ID BPTF_HUMAN Reviewed; 3046 AA. AC Q12830; Q6NX67; Q7Z7D6; Q9UIG2; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 27-MAR-2024, entry version 218. DE RecName: Full=Nucleosome-remodeling factor subunit BPTF; DE AltName: Full=Bromodomain and PHD finger-containing transcription factor; DE AltName: Full=Fetal Alz-50 clone 1 protein; DE AltName: Full=Fetal Alzheimer antigen; GN Name=BPTF; Synonyms=FAC1, FALZ; 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 2), AND TISSUE SPECIFICITY. RX PubMed=10662542; DOI=10.1006/geno.1999.6070; RA Jones M.H., Hamana N., Shimane M.; RT "Identification and characterization of BPTF, a novel bromodomain RT transcription factor."; RL Genomics 63:35-39(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 134-992 (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=7621746; DOI=10.1159/000111270; RA Bowser R., Giambrone A., Davies P.; RT "FAC1, a novel gene identified with the monoclonal antibody Alz50, is RT developmentally regulated in human brain."; RL Dev. Neurosci. 17:20-37(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-3046 (ISOFORM 4), FUNCTION, RP IDENTIFICATION IN THE NURF-1 ISWI CHROMATIN REMODELING COMPLEX, INTERACTION RP WITH SMARCA1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14609955; DOI=10.1093/emboj/cdg582; RA Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J., RA Shiekhattar R.; RT "Isolation of human NURF: a regulator of Engrailed gene expression."; RL EMBO J. 22:6089-6100(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2876-3046 (ISOFORM 1). RC TISSUE=Kidney; 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 [6] RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=9225734; DOI=10.1006/exnr.1997.6508; RA Mu X., Springer J.E., Bowser R.; RT "FAC1 expression and localization in motor neurons of developing, adult, RT and amyotrophic lateral sclerosis spinal cord."; RL Exp. Neurol. 146:17-24(1997). RN [7] RP DNA-BINDING, AND PHOSPHORYLATION. RX PubMed=10403843; DOI=10.1006/bbrc.1999.0986; RA Jordan-Sciutto K.L., Dragich J.M., Bowser R.; RT "DNA binding activity of the fetal Alz-50 clone 1 (FAC1) protein is RT enhanced by phosphorylation."; RL Biochem. Biophys. Res. Commun. 260:785-789(1999). RN [8] RP FUNCTION. RX PubMed=10575013; DOI=10.1074/jbc.274.49.35262; RA Jordan-Sciutto K.L., Dragich J.M., Rhodes J.L., Bowser R.; RT "Fetal Alz-50 clone 1, a novel zinc finger protein, binds a specific DNA RT sequence and acts as a transcriptional regulator."; RL J. Biol. Chem. 274:35262-35268(1999). RN [9] RP INTERACTION WITH MAZ, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=10727212; DOI=10.1021/bi992211q; RA Jordan-Sciutto K.L., Dragich J.M., Caltagarone J., Hall D.J., Bowser R.; RT "Fetal Alz-50 clone 1 (FAC1) protein interacts with the Myc-associated zinc RT finger protein (ZF87/MAZ) and alters its transcriptional activity."; RL Biochemistry 39:3206-3215(2000). RN [10] RP INTERACTION WITH KEAP1, AND SUBCELLULAR LOCATION. RX PubMed=15379550; DOI=10.1021/bi0494166; RA Strachan G.D., Morgan K.L., Otis L.L., Caltagarone J., Gittis A., RA Bowser R., Jordan-Sciutto K.L.; RT "Fetal Alz-50 clone 1 interacts with the human orthologue of the Kelch-like RT Ech-associated protein."; RL Biochemistry 43:12113-12122(2004). RN [11] RP IDENTIFICATION IN COMPLEXES WITH SMARCA1, AND INTERACTION WITH SMARCA1. RX PubMed=15310751; DOI=10.1074/jbc.m406212200; RA Barak O., Lazzaro M.A., Cooch N.S., Picketts D.J., Shiekhattar R.; RT "A tissue-specific, naturally occurring human SNF2L variant inactivates RT chromatin remodeling."; RL J. Biol. Chem. 279:45130-45138(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1064, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP FUNCTION, MUTAGENESIS OF TRP-2891, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16728976; DOI=10.1038/nature04815; RA Wysocka J., Swigut T., Xiao H., Milne T.A., Kwon S.Y., Landry J., Kauer M., RA Tackett A.J., Chait B.T., Badenhorst P., Wu C., Allis C.D.; RT "A PHD finger of NURF couples histone H3 lysine 4 trimethylation with RT chromatin remodelling."; RL Nature 442:86-90(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763; SER-1300 AND SER-2098, RP AND 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 [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY RP 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-880, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-763; SER-1310 AND RP SER-2098, AND 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 [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-572; SER-763; RP THR-1064; SER-1231; SER-1300; SER-1310 AND SER-2465, AND IDENTIFICATION BY RP 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-572; SER-1300; RP THR-1303 AND SER-2098, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [23] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2155; ARG-2162; ARG-2184 AND RP ARG-2191, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1088, AND IDENTIFICATION BY MASS RP 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 [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1088, 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 [26] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1088, AND IDENTIFICATION BY MASS RP 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 [28] RP INVOLVEMENT IN NEDDFL, AND VARIANTS NEDDFL THR-1924; ARG-2996 AND RP 3027-LYS--SER-3046 DEL. RX PubMed=28942966; DOI=10.1016/j.ajhg.2017.08.014; RG Deciphering Developmental Disorders Study; RA Stankiewicz P., Khan T.N., Szafranski P., Slattery L., Streff H., RA Vetrini F., Bernstein J.A., Brown C.W., Rosenfeld J.A., Rednam S., RA Scollon S., Bergstrom K.L., Parsons D.W., Plon S.E., Vieira M.W., RA Quaio C.R.D.C., Baratela W.A.R., Acosta Guio J.C., Armstrong R., RA Mehta S.G., Rump P., Pfundt R., Lewandowski R., Fernandes E.M., RA Shinde D.N., Tang S., Hoyer J., Zweier C., Reis A., Bacino C.A., Xiao R., RA Breman A.M., Smith J.L., Katsanis N., Bostwick B., Popp B., Davis E.E., RA Yang Y.; RT "Haploinsufficiency of the Chromatin Remodeler BPTF Causes Syndromic RT Developmental and Speech Delay, Postnatal Microcephaly, and Dysmorphic RT Features."; RL Am. J. Hum. Genet. 101:503-515(2017). RN [29] RP FUNCTION, IDENTIFICATION IN THE NURF-1 ISWI CHROMATIN REMODELING COMPLEX, RP IDENTIFICATION IN THE NURF-5 CHROMATIN REMODELING COMPLEX, AND INTERACTION RP WITH SMARCA1 AND SMARCA5. RX PubMed=28801535; DOI=10.15252/embr.201744011; RA Oppikofer M., Bai T., Gan Y., Haley B., Liu P., Sandoval W., Ciferri C., RA Cochran A.G.; RT "Expansion of the ISWI chromatin remodeler family with new active RT complexes."; RL EMBO Rep. 18:1697-1706(2017). RN [30] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1088; LYS-1138; LYS-1209 AND RP LYS-1730, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2865-3033, X-RAY CRYSTALLOGRAPHY RP (2.0 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH H3(1-154)K4ME3, X-RAY RP CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH RP H3(1-154)K4ME2, STRUCTURE BY NMR OF 2865-2922, STRUCTURE BY NMR OF RP 2865-2922 IN COMPLEX WITH H3(1-154)K4ME3, FUNCTION, AND MUTAGENESIS OF RP TYR-2869; TYR-2876; TYR-2882; GLY-2884; ASP-2886; GLN-2889 AND TRP-2891. RX PubMed=16728978; DOI=10.1038/nature04802; RA Li H., Ilin S., Wang W., Duncan E.M., Wysocka J., Allis C.D., Patel D.J.; RT "Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF RT PHD finger of NURF."; RL Nature 442:91-95(2006). RN [32] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH RP H3(1-154)K4ME2, FUNCTION, DOMAIN PHD-FINGER, AND MUTAGENESIS OF TYR-2876. RX PubMed=18042461; DOI=10.1016/j.molcel.2007.10.023; RA Li H., Fischle W., Wang W., Duncan E.M., Liang L., Murakami-Ishibe S., RA Allis C.D., Patel D.J.; RT "Structural basis for lower lysine methylation state-specific readout by RT MBT repeats of L3MBTL1 and an engineered PHD finger."; RL Mol. Cell 28:677-691(2007). RN [33] RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 2914-3037. RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013; RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., RA Gingras A.C., Arrowsmith C.H., Knapp S.; RT "Histone recognition and large-scale structural analysis of the human RT bromodomain family."; RL Cell 149:214-231(2012). CC -!- FUNCTION: Regulatory subunit of the ATP-dependent NURF-1 and NURF-5 CC ISWI chromatin remodeling complexes, which form ordered nucleosome CC arrays on chromatin and facilitate access to DNA during DNA-templated CC processes such as DNA replication, transcription, and repair CC (PubMed:14609955, PubMed:28801535). The NURF-1 ISWI chromatin CC remodeling complex has a lower ATP hydrolysis rate than the NURF-5 ISWI CC chromatin remodeling complex (PubMed:28801535). Within the NURF-1 ISWI CC chromatin-remodeling complex, binds to the promoters of En1 and En2 to CC positively regulate their expression and promote brain development CC (PubMed:14609955). Histone-binding protein which binds to H3 tails CC trimethylated on 'Lys-4' (H3K4me3), which mark transcription start CC sites of active genes (PubMed:16728976, PubMed:16728978). Binds to CC histone H3 tails dimethylated on 'Lys-4' (H3K4Me2) to a lesser extent CC (PubMed:16728976, PubMed:16728978, PubMed:18042461). May also regulate CC transcription through direct binding to DNA or transcription factors CC (PubMed:10575013). {ECO:0000269|PubMed:10575013, CC ECO:0000269|PubMed:14609955, ECO:0000269|PubMed:16728976, CC ECO:0000269|PubMed:16728978, ECO:0000269|PubMed:18042461, CC ECO:0000269|PubMed:28801535}. CC -!- SUBUNIT: Interacts with MAZ (PubMed:10727212). Interacts with KEAP1 CC (PubMed:15379550). Component of the NURF-1 ISWI chromatin remodeling CC complex (also called the nucleosome-remodeling factor (NURF) complex) CC at least composed of SMARCA1 (isoform 2), BPTF, RBBP4 and RBBP7 CC (PubMed:14609955, PubMed:28801535). Within the complex interacts with CC isoform 2 of SMARCA1 (PubMed:14609955, PubMed:15310751, CC PubMed:28801535). Component of the BPFT-SMARCA1 complex at least CC composed of SMARCA1 (isoform 1), BPFT, RBBP4 and RBBP7; the complex is CC catalytically inactive and does not remodel chromatin CC (PubMed:15310751). Within the complex interacts with isoform 1 of CC SMARCA1 (PubMed:15310751). Component of the NURF-5 ISWI chromatin CC remodeling complex at least composed of SMARCA5/SNF2H and BPTF CC (PubMed:28801535). Within NURF-5 ISWI chromatin remodeling complex CC interacts with SMARCA5/SNF2H (PubMed:28801535). CC {ECO:0000269|PubMed:10727212, ECO:0000269|PubMed:14609955, CC ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15379550, CC ECO:0000269|PubMed:28801535}. CC -!- INTERACTION: CC Q12830; P62805: H4C9; NbExp=3; IntAct=EBI-1560273, EBI-302023; CC Q12830; P28370: SMARCA1; NbExp=6; IntAct=EBI-1560273, EBI-2822460; CC Q12830-4; Q71DI3: H3C15; NbExp=2; IntAct=EBI-4288838, EBI-750650; CC Q12830-4; P62805: H4C9; NbExp=16; IntAct=EBI-4288838, EBI-302023; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15379550}. Nucleus CC {ECO:0000269|PubMed:10727212, ECO:0000269|PubMed:25593309, CC ECO:0000269|PubMed:9225734}. Note=Localizes to sites of DNA damage CC (PubMed:25593309). In brains of Alzheimer disease patients, present in CC a subset of amyloid-containing plaques (PubMed:10727212). CC {ECO:0000269|PubMed:10727212, ECO:0000269|PubMed:25593309}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q12830-1; Sequence=Displayed; CC Name=2; CC IsoId=Q12830-2; Sequence=VSP_020402; CC Name=4; CC IsoId=Q12830-4; Sequence=VSP_020405; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in CC testis. Present in kidney, liver and brain. In the brain, highest CC levels are found in motor cortex (at protein level). CC {ECO:0000269|PubMed:10662542, ECO:0000269|PubMed:10727212, CC ECO:0000269|PubMed:7621746, ECO:0000269|PubMed:9225734}. CC -!- DEVELOPMENTAL STAGE: Abundantly expressed in the fetal brain. Present CC throughout the gray and white matter of the developing spinal cord at CC 18-22 gestational weeks. Expressed at low levels in adult brain and CC spinal cord and reexpressed in neurodegenerative diseases (at protein CC level). {ECO:0000269|PubMed:9225734}. CC -!- DOMAIN: The second PHD-type zinc finger mediates binding to histone CC H3K4Me3. Has specificity for trimethyllysine; introducing a mutation in CC the Tyr-2876 residue can induce binding to dimethyllysine. CC {ECO:0000269|PubMed:18042461}. CC -!- PTM: Phosphorylation enhances DNA-binding. CC {ECO:0000269|PubMed:10403843}. CC -!- PTM: Highly susceptible to proteolysis. CC -!- DISEASE: Neurodevelopmental disorder with dysmorphic facies and distal CC limb anomalies (NEDDFL) [MIM:617755]: An autosomal dominant CC neurodevelopmental disorder characterized by variable degrees of CC developmental delay, intellectual disability, speech delay, postnatal CC microcephaly, dysmorphic features, and mild abnormalities of the hands CC and feet. {ECO:0000269|PubMed:28942966}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the PBTF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA97522.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAA97522.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305}; CC Sequence=BAA89208.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors in the N-terminal part.; 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; AB032251; BAA89208.1; ALT_SEQ; mRNA. DR EMBL; AC006534; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107377; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC134407; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U05237; AAA97522.1; ALT_SEQ; mRNA. DR EMBL; AY282495; AAP22284.1; -; mRNA. DR EMBL; BC067234; AAH67234.1; -; mRNA. DR CCDS; CCDS11673.1; -. [Q12830-2] DR PIR; G01252; G01252. DR RefSeq; NP_004450.3; NM_004459.6. [Q12830-4] DR RefSeq; NP_872579.2; NM_182641.3. [Q12830-2] DR PDB; 2F6J; X-ray; 2.00 A; A/B/C=2865-3033. DR PDB; 2F6N; X-ray; 2.00 A; A/B=2865-3033. DR PDB; 2FSA; X-ray; 1.90 A; A/B/C=2865-3033. DR PDB; 2FUI; NMR; -; A=2865-2921. DR PDB; 2FUU; NMR; -; A=2865-2921. DR PDB; 2RI7; X-ray; 1.45 A; A=2865-3033. DR PDB; 3QZS; X-ray; 1.80 A; A/B=2924-3033. DR PDB; 3QZT; X-ray; 1.50 A; A=2924-3033. DR PDB; 3QZV; X-ray; 2.00 A; A=2865-3033. DR PDB; 3UV2; X-ray; 1.58 A; A=2914-3037. DR PDB; 5H6Y; X-ray; 2.00 A; A=2921-3036. DR PDB; 5R4G; X-ray; 1.25 A; A=2917-3037. DR PDB; 5R4H; X-ray; 1.18 A; A=2917-3037. DR PDB; 5R4I; X-ray; 1.28 A; A=2917-3037. DR PDB; 5R4J; X-ray; 1.39 A; A=2917-3037. DR PDB; 5R4K; X-ray; 1.17 A; A=2917-3037. DR PDB; 5R4L; X-ray; 1.13 A; A=2917-3037. DR PDB; 5R4M; X-ray; 1.11 A; A=2917-3037. DR PDB; 5R4N; X-ray; 1.28 A; A=2917-3037. DR PDB; 5R4O; X-ray; 1.05 A; A=2917-3037. DR PDB; 6AZE; X-ray; 2.45 A; A=2866-3032. DR PDB; 6LU5; X-ray; 1.87 A; A=2925-3032. DR PDB; 6LU6; X-ray; 1.97 A; A=2924-3033. DR PDB; 7DMY; X-ray; 2.00 A; A=2917-3037. DR PDB; 7DN4; X-ray; 2.84 A; A/B/C/D/E/F=2917-3037. DR PDB; 7F5D; X-ray; 1.57 A; A=2924-3033. DR PDB; 7F5E; X-ray; 2.20 A; A=2924-3033. DR PDB; 7JT4; X-ray; 2.06 A; A=2917-3037. DR PDB; 7K6R; X-ray; 1.60 A; A=2917-3037. DR PDB; 7K6S; X-ray; 1.23 A; A=2917-3037. DR PDB; 7KDW; X-ray; 1.71 A; A/B=2917-3037. DR PDB; 7KDZ; X-ray; 1.54 A; A=2917-3037. DR PDB; 7LP0; X-ray; 1.66 A; A/B=2917-3037. DR PDB; 7LPK; X-ray; 1.39 A; A/B=2917-3037. DR PDB; 7LRK; X-ray; 1.44 A; A/B=2917-3037. DR PDB; 7LRO; X-ray; 1.45 A; A/B=2917-3037. DR PDB; 7M2E; X-ray; 1.75 A; A=2917-3037. DR PDB; 7RWN; X-ray; 1.39 A; A=2917-3037. DR PDB; 7RWO; X-ray; 1.58 A; A=2917-3037. DR PDB; 7RWP; X-ray; 1.73 A; A=2917-3037. DR PDB; 7RWQ; X-ray; 1.90 A; A=2917-3037. DR PDB; 7VD4; X-ray; 1.86 A; A=2924-3033. DR PDB; 8AG2; X-ray; 1.02 A; A=2917-3037. DR PDBsum; 2F6J; -. DR PDBsum; 2F6N; -. DR PDBsum; 2FSA; -. DR PDBsum; 2FUI; -. DR PDBsum; 2FUU; -. DR PDBsum; 2RI7; -. DR PDBsum; 3QZS; -. DR PDBsum; 3QZT; -. DR PDBsum; 3QZV; -. DR PDBsum; 3UV2; -. DR PDBsum; 5H6Y; -. DR PDBsum; 5R4G; -. DR PDBsum; 5R4H; -. DR PDBsum; 5R4I; -. DR PDBsum; 5R4J; -. DR PDBsum; 5R4K; -. DR PDBsum; 5R4L; -. DR PDBsum; 5R4M; -. DR PDBsum; 5R4N; -. DR PDBsum; 5R4O; -. DR PDBsum; 6AZE; -. DR PDBsum; 6LU5; -. DR PDBsum; 6LU6; -. DR PDBsum; 7DMY; -. DR PDBsum; 7DN4; -. DR PDBsum; 7F5D; -. DR PDBsum; 7F5E; -. DR PDBsum; 7JT4; -. DR PDBsum; 7K6R; -. DR PDBsum; 7K6S; -. DR PDBsum; 7KDW; -. DR PDBsum; 7KDZ; -. DR PDBsum; 7LP0; -. DR PDBsum; 7LPK; -. DR PDBsum; 7LRK; -. DR PDBsum; 7LRO; -. DR PDBsum; 7M2E; -. DR PDBsum; 7RWN; -. DR PDBsum; 7RWO; -. DR PDBsum; 7RWP; -. DR PDBsum; 7RWQ; -. DR PDBsum; 7VD4; -. DR PDBsum; 8AG2; -. DR SMR; Q12830; -. DR BioGRID; 108481; 180. DR ComplexPortal; CPX-688; NuRF chromatin remodeling complex. DR CORUM; Q12830; -. DR DIP; DIP-38919N; -. DR ELM; Q12830; -. DR IntAct; Q12830; 40. DR MINT; Q12830; -. DR STRING; 9606.ENSP00000307208; -. DR BindingDB; Q12830; -. DR ChEMBL; CHEMBL3085621; -. DR GuidetoPHARMACOLOGY; 2723; -. DR GlyConnect; 2901; 1 O-GlcNAc glycan (5 sites). DR GlyCosmos; Q12830; 26 sites, 2 glycans. DR GlyGen; Q12830; 64 sites, 2 O-linked glycans (64 sites). DR iPTMnet; Q12830; -. DR PhosphoSitePlus; Q12830; -. DR SwissPalm; Q12830; -. DR BioMuta; BPTF; -. DR DMDM; 215274183; -. DR EPD; Q12830; -. DR jPOST; Q12830; -. DR MassIVE; Q12830; -. DR MaxQB; Q12830; -. DR PaxDb; 9606-ENSP00000307208; -. DR PeptideAtlas; Q12830; -. DR ProteomicsDB; 58973; -. [Q12830-1] DR ProteomicsDB; 58974; -. [Q12830-2] DR ProteomicsDB; 58975; -. [Q12830-4] DR Pumba; Q12830; -. DR ABCD; Q12830; 1 sequenced antibody. DR Antibodypedia; 19216; 130 antibodies from 27 providers. DR DNASU; 2186; -. DR Ensembl; ENST00000306378.11; ENSP00000307208.6; ENSG00000171634.19. [Q12830-2] DR Ensembl; ENST00000321892.8; ENSP00000315454.4; ENSG00000171634.19. [Q12830-1] DR GeneID; 2186; -. DR KEGG; hsa:2186; -. DR MANE-Select; ENST00000306378.11; ENSP00000307208.6; NM_182641.4; NP_872579.2. [Q12830-2] DR UCSC; uc002jgf.4; human. [Q12830-1] DR AGR; HGNC:3581; -. DR CTD; 2186; -. DR DisGeNET; 2186; -. DR GeneCards; BPTF; -. DR HGNC; HGNC:3581; BPTF. DR HPA; ENSG00000171634; Low tissue specificity. DR MalaCards; BPTF; -. DR MIM; 601819; gene. DR MIM; 617755; phenotype. DR neXtProt; NX_Q12830; -. DR OpenTargets; ENSG00000171634; -. DR Orphanet; 529962; 17q24.2 microdeletion syndrome. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA162377557; -. DR VEuPathDB; HostDB:ENSG00000171634; -. DR eggNOG; KOG1473; Eukaryota. DR eggNOG; KOG1632; Eukaryota. DR eggNOG; KOG1827; Eukaryota. DR GeneTree; ENSGT00940000154830; -. DR HOGENOM; CLU_000284_1_0_1; -. DR InParanoid; Q12830; -. DR OMA; PEQYTNV; -. DR OrthoDB; 2878869at2759; -. DR PhylomeDB; Q12830; -. DR TreeFam; TF316840; -. DR PathwayCommons; Q12830; -. DR SignaLink; Q12830; -. DR SIGNOR; Q12830; -. DR BioGRID-ORCS; 2186; 263 hits in 1191 CRISPR screens. DR ChiTaRS; BPTF; human. DR EvolutionaryTrace; Q12830; -. DR GeneWiki; BPTF; -. DR GenomeRNAi; 2186; -. DR Pharos; Q12830; Tchem. DR PRO; PR:Q12830; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q12830; Protein. DR Bgee; ENSG00000171634; Expressed in sural nerve and 204 other cell types or tissues. DR ExpressionAtlas; Q12830; baseline and differential. DR GO; GO:1904949; C:ATPase complex; IDA:ComplexPortal. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016589; C:NURF complex; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:HGNC-UCL. DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl. DR GO; GO:0007420; P:brain development; IMP:HGNC-UCL. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl. DR GO; GO:0006338; P:chromatin remodeling; IDA:HGNC-UCL. DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl. DR GO; GO:0007492; P:endoderm development; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:HGNC-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:HGNC-UCL. DR CDD; cd05509; Bromo_gcn5_like; 1. DR CDD; cd15559; PHD1_BPTF; 1. DR CDD; cd15560; PHD2_3_BPTF; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR IDEAL; IID00071; -. DR InterPro; IPR038028; BPTF. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR018501; DDT_dom. DR InterPro; IPR028941; WHIM2_dom. 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; PTHR45975; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1. DR PANTHER; PTHR45975:SF2; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF02791; DDT; 1. DR Pfam; PF00628; PHD; 2. DR Pfam; PF15613; WSD; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SMART; SM00571; DDT; 1. DR SMART; SM00249; PHD; 2. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS50827; DDT; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 2. DR Genevisible; Q12830; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Bromodomain; KW Chromatin regulator; Coiled coil; Cytoplasm; Disease variant; KW Intellectual disability; Isopeptide bond; Metal-binding; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..3046 FT /note="Nucleosome-remodeling factor subunit BPTF" FT /id="PRO_0000087176" FT DOMAIN 240..300 FT /note="DDT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063" FT DOMAIN 2944..3014 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT ZN_FING 390..437 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 2867..2918 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 1..232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 567..774 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 640..749 FT /note="Interaction with KEAP1" FT /evidence="ECO:0000269|PubMed:15379550" FT REGION 839..921 FT /note="Interaction with MAZ" FT /evidence="ECO:0000269|PubMed:10727212" FT REGION 1057..1157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1215..1339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1371..1448 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1465..1537 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1605..1706 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1973..2003 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2041..2070 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2160..2180 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2232..2270 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2346..2549 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2714..2733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2795..2858 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 574..604 FT /evidence="ECO:0000255" FT COILED 978..1007 FT /evidence="ECO:0000255" FT COILED 2022..2050 FT /evidence="ECO:0000255" FT COILED 2706..2732 FT /evidence="ECO:0000255" FT COMPBIAS 18..35 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..88 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 129..187 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..205 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 214..229 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 567..626 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 627..671 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 687..726 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 727..741 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1063..1106 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1112..1153 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1217..1238 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1244..1283 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1284..1301 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1309..1324 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1371..1393 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1407..1443 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1485..1526 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1608..1660 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1667..1700 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2050..2070 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2346..2406 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2413..2549 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2714..2730 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2796..2821 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2834..2858 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 2869 FT /note="Histone H3K4me3 binding" FT SITE 2876 FT /note="Histone H3K4me3 binding" FT SITE 2882 FT /note="Histone H3K4me3 binding" FT SITE 2891 FT /note="Histone H3K4me3 binding" FT MOD_RES 216 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 572 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 763 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 817 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 880 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1064 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1231 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1300 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1303 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1310 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 2098 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 2155 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2162 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2184 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2191 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2465 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 1088 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:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1138 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1209 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1730 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 622..747 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10662542" FT /id="VSP_020402" FT VAR_SEQ 2522..2664 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14609955" FT /id="VSP_020405" FT VARIANT 1924 FT /note="A -> T (in NEDDFL; dbSNP:rs1425998598)" FT /evidence="ECO:0000269|PubMed:28942966" FT /id="VAR_080531" FT VARIANT 2996 FT /note="M -> R (in NEDDFL; dbSNP:rs782736894)" FT /evidence="ECO:0000269|PubMed:28942966" FT /id="VAR_080532" FT VARIANT 3027..3046 FT /note="Missing (in NEDDFL)" FT /evidence="ECO:0000269|PubMed:28942966" FT /id="VAR_080533" FT MUTAGEN 2869 FT /note="Y->T: Abolishes binding to histone H3K4me3." FT /evidence="ECO:0000269|PubMed:16728978" FT MUTAGEN 2876 FT /note="Y->E: Induces binding to histone H3K4me2." FT /evidence="ECO:0000269|PubMed:16728978, FT ECO:0000269|PubMed:18042461" FT MUTAGEN 2876 FT /note="Y->T: Strongly reduces binding to histone H3K4me3." FT /evidence="ECO:0000269|PubMed:16728978, FT ECO:0000269|PubMed:18042461" FT MUTAGEN 2882 FT /note="Y->S: Abolishes binding to histone H3K4me3." FT /evidence="ECO:0000269|PubMed:16728978" FT MUTAGEN 2884 FT /note="G->E,L: Strongly reduces binding to histone FT H3K4me3." FT /evidence="ECO:0000269|PubMed:16728978" FT MUTAGEN 2886 FT /note="D->N,A: Abolishes binding to histone H3K4me3." FT /evidence="ECO:0000269|PubMed:16728978" FT MUTAGEN 2889 FT /note="Q->K: Strongly reduces binding to histone H3K4me3." FT /evidence="ECO:0000269|PubMed:16728978" FT MUTAGEN 2891 FT /note="W->E,F: Abolishes binding to histone H3K4me3." FT /evidence="ECO:0000269|PubMed:16728976, FT ECO:0000269|PubMed:16728978" FT CONFLICT 752 FT /note="K -> T (in Ref. 3; AAA97522)" FT /evidence="ECO:0000305" FT CONFLICT 757 FT /note="N -> T (in Ref. 3; AAA97522)" FT /evidence="ECO:0000305" FT CONFLICT 969 FT /note="S -> F (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 1268 FT /note="E -> Q (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 1330 FT /note="S -> T (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 1842 FT /note="S -> T (in Ref. 1; BAA89208 and 4; AAP22284)" FT /evidence="ECO:0000305" FT CONFLICT 1926 FT /note="A -> V (in Ref. 1; BAA89208 and 4; AAP22284)" FT /evidence="ECO:0000305" FT CONFLICT 1932 FT /note="T -> S (in Ref. 1; BAA89208 and 4; AAP22284)" FT /evidence="ECO:0000305" FT CONFLICT 1960 FT /note="S -> F (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 2393 FT /note="E -> K (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 2404 FT /note="Q -> R (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 2540 FT /note="T -> S (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 2802..2803 FT /note="AP -> VL (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 2818 FT /note="A -> G (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 2832 FT /note="A -> V (in Ref. 1; BAA89208)" FT /evidence="ECO:0000305" FT CONFLICT 2876 FT /note="Y -> G (in Ref. 5; AAH67234)" FT /evidence="ECO:0000305" FT CONFLICT 2880 FT /note="K -> Q (in Ref. 5; AAH67234)" FT /evidence="ECO:0000305" FT TURN 2870..2873 FT /evidence="ECO:0007829|PDB:2RI7" FT STRAND 2882..2884 FT /evidence="ECO:0007829|PDB:2RI7" FT TURN 2886..2888 FT /evidence="ECO:0007829|PDB:2RI7" FT STRAND 2891..2893 FT /evidence="ECO:0007829|PDB:2RI7" FT HELIX 2894..2897 FT /evidence="ECO:0007829|PDB:2RI7" FT HELIX 2901..2904 FT /evidence="ECO:0007829|PDB:2RI7" FT HELIX 2913..2919 FT /evidence="ECO:0007829|PDB:2FUI" FT HELIX 2921..2925 FT /evidence="ECO:0007829|PDB:5R4O" FT HELIX 2930..2945 FT /evidence="ECO:0007829|PDB:8AG2" FT HELIX 2947..2952 FT /evidence="ECO:0007829|PDB:8AG2" FT HELIX 2958..2960 FT /evidence="ECO:0007829|PDB:8AG2" FT HELIX 2964..2967 FT /evidence="ECO:0007829|PDB:8AG2" FT HELIX 2974..2982 FT /evidence="ECO:0007829|PDB:8AG2" FT HELIX 2989..3006 FT /evidence="ECO:0007829|PDB:8AG2" FT HELIX 3012..3034 FT /evidence="ECO:0007829|PDB:8AG2" SQ SEQUENCE 3046 AA; 338262 MW; 37D7206977A8DB09 CRC64; MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR WAAAQAEVAP KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG RTGGGGGGGH LARTTAARRA VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG DAEETQDSED DEEDEMEEDD DDSDYPEEME DDDDDASYCT ESSFRSHSTY SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN EHIMNVIAIY EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE DYPYGPVENK IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG DLLCCETCSA VYHLECVKPP LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE EDTENENEKK IWYYSTKVQL AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK ARGSNKSFLA AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ SLEKDSDDKT PDDDPEQGKS EEPTEVGDKG NSVSANLGDN TTNATSEETS PSEGRSPVGC LSETPDSSNM AEKKVASELP QDVPEEPNKT CESSNTSATT TSIQPNLENS NSSSELNSSQ SESAKAADDP ENGERESHTP VSIQEEIVGD FKSEKSNGEL SESPGAGKGA SGSTRIITRL RNPDSKLSQL KSQQVAAAAH EANKLFKEGK EVLVVNSQGE ISRLSTKKEV IMKGNINNYF KLGQEGKYRV YHNQYSTNSF ALNKHQHRED HDKRRHLAHK FCLTPAGEFK WNGSVHGSKV LTISTLRLTI TQLENNIPSS FLHPNWASHR ANWIKAVQMC SKPREFALAL AILECAVKPV VMLPIWRESL GHTRLHRMTS IEREEKEKVK KKEKKQEEEE TMQQATWVKY TFPVKHQVWK QKGEEYRVTG YGGWSWISKT HVYRFVPKLP GNTNVNYRKS LEGTKNNMDE NMDESDKRKC SRSPKKIKIE PDSEKDEVKG SDAAKGADQN EMDISKITEK KDQDVKELLD SDSDKPCKEE PMEVDDDMKT ESHVNCQESS QVDVVNVSEG FHLRTSYKKK TKSSKLDGLL ERRIKQFTLE EKQRLEKIKL EGGIKGIGKT STNSSKNLSE SPVITKAKEG CQSDSMRQEQ SPNANNDQPE DLIQGCSESD SSVLRMSDPS HTTNKLYPKD RVLDDVSIRS PETKCPKQNS IENDIEEKVS DLASRGQEPS KSKTKGNDFF IDDSKLASAD DIGTLICKNK KPLIQEESDT IVSSSKSALH SSVPKSTNDR DATPLSRAMD FEGKLGCDSE SNSTLENSSD TVSIQDSSEE DMIVQNSNES ISEQFRTREQ DVEVLEPLKC ELVSGESTGN CEDRLPVKGT EANGKKPSQQ KKLEERPVNK CSDQIKLKNT TDKKNNENRE SEKKGQRTST FQINGKDNKP KIYLKGECLK EISESRVVSG NVEPKVNNIN KIIPENDIKS LTVKESAIRP FINGDVIMED FNERNSSETK SHLLSSSDAE GNYRDSLETL PSTKESDSTQ TTTPSASCPE SNSVNQVEDM EIETSEVKKV TSSPITSEEE SNLSNDFIDE NGLPINKNEN VNGESKRKTV ITEVTTMTST VATESKTVIK VEKGDKQTVV SSTENCAKST VTTTTTTVTK LSTPSTGGSV DIISVKEQSK TVVTTTVTDS LTTTGGTLVT SMTVSKEYST RDKVKLMKFS RPKKTRSGTA LPSYRKFVTK SSKKSIFVLP NDDLKKLARK GGIREVPYFN YNAKPALDIW PYPSPRPTFG ITWRYRLQTV KSLAGVSLML RLLWASLRWD DMAAKAPPGG GTTRTETSET EITTTEIIKR RDVGPYGIRS EYCIRKIICP IGVPETPKET PTPQRKGLRS SALRPKRPET PKQTGPVIIE TWVAEEELEL WEIRAFAERV EKEKAQAVEQ QAKKRLEQQK PTVIATSTTS PTSSTTSTIS PAQKVMVAPI SGSVTTGTKM VLTTKVGSPA TVTFQQNKNF HQTFATWVKQ GQSNSGVVQV QQKVLGIIPS STGTSQQTFT SFQPRTATVT IRPNTSGSGG TTSNSQVITG PQIRPGMTVI RTPLQQSTLG KAIIRTPVMV QPGAPQQVMT QIIRGQPVST AVSAPNTVSS TPGQKSLTSA TSTSNIQSSA SQPPRPQQGQ VKLTMAQLTQ LTQGHGGNQG LTVVIQGQGQ TTGQLQLIPQ GVTVLPGPGQ QLMQAAMPNG TVQRFLFTPL ATTATTASTT TTTVSTTAAG TGEQRQSKLS PQMQVHQDKT LPPAQSSSVG PAEAQPQTAQ PSAQPQPQTQ PQSPAQPEVQ TQPEVQTQTT VSSHVPSEAQ PTHAQSSKPQ VAAQSQPQSN VQGQSPVRVQ SPSQTRIRPS TPSQLSPGQQ SQVQTTTSQP IPIQPHTSLQ IPSQGQPQSQ PQVQSSTQTL SSGQTLNQVT VSSPSRPQLQ IQQPQPQVIA VPQLQQQVQV LSQIQSQVVA QIQAQQSGVP QQIKLQLPIQ IQQSSAVQTH QIQNVVTVQA ASVQEQLQRV QQLRDQQQKK KQQQIEIKRE HTLQASNQSE IIQKQVVMKH NAVIEHLKQK KSMTPAEREE NQRMIVCNQV MKYILDKIDK EEKQAAKKRK REESVEQKRS KQNATKLSAL LFKHKEQLRA EILKKRALLD KDLQIEVQEE LKRDLKIKKE KDLMQLAQAT AVAAPCPPVT PAPPAPPAPP PSPPPPPAVQ HTGLLSTPTL PAASQKRKRE EEKDSSSKSK KKKMISTTSK ETKKDTKLYC ICKTPYDESK FYIGCDRCQN WYHGRCVGIL QSEAELIDEY VCPQCQSTED AMTVLTPLTE KDYEGLKRVL RSLQAHKMAW PFLEPVDPND APDYYGVIKE PMDLATMEER VQRRYYEKLT EFVADMTKIF DNCRYYNPSD SPFYQCAEVL ESFFVQKLKG FKASRSHNNK LQSTAS //