 | Drosophila melanogaster (Fruit fly) | PR |
| Q14839 | CHD4 | Chromodomain-helicase-DNA-binding protein 4 | Homo sapiens (Human) | PR |
| Q12873 | CHD3 | Chromodomain-helicase-DNA-binding protein 3 | Homo sapiens (Human) | PR |
| Q8TDI0 | CHD5 | Chromodomain-helicase-DNA-binding protein 5 | Homo sapiens (Human) | PR |
| Q6PDQ2 | Chd4 | Chromodomain-helicase-DNA-binding protein 4 | Mus musculus (Mouse) | PR |
| P40201 | Chd1 | Chromodomain-helicase-DNA-binding protein 1 | 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 |
| MRGPLGTEEE | LPRLFAEEME | NEEEMSEEED | GGLEGFEDFF | PAEPVSLPKK | KPKKLKESKS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SKGKRKKKEG | SNDEMSDNEE | DLEEKSESEG | SDYSPTKKKK | KKLKEKKEKK | EKKEKRKKRG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EDEDDNDDGG | LKEPKSSGQL | MAEWGLDDVD | YLFSEDDYHT | LTNYKAFSQF | LRPLIAKKNP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KIPMSKMMTV | LGAKWREFSA | NNPFKGSSAA | AAAAAVAAAV | ETVTIAPPLA | ISPQQVPQTL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PIRKAKTKEG | KGPGVRKKNK | GAKDSKKKGR | GKRVAGLKFR | FGGISKRKKG | SSSEEDERED |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SDLDNASIHS | SSVRSECSAA | LGKKNKRRRK | KKRIDDGDGY | ETDHQDYCEV | CQQGGEIILC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DTCPRAYHLV | CLDPELEKAP | EGKWSCPHCE | KEGIQWEPKD | DDEEEEEGGC | EEEEDDHMEF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CRVCKDGGEL | LCCDACPSSY | HLHCLNPPLP | EIPNGEWLCP | RCTCPPLKGK | VQRILHWRWT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EPPAPFVVGL | PGPEVEPGMP | PPRPLEGIPE | REFFVKWAGL | SYWHCSWVKE | LQLELYHTVM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YRNYQRKNDM | DEPPPFDYGS | GDEDGKSEKR | KNKDPLYAKM | EERFYRYGIK | PEWMMVHRIL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NHSFDKKGDI | HYLIKWKDLP | YDQCTWEIDE | IDIPYYDNLK | QAYWGHRELM | LGEDARLPKR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LVKKGKKLKD | DKQEKPPDTP | IVDPTVKFDK | QPWYIDATGG | TLHPYQLEGL | NWLRFSWAQG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| TDTILADEMG | LGKTVQTIVF | LYSLYKEGHS | KGPYLVSAPL | STIINWEREF | EMWAPDFYVV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TYTGDKESRS | VIRENEFSFE | DNAIRGGKKV | FRMKKEVQIK | FHVLLTSYEL | ITIDQAILGS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| IEWACLVVDE | AHRLKNNQSK | FFRVLNSYKI | DYKLLLTGTP | LQNNLEELFH | LLNFLTPERF |
| 910 | 920 | 930 | 940 | 950 | 960 |
| NNLEGFLEEF | ADISKEDQIK | KLHDLLGPHM | LRRLKADVFK | NMPAKTELIV | RVELSQMQKK |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| YYKFILTRNF | EALNSKGGGN | QVSLLNIMMD | LKKCCNHPYL | FPVAAVEAPV | LPNGSYDGSS |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LVKSSGKLML | LQKMLKKLRD | EGHRVLIFSQ | MTKMLDLLED | FLEYEGYKYE | RIDGGITGGL |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| RQEAIDRFNA | PGAQQFCFLL | STRAGGLGIN | LATADTVIIY | DSDWNPHNDI | QAFSRAHRIG |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| QNKKVMIYRF | VTRASVEERI | TQVAKRKMML | THLVVRPGLG | SKSGSMTKQE | LDDILKFGTE |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| ELFKDDVEGM | MSQGQRPTTP | IPDIQSTKGG | SLTAGAKKKH | GSTPPGDNKD | VEDSSVIHYD |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| DAAISKLLDR | NQDATDDTEL | QNMNEYLSSF | KVAQYVVREE | DGVEEVEREV | IKQEENVDPD |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| YWEKLLRHHY | EQQQEDLARN | LGKGKRIRKQ | VNYNDASQED | QEWQDELSDN | QSEYSIGSED |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| EDEDFEERPE | GQSGRRQSRR | QLKSDRDKPL | PPLLARVGGN | IEVLGFNARQ | RKAFLNAIMR |
| 1450 | 1460 | 1470 | 1480 | 1490 | 1500 |
| WGMPPQDAFN | SHWLVRDLRG | KSEKEFRAYV | SLFMRHLCEP | GADGAETFAD | GVPREGLSRQ |
| 1510 | 1520 | 1530 | 1540 | 1550 | 1560 |
| HVLTRIGVMS | LVRKKVQEFE | HVNGKYSTPD | LVPEGAEGKK | PGEVISSDPN | TPVPASPAQL |
| 1570 | 1580 | 1590 | 1600 | 1610 | 1620 |
| PPAPLGLTDK | MEAQLGYTDE | KESGMQKPKK | SLEIQTLPTA | LDRVEGEDKH | QSSDSKDRAR |
| 1630 | 1640 | 1650 | 1660 | 1670 | 1680 |
| EERTEEVEKA | QGSPEQPLKE | EVLPDKEPIP | DKPELSLGHS | GDFRPDDPKT | EEKEPGETQQ |
| 1690 | 1700 | 1710 | 1720 | 1730 | 1740 |
| NGDREEDEEG | KKEDKNGKFK | FMFNIADGGF | TELHTLWQNE | ERAAVSSGKI | YEIWHRRHDY |
| 1750 | 1760 | 1770 | 1780 | 1790 | 1800 |
| WLLAGIVTHG | YARWQDIQND | PRYMILNEPF | KSEIHKGNYL | EMKNKFLARR | FKLLEQALVI |
| 1810 | 1820 | 1830 | 1840 | 1850 | 1860 |
| EEQLRRAAYL | NMTQDPNHPA | MALNARLAEV | ECLAESHQHL | SKESLAGNKP | ANAVLHKVLN |
| 1870 | 1880 | 1890 | 1900 | 1910 | 1920 |
| QLEELLSDMK | ADVTRLPSML | SRIPPVAARL | QMSERSILSR | LTNRAGDPTI | QQTSSRRRDF |
| 1930 | 1940 | ||||
| PLFQRSFPAE | PSHLPNPRGR | EKLQPF |