ID CHD4_HUMAN Reviewed; 1912 AA.
AC Q14839; Q8IXZ5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 27-MAR-2024, entry version 241.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 4;
DE Short=CHD-4;
DE EC=3.6.4.12 {ECO:0000269|PubMed:28977666};
DE AltName: Full=ATP-dependent helicase CHD4;
DE AltName: Full=Mi-2 autoantigen 218 kDa protein;
DE AltName: Full=Mi2-beta;
GN Name=CHD4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-139.
RX PubMed=7575689; DOI=10.1002/art.1780381006;
RA Seelig H.P., Moosbrugger I., Ehrfeld H., Fink T., Renz M., Genth E.;
RT "The major dermatomyositis specific Mi-2 autoantigen is a presumed helicase
RT involved in transcriptional activation.";
RL Arthritis Rheum. 38:1389-1399(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION AS A COMPONENT OF THE NURD COMPLEX, AND FUNCTION.
RX PubMed=9804427; DOI=10.1038/27699;
RA Tong J.K., Hassig C.A., Schnitzler G.R., Kingston R.E., Schreiber S.L.;
RT "Chromatin deacetylation by an ATP-dependent nucleosome remodelling
RT complex.";
RL Nature 395:917-921(1998).
RN [5]
RP IDENTIFICATION IN A COMPLEX CONTAINING ATR AND HDAC2, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=10545197; DOI=10.1021/bi991614n;
RA Schmidt D.R., Schreiber S.L.;
RT "Molecular association between ATR and two components of the nucleosome
RT remodeling and deacetylating complex, HDAC2 and CHD4.";
RL Biochemistry 38:14711-14717(1999).
RN [6]
RP INTERACTION WITH IKZF1 IN THE NURD COMPLEX.
RX PubMed=10204490; DOI=10.1016/s1074-7613(00)80034-5;
RA Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S.,
RA Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.;
RT "Ikaros DNA-binding proteins direct formation of chromatin remodeling
RT complexes in lymphocytes.";
RL Immunity 10:345-355(1999).
RN [7]
RP INTERACTION WITH HDAC2; SMARCA5 AND RAD21.
RX PubMed=12198550; DOI=10.1038/nature01024;
RA Hakimi M.-A., Bochar D.A., Schmiesing J.A., Dong Y., Barak O.G.,
RA Speicher D.W., Yokomori K., Shiekhattar R.;
RT "A chromatin remodelling complex that loads cohesin onto human
RT chromosomes.";
RL Nature 418:994-998(2002).
RN [8]
RP INTERACTION WITH TRIM27.
RX PubMed=14530259; DOI=10.1074/jbc.m309198200;
RA Shimono Y., Murakami H., Kawai K., Wade P.A., Shimokata K., Takahashi M.;
RT "Mi-2 beta associates with BRG1 and RET finger protein at the distinct
RT regions with transcriptional activating and repressing abilities.";
RL J. Biol. Chem. 278:51638-51645(2003).
RN [9]
RP INTERACTION WITH BCL6, AND IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=15454082; DOI=10.1016/j.cell.2004.09.014;
RA Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M.,
RA Wade P.A.;
RT "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte
RT differentiation.";
RL Cell 119:75-86(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-1531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH PCNT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17626165; DOI=10.1091/mbc.e06-07-0604;
RA Sillibourne J.E., Delaval B., Redick S., Sinha M., Doxsey S.J.;
RT "Chromatin remodeling proteins interact with pericentrin to regulate
RT centrosome integrity.";
RL Mol. Biol. Cell 18:3667-3680(2007).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE NURD COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16428440; DOI=10.1128/mcb.26.3.843-851.2006;
RA Le Guezennec X., Vermeulen M., Brinkman A.B., Hoeijmakers W.A., Cohen A.,
RA Lasonder E., Stunnenberg H.G.;
RT "MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical
RT and functional properties.";
RL Mol. Cell. Biol. 26:843-851(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515; THR-529; SER-531 AND
RP SER-1535, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP INTERACTION WITH ZGPAT.
RX PubMed=19644445; DOI=10.1038/emboj.2009.211;
RA Li R., Zhang H., Yu W., Chen Y., Gui B., Liang J., Wang Y., Sun L.,
RA Yang X., Zhang Y., Shi L., Li Y., Shang Y.;
RT "ZIP: a novel transcription repressor, represses EGFR oncogene and
RT suppresses breast carcinogenesis.";
RL EMBO J. 28:2763-2776(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1553, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1643, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-1531; SER-1535;
RP THR-1653 AND THR-1679, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP INTERACTION WITH BRD4.
RX PubMed=21555454; DOI=10.1128/mcb.01341-10;
RA Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W.,
RA Howley P.M.;
RT "The Brd4 extraterminal domain confers transcription activation independent
RT of pTEFb by recruiting multiple proteins, including NSD3.";
RL Mol. Cell. Biol. 31:2641-2652(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-303; SER-308;
RP SER-309; SER-310; SER-319; SER-428; SER-515; THR-517; SER-1535; SER-1537
RP AND SER-1602, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; THR-703; SER-1308;
RP SER-1531; SER-1535; SER-1537; THR-1553; SER-1570; SER-1576; SER-1602;
RP THR-1653 AND THR-1679, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP INTERACTION WITH SETX.
RX PubMed=23149945; DOI=10.1128/mcb.01195-12;
RA Yuce O., West S.C.;
RT "Senataxin, defective in the neurodegenerative disorder ataxia with
RT oculomotor apraxia 2, lies at the interface of transcription and the DNA
RT damage response.";
RL Mol. Cell. Biol. 33:406-417(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-367; SER-515; SER-531;
RP SER-1535 AND THR-1653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1304; LYS-1565; LYS-1572;
RP LYS-1647 AND LYS-1670, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1304, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1647 AND LYS-1670, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [29]
RP FUNCTION, INTERACTION WITH ZMYND8; HDAC1 AND HDAC2, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=25593309; DOI=10.1101/gad.252189.114;
RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W.,
RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.;
RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of
RT transcription-associated DNA damage that promotes homologous
RT recombination.";
RL Genes Dev. 29:197-211(2015).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1304; LYS-1572; LYS-1643;
RP LYS-1647 AND LYS-1670, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [31]
RP SUBCELLULAR LOCATION.
RX PubMed=27732854; DOI=10.1016/j.celrep.2016.09.037;
RA Spruijt C.G., Luijsterburg M.S., Menafra R., Lindeboom R.G., Jansen P.W.,
RA Edupuganti R.R., Baltissen M.P., Wiegant W.W., Voelker-Albert M.C.,
RA Matarese F., Mensinga A., Poser I., Vos H.R., Stunnenberg H.G.,
RA van Attikum H., Vermeulen M.;
RT "ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-
RT Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage.";
RL Cell Rep. 17:783-798(2016).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-146; LYS-179; LYS-297;
RP LYS-304; LYS-696; LYS-711; LYS-1212; LYS-1228; LYS-1239; LYS-1304;
RP LYS-1528; LYS-1529; LYS-1565; LYS-1572; LYS-1584; LYS-1606; LYS-1617;
RP LYS-1636; LYS-1643; LYS-1647; LYS-1660; LYS-1670; LYS-1687 AND LYS-1865,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [33]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE NURD COMPLEX,
RP INTERACTION WITH CBX1; CBX3; CBX5; HDAC1; MTA1 AND RBBP7, IDENTIFICATION BY
RP MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28977666; DOI=10.1093/nar/gkx711;
RA Hoffmeister H., Fuchs A., Erdel F., Pinz S., Groebner-Ferreira R.,
RA Bruckmann A., Deutzmann R., Schwartz U., Maldonado R., Huber C.,
RA Dendorfer A.S., Rippe K., Laengst G.;
RT "CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping
RT functionality.";
RL Nucleic Acids Res. 45:10534-10554(2017).
RN [34]
RP INTERACTION WITH ZMYND8.
RX PubMed=30134174; DOI=10.1016/j.celrep.2018.07.064;
RA Ghosh K., Tang M., Kumari N., Nandy A., Basu S., Mall D.P., Rai K.,
RA Biswas D.;
RT "Positive Regulation of Transcription by Human ZMYND8 through Its
RT Association with P-TEFb Complex.";
RL Cell Rep. 24:2141-2154(2018).
RN [35]
RP IDENTIFICATION IN THE NURD COMPLEX, INTERACTION WITH GATAD2A,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=33283408; DOI=10.1111/febs.15650;
RA Spruijt C.G., Graewe C., Kleinendorst S.C., Baltissen M.P.A., Vermeulen M.;
RT "Cross-linking mass spectrometry reveals the structural topology of
RT peripheral NuRD subunits relative to the core complex.";
RL FEBS J. 288:3231-3245(2021).
RN [36]
RP INTERACTION WITH ZMYND8 AND HDAC1.
RX PubMed=36064715; DOI=10.1038/s41419-022-05212-x;
RA Adhikary S., Singh V., Choudhari R., Yang B., Adhikari S., Ramos E.I.,
RA Chaudhuri S., Roy S., Gadad S.S., Das C.;
RT "ZMYND8 suppresses MAPT213 LncRNA transcription to promote neuronal
RT differentiation.";
RL Cell Death Dis. 13:766-766(2022).
RN [37] {ECO:0007744|PDB:1MM2, ECO:0007744|PDB:1MM3}
RP STRUCTURE BY NMR OF 446-501.
RX PubMed=12842043; DOI=10.1016/s0969-2126(03)00122-9;
RA Kwan A.H.Y., Gell D.A., Verger A., Crossley M., Matthews J.M., Mackay J.P.;
RT "Engineering a protein scaffold from a PHD finger.";
RL Structure 11:803-813(2003).
RN [38]
RP STRUCTURE BY NMR OF 618-674.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the chromo domain of human chromodomain helicase-
RT DNA-binding protein 4.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [39] {ECO:0007744|PDB:6BGG}
RP STRUCTURE BY NMR OF 290-301 IN COMPLEX WITH BRD3, INTERACTION WITH BRD3,
RP AND DOMAIN.
RX PubMed=29567837; DOI=10.1074/jbc.ra117.000678;
RA Wai D.C.C., Szyszka T.N., Campbell A.E., Kwong C., Wilkinson-White L.E.,
RA Silva A.P.G., Low J.K.K., Kwan A.H., Gamsjaeger R., Chalmers J.D.,
RA Patrick W.M., Lu B., Vakoc C.R., Blobel G.A., Mackay J.P.;
RT "The BRD3 ET domain recognizes a short peptide motif through a mechanism
RT that is conserved across chromatin remodelers and transcriptional
RT regulators.";
RL J. Biol. Chem. 293:7160-7175(2018).
RN [40] {ECO:0007744|PDB:6RYR, ECO:0007744|PDB:6RYU}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH
RP NUCLEOSOME AND ZINC, FUNCTION, COFACTOR, AND INTERACTION WITH HISTONES H3
RP AND H4.
RX PubMed=32543371; DOI=10.7554/elife.56178;
RA Farnung L., Ochmann M., Cramer P.;
RT "Nucleosome-CHD4 chromatin remodeler structure maps human disease
RT mutations.";
RL Elife 9:e56178-e56178(2020).
RN [41]
RP VARIANTS SIHIWES ASP-1003; GLN-1127; LEU-1148 AND LEU-1173, SUBCELLULAR
RP LOCATION, INTERACTION WITH HDAC1, INVOLVEMENT IN SIHIWES, AND
RP CHARACTERIZATION OF VARIANTS SIHIWES GLN-1127 AND LEU-1173.
RX PubMed=27616479; DOI=10.1016/j.ajhg.2016.08.001;
RG DDD Study;
RA Weiss K., Terhal P.A., Cohen L., Bruccoleri M., Irving M., Martinez A.F.,
RA Rosenfeld J.A., Machol K., Yang Y., Liu P., Walkiewicz M., Beuten J.,
RA Gomez-Ospina N., Haude K., Fong C.T., Enns G.M., Bernstein J.A., Fan J.,
RA Gotway G., Ghorbani M., van Gassen K., Monroe G.R., van Haaften G.,
RA Basel-Vanagaite L., Yang X.J., Campeau P.M., Muenke M.;
RT "De novo mutations in CHD4, an ATP-dependent chromatin remodeler gene,
RT cause an intellectual disability syndrome with distinctive dysmorphisms.";
RL Am. J. Hum. Genet. 99:934-941(2016).
RN [42]
RP VARIANTS SIHIWES TYR-851; HIS-1068 AND ILE-1608, AND INVOLVEMENT IN
RP SIHIWES.
RX PubMed=27479907; DOI=10.1038/ng.3627;
RG INTERVAL Study;
RG UK10K Consortium;
RG Deciphering Developmental Disorders Study;
RA Sifrim A., Hitz M.P., Wilsdon A., Breckpot J., Turki S.H., Thienpont B.,
RA McRae J., Fitzgerald T.W., Singh T., Swaminathan G.J., Prigmore E.,
RA Rajan D., Abdul-Khaliq H., Banka S., Bauer U.M., Bentham J., Berger F.,
RA Bhattacharya S., Bu'Lock F., Canham N., Colgiu I.G., Cosgrove C., Cox H.,
RA Daehnert I., Daly A., Danesh J., Fryer A., Gewillig M., Hobson E., Hoff K.,
RA Homfray T., Kahlert A.K., Ketley A., Kramer H.H., Lachlan K., Lampe A.K.,
RA Louw J.J., Manickara A.K., Manase D., McCarthy K.P., Metcalfe K., Moore C.,
RA Newbury-Ecob R., Omer S.O., Ouwehand W.H., Park S.M., Parker M.J.,
RA Pickardt T., Pollard M.O., Robert L., Roberts D.J., Sambrook J.,
RA Setchfield K., Stiller B., Thornborough C., Toka O., Watkins H.,
RA Williams D., Wright M., Mital S., Daubeney P.E., Keavney B., Goodship J.,
RA Abu-Sulaiman R.M., Klaassen S., Wright C.F., Firth H.V., Barrett J.C.,
RA Devriendt K., FitzPatrick D.R., Brook J.D., Hurles M.E.;
RT "Distinct genetic architectures for syndromic and nonsyndromic congenital
RT heart defects identified by exome sequencing.";
RL Nat. Genet. 48:1060-1065(2016).
CC -!- FUNCTION: ATP-dependent helicase that binds and distorts nucleosomal
CC DNA (PubMed:28977666, PubMed:32543371). Acts as a component of the
CC histone deacetylase NuRD complex which participates in the remodeling
CC of chromatin (PubMed:17626165, PubMed:9804427, PubMed:16428440,
CC PubMed:28977666). Localizes to acetylated damaged chromatin in a
CC ZMYND8-dependent manner, to promote transcriptional repression and
CC double-strand break repair by homologous recombination
CC (PubMed:25593309). Involved in neurogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q6PDQ2, ECO:0000269|PubMed:16428440,
CC ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:25593309,
CC ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:32543371,
CC ECO:0000269|PubMed:9804427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:28977666};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:32543371, ECO:0007744|PDB:6RYR,
CC ECO:0007744|PDB:6RYU};
CC -!- SUBUNIT: Component of the nucleosome remodeling and deacetylase (NuRD)
CC repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4,
CC RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins
CC CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5
CC (PubMed:33283408, PubMed:9804427, PubMed:10204490, PubMed:15454082,
CC PubMed:28977666, PubMed:16428440). The exact stoichiometry of the NuRD
CC complex is unknown, and some subunits such as MBD2 and MBD3, GATAD2A
CC and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive NuRD
CC complexes (PubMed:28977666, PubMed:16428440, PubMed:33283408).
CC Interacts with IKFZ1; the interaction is direct and when in part of the
CC NuRD complex (By similarity). Part of a complex containing ATR and
CC HDAC2 (PubMed:10545197). Interacts with HDAC2; the interaction is
CC direct (PubMed:12198550, PubMed:25593309). Interacts with the cohesin
CC complex component RAD21; the interaction is direct (PubMed:12198550).
CC Interacts with the ISWI chromatin remodeling complex component SMARCA5;
CC the interaction is direct (PubMed:12198550). Interacts with ZGPAT; the
CC interaction is direct (PubMed:19644445). Interacts with ZMYND8; the
CC interaction is direct, appears to occur with monomeric ZMYND8, and is
CC increased following DNA damage (PubMed:30134174, PubMed:25593309,
CC PubMed:36064715). Interacts with BCL6 (PubMed:15454082). Interacts with
CC BRD4 (PubMed:21555454). Interacts with CBX1 (PubMed:28977666).
CC Interacts with CBX3 (PubMed:28977666). Interacts with CBX5
CC (PubMed:28977666). Interacts with GATAD2A (PubMed:33283408). Interacts
CC with HDAC1 (PubMed:27616479, PubMed:25593309, PubMed:36064715,
CC PubMed:28977666). Interacts with KLF1; the interaction depends on
CC sumoylation of KLF1, and leads to its transcriptional repression (By
CC similarity). Interacts with MTA1 (PubMed:28977666). Interacts with PCNT
CC (PubMed:17626165). Interacts with RBBP7 (PubMed:28977666). Interacts
CC with SETX (PubMed:23149945). Interacts with TRIM27 (PubMed:14530259).
CC Interacts with histone H3 (PubMed:32543371). Interacts with histone H4
CC (PubMed:32543371). Does not interact with PWWP2A (By similarity). Does
CC not interact with PWWP2B (By similarity). Interacts (via KIKL motif)
CC with BRD3 (via NET domain) (PubMed:29567837).
CC {ECO:0000250|UniProtKB:Q6PDQ2, ECO:0000269|PubMed:10204490,
CC ECO:0000269|PubMed:10545197, ECO:0000269|PubMed:12198550,
CC ECO:0000269|PubMed:14530259, ECO:0000269|PubMed:15454082,
CC ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:17626165,
CC ECO:0000269|PubMed:19644445, ECO:0000269|PubMed:21555454,
CC ECO:0000269|PubMed:23149945, ECO:0000269|PubMed:25593309,
CC ECO:0000269|PubMed:27616479, ECO:0000269|PubMed:28977666,
CC ECO:0000269|PubMed:29567837, ECO:0000269|PubMed:30134174,
CC ECO:0000269|PubMed:33283408, ECO:0000269|PubMed:36064715,
CC ECO:0000269|PubMed:9804427}.
CC -!- INTERACTION:
CC Q14839; Q13547: HDAC1; NbExp=11; IntAct=EBI-372916, EBI-301834;
CC Q14839; P01106: MYC; NbExp=2; IntAct=EBI-372916, EBI-447544;
CC Q14839; Q17R98: ZNF827; NbExp=2; IntAct=EBI-372916, EBI-5564776;
CC Q14839; P70326: Tbx5; Xeno; NbExp=3; IntAct=EBI-372916, EBI-8411807;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17626165,
CC ECO:0000269|PubMed:27616479, ECO:0000269|PubMed:27732854,
CC ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17626165}. Note=Associates with centrosomes in
CC interphase (By similarity). Localizes to sites of DNA damage in a
CC manner dependent on ZMYND8 and ZNF687 (PubMed:28977666,
CC PubMed:27732854). {ECO:0000250|UniProtKB:Q6PDQ2,
CC ECO:0000269|PubMed:27732854, ECO:0000269|PubMed:28977666}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14839-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14839-2; Sequence=VSP_011416;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:28977666}.
CC -!- DOMAIN: The KIKL motif recognizes and binds the NET domain of BRD3.
CC {ECO:0000269|PubMed:29567837}.
CC -!- DISEASE: Sifrim-Hitz-Weiss syndrome (SIHIWES) [MIM:617159]: An
CC autosomal dominant syndrome characterized by intellectual disability,
CC variable congenital defects affecting cardiac, skeletal, and urogenital
CC systems. Short stature, macrocephaly, hearing impairment, and facial
CC dysmorphism are present in some patients. {ECO:0000269|PubMed:27479907,
CC ECO:0000269|PubMed:27616479}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: One of the main antigens reacting with anti-MI-2
CC positive sera of dermatomyositis.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; X86691; CAA60384.1; -; mRNA.
DR EMBL; AC006064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038596; AAH38596.1; -; mRNA.
DR CCDS; CCDS8552.1; -. [Q14839-1]
DR RefSeq; NP_001264.2; NM_001273.3. [Q14839-1]
DR RefSeq; NP_001284482.1; NM_001297553.1.
DR RefSeq; XP_006719021.1; XM_006718958.1.
DR PDB; 1MM2; NMR; -; A=446-501.
DR PDB; 1MM3; NMR; -; A=446-501.
DR PDB; 2EE1; NMR; -; A=618-674.
DR PDB; 2L5U; NMR; -; A=365-420.
DR PDB; 2L75; NMR; -; A=446-501.
DR PDB; 2N5N; NMR; -; A=145-225.
DR PDB; 4O9I; X-ray; 2.60 A; X=499-677.
DR PDB; 6BGG; NMR; -; A=290-301.
DR PDB; 6Q3M; X-ray; 2.52 A; A/B/C/D=444-679.
DR PDB; 6RYR; EM; 3.10 A; W=1-1912.
DR PDB; 6RYU; EM; 4.00 A; V/W=1-1912.
DR PDB; 8D4Y; X-ray; 2.90 A; A/B=1380-1810.
DR PDBsum; 1MM2; -.
DR PDBsum; 1MM3; -.
DR PDBsum; 2EE1; -.
DR PDBsum; 2L5U; -.
DR PDBsum; 2L75; -.
DR PDBsum; 2N5N; -.
DR PDBsum; 4O9I; -.
DR PDBsum; 6BGG; -.
DR PDBsum; 6Q3M; -.
DR PDBsum; 6RYR; -.
DR PDBsum; 6RYU; -.
DR PDBsum; 8D4Y; -.
DR AlphaFoldDB; Q14839; -.
DR BMRB; Q14839; -.
DR EMDB; EMD-10058; -.
DR EMDB; EMD-10059; -.
DR SMR; Q14839; -.
DR BioGRID; 107533; 906.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q14839; -.
DR DIP; DIP-31183N; -.
DR IntAct; Q14839; 101.
DR MINT; Q14839; -.
DR STRING; 9606.ENSP00000440542; -.
DR ChEMBL; CHEMBL4105742; -.
DR GlyGen; Q14839; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14839; -.
DR MetOSite; Q14839; -.
DR PhosphoSitePlus; Q14839; -.
DR SwissPalm; Q14839; -.
DR BioMuta; CHD4; -.
DR DMDM; 311033360; -.
DR EPD; Q14839; -.
DR jPOST; Q14839; -.
DR MassIVE; Q14839; -.
DR MaxQB; Q14839; -.
DR PaxDb; 9606-ENSP00000349508; -.
DR PeptideAtlas; Q14839; -.
DR ProteomicsDB; 60204; -. [Q14839-1]
DR ProteomicsDB; 60205; -. [Q14839-2]
DR Pumba; Q14839; -.
DR ABCD; Q14839; 2 sequenced antibodies.
DR Antibodypedia; 11019; 444 antibodies from 39 providers.
DR DNASU; 1108; -.
DR Ensembl; ENST00000544040.7; ENSP00000440542.2; ENSG00000111642.16. [Q14839-1]
DR Ensembl; ENST00000645095.1; ENSP00000496634.1; ENSG00000111642.16. [Q14839-2]
DR GeneID; 1108; -.
DR KEGG; hsa:1108; -.
DR MANE-Select; ENST00000544040.7; ENSP00000440542.2; NM_001273.5; NP_001264.2.
DR UCSC; uc001qpo.4; human. [Q14839-1]
DR AGR; HGNC:1919; -.
DR CTD; 1108; -.
DR DisGeNET; 1108; -.
DR GeneCards; CHD4; -.
DR GeneReviews; CHD4; -.
DR HGNC; HGNC:1919; CHD4.
DR HPA; ENSG00000111642; Low tissue specificity.
DR MalaCards; CHD4; -.
DR MIM; 603277; gene.
DR MIM; 617159; phenotype.
DR neXtProt; NX_Q14839; -.
DR OpenTargets; ENSG00000111642; -.
DR Orphanet; 653712; CHD4-related neurodevelopmental disorder.
DR PharmGKB; PA26455; -.
DR VEuPathDB; HostDB:ENSG00000111642; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000155088; -.
DR HOGENOM; CLU_000315_22_3_1; -.
DR InParanoid; Q14839; -.
DR OMA; XLKQLEE; -.
DR OrthoDB; 2910821at2759; -.
DR PhylomeDB; Q14839; -.
DR TreeFam; TF106448; -.
DR PathwayCommons; Q14839; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; Q14839; -.
DR SIGNOR; Q14839; -.
DR BioGRID-ORCS; 1108; 551 hits in 1158 CRISPR screens.
DR ChiTaRS; CHD4; human.
DR EvolutionaryTrace; Q14839; -.
DR GeneWiki; CHD4; -.
DR GenomeRNAi; 1108; -.
DR Pharos; Q14839; Tchem.
DR PRO; PR:Q14839; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q14839; Protein.
DR Bgee; ENSG00000111642; Expressed in ventricular zone and 198 other cell types or tissues.
DR ExpressionAtlas; Q14839; baseline and differential.
DR Genevisible; Q14839; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0150048; C:cerebellar granule cell to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:ARUK-UCL.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:ARUK-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; NAS:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProt.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; NAS:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; NAS:ComplexPortal.
DR GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0072553; P:terminal button organization; IEA:Ensembl.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd18056; DEXHc_CHD4; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR IDEAL; IID00322; -.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF22; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 4; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Chromatin regulator; Cytoplasm; Cytoskeleton; Disease variant; DNA-binding;
KW Helicase; Hydrolase; Intellectual disability; Isopeptide bond;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1912
FT /note="Chromodomain-helicase-DNA-binding protein 4"
FT /id="PRO_0000080228"
FT DOMAIN 494..594
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 622..697
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 738..922
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1054..1203
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 370..417
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 449..496
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1912
FT /note="Required for interaction with PCNT"
FT /evidence="ECO:0000269|PubMed:17626165"
FT REGION 1594..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 295..298
FT /note="KIKL"
FT /evidence="ECO:0000269|PubMed:29567837"
FT MOTIF 873..876
FT /note="DEAH box"
FT COMPBIAS 52..74
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 751..758
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 517
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 703
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDQ2"
FT MOD_RES 1308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12873"
FT MOD_RES 1531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1542
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDQ2"
FT MOD_RES 1549
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDQ2"
FT MOD_RES 1553
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1643
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1653
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1679
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 618
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12873"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 711
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12873"
FT CROSSLNK 711
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1606
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1617
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1636
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1643
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1687
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1865
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1353
FT /note="R -> RGVCGRPRPPPMGRSTRAVGPAHLPSLPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011416"
FT VARIANT 139
FT /note="E -> D (in dbSNP:rs1639122)"
FT /evidence="ECO:0000269|PubMed:7575689"
FT /id="VAR_031674"
FT VARIANT 851
FT /note="S -> Y (in SIHIWES; dbSNP:rs886039916)"
FT /evidence="ECO:0000269|PubMed:27479907"
FT /id="VAR_077146"
FT VARIANT 1003
FT /note="G -> D (in SIHIWES)"
FT /evidence="ECO:0000269|PubMed:27616479"
FT /id="VAR_077147"
FT VARIANT 1068
FT /note="R -> H (in SIHIWES; dbSNP:rs886039915)"
FT /evidence="ECO:0000269|PubMed:27479907"
FT /id="VAR_077148"
FT VARIANT 1127
FT /note="R -> Q (in SIHIWES; no effect on interaction with
FT HDAC1; no effect on nuclear localization;
FT dbSNP:rs886039917)"
FT /evidence="ECO:0000269|PubMed:27616479"
FT /id="VAR_077149"
FT VARIANT 1148
FT /note="W -> L (in SIHIWES; dbSNP:rs886039919)"
FT /evidence="ECO:0000269|PubMed:27616479"
FT /id="VAR_077150"
FT VARIANT 1173
FT /note="R -> L (in SIHIWES; no effect on interaction with
FT HDAC1; no effect on nuclear localization;
FT dbSNP:rs886039918)"
FT /evidence="ECO:0000269|PubMed:27616479"
FT /id="VAR_077151"
FT VARIANT 1608
FT /note="V -> I (in SIHIWES; uncertain significance;
FT dbSNP:rs201992075)"
FT /evidence="ECO:0000269|PubMed:27479907"
FT /id="VAR_077152"
FT VARIANT 1648
FT /note="S -> L (in dbSNP:rs35512811)"
FT /id="VAR_031675"
FT VARIANT 1655
FT /note="I -> V (in dbSNP:rs16932768)"
FT /id="VAR_031676"
FT CONFLICT 34..36
FT /note="Missing (in Ref. 3; AAH38596)"
FT /evidence="ECO:0000305"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2N5N"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:2N5N"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:2N5N"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:2N5N"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:2N5N"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:6BGG"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:2L5U"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:2L5U"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:2L5U"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:2L5U"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:1MM3"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:2L75"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:6Q3M"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 502..510
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 560..566
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 568..576
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 594..599
FT /evidence="ECO:0007829|PDB:4O9I"
FT HELIX 603..611
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 623..632
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 638..644
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:6Q3M"
FT HELIX 664..675
FT /evidence="ECO:0007829|PDB:6Q3M"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 717..720
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 728..742
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 757..771
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 778..782
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 787..790
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 791..795
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 810..820
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 846..851
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 852..857
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 858..862
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 863..865
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 868..874
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 875..877
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 884..891
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 897..900
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 907..909
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 910..919
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 921..923
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 928..930
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 939..949
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 951..954
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 960..962
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 969..976
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 980..990
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 994..997
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 1003..1006
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1011..1020
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1022..1024
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1026..1030
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 1036..1038
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1042..1047
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1050..1065
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1069..1072
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1078..1089
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1093..1095
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1098..1100
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1102..1112
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1114..1116
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1121..1124
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1126..1132
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1140..1143
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1148..1150
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1151..1157
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 1158..1160
FT /evidence="ECO:0007829|PDB:6RYR"
FT STRAND 1169..1179
FT /evidence="ECO:0007829|PDB:6RYR"
FT HELIX 1180..1191
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 1192..1194
FT /evidence="ECO:0007829|PDB:6RYR"
FT TURN 1197..1199
FT /evidence="ECO:0007829|PDB:6RYR"
SQ SEQUENCE 1912 AA; 218005 MW; 765ED8485B7BBB85 CRC64;
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
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