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Q14839

- CHD4_HUMAN

UniProt

Q14839 - CHD4_HUMAN

Protein

Chromodomain-helicase-DNA-binding protein 4

Gene

CHD4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    5. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    6. zinc ion binding Source: ProtInc

    GO - Biological processi

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

    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_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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1919. CHD4.

    Subcellular locationi

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

    GO - Cellular componenti

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

    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 residuei428 – 4281Phosphoserine2 Publications
    Modified residuei515 – 5151Phosphoserine2 Publications
    Modified residuei517 – 5171Phosphothreonine1 Publication
    Modified residuei529 – 5291Phosphothreonine1 Publication
    Modified residuei531 – 5311Phosphoserine1 Publication
    Modified residuei1349 – 13491Phosphoserine1 Publication
    Modified residuei1531 – 15311Phosphoserine2 Publications
    Modified residuei1535 – 15351Phosphoserine3 Publications
    Modified residuei1537 – 15371Phosphoserine1 Publication
    Modified residuei1553 – 15531Phosphothreonine1 Publication
    Modified residuei1602 – 16021Phosphoserine1 Publication
    Modified residuei1643 – 16431N6-acetyllysine1 Publication
    Modified residuei1653 – 16531Phosphothreonine1 Publication
    Modified residuei1679 – 16791Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14839.
    PaxDbiQ14839.
    PRIDEiQ14839.

    PTM databases

    PhosphoSiteiQ14839.

    Miscellaneous databases

    PMAP-CutDBQ14839.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14839.
    BgeeiQ14839.
    CleanExiHS_CHD4.
    GenevestigatoriQ14839.

    Organism-specific databases

    HPAiHPA012008.

    Interactioni

    Subunit structurei

    Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressor complex. Interacts directly with IKFZ1 in the NuRD complex. Interacts with TRIM27. Part of a complex containing ATR and HDAC2. Interacts with KLF1; the interaction depends on sumoylation of KLF1, and leads to its transcriptional repression. Interacts with ZGPAT; the interaction is direct. Interacts with BCL6, BRD4 and PCNT.7 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi107533. 83 interactions.
    DIPiDIP-31183N.
    IntActiQ14839. 24 interactions.
    MINTiMINT-349766.
    STRINGi9606.ENSP00000349508.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000231124.
    HOVERGENiHBG005326.
    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.
    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: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. Align

    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

    MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPE EDLSETETPK     50
    LKKKKKPKKP RDPKIPKSKR QKKERMLLCR QLGDSSGEGP EFVEEEEEVA 100
    LRSDSEGSDY TPGKKKKKKL GPKKEKKSKS KRKEEEEEED DDDDSKEPKS 150
    SAQLLEDWGM EDIDHVFSEE DYRTLTNYKA FSQFVRPLIA AKNPKIAVSK 200
    MMMVLGAKWR EFSTNNPFKG SSGASVAAAA AAAVAVVESM VTATEVAPPP 250
    PPVEVPIRKA KTKEGKGPNA RRKPKGSPRV PDAKKPKPKK VAPLKIKLGG 300
    FGSKRKRSSS EDDDLDVESD FDDASINSYS VSDGSTSRSS RSRKKLRTTK 350
    KKKKGEEEVT AVDGYETDHQ DYCEVCQQGG EIILCDTCPR AYHMVCLDPD 400
    MEKAPEGKWS CPHCEKEGIQ WEAKEDNSEG EEILEEVGGD LEEEDDHHME 450
    FCRVCKDGGE LLCCDTCPSS YHIHCLNPPL PEIPNGEWLC PRCTCPALKG 500
    KVQKILIWKW GQPPSPTPVP RPPDADPNTP SPKPLEGRPE RQFFVKWQGM 550
    SYWHCSWVSE LQLELHCQVM FRNYQRKNDM DEPPSGDFGG DEEKSRKRKN 600
    KDPKFAEMEE RFYRYGIKPE WMMIHRILNH SVDKKGHVHY LIKWRDLPYD 650
    QASWESEDVE IQDYDLFKQS YWNHRELMRG EEGRPGKKLK KVKLRKLERP 700
    PETPTVDPTV KYERQPEYLD ATGGTLHPYQ MEGLNWLRFS WAQGTDTILA 750
    DEMGLGKTVQ TAVFLYSLYK EGHSKGPFLV SAPLSTIINW EREFEMWAPD 800
    MYVVTYVGDK DSRAIIRENE FSFEDNAIRG GKKASRMKKE ASVKFHVLLT 850
    SYELITIDMA ILGSIDWACL IVDEAHRLKN NQSKFFRVLN GYSLQHKLLL 900
    TGTPLQNNLE ELFHLLNFLT PERFHNLEGF LEEFADIAKE DQIKKLHDML 950
    GPHMLRRLKA DVFKNMPSKT ELIVRVELSP MQKKYYKYIL TRNFEALNAR 1000
    GGGNQVSLLN VVMDLKKCCN HPYLFPVAAM EAPKMPNGMY DGSALIRASG 1050
    KLLLLQKMLK NLKEGGHRVL IFSQMTKMLD LLEDFLEHEG YKYERIDGGI 1100
    TGNMRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT VIIYDSDWNP 1150
    HNDIQAFSRA HRIGQNKKVM IYRFVTRASV EERITQVAKK KMMLTHLVVR 1200
    PGLGSKTGSM SKQELDDILK FGTEELFKDE ATDGGGDNKE GEDSSVIHYD 1250
    DKAIERLLDR NQDETEDTEL QGMNEYLSSF KVAQYVVREE EMGEEEEVER 1300
    EIIKQEESVD PDYWEKLLRH HYEQQQEDLA RNLGKGKRIR KQVNYNDGSQ 1350
    EDRDWQDDQS DNQSDYSVAS EEGDEDFDER SEAPRRPSRK GLRNDKDKPL 1400
    PPLLARVGGN IEVLGFNARQ RKAFLNAIMR YGMPPQDAFT TQWLVRDLRG 1450
    KSEKEFKAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS 1500
    LIRKKVQEFE HVNGRWSMPE LAEVEENKKM SQPGSPSPKT PTPSTPGDTQ 1550
    PNTPAPVPPA EDGIKIEENS LKEEESIEGE KEVKSTAPET AIECTQAPAP 1600
    ASEDEKVVVE PPEGEEKVEK AEVKERTEEP METEPKGAAD VEKVEEKSAI 1650
    DLTPIVVEDK EEKKEEEEKK EVMLQNGETP KDLNDEKQKK NIKQRFMFNI 1700
    ADGGFTELHS LWQNEERAAT VTKKTYEIWH RRHDYWLLAG IINHGYARWQ 1750
    DIQNDPRYAI LNEPFKGEMN RGNFLEIKNK FLARRFKLLE QALVIEEQLR 1800
    RAAYLNMSED PSHPSMALNT RFAEVECLAE SHQHLSKESM AGNKPANAVL 1850
    HKVLKQLEEL LSDMKADVTR LPATIARIPP VAVRLQMSER NILSRLANRA 1900
    PEPTPQQVAQ QQ 1912
    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:
    EMBL
    GenBank
    DDBJ
    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_001273.2. [Q14839-1]
    XP_006719021.1. XM_006718958.1. [Q14839-2]
    UniGeneiHs.162233.

    Genome annotation databases

    EnsembliENST00000357008; ENSP00000349508; ENSG00000111642. [Q14839-1]
    ENST00000544484; ENSP00000440392; ENSG00000111642.
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X86691 mRNA. Translation: CAA60384.1 .
    AC006064 Genomic DNA. No translation available.
    BC038596 mRNA. Translation: AAH38596.1 .
    CCDSi CCDS8552.1. [Q14839-1 ]
    RefSeqi NP_001264.2. NM_001273.2. [Q14839-1 ]
    XP_006719021.1. XM_006718958.1. [Q14839-2 ]
    UniGenei Hs.162233.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MM2 NMR - A 446-501 [» ]
    1MM3 NMR - A 446-476 [» ]
    A 490-501 [» ]
    2EE1 NMR - A 618-674 [» ]
    2L5U NMR - A 365-420 [» ]
    2L75 NMR - A 446-501 [» ]
    ProteinModelPortali Q14839.
    SMRi Q14839. Positions 365-420, 446-501, 618-674.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107533. 83 interactions.
    DIPi DIP-31183N.
    IntActi Q14839. 24 interactions.
    MINTi MINT-349766.
    STRINGi 9606.ENSP00000349508.

    PTM databases

    PhosphoSitei Q14839.

    Polymorphism databases

    DMDMi 311033360.

    Proteomic databases

    MaxQBi Q14839.
    PaxDbi Q14839.
    PRIDEi Q14839.

    Protocols and materials databases

    DNASUi 1108.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357008 ; ENSP00000349508 ; ENSG00000111642 . [Q14839-1 ]
    ENST00000544484 ; ENSP00000440392 ; ENSG00000111642 .
    GeneIDi 1108.
    KEGGi hsa:1108.
    UCSCi uc001qpo.3. human. [Q14839-1 ]
    uc001qpp.3. human. [Q14839-2 ]

    Organism-specific databases

    CTDi 1108.
    GeneCardsi GC12M006679.
    H-InvDB HIX0201859.
    HGNCi HGNC:1919. CHD4.
    HPAi HPA012008.
    MIMi 603277. gene.
    neXtProti NX_Q14839.
    PharmGKBi PA26455.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000231124.
    HOVERGENi HBG005326.
    KOi K11643.
    OMAi MLLCRQL.
    OrthoDBi EOG7C8GG7.
    PhylomeDBi Q14839.
    TreeFami TF106448.

    Enzyme and pathway databases

    Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    ChiTaRSi CHD4. human.
    EvolutionaryTracei Q14839.
    GeneWikii CHD4.
    GenomeRNAii 1108.
    NextBioi 4598.
    PMAP-CutDB Q14839.
    PROi Q14839.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14839.
    Bgeei Q14839.
    CleanExi HS_CHD4.
    Genevestigatori Q14839.

    Family and domain databases

    Gene3Di 3.30.40.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProi IPR028725. CHD4.
    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:SF554. PTHR10799:SF554. 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 PS00598. 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 ]
    ProtoNeti Search...

    Publicationsi

    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(1995) [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(2006) [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(2004) [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(1998) [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(1999) [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(1999) [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(2003) [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(2004) [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(2006) [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(2007) [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(2009) [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(2009) [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(2009) [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(2009) [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(2010) [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(2011) [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(2011) [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. Cited for: STRUCTURE BY NMR OF 446-501.
    22. "Solution structures of the chromo domain of human chromodomain helicase-DNA-binding protein 4."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-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: October 1, 2014
    This is version 164 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