ID A0A2R8Y4X2_HUMAN Unreviewed; 1262 AA. AC A0A2R8Y4X2; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 24-JUL-2024, entry version 35. DE SubName: Full=Chromodomain helicase DNA binding protein 4 {ECO:0000313|Ensembl:ENSP00000494126.1}; DE Flags: Fragment; GN Name=CHD4 {ECO:0000313|Ensembl:ENSP00000494126.1}; 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 {ECO:0000313|Ensembl:ENSP00000494126.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RG Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team; 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., 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., null.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [2] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS 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 [3] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [4] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [5] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; 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 [6] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [7] {ECO:0007829|PubMed:25218447} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; 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 [8] {ECO:0007829|PubMed:25772364} 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 [9] {ECO:0007829|PubMed:25755297} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.O114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson 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 [10] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [11] {ECO:0000313|Ensembl:ENSP00000494126.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2024) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC006064; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR MassIVE; A0A2R8Y4X2; -. DR PeptideAtlas; A0A2R8Y4X2; -. DR Antibodypedia; 11019; 416 antibodies from 40 providers. DR Ensembl; ENST00000647483.1; ENSP00000494126.1; ENSG00000111642.16. DR HGNC; HGNC:1919; CHD4. DR VEuPathDB; HostDB:ENSG00000111642; -. DR GeneTree; ENSGT00940000155088; -. DR ChiTaRS; CHD4; human. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000111642; Expressed in ventricular zone and 198 other cell types or tissues. DR ExpressionAtlas; A0A2R8Y4X2; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR CDD; cd18056; DEXHc_CHD4; 1. DR CDD; cd18793; SF2_C_SNF; 1. 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 InterPro; IPR012957; CHD_C2. DR InterPro; IPR009462; CHD_II_SANT-like. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR009463; DUF1087. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C-like. 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 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; PF06465; DUF1087; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00176; SNF2-rel_dom; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM01146; DUF1086; 1. DR SMART; SM01147; DUF1087; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A2R8Y4X2, KW ECO:0007829|ProteomicsDB:A0A2R8Y4X2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 72..256 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 388..537 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 678..751 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 870..956 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 678..710 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 729..750 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 886..908 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 915..937 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000494126.1" SQ SEQUENCE 1262 AA; 144231 MW; FB46CC83508D9464 CRC64; XKQSYWNHRE LMRGEEGRPG KKLKKVKLRK LERPPETPTV DPTVKYERQP EYLDATGGTL HPYQMEGLNW LRFSWAQGTD TILADEMGLG KTVQTAVFLY SLYKEGHSKG PFLVSAPLST IINWEREFEM WAPDMYVVTY VGDKDSRAII RENEFSFEDN AIRGGKKASR MKKEASVKFH VLLTSYELIT IDMAILGSID WACLIVDEAH RLKNNQSKFF RVLNGYSLQH KLLLTGTPLQ NNLEELFHLL NFLTPERFHN LEGFLEEFAD IAKEDQIKKL HDMLGPHMLR RLKADVFKNM PSKTELIVRV ELSPMQKKYY KYILTRNFEA LNARGGGNQV SLLNVVMDLK KCCNHPYLFP VAAMEAPKMP NGMYDGSALI RASGKLLLLQ KMLKNLKEGG HRVLIFSQMT KMLDLLEDFL EHEGYKYERI DGGITGNMRQ EAIDRFNAPG AQQFCFLLST RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRIGQN KKVMIYRFVT RASVEERITQ VAKKKMMLTH LVVRPGLGSK TGSMSKQELD DILKFGTEEL FKDEATDGGE VVRNLRFGVG LGLSKGGDNK EGEDSSVIHY DDKAIERLLD RNQDETEDTE LQGMNEYLSS FKVAQYVVRE EEMGEEEVER 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 //