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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri370 – 41748PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri449 – 49648PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi751 – 7588ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent DNA helicase activity Source: ProtInc
  3. DNA binding Source: ProtInc
  4. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  5. zinc ion binding Source: ProtInc

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: UniProtKB
  2. chromatin organization Source: Reactome
  3. DNA duplex unwinding Source: GOC
  4. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  5. spindle assembly Source: InterPro
  6. transcription, DNA-templated Source: UniProtKB-KW
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

ReactomeiREACT_263923. HDACs deacetylate histones.
REACT_953. 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
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1919. CHD4.

Subcellular locationi

Nucleus 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
Note: Associates with centrosomes in interphase.By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nuclear chromatin Source: UniProtKB
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: HPA
  7. NuRD complex Source: UniProtKB
  8. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19121912Chromodomain-helicase-DNA-binding protein 4PRO_0000080228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Phosphoserine2 Publications
Modified residuei303 – 3031Phosphoserine1 Publication
Modified residuei308 – 3081Phosphoserine1 Publication
Modified residuei309 – 3091Phosphoserine1 Publication
Modified residuei310 – 3101Phosphoserine1 Publication
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei367 – 3671Phosphothreonine1 Publication
Modified residuei428 – 4281Phosphoserine2 Publications
Modified residuei515 – 5151Phosphoserine3 Publications
Modified residuei517 – 5171Phosphothreonine1 Publication
Modified residuei529 – 5291Phosphothreonine1 Publication
Modified residuei531 – 5311Phosphoserine2 Publications
Modified residuei1349 – 13491Phosphoserine1 Publication
Modified residuei1531 – 15311Phosphoserine2 Publications
Modified residuei1535 – 15351Phosphoserine4 Publications
Modified residuei1537 – 15371Phosphoserine1 Publication
Modified residuei1553 – 15531Phosphothreonine1 Publication
Modified residuei1602 – 16021Phosphoserine1 Publication
Modified residuei1643 – 16431N6-acetyllysine1 Publication
Modified residuei1653 – 16531Phosphothreonine2 Publications
Modified residuei1679 – 16791Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14839.
PaxDbiQ14839.
PRIDEiQ14839.

PTM databases

PhosphoSiteiQ14839.

Miscellaneous databases

PMAP-CutDBQ14839.

Expressioni

Gene expression databases

BgeeiQ14839.
CleanExiHS_CHD4.
ExpressionAtlasiQ14839. baseline and differential.
GenevestigatoriQ14839.

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

Protein-protein interaction databases

BioGridi107533. 105 interactions.
DIPiDIP-31183N.
IntActiQ14839. 26 interactions.
MINTiMINT-349766.
STRINGi9606.ENSP00000349508.

Structurei

Secondary structure

1
1912
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni374 – 3763Combined sources
Beta strandi386 – 3894Combined sources
Helixi394 – 3974Combined sources
Helixi414 – 4174Combined sources
Beta strandi450 – 4523Combined sources
Turni453 – 4553Combined sources
Beta strandi459 – 4635Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi473 – 4786Combined sources
Turni491 – 4966Combined sources
Beta strandi629 – 6324Combined sources
Beta strandi638 – 6425Combined sources
Turni649 – 6513Combined sources
Beta strandi653 – 6564Combined sources
Helixi664 – 67310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MM2NMR-A446-501[»]
1MM3NMR-A446-476[»]
A490-501[»]
2EE1NMR-A618-674[»]
2L5UNMR-A365-420[»]
2L75NMR-A446-501[»]
ProteinModelPortaliQ14839.
SMRiQ14839. Positions 365-420, 446-501, 618-674.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini494 – 594101Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini622 – 69776Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini738 – 922185Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1054 – 1203150Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1577 – 1912336Required for interaction with PCNTAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi873 – 8764DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi50 – 5910Poly-Lys
Compositional biasi94 – 985Poly-Glu
Compositional biasi114 – 1196Poly-Lys
Compositional biasi134 – 1385Poly-Glu
Compositional biasi139 – 1446Poly-Asp
Compositional biasi227 – 2359Poly-Ala
Compositional biasi248 – 2525Poly-Pro
Compositional biasi350 – 3545Poly-Lys
Compositional biasi1052 – 10554Poly-Leu
Compositional biasi1294 – 13018Poly-Glu
Compositional biasi1665 – 16684Poly-Glu

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 fingeri370 – 41748PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri449 – 49648PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ14839.
KOiK11643.
OMAiMLLCRQL.
OrthoDBiEOG7C8GG7.
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.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10799:SF554. PTHR10799:SF554. 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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 363Missing in AAH38596 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391E → D.1 Publication
Corresponds to variant rs1639122 [ dbSNP | Ensembl ].
VAR_031674
Natural varianti1648 – 16481S → L.
Corresponds to variant rs35512811 [ dbSNP | Ensembl ].
VAR_031675
Natural varianti1655 – 16551I → V.
Corresponds to variant rs16932768 [ dbSNP | Ensembl ].
VAR_031676

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1353 – 13531R → RGVCGRPRPPPMGRSTRAVG PAHLPSLPP in isoform 2. 1 PublicationVSP_011416

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.3. human. [Q14839-1]
uc001qpp.3. human. [Q14839-2]

Polymorphism databases

DMDMi311033360.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1MM2NMR-A446-501[»]
1MM3NMR-A446-476[»]
A490-501[»]
2EE1NMR-A618-674[»]
2L5UNMR-A365-420[»]
2L75NMR-A446-501[»]
ProteinModelPortaliQ14839.
SMRiQ14839. Positions 365-420, 446-501, 618-674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107533. 105 interactions.
DIPiDIP-31183N.
IntActiQ14839. 26 interactions.
MINTiMINT-349766.
STRINGi9606.ENSP00000349508.

PTM databases

PhosphoSiteiQ14839.

Polymorphism databases

DMDMi311033360.

Proteomic databases

MaxQBiQ14839.
PaxDbiQ14839.
PRIDEiQ14839.

Protocols and materials databases

DNASUi1108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357008; ENSP00000349508; ENSG00000111642. [Q14839-1]
GeneIDi1108.
KEGGihsa:1108.
UCSCiuc001qpo.3. human. [Q14839-1]
uc001qpp.3. human. [Q14839-2]

Organism-specific databases

CTDi1108.
GeneCardsiGC12M006679.
H-InvDBHIX0201859.
HGNCiHGNC:1919. CHD4.
MIMi603277. gene.
neXtProtiNX_Q14839.
PharmGKBiPA26455.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ14839.
KOiK11643.
OMAiMLLCRQL.
OrthoDBiEOG7C8GG7.
PhylomeDBiQ14839.
TreeFamiTF106448.

Enzyme and pathway databases

ReactomeiREACT_263923. HDACs deacetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiCHD4. human.
EvolutionaryTraceiQ14839.
GeneWikiiCHD4.
GenomeRNAii1108.
NextBioi4598.
PMAP-CutDBQ14839.
PROiQ14839.
SOURCEiSearch...

Gene expression databases

BgeeiQ14839.
CleanExiHS_CHD4.
ExpressionAtlasiQ14839. baseline and differential.
GenevestigatoriQ14839.

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.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10799:SF554. PTHR10799:SF554. 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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The major dermatomyositis specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation."
    Seelig H.P., Moosbrugger I., Ehrfeld H., Fink T., Renz M., Genth E.
    Arthritis Rheum. 38:1389-1399(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-139.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Skin.
  4. "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex."
    Tong J.K., Hassig C.A., Schnitzler G.R., Kingston R.E., Schreiber S.L.
    Nature 395:917-921(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A COMPONENT OF THE NURD COMPLEX, FUNCTION.
  5. "Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4."
    Schmidt D.R., Schreiber S.L.
    Biochemistry 38:14711-14717(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX CONTAINING ATR AND HDAC2, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes."
    Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.
    Immunity 10:345-355(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKZF1 IN THE NURD COMPLEX.
  7. "Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities."
    Shimono Y., Murakami H., Kawai K., Wade P.A., Shimokata K., Takahashi M.
    J. Biol. Chem. 278:51638-51645(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM27.
  8. "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation."
    Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.
    Cell 119:75-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL6, IDENTIFICATION IN THE NURD COMPLEX.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-1531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity."
    Sillibourne J.E., Delaval B., Redick S., Sinha M., Doxsey S.J.
    Mol. Biol. Cell 18:3667-3680(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCNT, SUBCELLULAR LOCATION, FUNCTION.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515; THR-529; SER-531 AND SER-1535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "ZIP: a novel transcription repressor, represses EGFR oncogene and suppresses breast carcinogenesis."
    Li R., Zhang H., Yu W., Chen Y., Gui B., Liang J., Wang Y., Sun L., Yang X., Zhang Y., Shi L., Li Y., Shang Y.
    EMBO J. 28:2763-2776(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZGPAT.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-1531; SER-1535; THR-1653 AND THR-1679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
    Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
    Mol. Cell. Biol. 31:2641-2652(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRD4.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-303; SER-308; SER-309; SER-310; SER-319; SER-428; SER-515; THR-517; SER-1535; SER-1537 AND SER-1602, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Senataxin, defective in the neurodegenerative disorder ataxia with oculomotor apraxia 2, lies at the interface of transcription and the DNA damage response."
    Yuce O., West S.C.
    Mol. Cell. Biol. 33:406-417(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETX.
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-367; SER-515; SER-531; SER-1535 AND THR-1653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. Cited for: STRUCTURE BY NMR OF 446-501.
  24. "Solution structures of the chromo domain of human chromodomain helicase-DNA-binding protein 4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 618-674.

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: April 1, 2015
This is version 169 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

External Data

Dasty 3

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 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.