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Q8TDI0

- CHD5_HUMAN

UniProt

Q8TDI0 - CHD5_HUMAN

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Protein

Chromodomain-helicase-DNA-binding protein 5

Gene

CHD5

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri343 – 39048PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri416 – 46348PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi725 – 7328ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. DNA binding Source: UniProtKB-KW
  4. H3K27me3 modified histone binding Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. cerebral cortex neuron differentiation Source: UniProtKB
  2. histone H3-K27 trimethylation Source: UniProtKB
  3. histone H4 acetylation Source: UniProtKB
  4. negative regulation of cell proliferation Source: UniProtKB
  5. positive regulation of signal transduction by p53 class mediator Source: UniProtKB
  6. regulation of transcription involved in cell fate commitment Source: UniProtKB
  7. spermatogenesis, exchange of chromosomal proteins Source: UniProtKB
  8. 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:CHD5Imported
Synonyms:KIAA0444
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16816. CHD5.

Subcellular locationi

Nucleus 2 Publications
Note: Associates with heterochromatin.By similarity

GO - Cellular componenti

  1. heterochromatin Source: UniProtKB
  2. membrane Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. NuRD complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in CHD5 may be a cause of the development of cancers from epithelial, neural and hematopoietic origin. CHD5 is one of the missing genes in the del(1p36), a deletion which is extremely common in this type of cancers. A decrease of its expression, results in increased susceptibility of cells to Ras-mediated transformation in vitro and in vivo (PubMed:17289567).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi518 – 5181L → A: Reduced affinity for trimethylated histone H3K27me3. 1 Publication
Mutagenesisi619 – 6191Y → E: Reduced affinity for trimethylated histone H3K27me3. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134969178.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19541954Chromodomain-helicase-DNA-binding protein 5PRO_0000080230Add
BLAST

Proteomic databases

MaxQBiQ8TDI0.
PaxDbiQ8TDI0.
PRIDEiQ8TDI0.

PTM databases

PhosphoSiteiQ8TDI0.

Expressioni

Tissue specificityi

Preferentially expressed in total brain, fetal brain, and cerebellum. It is also moderately expressed in the adrenal gland and detected in testis.2 Publications

Gene expression databases

BgeeiQ8TDI0.
CleanExiHS_CHD5.
ExpressionAtlasiQ8TDI0. baseline.
GenevestigatoriQ8TDI0.

Organism-specific databases

HPAiHPA015809.

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.By similarity

Protein-protein interaction databases

BioGridi117504. 4 interactions.
IntActiQ8TDI0. 3 interactions.
STRINGi9606.ENSP00000262450.

Structurei

3D structure databases

ProteinModelPortaliQ8TDI0.
SMRiQ8TDI0. Positions 315-468, 588-644, 943-1195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini497 – 55458Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini592 – 65362Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini712 – 896185Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1028 – 1193166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 653311Histone-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi847 – 8504DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 11668Lys-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.By similarity
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.Sequence Analysis
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 fingeri343 – 39048PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri416 – 46348PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ8TDI0.
KOiK14435.
OMAiKRIDDGD.
OrthoDBiEOG7C8GG7.
PhylomeDBiQ8TDI0.
TreeFamiTF106448.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028727. CHD5.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
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.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10799:SF583. PTHR10799:SF583. 1 hit.
PfamiPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 2 hits.
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.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 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.

Q8TDI0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRGPVGTEEE LPRLFAEEME NEDEMSEEED GGLEAFDDFF PVEPVSLPKK
60 70 80 90 100
KKPKKLKENK CKGKRKKKEG SNDELSENEE DLEEKSESEG SDYSPNKKKK
110 120 130 140 150
KKLKDKKEKK AKRKKKDEDE DDNDDGCLKE PKSSGQLMAE WGLDDVDYLF
160 170 180 190 200
SEEDYHTLTN YKAFSQFLRP LIAKKNPKIP MSKMMTVLGA KWREFSANNP
210 220 230 240 250
FKGSSAAAAA AAVAAAVETV TISPPLAVSP PQVPQPVPIR KAKTKEGKGP
260 270 280 290 300
GVRKKIKGSK DGKKKGKGKK TAGLKFRFGG ISNKRKKGSS SEEDEREESD
310 320 330 340 350
FDSASIHSAS VRSECSAALG KKSKRRRKKK RIDDGDGYET DHQDYCEVCQ
360 370 380 390 400
QGGEIILCDT CPRAYHLVCL DPELEKAPEG KWSCPHCEKE GIQWEPKDDD
410 420 430 440 450
DEEEEGGCEE EEDDHMEFCR VCKDGGELLC CDACPSSYHL HCLNPPLPEI
460 470 480 490 500
PNGEWLCPRC TCPPLKGKVQ RILHWRWTEP PAPFMVGLPG PDVEPSLPPP
510 520 530 540 550
KPLEGIPERE FFVKWAGLSY WHCSWVKELQ LELYHTVMYR NYQRKNDMDE
560 570 580 590 600
PPPFDYGSGD EDGKSEKRKN KDPLYAKMEE RFYRYGIKPE WMMIHRILNH
610 620 630 640 650
SFDKKGDVHY LIKWKDLPYD QCTWEIDDID IPYYDNLKQA YWGHRELMLG
660 670 680 690 700
EDTRLPKRLL KKGKKLRDDK QEKPPDTPIV DPTVKFDKQP WYIDSTGGTL
710 720 730 740 750
HPYQLEGLNW LRFSWAQGTD TILADEMGLG KTVQTIVFLY SLYKEGHSKG
760 770 780 790 800
PYLVSAPLST IINWEREFEM WAPDFYVVTY TGDKESRSVI RENEFSFEDN
810 820 830 840 850
AIRSGKKVFR MKKEVQIKFH VLLTSYELIT IDQAILGSIE WACLVVDEAH
860 870 880 890 900
RLKNNQSKFF RVLNSYKIDY KLLLTGTPLQ NNLEELFHLL NFLTPERFNN
910 920 930 940 950
LEGFLEEFAD ISKEDQIKKL HDLLGPHMLR RLKADVFKNM PAKTELIVRV
960 970 980 990 1000
ELSQMQKKYY KFILTRNFEA LNSKGGGNQV SLLNIMMDLK KCCNHPYLFP
1010 1020 1030 1040 1050
VAAVEAPVLP NGSYDGSSLV KSSGKLMLLQ KMLKKLRDEG HRVLIFSQMT
1060 1070 1080 1090 1100
KMLDLLEDFL EYEGYKYERI DGGITGGLRQ EAIDRFNAPG AQQFCFLLST
1110 1120 1130 1140 1150
RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRIGQN KKVMIYRFVT
1160 1170 1180 1190 1200
RASVEERITQ VAKRKMMLTH LVVRPGLGSK SGSMTKQELD DILKFGTEEL
1210 1220 1230 1240 1250
FKDDVEGMMS QGQRPVTPIP DVQSSKGGNL AASAKKKHGS TPPGDNKDVE
1260 1270 1280 1290 1300
DSSVIHYDDA AISKLLDRNQ DATDDTELQN MNEYLSSFKV AQYVVREEDG
1310 1320 1330 1340 1350
VEEVEREIIK QEENVDPDYW EKLLRHHYEQ QQEDLARNLG KGKRIRKQVN
1360 1370 1380 1390 1400
YNDASQEDQE WQDELSDNQS EYSIGSEDED EDFEERPEGQ SGRRQSRRQL
1410 1420 1430 1440 1450
KSDRDKPLPP LLARVGGNIE VLGFNARQRK AFLNAIMRWG MPPQDAFNSH
1460 1470 1480 1490 1500
WLVRDLRGKS EKEFRAYVSL FMRHLCEPGA DGAETFADGV PREGLSRQHV
1510 1520 1530 1540 1550
LTRIGVMSLV RKKVQEFEHV NGKYSTPDLI PEGPEGKKSG EVISSDPNTP
1560 1570 1580 1590 1600
VPASPAHLLP APLGLPDKME AQLGYMDEKD PGAQKPRQPL EVQALPAALD
1610 1620 1630 1640 1650
RVESEDKHES PASKERAREE RPEETEKAPP SPEQLPREEV LPEKEKILDK
1660 1670 1680 1690 1700
LELSLIHSRG DSSELRPDDT KAEEKEPIET QQNGDKEEDD EGKKEDKKGK
1710 1720 1730 1740 1750
FKFMFNIADG GFTELHTLWQ NEERAAVSSG KIYDIWHRRH DYWLLAGIVT
1760 1770 1780 1790 1800
HGYARWQDIQ NDPRYMILNE PFKSEVHKGN YLEMKNKFLA RRFKLLEQAL
1810 1820 1830 1840 1850
VIEEQLRRAA YLNMTQDPNH PAMALNARLA EVECLAESHQ HLSKESLAGN
1860 1870 1880 1890 1900
KPANAVLHKV LNQLEELLSD MKADVTRLPS MLSRIPPVAA RLQMSERSIL
1910 1920 1930 1940 1950
SRLTNRAGDP TIQQGAFGSS QMYSNNFGPN FRGPGPGGIV NYNQMPLGPY

VTDI
Length:1,954
Mass (Da):223,050
Last modified:June 1, 2002 - v1
Checksum:iE333062B5B55E71F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451V → M in a breast cancer sample; somatic mutation. 1 Publication
VAR_035475
Natural varianti119 – 1191D → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_035476
Natural varianti667 – 6671R → G in a breast cancer sample; somatic mutation. 1 Publication
VAR_035477
Natural varianti1253 – 12531S → I.
Corresponds to variant rs6657997 [ dbSNP | Ensembl ].
VAR_048729
Natural varianti1539 – 15391S → P.2 Publications
Corresponds to variant rs2843493 [ dbSNP | Ensembl ].
VAR_048730

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF425231 mRNA. Translation: AAL98962.1.
AL031847, AL035406 Genomic DNA. Translation: CAI19450.1.
AL035406, AL031847 Genomic DNA. Translation: CAI19891.1.
AL117491 mRNA. Translation: CAB55959.1.
AB007913 mRNA. Translation: BAA32289.1.
CCDSiCCDS57.1.
PIRiT17269.
RefSeqiNP_056372.1. NM_015557.2.
UniGeneiHs.522898.

Genome annotation databases

EnsembliENST00000262450; ENSP00000262450; ENSG00000116254.
GeneIDi26038.
KEGGihsa:26038.
UCSCiuc001amb.2. human.

Polymorphism databases

DMDMi51701343.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF425231 mRNA. Translation: AAL98962.1 .
AL031847 , AL035406 Genomic DNA. Translation: CAI19450.1 .
AL035406 , AL031847 Genomic DNA. Translation: CAI19891.1 .
AL117491 mRNA. Translation: CAB55959.1 .
AB007913 mRNA. Translation: BAA32289.1 .
CCDSi CCDS57.1.
PIRi T17269.
RefSeqi NP_056372.1. NM_015557.2.
UniGenei Hs.522898.

3D structure databases

ProteinModelPortali Q8TDI0.
SMRi Q8TDI0. Positions 315-468, 588-644, 943-1195.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117504. 4 interactions.
IntActi Q8TDI0. 3 interactions.
STRINGi 9606.ENSP00000262450.

PTM databases

PhosphoSitei Q8TDI0.

Polymorphism databases

DMDMi 51701343.

Proteomic databases

MaxQBi Q8TDI0.
PaxDbi Q8TDI0.
PRIDEi Q8TDI0.

Protocols and materials databases

DNASUi 26038.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262450 ; ENSP00000262450 ; ENSG00000116254 .
GeneIDi 26038.
KEGGi hsa:26038.
UCSCi uc001amb.2. human.

Organism-specific databases

CTDi 26038.
GeneCardsi GC01M006161.
HGNCi HGNC:16816. CHD5.
HPAi HPA015809.
MIMi 610771. gene.
neXtProti NX_Q8TDI0.
PharmGKBi PA134969178.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00760000119067.
HOGENOMi HOG000231124.
HOVERGENi HBG005326.
InParanoidi Q8TDI0.
KOi K14435.
OMAi KRIDDGD.
OrthoDBi EOG7C8GG7.
PhylomeDBi Q8TDI0.
TreeFami TF106448.

Miscellaneous databases

ChiTaRSi CHD5. human.
GeneWikii CHD5.
GenomeRNAii 26038.
NextBioi 47863.
PROi Q8TDI0.
SOURCEi Search...

Gene expression databases

Bgeei Q8TDI0.
CleanExi HS_CHD5.
ExpressionAtlasi Q8TDI0. baseline.
Genevestigatori Q8TDI0.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProi IPR028727. CHD5.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
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.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
PANTHERi PTHR10799:SF583. PTHR10799:SF583. 1 hit.
Pfami PF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 2 hits.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "CHD5, a new member of the chromodomain gene family, is preferentially expressed in the nervous system."
    Thompson P.M., Gotoh T., Kok M., White P.S., Brodeur G.M.
    Oncogene 22:1002-1011(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1954, VARIANT PRO-1539.
    Tissue: Testis.
  4. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
    Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
    DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 977-1954, VARIANT PRO-1539.
    Tissue: Brain.
  5. Cited for: DISEASE.
  6. "CHD5, a brain-specific paralog of Mi2 chromatin remodeling enzymes, regulates expression of neuronal genes."
    Potts R.C., Zhang P., Wurster A.L., Precht P., Mughal M.R., Wood W.H., Zhang Y., Becker K.G., Mattson M.P., Pazin M.J.
    PLoS ONE 6:E24515-E24515(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "CHD5 is required for neurogenesis and has a dual role in facilitating gene expression and polycomb gene repression."
    Egan C.M., Nyman U., Skotte J., Streubel G., Turner S., O'Connell D.J., Rraklli V., Dolan M.J., Chadderton N., Hansen K., Farrar G.J., Helin K., Holmberg J., Bracken A.P.
    Dev. Cell 26:223-236(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TRANSCRIPTIONAL REGULATOR, FUNCTION IN NEURON DIFFERENTIATION, INTERACTION WITH HISTONE H3K27ME3, SUBCELLULAR LOCATION, CHROMO DOMAINS, MUTAGENESIS OF LEU-518 AND TYR-619.
  8. Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-45; ASN-119 AND GLY-667.

Entry informationi

Entry nameiCHD5_HUMAN
AccessioniPrimary (citable) accession number: Q8TDI0
Secondary accession number(s): O75032
, Q5TG89, Q7LGH2, Q9UFR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3