Details for: CHD4

Gene ID: 1108

Symbol: CHD4

Ensembl ID: ENSG00000111642

Description: chromodomain helicase DNA binding protein 4

Associated with

Other Information

Genular Protein ID: 3165157091

Symbol: CHD4_HUMAN

Name: Chromodomain-helicase-DNA-binding protein 4

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 7575689

Title: The major dermatomyositis specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation.

PubMed ID: 7575689

DOI: 10.1002/art.1780381006

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9804427

Title: Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex.

PubMed ID: 9804427

DOI: 10.1038/27699

PubMed ID: 10545197

Title: Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4.

PubMed ID: 10545197

DOI: 10.1021/bi991614n

PubMed ID: 10204490

Title: Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes.

PubMed ID: 10204490

DOI: 10.1016/s1074-7613(00)80034-5

PubMed ID: 12198550

Title: A chromatin remodelling complex that loads cohesin onto human chromosomes.

PubMed ID: 12198550

DOI: 10.1038/nature01024

PubMed ID: 14530259

Title: Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities.

PubMed ID: 14530259

DOI: 10.1074/jbc.m309198200

PubMed ID: 15454082

Title: MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation.

PubMed ID: 15454082

DOI: 10.1016/j.cell.2004.09.014

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17626165

Title: Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity.

PubMed ID: 17626165

DOI: 10.1091/mbc.e06-07-0604

PubMed ID: 16428440

Title: MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties.

PubMed ID: 16428440

DOI: 10.1128/mcb.26.3.843-851.2006

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19644445

Title: ZIP: a novel transcription repressor, represses EGFR oncogene and suppresses breast carcinogenesis.

PubMed ID: 19644445

DOI: 10.1038/emboj.2009.211

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21555454

Title: The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3.

PubMed ID: 21555454

DOI: 10.1128/mcb.01341-10

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23149945

Title: Senataxin, defective in the neurodegenerative disorder ataxia with oculomotor apraxia 2, lies at the interface of transcription and the DNA damage response.

PubMed ID: 23149945

DOI: 10.1128/mcb.01195-12

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25593309

Title: Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination.

PubMed ID: 25593309

DOI: 10.1101/gad.252189.114

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 27732854

Title: ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage.

PubMed ID: 27732854

DOI: 10.1016/j.celrep.2016.09.037

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 28977666

Title: CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality.

PubMed ID: 28977666

DOI: 10.1093/nar/gkx711

PubMed ID: 30134174

Title: Positive Regulation of Transcription by Human ZMYND8 through Its Association with P-TEFb Complex.

PubMed ID: 30134174

DOI: 10.1016/j.celrep.2018.07.064

PubMed ID: 33283408

Title: Cross-linking mass spectrometry reveals the structural topology of peripheral NuRD subunits relative to the core complex.

PubMed ID: 33283408

DOI: 10.1111/febs.15650

PubMed ID: 36064715

Title: ZMYND8 suppresses MAPT213 LncRNA transcription to promote neuronal differentiation.

PubMed ID: 36064715

DOI: 10.1038/s41419-022-05212-x

PubMed ID: 12842043

Title: Engineering a protein scaffold from a PHD finger.

PubMed ID: 12842043

DOI: 10.1016/s0969-2126(03)00122-9

PubMed ID: 32543371

Title: Nucleosome-CHD4 chromatin remodeler structure maps human disease mutations.

PubMed ID: 32543371

DOI: 10.7554/elife.56178

PubMed ID: 27616479

Title: De novo mutations in CHD4, an ATP-dependent chromatin remodeler gene, cause an intellectual disability syndrome with distinctive dysmorphisms.

PubMed ID: 27616479

DOI: 10.1016/j.ajhg.2016.08.001

PubMed ID: 27479907

Title: Distinct genetic architectures for syndromic and nonsyndromic congenital heart defects identified by exome sequencing.

PubMed ID: 27479907

DOI: 10.1038/ng.3627

Sequence Information:

  • Length: 1912
  • Mass: 218005
  • Checksum: 765ED8485B7BBB85
  • Sequence:
  • MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPE EDLSETETPK LKKKKKPKKP 
    RDPKIPKSKR QKKERMLLCR QLGDSSGEGP EFVEEEEEVA LRSDSEGSDY TPGKKKKKKL 
    GPKKEKKSKS KRKEEEEEED DDDDSKEPKS SAQLLEDWGM EDIDHVFSEE DYRTLTNYKA 
    FSQFVRPLIA AKNPKIAVSK MMMVLGAKWR EFSTNNPFKG SSGASVAAAA AAAVAVVESM 
    VTATEVAPPP PPVEVPIRKA KTKEGKGPNA RRKPKGSPRV PDAKKPKPKK VAPLKIKLGG 
    FGSKRKRSSS EDDDLDVESD FDDASINSYS VSDGSTSRSS RSRKKLRTTK KKKKGEEEVT 
    AVDGYETDHQ DYCEVCQQGG EIILCDTCPR AYHMVCLDPD MEKAPEGKWS CPHCEKEGIQ 
    WEAKEDNSEG EEILEEVGGD LEEEDDHHME FCRVCKDGGE LLCCDTCPSS YHIHCLNPPL 
    PEIPNGEWLC PRCTCPALKG KVQKILIWKW GQPPSPTPVP RPPDADPNTP SPKPLEGRPE 
    RQFFVKWQGM SYWHCSWVSE LQLELHCQVM FRNYQRKNDM DEPPSGDFGG DEEKSRKRKN 
    KDPKFAEMEE RFYRYGIKPE WMMIHRILNH SVDKKGHVHY LIKWRDLPYD QASWESEDVE 
    IQDYDLFKQS YWNHRELMRG EEGRPGKKLK KVKLRKLERP PETPTVDPTV KYERQPEYLD 
    ATGGTLHPYQ MEGLNWLRFS WAQGTDTILA DEMGLGKTVQ TAVFLYSLYK EGHSKGPFLV 
    SAPLSTIINW EREFEMWAPD MYVVTYVGDK DSRAIIRENE FSFEDNAIRG GKKASRMKKE 
    ASVKFHVLLT SYELITIDMA ILGSIDWACL IVDEAHRLKN NQSKFFRVLN GYSLQHKLLL 
    TGTPLQNNLE ELFHLLNFLT PERFHNLEGF LEEFADIAKE DQIKKLHDML GPHMLRRLKA 
    DVFKNMPSKT ELIVRVELSP MQKKYYKYIL TRNFEALNAR GGGNQVSLLN VVMDLKKCCN 
    HPYLFPVAAM EAPKMPNGMY DGSALIRASG KLLLLQKMLK NLKEGGHRVL IFSQMTKMLD 
    LLEDFLEHEG YKYERIDGGI TGNMRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT 
    VIIYDSDWNP HNDIQAFSRA HRIGQNKKVM IYRFVTRASV EERITQVAKK KMMLTHLVVR 
    PGLGSKTGSM SKQELDDILK FGTEELFKDE ATDGGGDNKE GEDSSVIHYD DKAIERLLDR 
    NQDETEDTEL QGMNEYLSSF KVAQYVVREE EMGEEEEVER EIIKQEESVD PDYWEKLLRH 
    HYEQQQEDLA RNLGKGKRIR KQVNYNDGSQ EDRDWQDDQS DNQSDYSVAS EEGDEDFDER 
    SEAPRRPSRK GLRNDKDKPL PPLLARVGGN IEVLGFNARQ RKAFLNAIMR YGMPPQDAFT 
    TQWLVRDLRG KSEKEFKAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS 
    LIRKKVQEFE HVNGRWSMPE LAEVEENKKM SQPGSPSPKT PTPSTPGDTQ PNTPAPVPPA 
    EDGIKIEENS LKEEESIEGE KEVKSTAPET AIECTQAPAP ASEDEKVVVE PPEGEEKVEK 
    AEVKERTEEP METEPKGAAD VEKVEEKSAI DLTPIVVEDK EEKKEEEEKK EVMLQNGETP 
    KDLNDEKQKK NIKQRFMFNI ADGGFTELHS LWQNEERAAT VTKKTYEIWH RRHDYWLLAG 
    IINHGYARWQ DIQNDPRYAI LNEPFKGEMN RGNFLEIKNK FLARRFKLLE QALVIEEQLR 
    RAAYLNMSED PSHPSMALNT RFAEVECLAE SHQHLSKESM AGNKPANAVL HKVLKQLEEL 
    LSDMKADVTR LPATIARIPP VAVRLQMSER NILSRLANRA PEPTPQQVAQ QQ

Genular Protein ID: 700169024

Symbol: F5GWX5_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.O114.044792

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 1905
  • Mass: 217103
  • Checksum: D7B59A71C25EB701
  • Sequence:
  • MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPE EDLSETETPK LKKKKKPKKP 
    RDPKIPKSKR QKKELGDSSG EGPEFVEEEE EVALRSDSEG SDYTPGKKKK KKLGPKKEKK 
    SKSKRKEEEE EEDDDDDSKE PKSSAQLLED WGMEDIDHVF SEEDYRTLTN YKAFSQFVRP 
    LIAAKNPKIA VSKMMMVLGA KWREFSTNNP FKGSSGASVA AAAAAAVAVV ESMVTATEVA 
    PPPPPVEVPI RKAKTKEGKG PNARRKPKGS PRVPDAKKPK PKKVAPLKIK LGGFGSKRKR 
    SSSEDDDLDV ESDFDDASIN SYSVSDGSTS RSSRSRKKLR TTKKKKKGEE EVTAVDGYET 
    DHQDYCEVCQ QGGEIILCDT CPRAYHMVCL DPDMEKAPEG KWSCPHCEKE GIQWEAKEDN 
    SEGEEILEEV GGDLEEEDDH HMEFCRVCKD GGELLCCDTC PSSYHIHCLN PPLPEIPNGE 
    WLCPRCTCPA LKGKVQKILI WKWGQPPSPT PVPRPPDADP NTPSPKPLEG RPERQFFVKW 
    QGMSYWHCSW VSELQLELHC QVMFRNYQRK NDMDEPPSGD FGGDEEKSRK RKNKDPKFAE 
    MEERFYRYGI KPEWMMIHRI LNHSVDKKGH VHYLIKWRDL PYDQASWESE DVEIQDYDLF 
    KQSYWNHREL MRGEEGRPGK KLKKVKLRKL ERPPETPTVD PTVKYERQPE YLDATGGTLH 
    PYQMEGLNWL RFSWAQGTDT ILADEMGLGK TVQTAVFLYS LYKEGHSKGP FLVSAPLSTI 
    INWEREFEMW APDMYVVTYV GDKDSRAIIR ENEFSFEDNA IRGGKKASRM KKEASVKFHV 
    LLTSYELITI DMAILGSIDW ACLIVDEAHR LKNNQSKFFR VLNGYSLQHK LLLTGTPLQN 
    NLEELFHLLN FLTPERFHNL EGFLEEFADI AKEDQIKKLH DMLGPHMLRR LKADVFKNMP 
    SKTELIVRVE LSPMQKKYYK YILTRNFEAL NARGGGNQVS LLNVVMDLKK CCNHPYLFPV 
    AAMEAPKMPN GMYDGSALIR ASGKLLLLQK MLKNLKEGGH RVLIFSQMTK MLDLLEDFLE 
    HEGYKYERID GGITGNMRQE AIDRFNAPGA QQFCFLLSTR AGGLGINLAT ADTVIIYDSD 
    WNPHNDIQAF SRAHRIGQNK KVMIYRFVTR ASVEERITQV AKKKMMLTHL VVRPGLGSKT 
    GSMSKQELDD ILKFGTEELF KDEATDGGGD NKEGEDSSVI HYDDKAIERL LDRNQDETED 
    TELQGMNEYL SSFKVAQYVV REEEMGEEEE VEREIIKQEE SVDPDYWEKL LRHHYEQQQE 
    DLARNLGKGK RIRKQVNYND GSQEDRDWQD DQSDNQSDYS VASEEGDEDF DERSEAPRRP 
    SRKGLRNDKD KPLPPLLARV GGNIEVLGFN ARQRKAFLNA IMRYGMPPQD AFTTQWLVRD 
    LRGKSEKEFK AYVSLFMRHL CEPGADGAET FADGVPREGL SRQHVLTRIG VMSLIRKKVQ 
    EFEHVNGRWS MPELAEVEEN KKMSQPGSPS PKTPTPSTPG DTQPNTPAPV PPAEDGIKIE 
    ENSLKEEESI EGEKEVKSTA PETAIECTQA PAPASEDEKV VVEPPEGEEK VEKAEVKERT 
    EEPMETEPKG AADVEKVEEK SAIDLTPIVV EDKEEKKEEE EKKEVMLQNG ETPKDLNDEK 
    QKKNIKQRFM FNIADGGFTE LHSLWQNEER AATVTKKTYE IWHRRHDYWL LAGIINHGYA 
    RWQDIQNDPR YAILNEPFKG EMNRGNFLEI KNKFLARRFK LLEQALVIEE QLRRAAYLNM 
    SEDPSHPSMA LNTRFAEVEC LAESHQHLSK ESMAGNKPAN AVLHKVLKQL EELLSDMKAD 
    VTRLPATIAR IPPVAVRLQM SERNILSRLA NRAPEPTPQQ VAQQQ

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.