CHD5_HUMAN
ID CHD5_HUMAN Reviewed; 1954 AA.
AC Q8TDI0; O75032; Q5TG89; Q7LGH2; Q9UFR9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 5;
DE Short=CHD-5;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD5;
GN Name=CHD5 {ECO:0000312|EMBL:AAL98962.1}; Synonyms=KIAA0444;
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] {ECO:0000305, ECO:0000312|EMBL:AAL98962.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12592387; DOI=10.1038/sj.onc.1206211;
RA Thompson P.M., Gotoh T., Kok M., White P.S., Brodeur G.M.;
RT "CHD5, a new member of the chromodomain gene family, is preferentially
RT expressed in the nervous system.";
RL Oncogene 22:1002-1011(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1954, AND VARIANT PRO-1539.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 977-1954, AND VARIANT PRO-1539.
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [5]
RP DISEASE.
RX PubMed=17289567; DOI=10.1016/j.cell.2006.11.052;
RA Bagchi A., Papazoglu C., Wu Y., Capurso D., Brodt M., Francis D.,
RA Bredel M., Vogel H., Mills A.A.;
RT "CHD5 is a tumor suppressor at human 1p36.";
RL Cell 128:459-475(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21931736; DOI=10.1371/journal.pone.0024515;
RA Potts R.C., Zhang P., Wurster A.L., Precht P., Mughal M.R., Wood W.H.,
RA Zhang Y., Becker K.G., Mattson M.P., Pazin M.J.;
RT "CHD5, a brain-specific paralog of Mi2 chromatin remodeling enzymes,
RT regulates expression of neuronal genes.";
RL PLoS ONE 6:E24515-E24515(2011).
RN [7]
RP FUNCTION AS A TRANSCRIPTIONAL REGULATOR, FUNCTION IN NEURON
RP DIFFERENTIATION, INTERACTION WITH HISTONE H3K27ME3, SUBCELLULAR LOCATION,
RP CHROMO DOMAINS, AND MUTAGENESIS OF LEU-518 AND TYR-619.
RX PubMed=23948251; DOI=10.1016/j.devcel.2013.07.008;
RA Egan C.M., Nyman U., Skotte J., Streubel G., Turner S., O'Connell D.J.,
RA Rraklli V., Dolan M.J., Chadderton N., Hansen K., Farrar G.J., Helin K.,
RA Holmberg J., Bracken A.P.;
RT "CHD5 is required for neurogenesis and has a dual role in facilitating gene
RT expression and polycomb gene repression.";
RL Dev. Cell 26:223-236(2013).
RN [8]
RP METHYLATION AT GLN-1390, AND MUTAGENESIS OF GLN-1390.
RX PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA Kusevic D., Kudithipudi S., Jeltsch A.;
RT "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT identification of novel substrates.";
RL J. Biol. Chem. 291:6124-6133(2016).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-45; ASN-119 AND GLY-667.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Chromatin-remodeling protein that binds DNA through histones
CC and regulates gene transcription. May specifically recognize and bind
CC trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone
CC H3. Plays a role in the development of the nervous system by activating
CC the expression of genes promoting neuron terminal differentiation. In
CC parallel, it may also positively regulate the trimethylation of histone
CC H3 at 'Lys-27' thereby specifically repressing genes that promote the
CC differentiation into non-neuronal cell lineages. Tumor suppressor, it
CC regulates the expression of genes involved in cell proliferation and
CC differentiation. Downstream activated genes may include CDKN2A that
CC positively regulates the p53/TP53 pathway, which in turn, prevents cell
CC proliferation. In spermatogenesis, it probably regulates histone
CC hyperacetylation and the replacement of histones by transition proteins
CC in chromatin, a crucial step in the condensation of spermatid chromatin
CC and the production of functional spermatozoa.
CC {ECO:0000269|PubMed:23948251}.
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 -!- SUBUNIT: May be part of a nucleosome remodeling and histone
CC deacetylation, NuRD-like, complex composed at least of GATAD2B, HDAC1,
CC HDAC2 and MTA3. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8TDI0; O75381: PEX14; NbExp=2; IntAct=EBI-1042816, EBI-594898;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21931736,
CC ECO:0000269|PubMed:23948251}. Note=Associates with heterochromatin.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in total brain, fetal
CC brain, and cerebellum. It is also moderately expressed in the adrenal
CC gland and detected in testis. {ECO:0000269|PubMed:12592387,
CC ECO:0000269|PubMed:21931736}.
CC -!- DOMAIN: The PHD domains mediate specific binding to histone H3
CC unmethylated at 'Lys-4' and may preferentially recruit the protein to
CC transcriptionally inactive genes. {ECO:0000250}.
CC -!- DOMAIN: The chromo domains mediate specific binding to histone H3
CC trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron
CC differentiation for proper gene regulation.
CC {ECO:0000269|PubMed:23948251}.
CC -!- PTM: Methylated at Gln-1390 by N6AMT1. {ECO:0000269|PubMed:26797129}.
CC -!- DISEASE: Note=Defects in CHD5 may be a cause of the development of
CC cancers from epithelial, neural and hematopoietic origin. CHD5 is one
CC of the missing genes in the del(1p36), a deletion which is extremely
CC common in this type of cancers. A decrease of its expression, results
CC in increased susceptibility of cells to Ras-mediated transformation in
CC vitro and in vivo (PubMed:17289567). {ECO:0000269|PubMed:17289567}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000255}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CHD5ID44521ch1p36.html";
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DR EMBL; AF425231; AAL98962.1; -; mRNA.
DR EMBL; AL031847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117491; CAB55959.1; -; mRNA.
DR EMBL; AB007913; BAA32289.1; -; mRNA.
DR CCDS; CCDS57.1; -.
DR PIR; T17269; T17269.
DR RefSeq; NP_056372.1; NM_015557.2.
DR PDB; 6GUU; X-ray; 2.95 A; A/B=412-649.
DR PDBsum; 6GUU; -.
DR AlphaFoldDB; Q8TDI0; -.
DR SMR; Q8TDI0; -.
DR BioGRID; 117504; 57.
DR IntAct; Q8TDI0; 18.
DR MINT; Q8TDI0; -.
DR STRING; 9606.ENSP00000262450; -.
DR iPTMnet; Q8TDI0; -.
DR PhosphoSitePlus; Q8TDI0; -.
DR BioMuta; CHD5; -.
DR DMDM; 51701343; -.
DR EPD; Q8TDI0; -.
DR jPOST; Q8TDI0; -.
DR MassIVE; Q8TDI0; -.
DR MaxQB; Q8TDI0; -.
DR PaxDb; Q8TDI0; -.
DR PeptideAtlas; Q8TDI0; -.
DR PRIDE; Q8TDI0; -.
DR ProteomicsDB; 74289; -.
DR Antibodypedia; 27125; 139 antibodies from 29 providers.
DR DNASU; 26038; -.
DR Ensembl; ENST00000262450.8; ENSP00000262450.3; ENSG00000116254.18.
DR GeneID; 26038; -.
DR KEGG; hsa:26038; -.
DR MANE-Select; ENST00000262450.8; ENSP00000262450.3; NM_015557.3; NP_056372.1.
DR UCSC; uc001amb.3; human.
DR CTD; 26038; -.
DR DisGeNET; 26038; -.
DR GeneCards; CHD5; -.
DR HGNC; HGNC:16816; CHD5.
DR HPA; ENSG00000116254; Group enriched (brain, pituitary gland, testis).
DR MIM; 610771; gene.
DR neXtProt; NX_Q8TDI0; -.
DR OpenTargets; ENSG00000116254; -.
DR PharmGKB; PA134969178; -.
DR VEuPathDB; HostDB:ENSG00000116254; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000159249; -.
DR HOGENOM; CLU_000315_22_1_1; -.
DR InParanoid; Q8TDI0; -.
DR OMA; DSPIKFH; -.
DR OrthoDB; 54215at2759; -.
DR PhylomeDB; Q8TDI0; -.
DR TreeFam; TF106448; -.
DR PathwayCommons; Q8TDI0; -.
DR SignaLink; Q8TDI0; -.
DR BioGRID-ORCS; 26038; 12 hits in 1083 CRISPR screens.
DR ChiTaRS; CHD5; human.
DR GeneWiki; CHD5; -.
DR GenomeRNAi; 26038; -.
DR Pharos; Q8TDI0; Tbio.
DR PRO; PR:Q8TDI0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8TDI0; protein.
DR Bgee; ENSG00000116254; Expressed in sperm and 133 other tissues.
DR ExpressionAtlas; Q8TDI0; baseline and differential.
DR Genevisible; Q8TDI0; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IMP:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:GO_Central.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR028727; CHD5.
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; 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:SF6; PTHR45623:SF6; 1.
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-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 3D-structure; ATP-binding; Chromatin regulator; Differentiation;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Methylation; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Spermatogenesis; Transcription; Transcription regulation; Tumor suppressor;
KW Zinc; Zinc-finger.
FT CHAIN 1..1954
FT /note="Chromodomain-helicase-DNA-binding protein 5"
FT /id="PRO_0000080230"
FT DOMAIN 497..554
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 592..653
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 712..896
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1028..1193
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 343..390
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 416..463
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..653
FT /note="Histone-binding"
FT REGION 549..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1658..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 847..850
FT /note="DEAH box"
FT COMPBIAS 15..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 725..732
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q14839,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1390
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:26797129"
FT MOD_RES 1554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2A8L1"
FT VARIANT 45
FT /note="V -> M (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1470692239)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035475"
FT VARIANT 119
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035476"
FT VARIANT 667
FT /note="R -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035477"
FT VARIANT 1253
FT /note="S -> I (in dbSNP:rs6657997)"
FT /id="VAR_048729"
FT VARIANT 1539
FT /note="S -> P (in dbSNP:rs2843493)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9455484"
FT /id="VAR_048730"
FT MUTAGEN 518
FT /note="L->A: Reduced affinity for trimethylated histone
FT H3K27me3."
FT /evidence="ECO:0000269|PubMed:23948251"
FT MUTAGEN 619
FT /note="Y->E: Reduced affinity for trimethylated histone
FT H3K27me3."
FT /evidence="ECO:0000269|PubMed:23948251"
FT MUTAGEN 1390
FT /note="Q->R: Abolishes methylation by N6AMT1."
FT /evidence="ECO:0000269|PubMed:26797129"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:6GUU"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 469..477
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 528..534
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 536..545
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 575..581
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 593..602
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:6GUU"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 634..642
FT /evidence="ECO:0007829|PDB:6GUU"
FT HELIX 644..647
FT /evidence="ECO:0007829|PDB:6GUU"
SQ SEQUENCE 1954 AA; 223050 MW; E333062B5B55E71F CRC64;
MRGPVGTEEE LPRLFAEEME NEDEMSEEED GGLEAFDDFF PVEPVSLPKK KKPKKLKENK
CKGKRKKKEG SNDELSENEE DLEEKSESEG SDYSPNKKKK KKLKDKKEKK AKRKKKDEDE
DDNDDGCLKE PKSSGQLMAE WGLDDVDYLF SEEDYHTLTN YKAFSQFLRP LIAKKNPKIP
MSKMMTVLGA KWREFSANNP FKGSSAAAAA AAVAAAVETV TISPPLAVSP PQVPQPVPIR
KAKTKEGKGP GVRKKIKGSK DGKKKGKGKK TAGLKFRFGG ISNKRKKGSS SEEDEREESD
FDSASIHSAS VRSECSAALG KKSKRRRKKK RIDDGDGYET DHQDYCEVCQ QGGEIILCDT
CPRAYHLVCL DPELEKAPEG KWSCPHCEKE GIQWEPKDDD DEEEEGGCEE EEDDHMEFCR
VCKDGGELLC CDACPSSYHL HCLNPPLPEI PNGEWLCPRC TCPPLKGKVQ RILHWRWTEP
PAPFMVGLPG PDVEPSLPPP KPLEGIPERE FFVKWAGLSY WHCSWVKELQ LELYHTVMYR
NYQRKNDMDE PPPFDYGSGD EDGKSEKRKN KDPLYAKMEE RFYRYGIKPE WMMIHRILNH
SFDKKGDVHY LIKWKDLPYD QCTWEIDDID IPYYDNLKQA YWGHRELMLG EDTRLPKRLL
KKGKKLRDDK QEKPPDTPIV DPTVKFDKQP WYIDSTGGTL HPYQLEGLNW LRFSWAQGTD
TILADEMGLG KTVQTIVFLY SLYKEGHSKG PYLVSAPLST IINWEREFEM WAPDFYVVTY
TGDKESRSVI RENEFSFEDN AIRSGKKVFR MKKEVQIKFH VLLTSYELIT IDQAILGSIE
WACLVVDEAH RLKNNQSKFF RVLNSYKIDY KLLLTGTPLQ NNLEELFHLL NFLTPERFNN
LEGFLEEFAD ISKEDQIKKL HDLLGPHMLR RLKADVFKNM PAKTELIVRV ELSQMQKKYY
KFILTRNFEA LNSKGGGNQV SLLNIMMDLK KCCNHPYLFP VAAVEAPVLP NGSYDGSSLV
KSSGKLMLLQ KMLKKLRDEG HRVLIFSQMT KMLDLLEDFL EYEGYKYERI DGGITGGLRQ
EAIDRFNAPG AQQFCFLLST RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRIGQN
KKVMIYRFVT RASVEERITQ VAKRKMMLTH LVVRPGLGSK SGSMTKQELD DILKFGTEEL
FKDDVEGMMS QGQRPVTPIP DVQSSKGGNL AASAKKKHGS TPPGDNKDVE DSSVIHYDDA
AISKLLDRNQ DATDDTELQN MNEYLSSFKV AQYVVREEDG VEEVEREIIK QEENVDPDYW
EKLLRHHYEQ QQEDLARNLG KGKRIRKQVN YNDASQEDQE WQDELSDNQS EYSIGSEDED
EDFEERPEGQ SGRRQSRRQL KSDRDKPLPP LLARVGGNIE VLGFNARQRK AFLNAIMRWG
MPPQDAFNSH WLVRDLRGKS EKEFRAYVSL FMRHLCEPGA DGAETFADGV PREGLSRQHV
LTRIGVMSLV RKKVQEFEHV NGKYSTPDLI PEGPEGKKSG EVISSDPNTP VPASPAHLLP
APLGLPDKME AQLGYMDEKD PGAQKPRQPL EVQALPAALD RVESEDKHES PASKERAREE
RPEETEKAPP SPEQLPREEV LPEKEKILDK LELSLIHSRG DSSELRPDDT KAEEKEPIET
QQNGDKEEDD EGKKEDKKGK FKFMFNIADG GFTELHTLWQ NEERAAVSSG KIYDIWHRRH
DYWLLAGIVT HGYARWQDIQ NDPRYMILNE PFKSEVHKGN YLEMKNKFLA RRFKLLEQAL
VIEEQLRRAA YLNMTQDPNH PAMALNARLA EVECLAESHQ HLSKESLAGN KPANAVLHKV
LNQLEELLSD MKADVTRLPS MLSRIPPVAA RLQMSERSIL SRLTNRAGDP TIQQGAFGSS
QMYSNNFGPN FRGPGPGGIV NYNQMPLGPY VTDI
