ID BRPF1_HUMAN Reviewed; 1214 AA. AC P55201; B4DEZ6; Q7Z6E0; Q8TCM6; Q9UHI0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 02-SEP-2026, entry version 215. DE RecName: Full=Peregrin {ECO:0000305}; DE AltName: Full=Bromodomain and PHD finger-containing protein 1 {ECO:0000312|HGNC:HGNC:14255}; DE AltName: Full=Protein Br140 {ECO:0000303|PubMed:7906940}; GN Name=BRPF1 {ECO:0000312|HGNC:HGNC:14255}; GN Synonyms=BR140 {ECO:0000303|PubMed:7906940}; 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), AND TISSUE SPECIFICITY. RX PubMed=7906940; DOI=10.1006/bbrc.1994.1162; RA Thompson K.A., Wang B., Argraves W.S., Giancotti F.G., Schranck D.P., RA Ruoslahti E.; RT "BR140, a novel zinc-finger protein with homology to the TAF250 subunit of RT TFIID."; RL Biochem. Biophys. Res. Commun. 198:1143-1152(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Hu S.N., Dong W., Zeng Y.X., Yu J., Yang H.M.; RT "Sequencing and analyzing of BAC DNA on 3p26."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Cerebellum; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Eye; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-462, AND RP IDENTIFICATION BY 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 [9] RP FUNCTION, AND IDENTIFICATION IN THE MOZ/MORF COMPLEX. RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007; RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., RA Lane W.S., Tan S., Yang X.-J., Cote J.; RT "ING tumor suppressor proteins are critical regulators of chromatin RT acetylation required for genome expression and perpetuation."; RL Mol. Cell 21:51-64(2006). RN [10] RP FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH ING5; RP MEAF6; KAT6A AND KAT6B, SUBCELLULAR LOCATION, AND ACETYLATION. RX PubMed=18794358; DOI=10.1128/mcb.01297-08; RA Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., RA Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., RA Yang X.-J.; RT "Molecular architecture of quartet MOZ/MORF histone acetyltransferase RT complexes."; RL Mol. Cell. Biol. 28:6828-6843(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-1187, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, 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 [13] RP IDENTIFICATION BY MASS 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; SER-462 AND SER-1076, RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; SER-462; SER-860 AND RP SER-1076, AND 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 [16] RP FUNCTION, IDENTIFICATION IN THE HBO1 COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=24065767; DOI=10.1101/gad.223396.113; RA Lalonde M.E., Avvakumov N., Glass K.C., Joncas F.H., Saksouk N., RA Holliday M., Paquet E., Yan K., Tong Q., Klein B.J., Tan S., Yang X.J., RA Kutateladze T.G., Cote J.; RT "Exchange of associated factors directs a switch in HBO1 acetyltransferase RT histone tail specificity."; RL Genes Dev. 27:2009-2024(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-462, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY RP 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 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 [20] RP STRUCTURE BY NMR OF 633-740. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the bromodomain of peregrin."; RL Submitted (JUN-2006) to the PDB data bank. RN [21] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1076-1205 IN COMPLEX WITH HISTONE RP H3 PEPTIDE, AND INTERACTION WITH HISTONE H3. RX PubMed=20400950; DOI=10.1038/nsmb.1797; RA Vezzoli A., Bonadies N., Allen M.D., Freund S.M., Santiveri C.M., RA Kvinlaug B.T., Huntly B.J., Gottgens B., Bycroft M.; RT "Molecular basis of histone H3K36me3 recognition by the PWWP domain of RT Brpf1."; RL Nat. Struct. Mol. Biol. 17:617-619(2010). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1079-1207 IN COMPLEX WITH RP TRIMETHYLATED HISTONE H3 PEPTIDE, AND INTERACTION WITH HISTONE H3. RX PubMed=21720545; DOI=10.1371/journal.pone.0018919; RA Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L., RA Qiu W., Wang Y., Min J.; RT "Structural and histone binding ability characterizations of human PWWP RT domains."; RL PLoS ONE 6:E18919-E18919(2011). RN [23] RP INVOLVEMENT IN IDDDFP, VARIANTS IDDDFP SER-370; 455-ARG--ASP-1214 DEL; RP 833-GLY--ASP-1214 DEL AND 1100-PRO--ASP-1214 DEL, CHARACTERIZATION OF RP VARIANTS IDDDFP SER-370; 455-ARG--ASP-1214 DEL; 833-GLY--ASP-1214 DEL AND RP 1100-PRO--ASP-1214 DEL, FUNCTION, SUBUNIT, INTERACTION WITH KAT7, AND RP SUBCELLULAR LOCATION. RX PubMed=27939640; DOI=10.1016/j.ajhg.2016.11.011; RG DDD Study; RG CAUSES Study; RA Yan K., Rousseau J., Littlejohn R.O., Kiss C., Lehman A., Rosenfeld J.A., RA Stumpel C.T., Stegmann A.P., Robak L., Scaglia F., Nguyen T.T., Fu H., RA Ajeawung N.F., Camurri M.V., Li L., Gardham A., Panis B., Almannai M., RA Sacoto M.J., Baskin B., Ruivenkamp C., Xia F., Bi W., Cho M.T., RA Potjer T.P., Santen G.W., Parker M.J., Canham N., McKinnon M., Potocki L., RA MacKenzie J.J., Roeder E.R., Campeau P.M., Yang X.J.; RT "Mutations in the chromatin regulator gene BRPF1 cause syndromic RT intellectual disability and deficient histone acetylation."; RL Am. J. Hum. Genet. 100:91-104(2017). RN [24] RP INVOLVEMENT IN IDDDFP, AND VARIANTS IDDDFP 35-TYR--ASP-1214 DEL; ARG-389 RP AND 988-LEU--ASP-1214 DEL. RX PubMed=27939639; DOI=10.1016/j.ajhg.2016.11.010; RA Mattioli F., Schaefer E., Magee A., Mark P., Mancini G.M., Dieterich K., RA Von Allmen G., Alders M., Coutton C., van Slegtenhorst M., Vieville G., RA Engelen M., Cobben J.M., Juusola J., Pujol A., Mandel J.L., Piton A.; RT "Mutations in histone acetylase modifier BRPF1 cause an autosomal-dominant RT form of intellectual disability with associated ptosis."; RL Am. J. Hum. Genet. 100:105-116(2017). CC -!- FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT) CC complexes, such as the MOZ/MORF and HBO1 complexes, which have a CC histone H3 acetyltransferase activity (PubMed:16387653, CC PubMed:24065767, PubMed:27939640). Plays a key role in HBO1 complex by CC directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation CC (H3K14ac) (PubMed:24065767). Some HAT complexes preferentially mediate CC histone H3 'Lys-23' (H3K23ac) acetylation (PubMed:27939640). Positively CC regulates the transcription of RUNX1 and RUNX2 (PubMed:18794358). CC {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:27939640}. CC -!- SUBUNIT: Component of some HBO1 complex composed of KAT7/HBO1, MEAF6, CC ING5, and BRPF1 (PubMed:24065767). Component of the MOZ/MORF complex CC composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, CC BRD1/BRPF2 and BRPF3 (PubMed:16387653, PubMed:18794358, CC PubMed:27939640). Interacts (via PHD-type zinc finger domains) with CC unmethylated histone H3 at 'Lys-4' (H3K4me0) (PubMed:24065767). CC Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3) CC (PubMed:20400950, PubMed:21720545). Interacts with ING5; interaction CC directs BRPF1 to H4K4me3-enriched chromatin at the 5' of active genes CC (PubMed:24065767). Interacts with KAT7 (PubMed:27939640). CC {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358, CC ECO:0000269|PubMed:20400950, ECO:0000269|PubMed:21720545, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:27939640}. CC -!- INTERACTION: CC P55201; P0C0S8: H2AC17; NbExp=8; IntAct=EBI-2837428, EBI-1390628; CC P55201; P62805: H4C9; NbExp=8; IntAct=EBI-2837428, EBI-302023; CC P55201-2; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-12065306, EBI-5278764; CC P55201-2; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-12065306, EBI-11522539; CC P55201-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-12065306, EBI-739624; CC P55201-2; Q8WYH8: ING5; NbExp=3; IntAct=EBI-12065306, EBI-488533; CC P55201-2; Q2KHM9: KIAA0753; NbExp=3; IntAct=EBI-12065306, EBI-2805604; CC P55201-2; Q8N987: NECAB1; NbExp=3; IntAct=EBI-12065306, EBI-11956853; CC P55201-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12065306, EBI-739895; CC P55201-2; Q9Y2K6: USP20; NbExp=3; IntAct=EBI-12065306, EBI-2511991; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18794358, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:25593309, CC ECO:0000269|PubMed:27939640}. Chromosome {ECO:0000269|PubMed:24065767}. CC Cytoplasm {ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:27939640}. CC Note=Localization to the nucleus depends on KAT6A, ING5 and MEAF6 CC (PubMed:18794358, PubMed:27939640). Localizes to transcription start CC sites (PubMed:24065767). {ECO:0000269|PubMed:18794358, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:27939640}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P55201-1; Sequence=Displayed; CC Name=2; CC IsoId=P55201-2; Sequence=VSP_037955; CC Name=3; CC IsoId=P55201-3; Sequence=VSP_037956; CC Name=4; CC IsoId=P55201-4; Sequence=VSP_037957; CC -!- TISSUE SPECIFICITY: High levels in testis. CC {ECO:0000269|PubMed:7906940}. CC -!- PTM: Acetylated by KAT6A. {ECO:0000269|PubMed:18794358}. CC -!- DISEASE: Intellectual developmental disorder with dysmorphic facies and CC ptosis (IDDDFP) [MIM:617333]: An autosomal dominant neurodevelopmental CC disorder characterized by delayed psychomotor development, intellectual CC disability, delayed language, and facial dysmorphisms, most notably CC ptosis. Additional features may include poor growth, hypotonia, and CC seizures. {ECO:0000269|PubMed:27939639, ECO:0000269|PubMed:27939640}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. 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; M91585; AAB02119.1; -; mRNA. DR EMBL; AF176815; AAF19605.1; -; Genomic_DNA. DR EMBL; AK293865; BAG57257.1; -; mRNA. DR EMBL; AL713696; CAD28495.1; -; mRNA. DR EMBL; AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW63976.1; -; Genomic_DNA. DR EMBL; BC053851; AAH53851.1; -; mRNA. DR CCDS; CCDS2575.1; -. [P55201-1] DR CCDS; CCDS33692.1; -. [P55201-2] DR CCDS; CCDS82729.1; -. [P55201-4] DR CCDS; CCDS82730.1; -. [P55201-3] DR PIR; JC2069; JC2069. DR RefSeq; NP_001003694.1; NM_001003694.2. [P55201-2] DR RefSeq; NP_001305978.1; NM_001319049.2. [P55201-4] DR RefSeq; NP_001305979.1; NM_001319050.2. [P55201-3] DR RefSeq; NP_001425272.1; NM_001438343.1. [P55201-3] DR RefSeq; NP_004625.2; NM_004634.3. [P55201-1] DR RefSeq; XP_047304832.1; XM_047448876.1. [P55201-2] DR RefSeq; XP_054203765.1; XM_054347790.1. [P55201-2] DR PDB; 2D9E; NMR; -; A=633-740. DR PDB; 2RS9; NMR; -; B=633-740. DR PDB; 2X35; X-ray; 2.00 A; A=1076-1205. DR PDB; 2X4W; X-ray; 1.50 A; A=1076-1205. DR PDB; 2X4X; X-ray; 1.85 A; A/C/E/G=1076-1205. DR PDB; 2X4Y; X-ray; 1.70 A; A/C/E/G/I/K/M/O=1076-1205. DR PDB; 3L42; X-ray; 1.30 A; A=1079-1207. DR PDB; 3MO8; X-ray; 1.69 A; A=1079-1207. DR PDB; 4LC2; X-ray; 1.65 A; A=626-740. DR PDB; 4QYD; X-ray; 1.94 A; A=629-742. DR PDB; 4QYL; X-ray; 1.80 A; A/B/C/D=629-742. DR PDB; 4UYE; X-ray; 1.65 A; A/B=622-738. DR PDB; 5C6S; X-ray; 1.30 A; A=1079-1207. DR PDB; 5C7N; X-ray; 1.75 A; A=626-740. DR PDB; 5C85; X-ray; 1.70 A; A=626-740. DR PDB; 5C87; X-ray; 1.55 A; A=626-740. DR PDB; 5C89; X-ray; 1.65 A; A=627-740. DR PDB; 5D7X; X-ray; 1.35 A; A=626-740. DR PDB; 5DY7; X-ray; 1.69 A; A=626-740. DR PDB; 5DYA; X-ray; 1.65 A; A=625-740. DR PDB; 5DYC; X-ray; 1.65 A; A=625-740. DR PDB; 5E3D; X-ray; 1.71 A; A=626-740. DR PDB; 5E3G; X-ray; 1.65 A; A=626-740. DR PDB; 5EM3; X-ray; 1.40 A; A=626-740. DR PDB; 5EPR; X-ray; 1.65 A; A=626-740. DR PDB; 5EPS; X-ray; 1.47 A; A=627-740. DR PDB; 5EQ1; X-ray; 1.55 A; A=626-740. DR PDB; 5ERC; X-ray; 2.05 A; A=274-450. DR PDB; 5ETB; X-ray; 1.33 A; A=626-740. DR PDB; 5ETD; X-ray; 1.40 A; A=626-740. DR PDB; 5EV9; X-ray; 1.45 A; A=626-740. DR PDB; 5EVA; X-ray; 1.45 A; A=626-740. DR PDB; 5EWC; X-ray; 1.75 A; A=626-740. DR PDB; 5EWD; X-ray; 1.58 A; A=626-740. DR PDB; 5EWH; X-ray; 1.63 A; A=626-740. DR PDB; 5EWV; X-ray; 1.67 A; A=626-740. DR PDB; 5EWW; X-ray; 1.73 A; A=626-740. DR PDB; 5FFV; X-ray; 1.30 A; A/B=626-740. DR PDB; 5FFW; X-ray; 1.50 A; A/B=626-740. DR PDB; 5FFY; X-ray; 1.55 A; A=626-740. DR PDB; 5FG4; X-ray; 1.65 A; A=626-740. DR PDB; 5FG5; X-ray; 1.50 A; A/B=626-740. DR PDB; 5G4R; X-ray; 1.96 A; A/B/C/D=622-738. DR PDB; 5G4S; X-ray; 1.60 A; A=624-738. DR PDB; 5MWG; X-ray; 1.50 A; A/B=626-740. DR PDB; 5MWH; X-ray; 1.65 A; A/B=626-740. DR PDB; 5MWZ; X-ray; 1.25 A; A=626-740. DR PDB; 5MYG; X-ray; 2.30 A; A/B/C/D=626-740. DR PDB; 5O4S; X-ray; 1.75 A; A/B=626-740. DR PDB; 5O4T; X-ray; 1.50 A; A=626-740. DR PDB; 5O55; X-ray; 1.45 A; A=626-740. DR PDB; 5O5A; X-ray; 1.60 A; A=626-740. DR PDB; 5O5F; X-ray; 1.30 A; A=626-740. DR PDB; 5O5H; X-ray; 1.85 A; A=626-740. DR PDB; 5OV8; X-ray; 1.80 A; A/B=626-740. DR PDB; 5OWA; X-ray; 1.95 A; A/B/C/D=626-740. DR PDB; 5OWB; X-ray; 1.65 A; A=626-740. DR PDB; 5OWE; X-ray; 1.70 A; A=626-740. DR PDB; 5T4U; X-ray; 1.50 A; A=627-740. DR PDB; 5T4V; X-ray; 1.65 A; A=627-740. DR PDB; 6EKQ; X-ray; 1.65 A; A/B=626-740. DR PDB; 6U04; X-ray; 2.20 A; A=271-454. DR PDB; 7C4I; X-ray; 1.37 A; A=625-740. DR PDB; 8QAZ; X-ray; 1.40 A; A=626-740. DR PDB; 8QB0; X-ray; 1.45 A; A=626-740. DR PDB; 8QB2; X-ray; 1.42 A; A=626-740. DR AlphaFoldDB; P55201; -. DR BMRB; P55201; -. DR MDposit; P55201; -. DR SMR; P55201; -. DR BioGRID; 113614; 84. DR ComplexPortal; CPX-727; MOZ1 histone acetyltransferase complex. DR ComplexPortal; CPX-738; MORF1 histone acetyltransferase complex. DR CORUM; P55201; -. DR DIP; DIP-59001N; -. DR FunCoup; P55201; 3776. DR IntAct; P55201; 46. DR MINT; P55201; -. DR STRING; 9606.ENSP00000373340; -. DR BindingDB; P55201; -. DR ChEMBL; CHEMBL3132741; -. DR GuidetoPHARMACOLOGY; 2730; -. DR GlyGen; P55201; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P55201; -. DR PhosphoSitePlus; P55201; -. DR SwissPalm; P55201; -. DR BioMuta; BRPF1; -. DR DMDM; 116241271; -. DR jPOST; P55201; -. DR MassIVE; P55201; -. DR PaxDb; 9606-ENSP00000373340; -. DR PeptideAtlas; P55201; -. DR ProteomicsDB; 56806; -. [P55201-1] DR ProteomicsDB; 56807; -. [P55201-2] DR ProteomicsDB; 56808; -. [P55201-3] DR ProteomicsDB; 56809; -. [P55201-4] DR Pumba; P55201; -. DR TopDownProteomics; P55201-2; -. [P55201-2] DR Antibodypedia; 933; 64 antibodies from 18 providers. DR DNASU; 7862; -. DR Ensembl; ENST00000383829.7; ENSP00000373340.2; ENSG00000156983.18. [P55201-2] DR Ensembl; ENST00000433861.6; ENSP00000402485.2; ENSG00000156983.18. [P55201-4] DR Ensembl; ENST00000683743.1; ENSP00000507469.1; ENSG00000156983.18. [P55201-1] DR Ensembl; ENST00000684199.1; ENSP00000506921.1; ENSG00000156983.18. [P55201-2] DR Ensembl; ENST00000684333.1; ENSP00000508256.1; ENSG00000156983.18. [P55201-3] DR Ensembl; ENST00000879789.1; ENSP00000549848.1; ENSG00000156983.18. [P55201-1] DR Ensembl; ENST00000919142.1; ENSP00000589201.1; ENSG00000156983.18. [P55201-3] DR GeneID; 7862; -. DR KEGG; hsa:7862; -. DR MANE-Select; ENST00000383829.7; ENSP00000373340.2; NM_001003694.2; NP_001003694.1. [P55201-2] DR UCSC; uc003bsf.4; human. [P55201-1] DR AGR; HGNC:14255; -. DR ClinPGx; PA25424; -. DR CTD; 7862; -. DR DisGeNET; 7862; -. DR GeneCards; BRPF1; -. DR HGNC; HGNC:14255; BRPF1. DR HPA; ENSG00000156983; Tissue enhanced (bone). DR MalaCards; BRPF1; -. DR MIM; 602410; gene. DR MIM; 617333; phenotype. DR OpenTargets; ENSG00000156983; -. DR Orphanet; 1620; Distal deletion 3p syndrome. DR Orphanet; 698090; Ophthalmological abnormalities-facial dysmorphism-intellectual disability syndrome. DR VEuPathDB; HostDB:ENSG00000156983; -. DR eggNOG; KOG0955; Eukaryota. DR GeneTree; ENSGT00940000157794; -. DR HOGENOM; CLU_003589_1_0_1; -. DR InParanoid; P55201; -. DR OMA; PDYMDIV; -. DR OrthoDB; 20839at2759; -. DR PAN-GO; P55201; 5 GO annotations based on evolutionary models. DR PhylomeDB; P55201; -. DR PathwayCommons; P55201; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation. DR SignaLink; P55201; -. DR Agora; ENSG00000156983; -. DR BioGRID-ORCS; 7862; 182 hits in 1184 CRISPR screens. DR ChiTaRS; BRPF1; human. DR EvolutionaryTrace; P55201; -. DR GenomeRNAi; 7862; -. DR Pharos; P55201; Tchem. DR PRO; PR:P55201; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P55201; protein. DR Bgee; ENSG00000156983; Expressed in oocyte and 176 other cell types or tissues. DR ExpressionAtlas; P55201; baseline and differential. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB. DR GO; GO:0140566; F:histone reader activity; IBA:GO_Central. DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0050793; P:regulation of developmental process; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:1903706; P:regulation of hemopoiesis; NAS:ComplexPortal. DR CDD; cd05512; Bromo_brd1_like; 1. DR CDD; cd15701; ePHD_BRPF1; 1. DR CDD; cd15676; PHD_BRPF1; 1. DR CDD; cd20156; PWWP_BRPF1; 1. DR FunFam; 3.30.40.10:FF:000008; Bromodomain containing 1, isoform CRA_a; 1. DR FunFam; 2.30.30.140:FF:000008; Bromodomain containing 1, isoform CRA_b; 1. DR FunFam; 3.30.40.10:FF:000007; Bromodomain containing 1, isoform CRA_b; 1. DR FunFam; 1.20.920.10:FF:000007; Bromodomain-containing protein 1; 1. DR Gene3D; 2.30.30.140; -; 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; IID00374; -. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR042008; BRPF1_PHD. DR InterPro; IPR049583; BRPF1_PWWP. DR InterPro; IPR019542; Enhancer_polycomb-like_N. DR InterPro; IPR034732; EPHD. DR InterPro; IPR050701; Histone_Mod_Regulator. DR InterPro; IPR042061; Peregrin_ePHD. DR InterPro; IPR000313; PWWP_dom. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. 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; PTHR13793:SF85; PEREGRIN; 1. DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF10513; EPL1; 1. DR Pfam; PF13831; PHD_2; 1. DR Pfam; PF00855; PWWP; 1. DR Pfam; PF13832; zf-HC5HC2H_2; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00293; PWWP; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS51805; EPHD; 1. DR PROSITE; PS50812; PWWP; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. DR PDBsum; 2D9E; -. DR PDBsum; 2RS9; -. DR PDBsum; 2X35; -. DR PDBsum; 2X4W; -. DR PDBsum; 2X4X; -. DR PDBsum; 2X4Y; -. DR PDBsum; 3L42; -. DR PDBsum; 3MO8; -. DR PDBsum; 4LC2; -. DR PDBsum; 4QYD; -. DR PDBsum; 4QYL; -. DR PDBsum; 4UYE; -. DR PDBsum; 5C6S; -. DR PDBsum; 5C7N; -. DR PDBsum; 5C85; -. DR PDBsum; 5C87; -. DR PDBsum; 5C89; -. DR PDBsum; 5D7X; -. DR PDBsum; 5DY7; -. DR PDBsum; 5DYA; -. DR PDBsum; 5DYC; -. DR PDBsum; 5E3D; -. DR PDBsum; 5E3G; -. DR PDBsum; 5EM3; -. DR PDBsum; 5EPR; -. DR PDBsum; 5EPS; -. DR PDBsum; 5EQ1; -. DR PDBsum; 5ERC; -. DR PDBsum; 5ETB; -. DR PDBsum; 5ETD; -. DR PDBsum; 5EV9; -. DR PDBsum; 5EVA; -. DR PDBsum; 5EWC; -. DR PDBsum; 5EWD; -. DR PDBsum; 5EWH; -. DR PDBsum; 5EWV; -. DR PDBsum; 5EWW; -. DR PDBsum; 5FFV; -. DR PDBsum; 5FFW; -. DR PDBsum; 5FFY; -. DR PDBsum; 5FG4; -. DR PDBsum; 5FG5; -. DR PDBsum; 5G4R; -. DR PDBsum; 5G4S; -. DR PDBsum; 5MWG; -. DR PDBsum; 5MWH; -. DR PDBsum; 5MWZ; -. DR PDBsum; 5MYG; -. DR PDBsum; 5O4S; -. DR PDBsum; 5O4T; -. DR PDBsum; 5O55; -. DR PDBsum; 5O5A; -. DR PDBsum; 5O5F; -. DR PDBsum; 5O5H; -. DR PDBsum; 5OV8; -. DR PDBsum; 5OWA; -. DR PDBsum; 5OWB; -. DR PDBsum; 5OWE; -. DR PDBsum; 5T4U; -. DR PDBsum; 5T4V; -. DR PDBsum; 6EKQ; -. DR PDBsum; 6U04; -. DR PDBsum; 7C4I; -. DR PDBsum; 8QAZ; -. DR PDBsum; 8QB0; -. DR PDBsum; 8QB2; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Bromodomain; KW Chromatin regulator; Chromosome; Cytoplasm; Disease variant; DNA-binding; KW Intellectual disability; Metal-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..1214 FT /note="Peregrin" FT /id="PRO_0000211187" FT DOMAIN 628..732 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1085..1168 FT /note="PWWP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162" FT ZN_FING 21..47 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 273..323 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 327..360 FT /note="C2HC pre-PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT ZN_FING 384..448 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT REGION 43..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 59..222 FT /note="Interaction with KAT6A and KAT6B" FT /evidence="ECO:0000269|PubMed:18794358" FT REGION 118..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 448..489 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..821 FT /note="Interaction with MEAF6 and ING5" FT /evidence="ECO:0000269|PubMed:18794358" FT REGION 543..1079 FT /note="Required for RUNX1 and RUNX2 transcriptional FT activation" FT REGION 819..1062 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 58..67 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 74..85 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 119..130 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 148..167 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 464..474 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 825..838 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 858..871 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 993..1021 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 147 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:B2RRD7" FT MOD_RES 238 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 460 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 462 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 580 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:B2RRD7" FT MOD_RES 858 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:B2RRD7" FT MOD_RES 860 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 917 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:B2RRD7" FT MOD_RES 922 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:B2RRD7" FT MOD_RES 926 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:B2RRD7" FT MOD_RES 1076 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 1187 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 660 FT /note="S -> SEVTELD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_037955" FT VAR_SEQ 765 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_037956" FT VAR_SEQ 873..967 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037957" FT VARIANT 35..1214 FT /note="Missing (in IDDDFP)" FT /evidence="ECO:0000269|PubMed:27939639" FT /id="VAR_078076" FT VARIANT 370 FT /note="P -> S (in IDDDFP; decreased histone H3-K23 FT acetylation; changed cytoplasmic localization; no effect on FT expression and assembly of the MOZ/MORF complex; FT dbSNP:rs1057519509)" FT /evidence="ECO:0000269|PubMed:27939640" FT /id="VAR_078077" FT VARIANT 389 FT /note="C -> R (in IDDDFP; dbSNP:rs1057519515)" FT /evidence="ECO:0000269|PubMed:27939639" FT /id="VAR_078078" FT VARIANT 455..1214 FT /note="Missing (in IDDDFP; decreased histone H3-K23 FT acetylation; increased localization to the nucleus; FT decreased expression and assembly of the MOZ/MORF complex)" FT /evidence="ECO:0000269|PubMed:27939640" FT /id="VAR_078079" FT VARIANT 833..1214 FT /note="Missing (in IDDDFP; no effect on histone H3-K23 FT acetylation; increased aggregation in the cytoplasm; no FT effect on expression and assembly of the MOZ/MORF complex)" FT /evidence="ECO:0000269|PubMed:27939640" FT /id="VAR_078080" FT VARIANT 988..1214 FT /note="Missing (in IDDDFP)" FT /evidence="ECO:0000269|PubMed:27939639" FT /id="VAR_078081" FT VARIANT 1100..1214 FT /note="Missing (in IDDDFP; no effect on histone H3-K23 FT acetylation; no effect on expression and assembly of the FT MOZ/MORF complex)" FT /evidence="ECO:0000269|PubMed:27939640" FT /id="VAR_078082" FT VARIANT 1117 FT /note="G -> E (in dbSNP:rs1042294)" FT /id="VAR_028232" FT VARIANT 1193 FT /note="H -> Q (in dbSNP:rs36081837)" FT /id="VAR_048430" FT CONFLICT 5 FT /note="F -> L (in Ref. 3; BAG57257)" FT /evidence="ECO:0000305" FT CONFLICT 299 FT /note="A -> E (in Ref. 1; AAB02119)" FT /evidence="ECO:0000305" FT CONFLICT 306 FT /note="G -> D (in Ref. 3; BAG57257)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="K -> R (in Ref. 3; BAG57257)" FT /evidence="ECO:0000305" FT CONFLICT 729 FT /note="L -> V (in Ref. 1; AAB02119)" FT /evidence="ECO:0000305" FT CONFLICT 1035 FT /note="F -> S (in Ref. 3; BAG57257)" FT /evidence="ECO:0000305" FT TURN 277..279 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:5ERC" FT TURN 294..296 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:5ERC" FT HELIX 302..305 FT /evidence="ECO:0007829|PDB:5ERC" FT HELIX 318..321 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:5ERC" FT HELIX 351..356 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:5ERC" FT TURN 365..368 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 369..372 FT /evidence="ECO:0007829|PDB:5ERC" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:5ERC" FT HELIX 380..383 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:6U04" FT TURN 387..389 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 392..395 FT /evidence="ECO:0007829|PDB:5ERC" FT HELIX 411..416 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 420..424 FT /evidence="ECO:0007829|PDB:5ERC" FT STRAND 439..443 FT /evidence="ECO:0007829|PDB:5ERC" FT HELIX 625..627 FT /evidence="ECO:0007829|PDB:5G4S" FT HELIX 630..647 FT /evidence="ECO:0007829|PDB:5MWZ" FT STRAND 653..655 FT /evidence="ECO:0007829|PDB:5FFV" FT HELIX 656..658 FT /evidence="ECO:0007829|PDB:5FFV" FT HELIX 659..661 FT /evidence="ECO:0007829|PDB:5MWZ" FT HELIX 665..668 FT /evidence="ECO:0007829|PDB:5MWZ" FT HELIX 675..683 FT /evidence="ECO:0007829|PDB:5MWZ" FT HELIX 690..707 FT /evidence="ECO:0007829|PDB:5MWZ" FT STRAND 710..712 FT /evidence="ECO:0007829|PDB:5FFW" FT HELIX 713..737 FT /evidence="ECO:0007829|PDB:5MWZ" FT STRAND 1081..1083 FT /evidence="ECO:0007829|PDB:3L42" FT STRAND 1088..1091 FT /evidence="ECO:0007829|PDB:3L42" FT STRAND 1099..1104 FT /evidence="ECO:0007829|PDB:3L42" FT STRAND 1113..1115 FT /evidence="ECO:0007829|PDB:3L42" FT STRAND 1118..1120 FT /evidence="ECO:0007829|PDB:3L42" FT HELIX 1121..1124 FT /evidence="ECO:0007829|PDB:3L42" FT HELIX 1125..1137 FT /evidence="ECO:0007829|PDB:3L42" FT STRAND 1138..1140 FT /evidence="ECO:0007829|PDB:3MO8" FT STRAND 1142..1149 FT /evidence="ECO:0007829|PDB:3L42" FT STRAND 1154..1158 FT /evidence="ECO:0007829|PDB:3L42" FT HELIX 1159..1161 FT /evidence="ECO:0007829|PDB:3L42" FT STRAND 1162..1167 FT /evidence="ECO:0007829|PDB:3L42" FT HELIX 1169..1176 FT /evidence="ECO:0007829|PDB:3L42" FT HELIX 1182..1202 FT /evidence="ECO:0007829|PDB:3L42" SQ SEQUENCE 1214 AA; 137499 MW; 618F359F21F4CBF7 CRC64; MGVDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDNP PPPQQTPLRK HKKKGRQSRP ANKQSPSPSE VSQSPGREVM SYAQAQRMVE VDLHGRVHRI SIFDNLDVVS EDEEAPEEAP ENGSNKENTE TPAATPKSGK HKNKEKRKDS NHHHHHNVSA STTPKLPEVV YRELEQDTPD APPRPTSYYR YIEKSAEELD EEVEYDMDEE DYIWLDIMNE RRKTEGVSPI PQEIFEYLMD RLEKESYFES HNKGDPNALV DEDAVCCICN DGECQNSNVI LFCDMCNLAV HQECYGVPYI PEGQWLCRRC LQSPSRAVDC ALCPNKGGAF KQTDDGRWAH VVCALWIPEV CFANTVFLEP IDSIEHIPPA RWKLTCYICK QRGSGACIQC HKANCYTAFH VTCAQQAGLY MKMEPVRETG ANGTSFSVRK TAYCDIHTPP GSARRLPALS HSEGEEDEDE EEDEGKGWSS EKVKKAKAKS RIKMKKARKI LAEKRAAAPV VSVPCIPPHR LSKITNRLTI QRKSQFMQRL HSYWTLKRQS RNGVPLLRRL QTHLQSQRNC DQVGRDSEDK NWALKEQLKS WQRLRHDLER ARLLVELIRK REKLKRETIK VQQIAMEMQL TPFLILLRKT LEQLQEKDTG NIFSEPVPLS EVPDYLDHIK KPMDFFTMKQ NLEAYRYLNF DDFEEDFNLI VSNCLKYNAK DTIFYRAAVR LREQGGAVLR QARRQAEKMG IDFETGMHIP HSLAGDEATH HTEDAAEEER LVLLENQKHL PVEEQLKLLL ERLDEVNASK QSVGRSRRAK MIKKEMTALR RKLAHQRETG RDGPERHGPS SRGSLTPHPA ACDKDGQTDS AAEESSSQET SKGLGPNMSS TPAHEVGRRT SVLFSKKNPK TAGPPKRPGR PPKNRESQMT PSHGGSPVGP PQLPIMSSLR QRKRGRSPRP SSSSDSDSDK STEDPPMDLP ANGFSGGNQP VKKSFLVYRN DCSLPRSSSD SESSSSSSSS AASDRTSTTP SKQGRGKPSF SRGTFPEDSS EDTSGTENEA YSVGTGRGVG HSMVRKSLGR GAGWLSEDED SPLDALDLVW AKCRGYPSYP ALIIDPKMPR EGMFHHGVPI PVPPLEVLKL GEQMTQEARE HLYLVLFFDN KRTWQWLPRT KLVPLGVNQD LDKEKMLEGR KSNIRKSVQI AYHRALQHRS KVQGEQSSET SDSD //