BRPF1_HUMAN
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 03-AUG-2022, entry version 196.
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 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 [20]
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 [21]
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 [22]
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 [23]
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; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-12065306, EBI-14096082;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18794358,
CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:27939640}. Chromosome
CC {ECO:0000269|PubMed:24065767}. Cytoplasm {ECO:0000269|PubMed:18794358,
CC ECO:0000269|PubMed:27939640}. Note=Localization to the nucleus depends
CC on KAT6A, ING5 and MEAF6 (PubMed:18794358, PubMed:27939640). Localizes
CC to transcription start sites (PubMed:24065767).
CC {ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:24065767,
CC 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.
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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_001003694.1. [P55201-2]
DR RefSeq; NP_001305978.1; NM_001319049.1. [P55201-4]
DR RefSeq; NP_001305979.1; NM_001319050.1. [P55201-3]
DR RefSeq; NP_004625.2; NM_004634.2. [P55201-1]
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=626-740.
DR PDB; 5DYC; X-ray; 1.65 A; A=626-740.
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 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 AlphaFoldDB; P55201; -.
DR BMRB; P55201; -.
DR SMR; P55201; -.
DR BioGRID; 113614; 63.
DR ComplexPortal; CPX-727; MOZ1 histone acetyltransferase complex.
DR ComplexPortal; CPX-738; MORF1 histone acetyltransferase complex.
DR CORUM; P55201; -.
DR DIP; DIP-59001N; -.
DR IntAct; P55201; 34.
DR MINT; P55201; -.
DR STRING; 9606.ENSP00000373340; -.
DR BindingDB; P55201; -.
DR ChEMBL; CHEMBL3132741; -.
DR GuidetoPHARMACOLOGY; 2730; -.
DR iPTMnet; P55201; -.
DR PhosphoSitePlus; P55201; -.
DR BioMuta; BRPF1; -.
DR DMDM; 116241271; -.
DR EPD; P55201; -.
DR jPOST; P55201; -.
DR MassIVE; P55201; -.
DR MaxQB; P55201; -.
DR PaxDb; P55201; -.
DR PeptideAtlas; P55201; -.
DR PRIDE; P55201; -.
DR ProteomicsDB; 56806; -. [P55201-1]
DR ProteomicsDB; 56807; -. [P55201-2]
DR ProteomicsDB; 56808; -. [P55201-3]
DR ProteomicsDB; 56809; -. [P55201-4]
DR TopDownProteomics; P55201-2; -. [P55201-2]
DR Antibodypedia; 933; 54 antibodies from 16 providers.
DR DNASU; 7862; -.
DR Ensembl; ENST00000383829.7; ENSP00000373340.2; ENSG00000156983.17. [P55201-2]
DR Ensembl; ENST00000433861.6; ENSP00000402485.2; ENSG00000156983.17. [P55201-4]
DR Ensembl; ENST00000683743.1; ENSP00000507469.1; ENSG00000156983.17. [P55201-1]
DR Ensembl; ENST00000684199.1; ENSP00000506921.1; ENSG00000156983.17. [P55201-2]
DR Ensembl; ENST00000684333.1; ENSP00000508256.1; ENSG00000156983.17. [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 CTD; 7862; -.
DR DisGeNET; 7862; -.
DR GeneCards; BRPF1; -.
DR HGNC; HGNC:14255; BRPF1.
DR HPA; ENSG00000156983; Low tissue specificity.
DR MalaCards; BRPF1; -.
DR MIM; 602410; gene.
DR MIM; 617333; phenotype.
DR neXtProt; NX_P55201; -.
DR OpenTargets; ENSG00000156983; -.
DR PharmGKB; PA25424; -.
DR VEuPathDB; HostDB:ENSG00000156983; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000157794; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR InParanoid; P55201; -.
DR OMA; RDCDRSY; -.
DR OrthoDB; 566217at2759; -.
DR PhylomeDB; P55201; -.
DR TreeFam; TF316118; -.
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 BioGRID-ORCS; 7862; 166 hits in 1100 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 174 other tissues.
DR ExpressionAtlas; P55201; baseline and differential.
DR Genevisible; P55201; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
DR GO; GO:0043972; P:histone H3-K23 acetylation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR CDD; cd05839; BR140_related; 1.
DR CDD; cd15701; ePHD_BRPF1; 1.
DR CDD; cd15676; PHD_BRPF1; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR IDEAL; IID00374; -.
DR InterPro; IPR035502; BR140-rel_PWWD.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR042008; BRPF1_PHD.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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 Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 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.
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 Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1214
FT /note="Peregrin"
FT /id="PRO_0000211187"
FT DOMAIN 645..715
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 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1051
FT /note="Polar residues"
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 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 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
