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Protein

Chromodomain-helicase-DNA-binding protein 4

Gene

CHD4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri370 – 417PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri449 – 496PHD-type 2PROSITE-ProRule annotationAdd BLAST48
Nucleotide bindingi751 – 758ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: ProtInc
  • DNA binding Source: ProtInc
  • histone deacetylase activity Source: Reactome
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • zinc ion binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111642-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein 4 (EC:3.6.4.12)
Short name:
CHD-4
Alternative name(s):
ATP-dependent helicase CHD4
Mi-2 autoantigen 218 kDa protein
Mi2-beta
Gene namesi
Name:CHD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1919. CHD4.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: HPA
  • NuRD complex Source: UniProtKB
  • protein complex Source: UniProtKB
  • protein-DNA complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi1108.
OpenTargetsiENSG00000111642.
PharmGKBiPA26455.

Polymorphism and mutation databases

BioMutaiCHD4.
DMDMi311033360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000802281 – 1912Chromodomain-helicase-DNA-binding protein 4Add BLAST1912

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44PhosphoserineCombined sources1
Modified residuei303PhosphoserineCombined sources1
Modified residuei308PhosphoserineCombined sources1
Modified residuei309PhosphoserineCombined sources1
Modified residuei310PhosphoserineCombined sources1
Modified residuei319PhosphoserineCombined sources1
Modified residuei367PhosphothreonineCombined sources1
Modified residuei428PhosphoserineCombined sources1
Modified residuei515PhosphoserineCombined sources1
Modified residuei517PhosphothreonineCombined sources1
Modified residuei529PhosphothreonineCombined sources1
Modified residuei531PhosphoserineCombined sources1
Modified residuei703PhosphothreonineCombined sources1
Modified residuei1209PhosphoserineBy similarity1
Cross-linki1304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1308PhosphoserineCombined sources1
Modified residuei1349PhosphoserineCombined sources1
Modified residuei1531PhosphoserineCombined sources1
Modified residuei1535PhosphoserineCombined sources1
Modified residuei1537PhosphoserineCombined sources1
Modified residuei1542PhosphothreonineBy similarity1
Modified residuei1549PhosphothreonineBy similarity1
Modified residuei1553PhosphothreonineCombined sources1
Cross-linki1565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1570PhosphoserineCombined sources1
Cross-linki1572Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1576PhosphoserineCombined sources1
Modified residuei1602PhosphoserineCombined sources1
Modified residuei1643N6-acetyllysine; alternateCombined sources1
Cross-linki1643Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1653PhosphothreonineCombined sources1
Cross-linki1670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1679PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14839.
MaxQBiQ14839.
PaxDbiQ14839.
PeptideAtlasiQ14839.
PRIDEiQ14839.

PTM databases

iPTMnetiQ14839.
PhosphoSitePlusiQ14839.
SwissPalmiQ14839.

Miscellaneous databases

PMAP-CutDBQ14839.

Expressioni

Gene expression databases

BgeeiENSG00000111642.
CleanExiHS_CHD4.
ExpressionAtlasiQ14839. baseline and differential.
GenevisibleiQ14839. HS.

Interactioni

Subunit structurei

Interacts with KLF1; the interaction depends on sumoylation of KLF1, and leads to its transcriptional repression (By similarity). Interacts directly with IKFZ1 in the NuRD complex. Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressor complex (PubMed:9804427, PubMed:10204490, PubMed:15454082). Part of a complex containing ATR and HDAC2 (PubMed:10545197). Interacts with TRIM27 (PubMed:14530259). Interacts with ZGPAT; the interaction is direct (PubMed:19644445). Interacts with BCL6 (PubMed:15454082). Interacts with BRD4 (PubMed:21555454). Interacts with PCNT (PubMed:17626165). Interacts with SETX (PubMed:23149945).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC1Q135476EBI-372916,EBI-301834
MYCP011062EBI-372916,EBI-447544

GO - Molecular functioni

  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107533. 131 interactors.
DIPiDIP-31183N.
IntActiQ14839. 46 interactors.
MINTiMINT-349766.
STRINGi9606.ENSP00000349508.

Structurei

Secondary structure

11912
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi145 – 147Combined sources3
Helixi151 – 157Combined sources7
Helixi169 – 174Combined sources6
Helixi178 – 190Combined sources13
Helixi198 – 215Combined sources18
Turni374 – 376Combined sources3
Beta strandi386 – 389Combined sources4
Helixi394 – 397Combined sources4
Helixi414 – 417Combined sources4
Beta strandi450 – 452Combined sources3
Turni453 – 455Combined sources3
Beta strandi459 – 463Combined sources5
Beta strandi465 – 467Combined sources3
Beta strandi473 – 478Combined sources6
Turni491 – 496Combined sources6
Beta strandi502 – 511Combined sources10
Beta strandi540 – 547Combined sources8
Helixi552 – 554Combined sources3
Beta strandi556 – 559Combined sources4
Helixi560 – 566Combined sources7
Helixi568 – 577Combined sources10
Beta strandi580 – 582Combined sources3
Helixi594 – 599Combined sources6
Helixi603 – 611Combined sources9
Helixi613 – 615Combined sources3
Helixi619 – 622Combined sources4
Beta strandi623 – 632Combined sources10
Beta strandi638 – 644Combined sources7
Helixi649 – 651Combined sources3
Beta strandi653 – 656Combined sources4
Helixi664 – 673Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MM2NMR-A446-501[»]
1MM3NMR-A446-476[»]
A490-501[»]
2EE1NMR-A618-674[»]
2L5UNMR-A365-420[»]
2L75NMR-A446-501[»]
2N5NNMR-A145-225[»]
4O9IX-ray2.60X499-677[»]
ProteinModelPortaliQ14839.
SMRiQ14839.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini494 – 594Chromo 1PROSITE-ProRule annotationAdd BLAST101
Domaini622 – 697Chromo 2PROSITE-ProRule annotationAdd BLAST76
Domaini738 – 922Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST185
Domaini1054 – 1203Helicase C-terminalPROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1577 – 1912Required for interaction with PCNT1 PublicationAdd BLAST336

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi873 – 876DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi50 – 59Poly-Lys10
Compositional biasi94 – 98Poly-Glu5
Compositional biasi114 – 119Poly-Lys6
Compositional biasi134 – 138Poly-Glu5
Compositional biasi139 – 144Poly-Asp6
Compositional biasi227 – 235Poly-Ala9
Compositional biasi248 – 252Poly-Pro5
Compositional biasi350 – 354Poly-Lys5
Compositional biasi1052 – 1055Poly-Leu4
Compositional biasi1294 – 1301Poly-Glu8
Compositional biasi1665 – 1668Poly-Glu4

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)DescriptionActionsGraphical viewLength
Zinc fingeri370 – 417PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri449 – 496PHD-type 2PROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ14839.
KOiK11643.
PhylomeDBiQ14839.
TreeFamiTF106448.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028725. CHD4.
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:SF554. PTHR10799:SF554. 6 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.
PROSITEiPS00598. CHROMO_1. 2 hits.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14839-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPE EDLSETETPK
60 70 80 90 100
LKKKKKPKKP RDPKIPKSKR QKKERMLLCR QLGDSSGEGP EFVEEEEEVA
110 120 130 140 150
LRSDSEGSDY TPGKKKKKKL GPKKEKKSKS KRKEEEEEED DDDDSKEPKS
160 170 180 190 200
SAQLLEDWGM EDIDHVFSEE DYRTLTNYKA FSQFVRPLIA AKNPKIAVSK
210 220 230 240 250
MMMVLGAKWR EFSTNNPFKG SSGASVAAAA AAAVAVVESM VTATEVAPPP
260 270 280 290 300
PPVEVPIRKA KTKEGKGPNA RRKPKGSPRV PDAKKPKPKK VAPLKIKLGG
310 320 330 340 350
FGSKRKRSSS EDDDLDVESD FDDASINSYS VSDGSTSRSS RSRKKLRTTK
360 370 380 390 400
KKKKGEEEVT AVDGYETDHQ DYCEVCQQGG EIILCDTCPR AYHMVCLDPD
410 420 430 440 450
MEKAPEGKWS CPHCEKEGIQ WEAKEDNSEG EEILEEVGGD LEEEDDHHME
460 470 480 490 500
FCRVCKDGGE LLCCDTCPSS YHIHCLNPPL PEIPNGEWLC PRCTCPALKG
510 520 530 540 550
KVQKILIWKW GQPPSPTPVP RPPDADPNTP SPKPLEGRPE RQFFVKWQGM
560 570 580 590 600
SYWHCSWVSE LQLELHCQVM FRNYQRKNDM DEPPSGDFGG DEEKSRKRKN
610 620 630 640 650
KDPKFAEMEE RFYRYGIKPE WMMIHRILNH SVDKKGHVHY LIKWRDLPYD
660 670 680 690 700
QASWESEDVE IQDYDLFKQS YWNHRELMRG EEGRPGKKLK KVKLRKLERP
710 720 730 740 750
PETPTVDPTV KYERQPEYLD ATGGTLHPYQ MEGLNWLRFS WAQGTDTILA
760 770 780 790 800
DEMGLGKTVQ TAVFLYSLYK EGHSKGPFLV SAPLSTIINW EREFEMWAPD
810 820 830 840 850
MYVVTYVGDK DSRAIIRENE FSFEDNAIRG GKKASRMKKE ASVKFHVLLT
860 870 880 890 900
SYELITIDMA ILGSIDWACL IVDEAHRLKN NQSKFFRVLN GYSLQHKLLL
910 920 930 940 950
TGTPLQNNLE ELFHLLNFLT PERFHNLEGF LEEFADIAKE DQIKKLHDML
960 970 980 990 1000
GPHMLRRLKA DVFKNMPSKT ELIVRVELSP MQKKYYKYIL TRNFEALNAR
1010 1020 1030 1040 1050
GGGNQVSLLN VVMDLKKCCN HPYLFPVAAM EAPKMPNGMY DGSALIRASG
1060 1070 1080 1090 1100
KLLLLQKMLK NLKEGGHRVL IFSQMTKMLD LLEDFLEHEG YKYERIDGGI
1110 1120 1130 1140 1150
TGNMRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT VIIYDSDWNP
1160 1170 1180 1190 1200
HNDIQAFSRA HRIGQNKKVM IYRFVTRASV EERITQVAKK KMMLTHLVVR
1210 1220 1230 1240 1250
PGLGSKTGSM SKQELDDILK FGTEELFKDE ATDGGGDNKE GEDSSVIHYD
1260 1270 1280 1290 1300
DKAIERLLDR NQDETEDTEL QGMNEYLSSF KVAQYVVREE EMGEEEEVER
1310 1320 1330 1340 1350
EIIKQEESVD PDYWEKLLRH HYEQQQEDLA RNLGKGKRIR KQVNYNDGSQ
1360 1370 1380 1390 1400
EDRDWQDDQS DNQSDYSVAS EEGDEDFDER SEAPRRPSRK GLRNDKDKPL
1410 1420 1430 1440 1450
PPLLARVGGN IEVLGFNARQ RKAFLNAIMR YGMPPQDAFT TQWLVRDLRG
1460 1470 1480 1490 1500
KSEKEFKAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS
1510 1520 1530 1540 1550
LIRKKVQEFE HVNGRWSMPE LAEVEENKKM SQPGSPSPKT PTPSTPGDTQ
1560 1570 1580 1590 1600
PNTPAPVPPA EDGIKIEENS LKEEESIEGE KEVKSTAPET AIECTQAPAP
1610 1620 1630 1640 1650
ASEDEKVVVE PPEGEEKVEK AEVKERTEEP METEPKGAAD VEKVEEKSAI
1660 1670 1680 1690 1700
DLTPIVVEDK EEKKEEEEKK EVMLQNGETP KDLNDEKQKK NIKQRFMFNI
1710 1720 1730 1740 1750
ADGGFTELHS LWQNEERAAT VTKKTYEIWH RRHDYWLLAG IINHGYARWQ
1760 1770 1780 1790 1800
DIQNDPRYAI LNEPFKGEMN RGNFLEIKNK FLARRFKLLE QALVIEEQLR
1810 1820 1830 1840 1850
RAAYLNMSED PSHPSMALNT RFAEVECLAE SHQHLSKESM AGNKPANAVL
1860 1870 1880 1890 1900
HKVLKQLEEL LSDMKADVTR LPATIARIPP VAVRLQMSER NILSRLANRA
1910
PEPTPQQVAQ QQ
Length:1,912
Mass (Da):218,005
Last modified:November 2, 2010 - v2
Checksum:i765ED8485B7BBB85
GO
Isoform 2 (identifier: Q14839-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1353-1353: R → RGVCGRPRPPPMGRSTRAVGPAHLPSLPP

Note: No experimental confirmation available.
Show »
Length:1,940
Mass (Da):220,848
Checksum:iC4D5E61DFE83B27B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34 – 36Missing in AAH38596 (PubMed:15489334).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031674139E → D.1 PublicationCorresponds to variant rs1639122dbSNPEnsembl.1
Natural variantiVAR_0316751648S → L.Corresponds to variant rs35512811dbSNPEnsembl.1
Natural variantiVAR_0316761655I → V.Corresponds to variant rs16932768dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0114161353R → RGVCGRPRPPPMGRSTRAVG PAHLPSLPP in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86691 mRNA. Translation: CAA60384.1.
AC006064 Genomic DNA. No translation available.
BC038596 mRNA. Translation: AAH38596.1.
CCDSiCCDS8552.1. [Q14839-1]
RefSeqiNP_001264.2. NM_001273.3. [Q14839-1]
NP_001284482.1. NM_001297553.1.
XP_006719021.1. XM_006718958.1. [Q14839-2]
UniGeneiHs.162233.

Genome annotation databases

EnsembliENST00000357008; ENSP00000349508; ENSG00000111642. [Q14839-1]
GeneIDi1108.
KEGGihsa:1108.
UCSCiuc001qpo.4. human. [Q14839-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86691 mRNA. Translation: CAA60384.1.
AC006064 Genomic DNA. No translation available.
BC038596 mRNA. Translation: AAH38596.1.
CCDSiCCDS8552.1. [Q14839-1]
RefSeqiNP_001264.2. NM_001273.3. [Q14839-1]
NP_001284482.1. NM_001297553.1.
XP_006719021.1. XM_006718958.1. [Q14839-2]
UniGeneiHs.162233.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MM2NMR-A446-501[»]
1MM3NMR-A446-476[»]
A490-501[»]
2EE1NMR-A618-674[»]
2L5UNMR-A365-420[»]
2L75NMR-A446-501[»]
2N5NNMR-A145-225[»]
4O9IX-ray2.60X499-677[»]
ProteinModelPortaliQ14839.
SMRiQ14839.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107533. 131 interactors.
DIPiDIP-31183N.
IntActiQ14839. 46 interactors.
MINTiMINT-349766.
STRINGi9606.ENSP00000349508.

PTM databases

iPTMnetiQ14839.
PhosphoSitePlusiQ14839.
SwissPalmiQ14839.

Polymorphism and mutation databases

BioMutaiCHD4.
DMDMi311033360.

Proteomic databases

EPDiQ14839.
MaxQBiQ14839.
PaxDbiQ14839.
PeptideAtlasiQ14839.
PRIDEiQ14839.

Protocols and materials databases

DNASUi1108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357008; ENSP00000349508; ENSG00000111642. [Q14839-1]
GeneIDi1108.
KEGGihsa:1108.
UCSCiuc001qpo.4. human. [Q14839-1]

Organism-specific databases

CTDi1108.
DisGeNETi1108.
GeneCardsiCHD4.
H-InvDBHIX0201859.
HGNCiHGNC:1919. CHD4.
MIMi603277. gene.
neXtProtiNX_Q14839.
OpenTargetsiENSG00000111642.
PharmGKBiPA26455.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ14839.
KOiK11643.
PhylomeDBiQ14839.
TreeFamiTF106448.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111642-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiCHD4. human.
EvolutionaryTraceiQ14839.
GeneWikiiCHD4.
GenomeRNAii1108.
PMAP-CutDBQ14839.
PROiQ14839.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111642.
CleanExiHS_CHD4.
ExpressionAtlasiQ14839. baseline and differential.
GenevisibleiQ14839. HS.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028725. CHD4.
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:SF554. PTHR10799:SF554. 6 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.
PROSITEiPS00598. CHROMO_1. 2 hits.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiCHD4_HUMAN
AccessioniPrimary (citable) accession number: Q14839
Secondary accession number(s): Q8IXZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 2, 2010
Last modified: November 30, 2016
This is version 188 of the entry and version 2 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

Miscellaneous

One of the main antigens reacting with anti-MI-2 positive sera of dermatomyositis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.