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Protein

Chromodomain-helicase-DNA-binding protein 5

Gene

Chd5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri345 – 39248PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri418 – 46548PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi727 – 7348ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

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
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Differentiation, Neurogenesis, Spermatogenesis, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:3036258. Chd5.

Subcellular locationi

GO - Cellular componenti

  • heterochromatin Source: UniProtKB
  • membrane Source: MGI
  • nucleus Source: UniProtKB
  • NuRD complex Source: UniProtKB
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi346 – 3461D → 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 Publication
Mutagenesisi355 – 3551G → A: Loss of the ability to negatively regulate cell proliferation. 1 Publication
Mutagenesisi361 – 3611D → 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 Publication
Mutagenesisi415 – 4151D → A: Loss of interaction with histone H3 unmethylated at 'Lys-4'. Loss of the ability to negatively regulate cell proliferation. 1 Publication
Mutagenesisi432 – 4321C → W: Loss of the ability to negatively regulate cell proliferation. 1 Publication
Mutagenesisi434 – 4341D → 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 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19461946Chromodomain-helicase-DNA-binding protein 5PRO_0000429326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1556 – 15561PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiA2A8L1.
PaxDbiA2A8L1.
PeptideAtlasiA2A8L1.
PRIDEiA2A8L1.

PTM databases

iPTMnetiA2A8L1.
PhosphoSiteiA2A8L1.

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 interactions.
IntActiA2A8L1. 1 interaction.
STRINGi10090.ENSMUSP00000030775.

Structurei

3D structure databases

ProteinModelPortaliA2A8L1.
SMRiA2A8L1. Positions 340-395, 415-649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini499 – 55658Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini594 – 65562Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini714 – 898185Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1030 – 1195166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni345 – 655311Histone-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi849 – 8524DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 11870Lys-richAdd
BLAST

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
Contains 2 chromo domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri345 – 39248PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri418 – 46548PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IREB. Eukaryota.
ENOG410XNUT. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
PhylomeDBiA2A8L1.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028727. CHD5.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
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.
[Graphical view]
PANTHERiPTHR10799:SF583. PTHR10799:SF583. 4 hits.
PfamiPF08074. 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.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50013. 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.
[Graphical view]

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_006538932.1.
UniGeneiMm.40192.

Genome annotation databases

EnsembliENSMUST00000005175; ENSMUSP00000005175; ENSMUSG00000005045.
GeneIDi269610.

Cross-referencesi

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_006538932.1.
UniGeneiMm.40192.

3D structure databases

ProteinModelPortaliA2A8L1.
SMRiA2A8L1. Positions 340-395, 415-649.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234678. 8 interactions.
IntActiA2A8L1. 1 interaction.
STRINGi10090.ENSMUSP00000030775.

PTM databases

iPTMnetiA2A8L1.
PhosphoSiteiA2A8L1.

Proteomic databases

MaxQBiA2A8L1.
PaxDbiA2A8L1.
PeptideAtlasiA2A8L1.
PRIDEiA2A8L1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005175; ENSMUSP00000005175; ENSMUSG00000005045.
GeneIDi269610.

Organism-specific databases

CTDi26038.
MGIiMGI:3036258. Chd5.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IREB. Eukaryota.
ENOG410XNUT. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
PhylomeDBiA2A8L1.

Miscellaneous databases

PROiA2A8L1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005045.
ExpressionAtlasiA2A8L1. baseline and differential.
GenevisibleiA2A8L1. MM.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028727. CHD5.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
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.
[Graphical view]
PANTHERiPTHR10799:SF583. PTHR10799:SF583. 4 hits.
PfamiPF08074. 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.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50013. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHD5_MOUSE
AccessioniPrimary (citable) accession number: A2A8L1
Secondary accession number(s): Q6ZQB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: February 20, 2007
Last modified: September 7, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.