BPTF_HUMAN
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 03-AUG-2022, entry version 209.
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 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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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. Nucleus. Note=In brains of Alzheimer
CC disease patients, present in a subset of amyloid-containing plaques.
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};
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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; 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; 7M2E; X-ray; 1.75 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; 7JT4; -.
DR PDBsum; 7K6R; -.
DR PDBsum; 7K6S; -.
DR PDBsum; 7KDW; -.
DR PDBsum; 7KDZ; -.
DR PDBsum; 7M2E; -.
DR SMR; Q12830; -.
DR BioGRID; 108481; 147.
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-Linked glycan (5 sites).
DR GlyGen; Q12830; 26 sites, 2 O-linked glycans (26 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; Q12830; -.
DR PeptideAtlas; Q12830; -.
DR PRIDE; Q12830; -.
DR ProteomicsDB; 58973; -. [Q12830-1]
DR ProteomicsDB; 58974; -. [Q12830-2]
DR ProteomicsDB; 58975; -. [Q12830-4]
DR ABCD; Q12830; 1 sequenced antibody.
DR Antibodypedia; 19216; 109 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 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; CESDREF; -.
DR OrthoDB; 343959at2759; -.
DR PhylomeDB; Q12830; -.
DR TreeFam; TF316840; -.
DR PathwayCommons; Q12830; -.
DR SignaLink; Q12830; -.
DR SIGNOR; Q12830; -.
DR BioGRID-ORCS; 2186; 249 hits in 1101 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 202 other tissues.
DR ExpressionAtlas; Q12830; baseline and differential.
DR Genevisible; Q12830; HS.
DR GO; GO:1904949; C:ATPase complex; IDA:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
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: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:0006357; P:regulation of transcription by RNA polymerase II; IMP:HGNC-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 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; PTHR45975; 2.
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; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 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.
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..2944
FT /evidence="ECO:0007829|PDB:5R4O"
FT HELIX 2947..2949
FT /evidence="ECO:0007829|PDB:2RI7"
FT HELIX 2950..2952
FT /evidence="ECO:0007829|PDB:5R4O"
FT TURN 2958..2960
FT /evidence="ECO:0007829|PDB:5R4O"
FT HELIX 2964..2967
FT /evidence="ECO:0007829|PDB:5R4O"
FT HELIX 2974..2982
FT /evidence="ECO:0007829|PDB:5R4O"
FT HELIX 2989..3006
FT /evidence="ECO:0007829|PDB:5R4O"
FT HELIX 3012..3036
FT /evidence="ECO:0007829|PDB:5R4O"
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
