DPF3_HUMAN
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 03-AUG-2022, entry version 170.
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 FUNCTION (ISOFORM 2), INTERACTION WITH HDGFL2; SMARCA4; SMARCC1 AND SMARCD1
RP (ISOFORM 2), PHOSPHORYLATION AT SER-323 (ISOFORM 2), AND MUTAGENESIS OF
RP SER-323; PHE-325 AND PHE-328 (ISOFORM 2).
RX PubMed=32459350; DOI=10.1093/nar/gkaa441;
RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z.,
RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.;
RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin
RT remodeling to regulate myogenic gene transcription.";
RL Nucleic Acids Res. 48:6563-6582(2020).
RN [8]
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 -!- FUNCTION: [Isoform 2]: Acts as a regulator of myogenesis in cooperation
CC with HDGFL2 (PubMed:32459350). Mediates the interaction of HDGFL2 with
CC the BAF complex (PubMed:32459350). HDGFL2-DPF3a activate myogenic genes
CC by increasing chromatin accessibility through recruitment of
CC SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic
CC gene promoters (PubMed:32459350). {ECO:0000269|PubMed:32459350}.
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 (PubMed:18765789). In muscle cells,
CC the BAF complex also contains DPF3 (PubMed:18765789). Interacts with
CC acetylated histones H3 and H4 (PubMed:18765789). Component of neuron-
CC specific chromatin remodeling complex (nBAF complex) composed of at
CC least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity).
CC {ECO:0000250|UniProtKB:P58269, ECO:0000269|PubMed:18765789}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with HDGFL2, SMARCA4/BRG1/BAF190A,
CC SMARCC1/BAF155 and SMARCD1/BAF60A. {ECO:0000269|PubMed:32459350}.
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 -!- PTM: [Isoform 2]: Phosphorylation at Ser-323 enhances its interaction
CC with HDGFL2. {ECO:0000269|PubMed:32459350}.
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};
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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 AlphaFoldDB; Q92784; -.
DR BMRB; Q92784; -.
DR SMR; Q92784; -.
DR BioGRID; 113779; 68.
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; 36.
DR MINT; Q92784; -.
DR STRING; 9606.ENSP00000479526; -.
DR iPTMnet; Q92784; -.
DR PhosphoSitePlus; Q92784; -.
DR SwissPalm; Q92784; -.
DR BioMuta; DPF3; -.
DR DMDM; 215274167; -.
DR EPD; Q92784; -.
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; 134 antibodies from 23 providers.
DR DNASU; 8110; -.
DR Ensembl; ENST00000381216.8; ENSP00000370614.4; ENSG00000205683.12. [Q92784-2]
DR Ensembl; ENST00000556509.6; ENSP00000450518.1; ENSG00000205683.12. [Q92784-1]
DR Ensembl; ENST00000614862.5; ENSP00000481992.1; ENSG00000205683.12. [Q92784-5]
DR GeneID; 8110; -.
DR KEGG; hsa:8110; -.
DR MANE-Select; ENST00000556509.6; ENSP00000450518.1; NM_001280542.3; NP_001267471.1.
DR UCSC; uc001xnc.4; human. [Q92784-1]
DR CTD; 8110; -.
DR DisGeNET; 8110; -.
DR GeneCards; DPF3; -.
DR HGNC; HGNC:17427; DPF3.
DR HPA; ENSG00000205683; Tissue enhanced (brain, retina, skeletal muscle).
DR MIM; 601672; gene.
DR neXtProt; NX_Q92784; -.
DR OpenTargets; ENSG00000205683; -.
DR PharmGKB; PA134888535; -.
DR VEuPathDB; HostDB:ENSG00000205683; -.
DR eggNOG; KOG1244; Eukaryota.
DR GeneTree; ENSGT00940000159153; -.
DR HOGENOM; CLU_038980_0_1_1; -.
DR InParanoid; Q92784; -.
DR OMA; HYTHFHN; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; Q92784; -.
DR TreeFam; TF318971; -.
DR PathwayCommons; Q92784; -.
DR SignaLink; Q92784; -.
DR BioGRID-ORCS; 8110; 12 hits in 1076 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 left ventricle myocardium and 150 other tissues.
DR ExpressionAtlas; Q92784; baseline and differential.
DR Genevisible; Q92784; HS.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016514; C:SWI/SNF complex; IC:ComplexPortal.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
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:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00418; -.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR038047; DPF3.
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; Myogenesis; Neurogenesis; Nucleus;
KW Phosphoprotein; 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 REGION 145..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|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:0007829|PDB:5SZC"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 293..297
FT /evidence="ECO:0007829|PDB:5SZC"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:5SZC"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5SZC"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:5SZC"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:5SZC"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:5SZC"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5SZC"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:2KWO"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:5SZC"
FT REGION Q92784-2:317..332
FT /note="Interaction with HDGFL2"
FT /evidence="ECO:0000269|PubMed:32459350"
FT MOD_RES Q92784-2:323
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:32459350"
FT VARIANT Q92784-2:326
FT /note="H -> R (in dbSNP:rs17855716)"
FT /evidence="ECO:0000305"
FT /id="VAR_082912"
FT MUTAGEN Q92784-2:323
FT /note="S->A: Phosphorylation-null mutant. Loss of
FT interaction with HDGFL2."
FT /evidence="ECO:0000269|PubMed:32459350"
FT MUTAGEN Q92784-2:323
FT /note="S->D,E: Phosphomimetic mutant. Increased interaction
FT with HDGFL2."
FT /evidence="ECO:0000269|PubMed:32459350"
FT MUTAGEN Q92784-2:325
FT /note="F->A: Loss of interaction with HDGFL2. No effect on
FT interaction with SMARCA4, SMARCC1 and SMARCD1."
FT /evidence="ECO:0000269|PubMed:32459350"
FT MUTAGEN Q92784-2:328
FT /note="F->A: Loss of interaction with HDGFL2. No effect on
FT interaction with SMARCA4, SMARCC1 and SMARCD1."
FT /evidence="ECO:0000269|PubMed:32459350"
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
