ID A0A2R8Y8C1_HUMAN Unreviewed; 1669 AA. AC A0A2R8Y8C1; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 19-JAN-2022, entry version 23. DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551}; DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551}; DE Flags: Fragment; GN Name=CHD4 {ECO:0000313|Ensembl:ENSP00000496707}; 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:ENSP00000496707, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000496707, 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: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 [4] {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 [5] {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 [6] {ECO:0000313|Ensembl:ENSP00000496707} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2018) to UniProtKB. 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:0000256|ARBA:ARBA00001665}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CC {ECO:0000256|ARBA:ARBA00007025}. 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 SMR; A0A2R8Y8C1; -. DR PeptideAtlas; A0A2R8Y8C1; -. DR Antibodypedia; 11019; 366 antibodies from 39 providers. DR Ensembl; ENST00000644289; ENSP00000496707; ENSG00000111642. DR HGNC; HGNC:1919; CHD4. DR OpenTargets; ENSG00000111642; -. DR VEuPathDB; HostDB:ENSG00000111642; -. DR GeneTree; ENSGT00940000155088; -. DR ChiTaRS; CHD4; human. DR Proteomes; UP000005640; Chromosome 12. DR ExpressionAtlas; A0A2R8Y8C1; baseline and differential. DR GO; GO:0043233; C:organelle lumen; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 2. DR Gene3D; 3.40.50.10810; -; 1. DR Gene3D; 3.40.50.300; -; 1. 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; 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 Pfam; PF08073; CHDNT; 1. DR Pfam; PF00385; Chromo; 1. DR Pfam; PF06461; DUF1086; 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; SSF52540; SSF52540; 2. DR SUPFAM; SSF54160; SSF54160; 2. DR SUPFAM; SSF57903; SSF57903; 1. 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Proteomics identification {ECO:0007829|EPD:A0A2R8Y8C1, KW ECO:0007829|MaxQB:A0A2R8Y8C1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00146}. FT DOMAIN 359..406 FT /note="PHD-type" FT /evidence="ECO:0000259|PROSITE:PS50016" FT DOMAIN 438..485 FT /note="PHD-type" FT /evidence="ECO:0000259|PROSITE:PS50016" FT DOMAIN 518..575 FT /note="Chromo" FT /evidence="ECO:0000259|PROSITE:PS50013" FT DOMAIN 611..646 FT /note="Chromo" FT /evidence="ECO:0000259|PROSITE:PS50013" FT DOMAIN 727..911 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1043..1192 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 1..146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 232..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 499..527 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 567..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1318..1420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1542..1669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1277..1297 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 48..62 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..91 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 246..278 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 312..326 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 502..523 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1318..1336 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1396..1417 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1553..1575 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1582..1604 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1623..1669 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000496707" FT NON_TER 1669 FT /evidence="ECO:0000313|Ensembl:ENSP00000496707" SQ SEQUENCE 1669 AA; 189386 MW; 1559BE9F943A5BB1 CRC64; LGSPSPCSAG SEEEDMDALL NNSLPPPHPE NEEDPEEDLS ETETPKLKKK KKPKKPRDPK IPKSKRQKKE LGDSSGEGPE FVEEEEEVAL RSDSEGSDYT PGKKKKKKLG PKKEKKSKSK RKEEEEEEDD DDDSKEPKSS AQLLEDWGME DIDHVFSEED YRTLTNYKAF SQFVRPLIAA KNPKIAVSKM MMVLGAKWRE FSTNNPFKGS SGASVAAAAA AAVAVVESMV TATEVAPPPP PVEVPIRKAK TKEGKGPNAR RKPKGSPRVP DAKKPKPKKV APLKIKLGGF GSKRKRSSSE DDDLDVESDF DDASINSYSV SDGSTSRSSR SRKKLRTTKK KKKGEEEVTA VDGYETDHQD YCEVCQQGGE IILCDTCPRA YHMVCLDPDM EKAPEGKWSC PHCEKEGIQW EAKEDNSEGE EILEEVGGDL EEEDDHHMEF CRVCKDGGEL LCCDTCPSSY HIHCLNPPLP EIPNGEWLCP RCTCPALKGK VQKILIWKWG QPPSPTPVPR PPDADPNTPS PKPLEGRPER QFFVKWQGMS YWHCSWVSEL QLELHCQVMF RNYQRKNDMD EPPSGDFGGD EEKSRKRKNK DPKFAEMEER FYRYGIKPEW MMIHRILNHS VDKKGHVHYL IKWRDLPYDQ ASWESEDVEI QDYDLFKQSY WNHRELMRGE EGRPGKKLKK VKLRKLERPP ETPTVDPTVK YERQPEYLDA TGGTLHPYQM EGLNWLRFSW AQGTDTILAD EMGLGKTVQT AVFLYSLYKE GHSKGPFLVS APLSTIINWE REFEMWAPDM YVVTYVGDKD SRAIIRENEF SFEDNAIRGG KKASRMKKEA SVKFHVLLTS YELITIDMAI LGSIDWACLI VDEAHRLKNN QSKFFRVLNG YSLQHKLLLT GTPLQNNLEE LFHLLNFLTP ERFHNLEGFL EEFADIAKED QIKKLHDMLG PHMLRRLKAD VFKNMPSKTE LIVRVELSPM QKKYYKYILT RNFEALNARG GGNQVSLLNV VMDLKKCCNH PYLFPVAAME APKMPNGMYD GSALIRASGK LLLLQKMLKN LKEGGHRVLI FSQMTKMLDL LEDFLEHEGY KYERIDGGIT GNMRQEAIDR FNAPGAQQFC FLLSTRAGGL GINLATADTV IIYDSDWNPH NDIQAFSRAH RIGQNKKVMI YRFVTRASVE ERITQVAKKK MMLTHLVVRP GLGSKTGSMS KQELDDILKF GTEELFKDEA TDGGGDNKEG EDSSVIHYDD KAIERLLDRN QDETEDTELQ GMNEYLSSFK VAQYVVREEE MGEEEEVERE IIKQEESVDP DYWEKLLRHH YEQQQEDLAR NLGKGKRIRK QVNYNDGSQE DRGVCGRPRP PPMGRSTRAV GPAHLPSLPP DWQDDQSDNQ SDYSVASEEG DEDFDERSEA PRRPSRKGLR NDKDKPLPPL LARVGGNIEV LGFNARQRKA FLNAIMRYGM PPQDAFTTQW LVRDLRGKSE KEFKAYVSLF MRHLCEPGAD GAETFADGVP REGLSRQHVL TRIGVMSLIR KKVQEFEHVN GRWSMPELAE VEENKKMSQP GSPSPKTPTP STPGDTQPNT PAPVPPAEDG IKIEENSLKE EESIEGEKEV KSTAPETAIE CTQAPAPASE DEKVVVEPPE GEEKVEKAEV KERTEEPMET EPKGAADVEK VEEKSAIDL //