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Protein

Chromodomain-helicase-DNA-binding protein 5

Gene

Chd5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa.4 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri345 – 392PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri418 – 465PHD-type 2PROSITE-ProRule annotationAdd BLAST48
Nucleotide bindingi727 – 734ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • H3K27me3 modified histone binding Source: UniProtKB
  • helicase activity Source: UniProtKB-KW
  • histone deacetylase binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cerebral cortex neuron differentiation Source: UniProtKB
  • histone H3-K27 trimethylation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • positive regulation of signal transduction by p53 class mediator Source: UniProtKB
  • regulation of cell differentiation Source: UniProtKB
  • regulation of transcription involved in cell fate commitment Source: UniProtKB
  • spermatogenesis, exchange of chromosomal proteins Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionChromatin regulator, DNA-binding, Helicase, Hydrolase
Biological processDifferentiation, Neurogenesis, Spermatogenesis, Transcription, Transcription regulation
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein 5 (EC:3.6.4.12)
Short name:
CHD-5
Alternative name(s):
ATP-dependent helicase CHD5
Gene namesi
Name:Chd5
Synonyms:Kiaa0444
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:3036258 Chd5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant males are infertile. Mating occurs, but the males are sterile, displaying abnormal spermatogenesis. Disruption of the gene has no effect on the fertility of females. Infertility is due to sperm morphological abnormalities and complete immotility that are observed in all mice. A variable sperm counts, with a complete absence is some individuals is also observed. Spermatogenesis is normal from spermatogonia through meiotic division of spermatocytes. However, at stage IX, step 9, abnormal nuclear morphology of differentiating spermatids appears. It is associated with increased histone retention and decreased histone H4 hyperacetylation, an important step in spermatid chromatid condensation. Finally, spermiation is also affected.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi346D → A: No effect on interaction with histone H3 unmethylated at 'Lys-4'. No significant effect on the ability to repress target genes expression. No effect on regulation of cell proliferation. 1 Publication1
Mutagenesisi355G → A: Loss of the ability to negatively regulate cell proliferation. 1 Publication1
Mutagenesisi361D → A: Loss of interaction with histone H3 unmethylated at 'Lys-4'. Loss of the ability to repress target genes expression. Loss of the ability to negatively regulate cell proliferation. 1 Publication1
Mutagenesisi415D → A: Loss of interaction with histone H3 unmethylated at 'Lys-4'. Loss of the ability to negatively regulate cell proliferation. 1 Publication1
Mutagenesisi432C → W: Loss of the ability to negatively regulate cell proliferation. 1 Publication1
Mutagenesisi434D → A: Loss of interaction with histone H3 unmethylated at 'Lys-4'. Loss of the ability to repress target genes expression. Loss of the ability to negatively regulate cell proliferation. 1 Publication1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004293261 – 1946Chromodomain-helicase-DNA-binding protein 5Add BLAST1946

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1556PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiA2A8L1
PaxDbiA2A8L1
PeptideAtlasiA2A8L1
PRIDEiA2A8L1

PTM databases

iPTMnetiA2A8L1
PhosphoSitePlusiA2A8L1

Expressioni

Tissue specificityi

Specifically expressed by neurons in brain, retina and adrenal gland (at protein level). Also detected in testis.3 Publications

Developmental stagei

Detected at E15.5, expression increases after birth and to adulthood. Expression increases in late-stage neuronal progenitor during their terminal differentiation.2 Publications

Gene expression databases

BgeeiENSMUSG00000005045
ExpressionAtlasiA2A8L1 baseline and differential
GenevisibleiA2A8L1 MM

Interactioni

Subunit structurei

May be part of a nucleosome remodeling and histone deacetylation, NuRD-like, complex composed at least of GATAD2B, HDAC1, HDAC2 and MTA3.1 Publication

GO - Molecular functioni

  • H3K27me3 modified histone binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi234678, 8 interactors
IntActiA2A8L1, 1 interactor
STRINGi10090.ENSMUSP00000030775

Structurei

3D structure databases

ProteinModelPortaliA2A8L1
SMRiA2A8L1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini499 – 556Chromo 1PROSITE-ProRule annotationAdd BLAST58
Domaini594 – 655Chromo 2PROSITE-ProRule annotationAdd BLAST62
Domaini714 – 898Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST185
Domaini1030 – 1195Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni345 – 655Histone-bindingBy similarityAdd BLAST311

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi849 – 852DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi49 – 118Lys-richAdd BLAST70

Domaini

The PHD domains mediate specific binding to histone H3 unmethylated at 'Lys-4' and may preferentially recruit the protein to transcriptionally inactive genes.1 Publication
The chromo domains mediate specific binding to histone H3 trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron differentiation for proper gene regulation.1 Publication

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri345 – 392PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri418 – 465PHD-type 2PROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IREB Eukaryota
ENOG410XNUT LUCA
GeneTreeiENSGT00760000119067
HOGENOMiHOG000231124
HOVERGENiHBG005326
PhylomeDBiA2A8L1

Family and domain databases

CDDicd00024 CHROMO, 2 hits
cd00079 HELICc, 1 hit
Gene3Di3.30.40.10, 2 hits
3.40.50.10810, 1 hit
InterProiView protein in InterPro
IPR028727 CHD5
IPR012957 CHD_C2
IPR012958 CHD_N
IPR016197 Chromo-like_dom_sf
IPR000953 Chromo/chromo_shadow_dom
IPR023780 Chromo_domain
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR009462 DUF1086
IPR009463 DUF1087
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR038718 SNF2-like_sf
IPR000330 SNF2_N
IPR019786 Zinc_finger_PHD-type_CS
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR10799:SF583 PTHR10799:SF583, 2 hits
PfamiView protein in Pfam
PF08074 CHDCT2, 1 hit
PF08073 CHDNT, 1 hit
PF00385 Chromo, 1 hit
PF06461 DUF1086, 1 hit
PF06465 DUF1087, 1 hit
PF00271 Helicase_C, 1 hit
PF00628 PHD, 2 hits
PF00176 SNF2_N, 1 hit
SMARTiView protein in SMART
SM00298 CHROMO, 2 hits
SM00487 DEXDc, 1 hit
SM01146 DUF1086, 1 hit
SM01147 DUF1087, 1 hit
SM00490 HELICc, 1 hit
SM00249 PHD, 2 hits
SUPFAMiSSF52540 SSF52540, 2 hits
SSF54160 SSF54160, 3 hits
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50013 CHROMO_2, 2 hits
PS00690 DEAH_ATP_HELICASE, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS01359 ZF_PHD_1, 2 hits
PS50016 ZF_PHD_2, 2 hits

Sequencei

Sequence statusi: Complete.

A2A8L1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGPLGTEEE LPRLFAEEME NEEEMSEEED GGLEGFEDFF PAEPVSLPKK
60 70 80 90 100
KPKKLKESKS SKGKRKKKEG SNDEMSDNEE DLEEKSESEG SDYSPTKKKK
110 120 130 140 150
KKLKEKKEKK EKKEKRKKRG EDEDDNDDGG LKEPKSSGQL MAEWGLDDVD
160 170 180 190 200
YLFSEDDYHT LTNYKAFSQF LRPLIAKKNP KIPMSKMMTV LGAKWREFSA
210 220 230 240 250
NNPFKGSSAA AAAAAVAAAV ETVTIAPPLA ISPQQVPQTL PIRKAKTKEG
260 270 280 290 300
KGPGVRKKNK GAKDSKKKGR GKRVAGLKFR FGGISKRKKG SSSEEDERED
310 320 330 340 350
SDLDNASIHS SSVRSECSAA LGKKNKRRRK KKRIDDGDGY ETDHQDYCEV
360 370 380 390 400
CQQGGEIILC DTCPRAYHLV CLDPELEKAP EGKWSCPHCE KEGIQWEPKD
410 420 430 440 450
DDEEEEEGGC EEEEDDHMEF CRVCKDGGEL LCCDACPSSY HLHCLNPPLP
460 470 480 490 500
EIPNGEWLCP RCTCPPLKGK VQRILHWRWT EPPAPFVVGL PGPEVEPGMP
510 520 530 540 550
PPRPLEGIPE REFFVKWAGL SYWHCSWVKE LQLELYHTVM YRNYQRKNDM
560 570 580 590 600
DEPPPFDYGS GDEDGKSEKR KNKDPLYAKM EERFYRYGIK PEWMMVHRIL
610 620 630 640 650
NHSFDKKGDI HYLIKWKDLP YDQCTWEIDE IDIPYYDNLK QAYWGHRELM
660 670 680 690 700
LGEDARLPKR LVKKGKKLKD DKQEKPPDTP IVDPTVKFDK QPWYIDATGG
710 720 730 740 750
TLHPYQLEGL NWLRFSWAQG TDTILADEMG LGKTVQTIVF LYSLYKEGHS
760 770 780 790 800
KGPYLVSAPL STIINWEREF EMWAPDFYVV TYTGDKESRS VIRENEFSFE
810 820 830 840 850
DNAIRGGKKV FRMKKEVQIK FHVLLTSYEL ITIDQAILGS IEWACLVVDE
860 870 880 890 900
AHRLKNNQSK FFRVLNSYKI DYKLLLTGTP LQNNLEELFH LLNFLTPERF
910 920 930 940 950
NNLEGFLEEF ADISKEDQIK KLHDLLGPHM LRRLKADVFK NMPAKTELIV
960 970 980 990 1000
RVELSQMQKK YYKFILTRNF EALNSKGGGN QVSLLNIMMD LKKCCNHPYL
1010 1020 1030 1040 1050
FPVAAVEAPV LPNGSYDGSS LVKSSGKLML LQKMLKKLRD EGHRVLIFSQ
1060 1070 1080 1090 1100
MTKMLDLLED FLEYEGYKYE RIDGGITGGL RQEAIDRFNA PGAQQFCFLL
1110 1120 1130 1140 1150
STRAGGLGIN LATADTVIIY DSDWNPHNDI QAFSRAHRIG QNKKVMIYRF
1160 1170 1180 1190 1200
VTRASVEERI TQVAKRKMML THLVVRPGLG SKSGSMTKQE LDDILKFGTE
1210 1220 1230 1240 1250
ELFKDDVEGM MSQGQRPTTP IPDIQSTKGG SLTAGAKKKH GSTPPGDNKD
1260 1270 1280 1290 1300
VEDSSVIHYD DAAISKLLDR NQDATDDTEL QNMNEYLSSF KVAQYVVREE
1310 1320 1330 1340 1350
DGVEEVEREV IKQEENVDPD YWEKLLRHHY EQQQEDLARN LGKGKRIRKQ
1360 1370 1380 1390 1400
VNYNDASQED QEWQDELSDN QSEYSIGSED EDEDFEERPE GQSGRRQSRR
1410 1420 1430 1440 1450
QLKSDRDKPL PPLLARVGGN IEVLGFNARQ RKAFLNAIMR WGMPPQDAFN
1460 1470 1480 1490 1500
SHWLVRDLRG KSEKEFRAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ
1510 1520 1530 1540 1550
HVLTRIGVMS LVRKKVQEFE HVNGKYSTPD LVPEGAEGKK PGEVISSDPN
1560 1570 1580 1590 1600
TPVPASPAQL PPAPLGLTDK MEAQLGYTDE KESGMQKPKK SLEIQTLPTA
1610 1620 1630 1640 1650
LDRVEGEDKH QSSDSKDRAR EERTEEVEKA QGSPEQPLKE EVLPDKEPIP
1660 1670 1680 1690 1700
DKPELSLGHS GDFRPDDPKT EEKEPGETQQ NGDREEDEEG KKEDKNGKFK
1710 1720 1730 1740 1750
FMFNIADGGF TELHTLWQNE ERAAVSSGKI YEIWHRRHDY WLLAGIVTHG
1760 1770 1780 1790 1800
YARWQDIQND PRYMILNEPF KSEIHKGNYL EMKNKFLARR FKLLEQALVI
1810 1820 1830 1840 1850
EEQLRRAAYL NMTQDPNHPA MALNARLAEV ECLAESHQHL SKESLAGNKP
1860 1870 1880 1890 1900
ANAVLHKVLN QLEELLSDMK ADVTRLPSML SRIPPVAARL QMSERSILSR
1910 1920 1930 1940
LTNRAGDPTI QQTSSRRRDF PLFQRSFPAE PSHLPNPRGR EKLQPF
Length:1,946
Mass (Da):222,515
Last modified:February 20, 2007 - v1
Checksum:i5B94AB11A9C9BB03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL611985 Genomic DNA No translation available.
AK129145 mRNA Translation: BAC97955.1
RefSeqiXP_006538995.1, XM_006538932.2
UniGeneiMm.40192

Genome annotation databases

EnsembliENSMUST00000005175; ENSMUSP00000005175; ENSMUSG00000005045
GeneIDi269610

Similar proteinsi

Entry informationi

Entry nameiCHD5_MOUSE
AccessioniPrimary (citable) accession number: A2A8L1
Secondary accession number(s): Q6ZQB2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: February 20, 2007
Last modified: April 25, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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