ID DPF3_HUMAN Reviewed; 378 AA. AC Q92784; A8MSI3; B7Z276; F5H575; Q32UJ0; Q6P9E6; Q6ZT41; Q9H7Y5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 12-AUG-2020, entry version 161. DE RecName: Full=Zinc finger protein DPF3; DE AltName: Full=BRG1-associated factor 45C; DE Short=BAF45C; DE AltName: Full=Zinc finger protein cer-d4; GN Name=DPF3; Synonyms=BAF45C, CERD4; 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] (ISOFORMS 1 AND 2), FUNCTION, IDENTIFICATION IN RP THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, INTERACTION RP WITH HISTONES, AND MUTAGENESIS OF TRP-358; CYS-360 AND CYS-363. RC TISSUE=Heart; RX PubMed=18765789; DOI=10.1101/gad.471408; RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.; RT "Regulation of muscle development by DPF3, a novel histone acetylation and RT methylation reader of the BAF chromatin remodeling complex."; RL Genes Dev. 22:2370-2384(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5). RC TISSUE=Brain, and Embryo; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT HIS-177. RC TISSUE=Brain; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-64. RX PubMed=8812431; DOI=10.1006/geno.1996.0440; RA Chestkov A.V., Baka I.D., Kost M.V., Georgiev G.P., Buchman V.L.; RT "The d4 gene family in the human genome."; RL Genomics 36:174-177(1996). RN [6] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99, AND IDENTIFICATION BY MASS RP 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 [7] RP STRUCTURE BY NMR OF 261-372, AND DOMAIN PHD. RX PubMed=20613843; DOI=10.1038/nature09139; RA Zeng L., Zhang Q., Li S., Plotnikov A.N., Walsh M.J., Zhou M.M.; RT "Mechanism and regulation of acetylated histone binding by the tandem PHD RT finger of DPF3b."; RL Nature 466:258-262(2010). CC -!- FUNCTION: Belongs to the neuron-specific chromatin remodeling complex CC (nBAF complex). During neural development a switch from a CC stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs CC as neurons exit the cell cycle and become committed to their adult CC state. The transition from proliferating neural stem/progenitor cells CC to post-mitotic neurons requires a switch in subunit composition of the CC npBAF and nBAF complexes. As neural progenitors exit mitosis and CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A CC and PHF10/BAF45A, are exchanged for homologous alternative CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- CC specific complexes (nBAF). The npBAF complex is essential for the self- CC renewal/proliferative capacity of the multipotent neural stem cells. CC The nBAF complex along with CREST plays a role regulating the activity CC of genes essential for dendrite growth (By similarity). Muscle-specific CC component of the BAF complex, a multiprotein complex involved in CC transcriptional activation and repression of select genes by chromatin CC remodeling (alteration of DNA-nucleosome topology). Specifically binds CC acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, CC H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor CC between histone acetylations and methylations and chromatin remodeling. CC It thereby probably plays an essential role in heart and skeletal CC muscle development. {ECO:0000250, ECO:0000269|PubMed:18765789}. CC -!- SUBUNIT: Component of the BAF complex, which includes at least actin CC (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, CC ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, CC SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, CC SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex CC also contains DPF3. Interacts with acetylated histones H3 and H4. CC Component of neuron-specific chromatin remodeling complex (nBAF CC complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, CC SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, CC SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=DPF3b; CC IsoId=Q92784-1; Sequence=Displayed; CC Name=2; Synonyms=DPF3a; CC IsoId=Q92784-2; Sequence=VSP_035884; CC Name=3; CC IsoId=Q92784-3; Sequence=VSP_035882, VSP_035884; CC Name=4; CC IsoId=Q92784-4; Sequence=VSP_035883; CC Name=5; CC IsoId=Q92784-5; Sequence=VSP_055748, VSP_035884; CC -!- DOMAIN: The PHD-type zinc fingers mediate the binding to acetylated CC histones. {ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:20613843}. CC -!- MISCELLANEOUS: [Isoform 2]: Lacks PHD-type zinc fingers and does not CC bind to acetylated histones H3 and H4. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: [Isoform 4]: CC Sequence=BAB14838.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AY803021; AAX20019.1; -; mRNA. DR EMBL; AK024141; BAB14838.1; ALT_FRAME; mRNA. DR EMBL; AK126933; BAC86753.1; -; mRNA. DR EMBL; AK294425; BAH11762.1; -; mRNA. DR EMBL; AC004828; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006360; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL392024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC060801; AAH60801.1; -; mRNA. DR EMBL; U43919; AAC50686.1; -; Genomic_DNA. DR CCDS; CCDS45133.1; -. [Q92784-2] DR CCDS; CCDS61495.1; -. [Q92784-5] DR CCDS; CCDS61496.1; -. [Q92784-3] DR CCDS; CCDS61497.1; -. [Q92784-1] DR RefSeq; NP_001267471.1; NM_001280542.1. [Q92784-1] DR RefSeq; NP_001267472.1; NM_001280543.1. [Q92784-5] DR RefSeq; NP_001267473.1; NM_001280544.1. DR RefSeq; NP_036206.3; NM_012074.4. [Q92784-2] DR RefSeq; XP_016877159.1; XM_017021670.1. DR RefSeq; XP_016877160.1; XM_017021671.1. DR PDB; 2KWJ; NMR; -; A=261-372. DR PDB; 2KWK; NMR; -; A=261-372. DR PDB; 2KWN; NMR; -; A=261-372. DR PDB; 2KWO; NMR; -; A=261-372. DR PDB; 5I3L; X-ray; 1.85 A; A/B=254-368. DR PDB; 5SZB; X-ray; 1.20 A; A=254-368. DR PDB; 5SZC; X-ray; 1.19 A; A=254-368. DR PDBsum; 2KWJ; -. DR PDBsum; 2KWK; -. DR PDBsum; 2KWN; -. DR PDBsum; 2KWO; -. DR PDBsum; 5I3L; -. DR PDBsum; 5SZB; -. DR PDBsum; 5SZC; -. DR SMR; Q92784; -. DR BioGRID; 113779; 55. DR ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant. DR DIP; DIP-59245N; -. DR IntAct; Q92784; 33. DR MINT; Q92784; -. DR STRING; 9606.ENSP00000479526; -. DR iPTMnet; Q92784; -. DR PhosphoSitePlus; Q92784; -. DR SwissPalm; Q92784; -. DR BioMuta; DPF3; -. DR DMDM; 215274167; -. DR jPOST; Q92784; -. DR MassIVE; Q92784; -. DR MaxQB; Q92784; -. DR PaxDb; Q92784; -. DR PeptideAtlas; Q92784; -. DR PRIDE; Q92784; -. DR ProteomicsDB; 26794; -. DR ProteomicsDB; 75465; -. [Q92784-1] DR ProteomicsDB; 75466; -. [Q92784-2] DR ProteomicsDB; 75467; -. [Q92784-3] DR ProteomicsDB; 75468; -. [Q92784-4] DR Antibodypedia; 25263; 127 antibodies. DR DNASU; 8110; -. DR Ensembl; ENST00000381216; ENSP00000370614; ENSG00000205683. [Q92784-2] DR Ensembl; ENST00000541685; ENSP00000441640; ENSG00000205683. [Q92784-2] DR Ensembl; ENST00000546183; ENSP00000444662; ENSG00000205683. [Q92784-5] DR Ensembl; ENST00000556509; ENSP00000450518; ENSG00000205683. [Q92784-1] DR Ensembl; ENST00000614862; ENSP00000481992; ENSG00000205683. [Q92784-5] DR GeneID; 8110; -. DR KEGG; hsa:8110; -. DR UCSC; uc001xnc.4; human. [Q92784-1] DR CTD; 8110; -. DR DisGeNET; 8110; -. DR EuPathDB; HostDB:ENSG00000205683.11; -. DR GeneCards; DPF3; -. DR HGNC; HGNC:17427; DPF3. DR HPA; ENSG00000205683; Tissue enhanced (brain, skeletal muscle). DR MIM; 601672; gene. DR neXtProt; NX_Q92784; -. DR OpenTargets; ENSG00000205683; -. DR PharmGKB; PA134888535; -. DR eggNOG; KOG1244; Eukaryota. DR GeneTree; ENSGT00940000159153; -. DR HOGENOM; CLU_038980_0_1_1; -. DR InParanoid; Q92784; -. DR KO; K22198; -. DR OMA; ATEMKYI; -. DR OrthoDB; 708781at2759; -. DR PhylomeDB; Q92784; -. DR TreeFam; TF318971; -. DR PathwayCommons; Q92784; -. DR BioGRID-ORCS; 8110; 7 hits in 876 CRISPR screens. DR ChiTaRS; DPF3; human. DR EvolutionaryTrace; Q92784; -. DR GenomeRNAi; 8110; -. DR Pharos; Q92784; Tbio. DR PRO; PR:Q92784; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q92784; protein. DR Bgee; ENSG00000205683; Expressed in cerebellum and 194 other tissues. DR ExpressionAtlas; Q92784; baseline and differential. DR Genevisible; Q92784; HS. DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central. DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB. DR GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 3.30.40.10; -; 1. DR IDEAL; IID00418; -. DR InterPro; IPR038047; DPF3. DR InterPro; IPR025750; Requiem/DPF_N_dom. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. 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; PTHR10615:SF120; PTHR10615:SF120; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF14051; Requiem_N; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00355; ZnF_C2H2; 1. DR SUPFAM; SSF57667; SSF57667; 1. DR SUPFAM; SSF57903; SSF57903; 2. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Chromatin regulator; KW Isopeptide bond; Metal-binding; Neurogenesis; Nucleus; Polymorphism; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..378 FT /note="Zinc finger protein DPF3" FT /id="PRO_0000168154" FT ZN_FING 198..221 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 259..319 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 316..366 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT CROSSLNK 99 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT VAR_SEQ 1..11 FT /note="MATVIHNPLKA -> MFYGRINGRNFAASSLPVAFAATPLMLFLPNPQLICS FT FPISSRNHITGLMPPGKLKLENLFHMCTR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035882" FT VAR_SEQ 1..11 FT /note="MATVIHNPLKA -> MGFTDLEEPISGCPGGPWALG (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055748" FT VAR_SEQ 177..378 FT /note="RGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGD FT EAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADC FT GRSGHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYHMYCL FT NPPVAEPPEGSWSCHLCWELLKEKASAFGCQA -> RCPLPSLHCFLPSLCRDRC (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035883" FT VAR_SEQ 291..378 FT /note="GHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYH FT MYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA -> AHLGGEGRKEKEAAAAART FT TEDLFGSTSESDTSTFHGFDEDDLEEPRSCRGRRSGRGSPTADKKGSC (in FT isoform 2, isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:18765789" FT /id="VSP_035884" FT VARIANT 177 FT /note="R -> H (in dbSNP:rs17855717)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_047771" FT MUTAGEN 358 FT /note="W->E: Abolishes binding to acetylated histones H3 FT and H4." FT /evidence="ECO:0000269|PubMed:18765789" FT MUTAGEN 360 FT /note="C->R: Abolishes binding to acetylated histones H3 FT and H4; when associated with R-363." FT /evidence="ECO:0000269|PubMed:18765789" FT MUTAGEN 363 FT /note="C->R: Abolishes binding to acetylated histones H3 FT and H4; when associated with R-360." FT /evidence="ECO:0000269|PubMed:18765789" FT CONFLICT 12 FT /note="L -> V (in Ref. 5; AAC50686)" FT /evidence="ECO:0000305" FT CONFLICT 24 FT /note="C -> S (in Ref. 5; AAC50686)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="C -> S (in Ref. 2; BAB14838)" FT /evidence="ECO:0000305" FT CONFLICT 170 FT /note="N -> D (in Ref. 2; BAB14838)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="Y -> H (in Ref. 2; BAC86753)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="H -> Y (in Ref. 2; BAC86753)" FT /evidence="ECO:0000305" FT STRAND 260..262 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 263..265 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 273..276 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 285..287 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 293..297 FT /evidence="ECO:0000244|PDB:5SZC" FT HELIX 300..306 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 307..310 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 314..316 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 320..322 FT /evidence="ECO:0000244|PDB:5SZC" FT HELIX 328..330 FT /evidence="ECO:0000244|PDB:5SZC" FT STRAND 331..333 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 335..337 FT /evidence="ECO:0000244|PDB:5SZC" FT STRAND 340..342 FT /evidence="ECO:0000244|PDB:5SZC" FT TURN 343..345 FT /evidence="ECO:0000244|PDB:5SZC" FT STRAND 346..348 FT /evidence="ECO:0000244|PDB:5SZC" FT STRAND 355..357 FT /evidence="ECO:0000244|PDB:2KWO" FT HELIX 361..367 FT /evidence="ECO:0000244|PDB:5SZC" FT VARIANT Q92784-2:326 FT /note="H -> R (in dbSNP:rs17855716)" FT /evidence="ECO:0000305" FT /id="VAR_082912" FT CONFLICT Q92784-5:358 FT /note="S -> P (in Ref. 2; BAH11762)" FT /evidence="ECO:0000305" SQ SEQUENCE 378 AA; 43084 MW; 7E6A6FD07A0E4668 CRC64; MATVIHNPLK ALGDQFYKEA IEHCRSYNSR LCAERSVRLP FLDSQTGVAQ NNCYIWMEKR HRGPGLAPGQ LYTYPARCWR KKRRLHPPED PKLRLLEIKP EVELPLKKDG FTSESTTLEA LLRGEGVEKK VDAREEESIQ EIQRVLENDE NVEEGNEEED LEEDIPKRKN RTRGRARGSA GGRRRHDAAS QEDHDKPYVC DICGKRYKNR PGLSYHYAHT HLASEEGDEA QDQETRSPPN HRNENHRPQK GPDGTVIPNN YCDFCLGGSN MNKKSGRPEE LVSCADCGRS GHPTCLQFTL NMTEAVKTYK WQCIECKSCI LCGTSENDDQ LLFCDDCDRG YHMYCLNPPV AEPPEGSWSC HLCWELLKEK ASAFGCQA //