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Database: UniProt
Entry: Q12873
LinkDB: Q12873
Original site: Q12873 
ID   CHD3_HUMAN              Reviewed;        2000 AA.
AC   Q12873; D3DTQ9; E9PG89; Q9Y4I0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 3.
DT   16-OCT-2019, entry version 208.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 3;
DE            Short=CHD-3;
DE            EC=3.6.4.12 {ECO:0000269|PubMed:30397230};
DE   AltName: Full=ATP-dependent helicase CHD3;
DE   AltName: Full=Mi-2 autoantigen 240 kDa protein;
DE   AltName: Full=Mi2-alpha;
DE   AltName: Full=Zinc finger helicase;
DE            Short=hZFH;
GN   Name=CHD3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=9688266; DOI=10.1046/j.1432-1327.1998.2540558.x;
RA   Aubry F., Mattei M.-G., Galibert F.;
RT   "Identification of a human 17p-located cDNA encoding a protein of the
RT   Snf2-like helicase family.";
RL   Eur. J. Biochem. 254:558-564(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-1966 (ISOFORM 2).
RC   TISSUE=Fetus;
RX   PubMed=9326634; DOI=10.1073/pnas.94.21.11472;
RA   Woodage T., Basrai M.A., Baxevanis A.D., Hieter P., Collins F.S.;
RT   "Characterization of the CHD family of proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11472-11477(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 121-654.
RC   TISSUE=Thymus;
RX   PubMed=7560064; DOI=10.1172/jci118218;
RA   Ge Q., Nilasena D.S., O'Brien C.A., Frank M.B., Targoff I.N.;
RT   "Molecular analysis of a major antigenic region of the 240 kD protein
RT   of Mi-2 autoantigen.";
RL   J. Clin. Invest. 96:1730-1737(1995).
RN   [6]
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.,
RA   Schreiber S.L.;
RT   "Chromatin deacetylation by an ATP-dependent nucleosome remodelling
RT   complex.";
RL   Nature 395:917-921(1998).
RN   [7]
RP   INTERACTION WITH TRIM28.
RX   PubMed=11230151; DOI=10.1101/gad.869501;
RA   Schultz D.C., Friedman J.R., Rauscher F.J. III;
RT   "Targeting histone deacetylase complexes via KRAB-zinc finger
RT   proteins: the PHD and bromodomains of KAP-1 form a cooperative unit
RT   that recruits a novel isoform of the Mi-2alpha subunit of NuRD.";
RL   Genes Dev. 15:428-443(2001).
RN   [8]
RP   INTERACTION WITH HABP4 AND SERBP1.
RX   PubMed=12505151; DOI=10.1016/s0014-5793(02)03737-7;
RA   Lemos T.A., Passos D.O., Nery F.C., Kobarg J.;
RT   "Characterization of a new family of proteins that interact with the
RT   C-terminal region of the chromatin-remodeling factor CHD-3.";
RL   FEBS Lett. 533:14-20(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-1601 AND
RP   SER-1605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1367; SER-1601
RP   AND SER-1605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [13]
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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1601 AND
RP   SER-1605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601 AND SER-1605, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [16]
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.,
RA   Buerckstuemmer T., 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-597; SER-713;
RP   SER-1601; SER-1605 AND THR-1646, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE 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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1308, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   [20]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-721, AND IDENTIFICATION BY
RP   MASS 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   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-627; LYS-1308 AND LYS-1988,
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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [22]
RP   INVOLVEMENT IN SNIBCPS, AND VARIANT SNIBCPS TRP-1169.
RX   PubMed=29463886; DOI=10.1038/s41380-018-0020-x;
RA   Eising E., Carrion-Castillo A., Vino A., Strand E.A., Jakielski K.J.,
RA   Scerri T.S., Hildebrand M.S., Webster R., Ma A., Mazoyer B.,
RA   Francks C., Bahlo M., Scheffer I.E., Morgan A.T., Shriberg L.D.,
RA   Fisher S.E.;
RT   "A set of regulatory genes co-expressed in embryonic human brain is
RT   implicated in disrupted speech development.";
RL   Mol. Psychiatry 0:0-0(2018).
RN   [23]
RP   FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN SNIBCPS, VARIANTS SNIBCPS
RP   457-GLU--ASP-2000 DEL; ARG-886; PHE-915; LYS-921; GLU-961; GLN-985;
RP   TRP-985; GLY-1109 DEL; HIS-1120; PRO-1121; ILE-1136; ARG-1158;
RP   LYS-1159; ARG-1161; TRP-1169; ARG-1171; GLN-1172; PRO-1187; PRO-1236;
RP   GLN-1342 AND LEU-1881, AND CHARACTERIZATION OF VARIANTS SNIBCPS
RP   PHE-915; PRO-1121; ARG-1158; LYS-1159; GLN-1172 AND PRO-1187.
RX   PubMed=30397230; DOI=10.1038/s41467-018-06014-6;
RA   Snijders Blok L., Rousseau J., Twist J., Ehresmann S., Takaku M.,
RA   Venselaar H., Rodan L.H., Nowak C.B., Douglas J., Swoboda K.J.,
RA   Steeves M.A., Sahai I., Stumpel C.T.R.M., Stegmann A.P.A., Wheeler P.,
RA   Willing M., Fiala E., Kochhar A., Gibson W.T., Cohen A.S.A.,
RA   Agbahovbe R., Innes A.M., Au P.Y.B., Rankin J., Anderson I.J.,
RA   Skinner S.A., Louie R.J., Warren H.E., Afenjar A., Keren B., Nava C.,
RA   Buratti J., Isapof A., Rodriguez D., Lewandowski R., Propst J.,
RA   van Essen T., Choi M., Lee S., Chae J.H., Price S., Schnur R.E.,
RA   Douglas G., Wentzensen I.M., Zweier C., Reis A., Bialer M.G.,
RA   Moore C., Koopmans M., Brilstra E.H., Monroe G.R., van Gassen K.L.I.,
RA   van Binsbergen E., Newbury-Ecob R., Bownass L., Bader I., Mayr J.A.,
RA   Wortmann S.B., Jakielski K.J., Strand E.A., Kloth K., Bierhals T.,
RA   Roberts J.D., Petrovich R.M., Machida S., Kurumizaka H., Lelieveld S.,
RA   Pfundt R., Jansen S., Deriziotis P., Faive L., Thevenon J., Assoum M.,
RA   Shriberg L., Kleefstra T., Brunner H.G., Wade P.A., Fisher S.E.,
RA   Campeau P.M.;
RT   "CHD3 helicase domain mutations cause a neurodevelopmental syndrome
RT   with macrocephaly and impaired speech and language.";
RL   Nat. Commun. 9:4619-4619(2018).
CC   -!- FUNCTION: Component of the histone deacetylase NuRD complex which
CC       participates in the remodeling of chromatin by deacetylating
CC       histones. Required for anchoring centrosomal pericentrin in both
CC       interphase and mitosis, for spindle organization and centrosome
CC       integrity. {ECO:0000269|PubMed:17626165,
CC       ECO:0000269|PubMed:30397230, 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:30397230};
CC   -!- SUBUNIT: Central component of the nucleosome remodeling and
CC       histone deacetylase (NuRD) repressive complex. Interacts with
CC       TRIM28 and SERBP1. Interacts (via its C-terminal) with HABP4.
CC       Interacts with PCNT; the interaction regulates centrosome
CC       integrity. {ECO:0000269|PubMed:11230151,
CC       ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:17626165}.
CC   -!- INTERACTION:
CC       Q99728:BARD1; NbExp=2; IntAct=EBI-523590, EBI-473181;
CC       P17844:DDX5; NbExp=4; IntAct=EBI-523590, EBI-351962;
CC       Q9Y2X7:GIT1; NbExp=2; IntAct=EBI-523590, EBI-466061;
CC       P42858:HTT; NbExp=3; IntAct=EBI-523590, EBI-466029;
CC       O60341:KDM1A; NbExp=4; IntAct=EBI-523590, EBI-710124;
CC       O75400:PRPF40A; NbExp=2; IntAct=EBI-523590, EBI-473291;
CC       Q8NC51:SERBP1; NbExp=5; IntAct=EBI-523590, EBI-523558;
CC       P61956:SUMO2; NbExp=3; IntAct=EBI-523590, EBI-473220;
CC       Q13263:TRIM28; NbExp=4; IntAct=EBI-523590, EBI-78139;
CC       O95365:ZBTB7A; NbExp=2; IntAct=EBI-523590, EBI-2795384;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17626165}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:17626165}. Note=Associates with centrosomes in
CC       interphase and mitosis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q12873-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12873-2; Sequence=VSP_017231;
CC       Name=3;
CC         IsoId=Q12873-3; Sequence=VSP_047097;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:9688266}.
CC   -!- DISEASE: Snijders Blok-Campeau syndrome (SNIBCPS) [MIM:618205]: An
CC       autosomal dominant neurodevelopmental disorder characterized by
CC       intellectual disability with a wide range of severity,
CC       developmental delay, and impaired speech and language skills.
CC       Speech-related problems include dysarthria, speech apraxia,
CC       oromotor problems, and stuttering. Additional clinical features
CC       are macrocephaly, characteristic facial features such as prominent
CC       forehead and hypertelorism, hypotonia, and joint laxity.
CC       {ECO:0000269|PubMed:29463886, ECO:0000269|PubMed:30397230}.
CC       Note=The disease is caused by mutations affecting the gene
CC       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.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB87383.1; Type=Miscellaneous discrepancy; Note=Differs from position 1967 onward for unknown reasons.; Evidence={ECO:0000305};
DR   EMBL; U91543; AAC39923.1; -; mRNA.
DR   EMBL; AC104581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90114.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90116.1; -; Genomic_DNA.
DR   EMBL; AF006515; AAB87383.1; ALT_TERM; mRNA.
DR   EMBL; U08379; AAC50228.1; -; mRNA.
DR   CCDS; CCDS32553.2; -. [Q12873-3]
DR   CCDS; CCDS32554.1; -. [Q12873-1]
DR   CCDS; CCDS32555.1; -. [Q12873-2]
DR   RefSeq; NP_001005271.2; NM_001005271.2. [Q12873-3]
DR   RefSeq; NP_001005273.1; NM_001005273.2. [Q12873-1]
DR   RefSeq; NP_005843.2; NM_005852.3. [Q12873-2]
DR   SMR; Q12873; -.
DR   BioGrid; 107532; 649.
DR   ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR   ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR   CORUM; Q12873; -.
DR   DIP; DIP-32496N; -.
DR   ELM; Q12873; -.
DR   IntAct; Q12873; 133.
DR   MINT; Q12873; -.
DR   STRING; 9606.ENSP00000369716; -.
DR   MoonDB; Q12873; Predicted.
DR   iPTMnet; Q12873; -.
DR   PhosphoSitePlus; Q12873; -.
DR   SwissPalm; Q12873; -.
DR   BioMuta; CHD3; -.
DR   DMDM; 88911273; -.
DR   EPD; Q12873; -.
DR   jPOST; Q12873; -.
DR   MassIVE; Q12873; -.
DR   MaxQB; Q12873; -.
DR   PaxDb; Q12873; -.
DR   PeptideAtlas; Q12873; -.
DR   PRIDE; Q12873; -.
DR   ProteomicsDB; 20268; -.
DR   ProteomicsDB; 58995; -. [Q12873-1]
DR   ProteomicsDB; 58996; -. [Q12873-2]
DR   Ensembl; ENST00000330494; ENSP00000332628; ENSG00000170004. [Q12873-1]
DR   Ensembl; ENST00000358181; ENSP00000350907; ENSG00000170004. [Q12873-2]
DR   Ensembl; ENST00000380358; ENSP00000369716; ENSG00000170004. [Q12873-3]
DR   GeneID; 1107; -.
DR   KEGG; hsa:1107; -.
DR   UCSC; uc002gjd.3; human. [Q12873-1]
DR   CTD; 1107; -.
DR   DisGeNET; 1107; -.
DR   GeneCards; CHD3; -.
DR   HGNC; HGNC:1918; CHD3.
DR   HPA; HPA043368; -.
DR   HPA; HPA076524; -.
DR   MalaCards; CHD3; -.
DR   MIM; 602120; gene.
DR   MIM; 618205; phenotype.
DR   neXtProt; NX_Q12873; -.
DR   OpenTargets; ENSG00000170004; -.
DR   PharmGKB; PA26454; -.
DR   eggNOG; KOG0383; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00940000158001; -.
DR   HOGENOM; HOG000231124; -.
DR   InParanoid; Q12873; -.
DR   KO; K11642; -.
DR   OMA; TWERDDM; -.
DR   OrthoDB; 54215at2759; -.
DR   PhylomeDB; Q12873; -.
DR   TreeFam; TF106448; -.
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-4551638; SUMOylation of chromatin organization proteins.
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   ChiTaRS; CHD3; human.
DR   GeneWiki; CHD3; -.
DR   GenomeRNAi; 1107; -.
DR   Pharos; Q12873; -.
DR   PRO; PR:Q12873; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000170004; Expressed in 216 organ(s), highest expression level in frontal cortex.
DR   ExpressionAtlas; Q12873; baseline and differential.
DR   Genevisible; Q12873; HS.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0003678; F:DNA helicase activity; TAS:ProtInc.
DR   GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0004386; F:helicase activity; NAS:UniProtKB.
DR   GO; GO:0070615; F:nucleosome-dependent ATPase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IMP:UniProtKB.
DR   GO; GO:0007098; P:centrosome cycle; IDA:UniProtKB.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:Ensembl.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0007051; P:spindle organization; IDA:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 2.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR012957; CHD_C2.
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; IPR023779; Chromodomain_CS.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009462; DUF1086.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR036910; HMG_box_dom_sf.
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; PF08074; CHDCT2; 1.
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_N; 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; SSF47095; SSF47095; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS00598; CHROMO_1; 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   Alternative splicing; ATP-binding; Chromatin regulator;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
KW   DNA-binding; Helicase; Hydrolase; Isopeptide bond; Mental retardation;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   2000       Chromodomain-helicase-DNA-binding protein
FT                                3.
FT                                /FTId=PRO_0000080227.
FT   DOMAIN      494    594       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      631    673       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      748    932       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1064   1229       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   ZN_FING     379    426       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     456    503       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   NP_BIND     761    768       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION     1566   1966       Required for interaction with PCNT.
FT                                {ECO:0000269|PubMed:17626165}.
FT   MOTIF       883    886       DEAH box.
FT   COMPBIAS    206    221       Poly-Ala.
FT   COMPBIAS    243    246       Poly-Pro.
FT   COMPBIAS    355    358       Poly-Lys.
FT   COMPBIAS    434    446       Poly-Glu.
FT   COMPBIAS    697    703       Poly-Lys.
FT   MOD_RES      79     79       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     308    308       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES     324    324       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983}.
FT   MOD_RES     376    376       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES     597    597       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     713    713       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1219   1219       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6PDQ2}.
FT   MOD_RES    1367   1367       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1532   1532       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES    1538   1538       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES    1601   1601       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1605   1605       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1646   1646       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CROSSLNK    120    120       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK    163    163       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK    295    295       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK    302    302       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK    627    627       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    721    721       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate. {ECO:0000244|PubMed:25114211}.
FT   CROSSLNK    721    721       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK   1222   1222       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK   1238   1238       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK   1246   1246       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK   1308   1308       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1573   1573       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK   1585   1585       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK   1876   1876       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   CROSSLNK   1988   1988       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1     32       MKAADTVILWARSKNDQLRISFPPGLCWGDRM -> MASPL
FT                                RDEEEEEEEMVVSEEEEEEEEEGDEEEEEEVEAADEDDEED
FT                                DDEGVLGRGPGHDRGRDRHSPPGCHLFPPPPPPPPPLPPPP
FT                                PPPP (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_047097.
FT   VAR_SEQ    1642   1675       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9326634,
FT                                ECO:0000303|PubMed:9688266}.
FT                                /FTId=VSP_017231.
FT   VARIANT       3      3       A -> V (in dbSNP:rs931543).
FT                                /FTId=VAR_048728.
FT   VARIANT     457   2000       Missing (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081506.
FT   VARIANT     886    886       H -> R (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081507.
FT   VARIANT     915    915       L -> F (in SNIBCPS; increased function in
FT                                chromatin remodeling).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081508.
FT   VARIANT     921    921       E -> K (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081509.
FT   VARIANT     961    961       G -> E (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081510.
FT   VARIANT     985    985       R -> Q (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081511.
FT   VARIANT     985    985       R -> W (in SNIBCPS; dbSNP:rs1555611722).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081512.
FT   VARIANT    1109   1109       Missing (in SNIBCPS; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081513.
FT   VARIANT    1120   1120       D -> H (in SNIBCPS; the patient also
FT                                carries a truncating variant in CIC; both
FT                                variants may contribute to disease
FT                                phenotype).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081514.
FT   VARIANT    1121   1121       R -> P (in SNIBCPS; decreased function in
FT                                chromatin remodeling; decreased ATPase
FT                                activity). {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081515.
FT   VARIANT    1136   1136       T -> I (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081516.
FT   VARIANT    1158   1158       W -> R (in SNIBCPS; highly decreased
FT                                function in chromatin remodeling).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081517.
FT   VARIANT    1159   1159       N -> K (in SNIBCPS; highly decreased
FT                                function in chromatin remodeling).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081518.
FT   VARIANT    1161   1161       H -> R (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081519.
FT   VARIANT    1169   1169       R -> W (in SNIBCPS).
FT                                {ECO:0000269|PubMed:29463886,
FT                                ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081520.
FT   VARIANT    1171   1171       H -> R (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081521.
FT   VARIANT    1172   1172       R -> Q (in SNIBCPS; decreased function in
FT                                chromatin remodeling; decreased ATPase
FT                                activity). {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081522.
FT   VARIANT    1187   1187       R -> P (in SNIBCPS; unknown pathological
FT                                significance; does not affect function in
FT                                chromatin remodeling; no effect on ATPase
FT                                activity). {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081523.
FT   VARIANT    1236   1236       L -> P (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081524.
FT   VARIANT    1342   1342       R -> Q (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081525.
FT   VARIANT    1881   1881       R -> L (in SNIBCPS).
FT                                {ECO:0000269|PubMed:30397230}.
FT                                /FTId=VAR_081526.
FT   CONFLICT    121    126       GEGDGG -> PHFQQK (in Ref. 5; AAC50228).
FT                                {ECO:0000305}.
FT   CONFLICT    309    312       Missing (in Ref. 5; AAC50228).
FT                                {ECO:0000305}.
FT   CONFLICT    653    653       W -> G (in Ref. 5; AAC50228).
FT                                {ECO:0000305}.
FT   CONFLICT   1704   1704       K -> N (in Ref. 1; AAC39923).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2000 AA;  226592 MW;  4494F56E5D0E7083 CRC64;
     MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR KRGPKKQKEN
     KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG RKRRRKHREK KEKKTKRRKK
     GEGDGGQKQV EQKSSATLLL TWGLEDVEHV FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI
     PMSKMMTILG AKWREFSANN PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP
     ALPPPPAADI QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG
     GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG RPGRKKKKVL
     GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA YHLVCLDPEL DRAPEGKWSC
     PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE EEDDHMEYCR VCKDGGELLC CDACISSYHI
     HCLNPPLPDI PNGEWLCPRC TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR
     PLQGRSEREF FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED
     DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL VKWRDLPYDQ
     STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK KKKELQGDGP PSSPTNDPTV
     KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK
     EGHTKGPFLV SAPLSTIINW EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG
     GKKAFKMKRE AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN
     GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE DQIKKLHDLL
     GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL TRNFEALNSR GGGNQVSLLN
     IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY EGGALIKSSG KLMLLQKMLR KLKEQGHRVL
     IFSQMTKMLD LLEDFLDYEG YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG
     LGINLATADT VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR
     KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS SVIHYDNEAI
     ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE EIEREIIKQE ENVDPDYWEK
     LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG
     RRQSKRQLRN EKDKPLPPLL ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL
     VRDLRGKTEK EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK
     KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP CTSKPATPAP
     SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP SPAPSLGERL EPRKIPLEDE
     VPGVPGEMEP EPGYRGDREK SATESTPGER GEEKPLDGQE HRERPEGETG DLGKREDVKG
     DRELRPGPRD EPRSNGRREE KTEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW
     HRRHDYWLLA GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL
     EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES LAGNKPANAV
     LHKVLNQLEE LLSDMKADVT RLPATLSRIP PIAARLQMSE RSILSRLASK GTEPHPTPAY
     PPGPYATPPG YGAAFSAAPV GALAAAGANY SQMPAGSFIT AATNGPPVLV KKEKEMVGAL
     VSDGLDRKEP RAGEVICIDD
//
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