ID REQU_HUMAN Reviewed; 391 AA. AC Q92785; A8K7C9; B4DT58; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-OCT-2024, entry version 220. DE RecName: Full=Zinc finger protein ubi-d4; DE AltName: Full=Apoptosis response zinc finger protein; DE AltName: Full=BRG1-associated factor 45D; DE Short=BAF45D; DE AltName: Full=D4, zinc and double PHD fingers family 2; DE AltName: Full=Protein requiem; GN Name=DPF2; Synonyms=BAF45D, REQ, UBID4; 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] (ISOFORM 1). RX PubMed=9253601; DOI=10.1101/gr.7.7.725; RA Guru S.C., Agarwal S.K., Manickam P., Olufemi S.-E., Crabtree J.S., RA Weisemann J.M., Kester M.B., Kim Y.S., Wang Y., Emmert-Buck M.R., RA Liotta L.A., Spiegel A.M., Boguski M.S., Roe B.A., Collins F.S., RA Burns A.L., Marx S.J., Chandrasekharappa S.C.; RT "A transcript map for the 2.8-Mb region containing the multiple endocrine RT neoplasia type 1 locus."; RL Genome Res. 7:725-735(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9680388; DOI=10.1007/s003359900840; RA Gabig T.G., Crean C.D., Klenk A., Long H., Copeland N.G., Gilbert D.J., RA Jenkins N.A., Quincey D., Parente F., Lespinasse F., Carle G.F., RA Gaudray P., Zhang C.X., Calender A., Hoeppener J., Kas K., Thakker R.V., RA Farnebo F., Teh B.T., Larsson C., Piehl F., Lagercrantz J., Khodaei S., RA Carson E., Weber G.; RT "Expression and chromosomal localization of the Requiem gene."; RL Mamm. Genome 9:660-665(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Pericardium; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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 [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND THR-176, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; TYR-172 AND THR-176, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [13] RP FUNCTION, AND INTERACTION WITH SMARCA2; SMARCA4; SMARCB1 AND SMARCB1. RX PubMed=20460684; DOI=10.1074/jbc.m109.087783; RA Tando T., Ishizaka A., Watanabe H., Ito T., Iida S., Haraguchi T., RA Mizutani T., Izumi T., Isobe T., Akiyama T., Inoue J., Iba H.; RT "Requiem protein links RelB/p52 and the Brm-type SWI/SNF complex in a RT noncanonical NF-kappaB pathway."; RL J. Biol. Chem. 285:21951-21960(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-176 AND SER-200, 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] 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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-176 AND SER-244, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-176; SER-200 AND RP SER-280, AND IDENTIFICATION BY MASS 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 IDENTIFICATION 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99 AND LYS-107, AND RP IDENTIFICATION BY 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-10, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99 AND LYS-107, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-99; LYS-107; LYS-108; RP LYS-178; LYS-196 AND LYS-281, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [23] RP SUBUNIT, SUBCELLULAR LOCATION, INVOLVEMENT IN CSS7, VARIANTS CSS7 PHE-276; RP TRP-330; GLY-346; HIS-350 AND ARG-369, AND CHARACTERIZATION OF VARIANTS RP CSS7 PHE-276; TRP-330 AND HIS-350. RX PubMed=29429572; DOI=10.1016/j.ajhg.2018.01.014; RG Deciphering Developmental Disorders Study; RA Vasileiou G., Vergarajauregui S., Endele S., Popp B., Buettner C., RA Ekici A.B., Gerard M., Bramswig N.C., Albrecht B., Clayton-Smith J., RA Morton J., Tomkins S., Low K., Weber A., Wenzel M., Altmueller J., Li Y., RA Wollnik B., Hoganson G., Plona M.R., Cho M.T., Thiel C.T., Luedecke H.J., RA Strom T.M., Calpena E., Wilkie A.O.M., Wieczorek D., Engel F.B., Reis A.; RT "Mutations in the BAF-complex subunit DPF2 are associated with Coffin-Siris RT syndrome."; RL Am. J. Hum. Genet. 102:468-479(2018). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 203-249. RX PubMed=21888896; DOI=10.1016/j.bbrc.2011.08.043; RA Zhang W., Xu C., Bian C., Tempel W., Crombet L., MacKenzie F., Min J., RA Liu Z., Qi C.; RT "Crystal structure of the Cys2His2-type zinc finger domain of human DPF2."; RL Biochem. Biophys. Res. Commun. 413:58-61(2011). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 270-391, FUNCTION, SUBUNIT, AND RP INTERACTION WITH NUCLEOSOMES. RX PubMed=27775714; DOI=10.1038/nchembio.2218; RA Xiong X., Panchenko T., Yang S., Zhao S., Yan P., Zhang W., Xie W., Li Y., RA Zhao Y., Allis C.D., Li H.; RT "Selective recognition of histone crotonylation by double PHD fingers of RT MOZ and DPF2."; RL Nat. Chem. Biol. 12:1111-1118(2016). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 270-391, FUNCTION, SUBCELLULAR RP LOCATION, SUBUNIT, INTERACTION WITH SMARCC1; SMARCC2; ACTL6A AND RUNX1, AND RP MUTAGENESIS OF PHE-275; ARG-300 AND ASP-346. RX PubMed=28533407; DOI=10.1073/pnas.1700328114; RA Huber F.M., Greenblatt S.M., Davenport A.M., Martinez C., Xu Y., Vu L.P., RA Nimer S.D., Hoelz A.; RT "Histone-binding of DPF2 mediates its repressive role in myeloid RT differentiation."; RL Proc. Natl. Acad. Sci. U.S.A. 114:6016-6021(2017). CC -!- FUNCTION: Plays an active role in transcriptional regulation by binding CC modified histones H3 and H4 (PubMed:27775714, PubMed:28533407). Is a CC negative regulator of myeloid differentiation of hematopoietic CC progenitor cells (PubMed:28533407). Might also have a role in the CC development and maturation of lymphoid cells (By similarity). Involved CC in the regulation of non-canonical NF-kappa-B pathway CC (PubMed:20460684). {ECO:0000250|UniProtKB:Q61103, CC ECO:0000269|PubMed:20460684, ECO:0000269|PubMed:27775714, CC ECO:0000269|PubMed:28533407}. CC -!- SUBUNIT: Interacts with the nucleosomes, in particular nucleosomes CC bearing histone H3 crotonylated at 'Lys-14' (H3K14cr) for which DPF2 CC has high affinity (PubMed:27775714). Also interacts (via PHD-type zinc CC finger domains) with histone H3 butyrylated at 'Lys-14' (H3K14bu), CC histone H3 propionylated at 'Lys-14' (H3K14pr), and histone H3 CC acetylated at 'Lys-14' (H3K14ac) (PubMed:27775714, PubMed:28533407, CC PubMed:29429572). Interacts with histone H3 acetylated at 'Lys-9' CC (H3K9ac), histone H3 di-methylated at 'Lys-9' (H3K9me2), and histone H3 CC tri-methylated at 'Lys-9' (H3K9me3) (PubMed:29429572). Interacts with CC histone H4 acetylated at 'Lys-12' (H4K12ac) (PubMed:29429572). CC Interacts with histone H4 acetylated at 'Lys-16' (H4K16ac) CC (PubMed:28533407). Interacts with SWI/SNF complex components CC (PubMed:20460684, PubMed:28533407). Interacts with SMARCA2, SMARCA4, CC SMARCB1 and SMARCD1 (PubMed:20460684). Interacts with SMARCC1, SMARCC2 CC and ACTL6A (PubMed:28533407). Interacts with RUNX1 (PubMed:28533407). CC {ECO:0000269|PubMed:20460684, ECO:0000269|PubMed:28533407, CC ECO:0000269|PubMed:29429572}. CC -!- INTERACTION: CC Q92785; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-359932, EBI-5916454; CC Q92785; O75031: HSF2BP; NbExp=6; IntAct=EBI-359932, EBI-7116203; CC Q92785; O95751: LDOC1; NbExp=6; IntAct=EBI-359932, EBI-740738; CC Q92785; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-359932, EBI-739832; CC Q92785; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-359932, EBI-16439278; CC Q92785; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-359932, EBI-79165; CC Q92785; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-359932, EBI-726876; CC Q92785; Q92622: RUBCN; NbExp=3; IntAct=EBI-359932, EBI-2952709; CC Q92785; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-359932, EBI-8656864; CC Q92785; O95881: TXNDC12; NbExp=3; IntAct=EBI-359932, EBI-2564581; CC Q92785; Q8N720: ZNF655; NbExp=3; IntAct=EBI-359932, EBI-625509; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28533407, CC ECO:0000269|PubMed:29429572}. Cytoplasm {ECO:0000269|PubMed:28533407}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92785-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92785-2; Sequence=VSP_055860; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DISEASE: Coffin-Siris syndrome 7 (CSS7) [MIM:618027]: A form of Coffin- CC Siris syndrome, a congenital multiple malformation syndrome with broad CC phenotypic and genetic variability. Cardinal features are intellectual CC disability, coarse facial features, hypertrichosis, and hypoplastic or CC absent fifth digit nails or phalanges. Additional features include CC malformations of the cardiac, gastrointestinal, genitourinary, and/or CC central nervous systems. Sucking/feeding difficulties, poor growth, CC ophthalmologic abnormalities, hearing impairment, and spinal anomalies CC are common findings. Both autosomal dominant and autosomal recessive CC inheritance patterns have been reported. CSS7 inheritance is autosomal CC dominant. {ECO:0000269|PubMed:29429572}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the requiem/DPF family. {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; AF001433; AAB81203.1; -; mRNA. DR EMBL; U94585; AAB58307.1; -; mRNA. DR EMBL; BT006718; AAP35364.1; -; mRNA. DR EMBL; AY220877; AAO26041.1; -; Genomic_DNA. DR EMBL; AK291944; BAF84633.1; -; mRNA. DR EMBL; AK300061; BAG61870.1; -; mRNA. DR EMBL; AP000944; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74375.1; -; Genomic_DNA. DR EMBL; BC014889; AAH14889.1; -; mRNA. DR EMBL; U43920; AAC50687.1; -; Genomic_DNA. DR CCDS; CCDS8100.1; -. [Q92785-1] DR RefSeq; NP_006259.1; NM_006268.4. [Q92785-1] DR PDB; 3IUF; X-ray; 1.80 A; A=203-249. DR PDB; 5B79; X-ray; 2.60 A; A=270-391. DR PDB; 5VDC; X-ray; 1.60 A; A=270-391. DR PDB; 6LTH; EM; 3.00 A; R=1-391. DR PDB; 6LTJ; EM; 3.70 A; R=1-100, R=209-391. DR PDBsum; 3IUF; -. DR PDBsum; 5B79; -. DR PDBsum; 5VDC; -. DR PDBsum; 6LTH; -. DR PDBsum; 6LTJ; -. DR AlphaFoldDB; Q92785; -. DR EMDB; EMD-0974; -. DR SMR; Q92785; -. DR BioGRID; 111909; 347. DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex. DR CORUM; Q92785; -. DR DIP; DIP-27575N; -. DR IntAct; Q92785; 117. DR MINT; Q92785; -. DR STRING; 9606.ENSP00000252268; -. DR GlyGen; Q92785; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q92785; -. DR PhosphoSitePlus; Q92785; -. DR SwissPalm; Q92785; -. DR BioMuta; DPF2; -. DR DMDM; 2842711; -. DR jPOST; Q92785; -. DR MassIVE; Q92785; -. DR PaxDb; 9606-ENSP00000436901; -. DR PeptideAtlas; Q92785; -. DR ProteomicsDB; 5076; -. DR ProteomicsDB; 75469; -. [Q92785-1] DR Pumba; Q92785; -. DR Antibodypedia; 15846; 386 antibodies from 39 providers. DR DNASU; 5977; -. DR Ensembl; ENST00000415073.6; ENSP00000399714.2; ENSG00000133884.11. [Q92785-2] DR Ensembl; ENST00000528416.6; ENSP00000436901.1; ENSG00000133884.11. [Q92785-1] DR GeneID; 5977; -. DR KEGG; hsa:5977; -. DR MANE-Select; ENST00000528416.6; ENSP00000436901.1; NM_006268.5; NP_006259.1. DR UCSC; uc001odm.4; human. [Q92785-1] DR AGR; HGNC:9964; -. DR CTD; 5977; -. DR DisGeNET; 5977; -. DR GeneCards; DPF2; -. DR GeneReviews; DPF2; -. DR HGNC; HGNC:9964; DPF2. DR HPA; ENSG00000133884; Low tissue specificity. DR MalaCards; DPF2; -. DR MIM; 601671; gene. DR MIM; 618027; phenotype. DR neXtProt; NX_Q92785; -. DR OpenTargets; ENSG00000133884; -. DR Orphanet; 1465; Coffin-Siris syndrome. DR PharmGKB; PA34331; -. DR VEuPathDB; HostDB:ENSG00000133884; -. DR eggNOG; KOG1244; Eukaryota. DR GeneTree; ENSGT00940000155070; -. DR HOGENOM; CLU_038980_0_1_1; -. DR InParanoid; Q92785; -. DR OrthoDB; 5490909at2759; -. DR PhylomeDB; Q92785; -. DR TreeFam; TF318971; -. DR PathwayCommons; Q92785; -. DR Reactome; R-HSA-9824585; Regulation of MITF-M-dependent genes involved in pigmentation. DR Reactome; R-HSA-9845323; Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs). DR SignaLink; Q92785; -. DR SIGNOR; Q92785; -. DR BioGRID-ORCS; 5977; 169 hits in 1184 CRISPR screens. DR ChiTaRS; DPF2; human. DR EvolutionaryTrace; Q92785; -. DR GeneWiki; DPF2; -. DR GenomeRNAi; 5977; -. DR Pharos; Q92785; Tbio. DR PRO; PR:Q92785; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q92785; protein. DR Bgee; ENSG00000133884; Expressed in oocyte and 201 other cell types or tissues. DR ExpressionAtlas; Q92785; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0071565; C:nBAF complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016514; C:SWI/SNF complex; NAS:ComplexPortal. DR GO; GO:0062072; F:H3K9me3 modified histone binding; IDA:UniProtKB. DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003714; F:transcription corepressor activity; TAS:ARUK-UCL. DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc. DR GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal. DR GO; GO:1905454; P:negative regulation of myeloid progenitor cell differentiation; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ARUK-UCL. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR CDD; cd15691; PHD1_DPF2_like; 1. DR CDD; cd15530; PHD2_d4; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR025750; DPF1-3_N. DR InterPro; IPR051580; ZnF-Chromatin_assoc. 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; PTHR23057; JUXTAPOSED WITH ANOTHER ZINC FINGER PROTEIN 1; 1. DR PANTHER; PTHR23057:SF3; ZINC FINGER PROTEIN DPF3; 1. DR Pfam; PF14051; DPF1-3_N; 1. DR Pfam; PF00628; PHD; 2. DR SMART; SM00249; PHD; 2. DR SMART; SM00355; ZnF_C2H2; 1. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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; Acetylation; Alternative splicing; Apoptosis; KW Chromatin regulator; Cytoplasm; Disease variant; Intellectual disability; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..391 FT /note="Zinc finger protein ubi-d4" FT /id="PRO_0000168149" FT ZN_FING 209..232 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 270..330 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 327..377 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 79..146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 165..196 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 233..266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 124..142 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 172 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 176 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 200 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 10 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 99 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 107 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 108 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 178 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 196 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 281 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 156..339 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055860" FT VARIANT 276 FT /note="C -> F (in CSS7; abolishes interaction with FT acetylated or methylated histone H3; dbSNP:rs1555031372)" FT /evidence="ECO:0000269|PubMed:29429572" FT /id="VAR_081047" FT VARIANT 330 FT /note="C -> W (in CSS7; abolishes interaction with FT acetylated or methylated histone H3; dbSNP:rs1555031500)" FT /evidence="ECO:0000269|PubMed:29429572" FT /id="VAR_081048" FT VARIANT 346 FT /note="D -> G (in CSS7; dbSNP:rs1555032044)" FT /evidence="ECO:0000269|PubMed:29429572" FT /id="VAR_081049" FT VARIANT 350 FT /note="R -> H (in CSS7; abolishes interaction with FT acetylated histone H3; strongly decreased interaction with FT methylated histone H3; dbSNP:rs1555032051)" FT /evidence="ECO:0000269|PubMed:29429572" FT /id="VAR_081050" FT VARIANT 369 FT /note="W -> R (in CSS7)" FT /evidence="ECO:0000269|PubMed:29429572" FT /id="VAR_081051" FT MUTAGEN 275 FT /note="F->A: Strongly decreased interaction with histones FT H3 and H4 and loss of function; when associated with A-300 FT and A-346." FT /evidence="ECO:0000269|PubMed:28533407" FT MUTAGEN 300 FT /note="R->A: Strongly decreased interaction with histones FT H3 and H4 and loss of function; when associated with A-275 FT and A-346." FT /evidence="ECO:0000269|PubMed:28533407" FT MUTAGEN 346 FT /note="D->A: Strongly decreased interaction with histones FT H3 and H4 and loss of function; when associated with A-275 FT and A-300." FT /evidence="ECO:0000269|PubMed:28533407" FT HELIX 14..37 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:6LTH" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:3IUF" FT TURN 212..214 FT /evidence="ECO:0007829|PDB:3IUF" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:3IUF" FT HELIX 221..230 FT /evidence="ECO:0007829|PDB:3IUF" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 296..298 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 304..308 FT /evidence="ECO:0007829|PDB:5VDC" FT HELIX 311..316 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 317..321 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 325..327 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:5VDC" FT HELIX 339..341 FT /evidence="ECO:0007829|PDB:5VDC" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 346..348 FT /evidence="ECO:0007829|PDB:5VDC" FT STRAND 351..353 FT /evidence="ECO:0007829|PDB:5VDC" FT TURN 354..356 FT /evidence="ECO:0007829|PDB:5VDC" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:5VDC" FT HELIX 372..378 FT /evidence="ECO:0007829|PDB:5VDC" FT HELIX 379..381 FT /evidence="ECO:0007829|PDB:5VDC" SQ SEQUENCE 391 AA; 44155 MW; 1044B4D3036075FC CRC64; MAAVVENVVK LLGEQYYKDA MEQCHNYNAR LCAERSVRLP FLDSQTGVAQ SNCYIWMEKR HRGPGLASGQ LYSYPARRWR KKRRAHPPED PRLSFPSIKP DTDQTLKKEG LISQDGSSLE ALLRTDPLEK RGAPDPRVDD DSLGEFPVTN SRARKRILEP DDFLDDLDDE DYEEDTPKRR GKGKSKGKGV GSARKKLDAS ILEDRDKPYA CDICGKRYKN RPGLSYHYAH SHLAEEEGED KEDSQPPTPV SQRSEEQKSK KGPDGLALPN NYCDFCLGDS KINKKTGQPE ELVSCSDCGR SGHPSCLQFT PVMMAAVKTY RWQCIECKCC NICGTSENDD QLLFCDDCDR GYHMYCLTPS MSEPPEGSWS CHLCLDLLKE KASIYQNQNS S //