AN32E_HUMAN
ID AN32E_HUMAN Reviewed; 268 AA.
AC Q9BTT0; B4E0I6; E9PEA6; Q5TB18; Q5TB20; Q8N1S4; Q8WWW9;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member E;
DE AltName: Full=LANP-like protein;
DE Short=LANP-L;
GN Name=ANP32E;
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.
RC TISSUE=Fetal brain;
RX PubMed=12438741; DOI=10.1159/000064058;
RA Jiang M., Ma Y., Ni X., Cao G., Ji C., Cheng H., Tang R., Xie Y., Mao Y.;
RT "Molecular cloning and characterization of a novel human gene (ANP32E alias
RT LANPL) from human fetal brain.";
RL Cytogenet. Genome Res. 97:68-71(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pulmonary artery, Thymus, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS
RP 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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 215-240 IN COMPLEX WITH HISTONES
RP H2AZ1 AND H2B, FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX,
RP INTERACTION WITH H2AZ1, AND MUTAGENESIS OF 218-LEU--MET-222 AND
RP 232-ASP--TYR-235.
RX PubMed=24463511; DOI=10.1038/nature12922;
RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M.,
RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C.,
RA Hamiche A.;
RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
RL Nature 505:648-653(2014).
CC -!- FUNCTION: Histone chaperone that specifically mediates the genome-wide
CC removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1
CC from its normal sites of deposition, especially from enhancer and
CC insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the
CC nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus
CC shifting the equilibrium towards dissociation and the off-chromatin
CC state (PubMed:24463511). Inhibits activity of protein phosphatase 2A
CC (PP2A). Does not inhibit protein phosphatase 1. May play a role in
CC cerebellar development and synaptogenesis.
CC {ECO:0000269|PubMed:24463511}.
CC -!- SUBUNIT: Interacts with the importin alpha KPNA1 and KPNA2 (By
CC similarity). Component of a SWR1-like complex, composed of EP400,
CC KAT5/TIP60, TRRAP, BRD8, RUVBL1, RUVBL2, ING3 and ANP32E; the complex
CC does not contain SRCAP. Interacts with H2A.Z/H2AZ1. {ECO:0000250,
CC ECO:0000269|PubMed:24463511}.
CC -!- INTERACTION:
CC Q9BTT0; Q9NV56: MRGBP; NbExp=4; IntAct=EBI-2685059, EBI-399076;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BTT0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTT0-2; Sequence=VSP_045618;
CC Name=3;
CC IsoId=Q9BTT0-3; Sequence=VSP_047262;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes, colon,
CC small intestine, prostate, thymus, spleen, skeletal muscle, liver and
CC kidney. {ECO:0000269|PubMed:12438741}.
CC -!- DOMAIN: The H2A.Z-interacting domain (ZID) mediates a direct
CC interaction with H2A.Z/H2AZ1. {ECO:0000269|PubMed:24463511}.
CC -!- PTM: Phosphorylated. The phosphorylation is nuclear localization signal
CC (NLS)-dependent (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR EMBL; AY057381; AAL25814.1; -; mRNA.
DR EMBL; AK095228; BAC04505.1; -; mRNA.
DR EMBL; AK092672; BAC03942.1; -; mRNA.
DR EMBL; AK303392; BAG64448.1; -; mRNA.
DR EMBL; AL832674; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL138795; CAI22806.1; -; Genomic_DNA.
DR EMBL; AL138795; CAI22808.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53575.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53577.1; -; Genomic_DNA.
DR EMBL; BC003380; AAH03380.1; -; mRNA.
DR CCDS; CCDS44214.1; -. [Q9BTT0-2]
DR CCDS; CCDS44215.1; -. [Q9BTT0-3]
DR CCDS; CCDS946.1; -. [Q9BTT0-1]
DR RefSeq; NP_001129950.1; NM_001136478.3. [Q9BTT0-2]
DR RefSeq; NP_001129951.1; NM_001136479.2. [Q9BTT0-3]
DR RefSeq; NP_001267488.1; NM_001280559.1.
DR RefSeq; NP_001267489.1; NM_001280560.1.
DR RefSeq; NP_112182.1; NM_030920.4. [Q9BTT0-1]
DR PDB; 4CAY; X-ray; 1.48 A; C=215-240.
DR PDB; 4NFT; X-ray; 2.61 A; E/F=185-232.
DR PDBsum; 4CAY; -.
DR PDBsum; 4NFT; -.
DR AlphaFoldDB; Q9BTT0; -.
DR SMR; Q9BTT0; -.
DR BioGRID; 123548; 88.
DR IntAct; Q9BTT0; 54.
DR MINT; Q9BTT0; -.
DR STRING; 9606.ENSP00000463154; -.
DR GlyGen; Q9BTT0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BTT0; -.
DR PhosphoSitePlus; Q9BTT0; -.
DR BioMuta; ANP32E; -.
DR DMDM; 30580363; -.
DR EPD; Q9BTT0; -.
DR jPOST; Q9BTT0; -.
DR MassIVE; Q9BTT0; -.
DR MaxQB; Q9BTT0; -.
DR PaxDb; Q9BTT0; -.
DR PeptideAtlas; Q9BTT0; -.
DR PRIDE; Q9BTT0; -.
DR ProteomicsDB; 19845; -.
DR ProteomicsDB; 64883; -.
DR ProteomicsDB; 79007; -. [Q9BTT0-1]
DR TopDownProteomics; Q9BTT0-1; -. [Q9BTT0-1]
DR Antibodypedia; 20276; 139 antibodies from 29 providers.
DR DNASU; 81611; -.
DR Ensembl; ENST00000436748.6; ENSP00000393718.2; ENSG00000143401.15. [Q9BTT0-2]
DR Ensembl; ENST00000583931.6; ENSP00000463154.1; ENSG00000143401.15. [Q9BTT0-1]
DR Ensembl; ENST00000616917.4; ENSP00000481415.1; ENSG00000143401.15. [Q9BTT0-3]
DR GeneID; 81611; -.
DR KEGG; hsa:81611; -.
DR MANE-Select; ENST00000583931.6; ENSP00000463154.1; NM_030920.5; NP_112182.1.
DR UCSC; uc031uxy.2; human. [Q9BTT0-1]
DR CTD; 81611; -.
DR DisGeNET; 81611; -.
DR GeneCards; ANP32E; -.
DR HGNC; HGNC:16673; ANP32E.
DR HPA; ENSG00000143401; Low tissue specificity.
DR MIM; 609611; gene.
DR neXtProt; NX_Q9BTT0; -.
DR OpenTargets; ENSG00000143401; -.
DR PharmGKB; PA134880751; -.
DR VEuPathDB; HostDB:ENSG00000143401; -.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR HOGENOM; CLU_063314_1_1_1; -.
DR InParanoid; Q9BTT0; -.
DR OMA; MPNNQVS; -.
DR OrthoDB; 1622194at2759; -.
DR PhylomeDB; Q9BTT0; -.
DR TreeFam; TF317206; -.
DR PathwayCommons; Q9BTT0; -.
DR SignaLink; Q9BTT0; -.
DR BioGRID-ORCS; 81611; 35 hits in 1085 CRISPR screens.
DR ChiTaRS; ANP32E; human.
DR GeneWiki; ANP32E; -.
DR GenomeRNAi; 81611; -.
DR Pharos; Q9BTT0; Tbio.
DR PRO; PR:Q9BTT0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BTT0; protein.
DR Bgee; ENSG00000143401; Expressed in trabecular bone tissue and 210 other tissues.
DR ExpressionAtlas; Q9BTT0; baseline and differential.
DR Genevisible; Q9BTT0; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; IDA:UniProtKB.
DR GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR DisProt; DP02409; -.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR045081; AN32.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR11375; PTHR11375; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Chromatin regulator; Cytoplasm; Isopeptide bond; Leucine-rich repeat;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..268
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member E"
FT /id="PRO_0000137599"
FT REPEAT 18..38
FT /note="LRR 1"
FT REPEAT 43..64
FT /note="LRR 2"
FT REPEAT 65..87
FT /note="LRR 3"
FT REPEAT 89..110
FT /note="LRR 4"
FT DOMAIN 123..161
FT /note="LRRCT"
FT REGION 149..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..268
FT /note="ZID domain"
FT COMPBIAS 150..211
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047262"
FT VAR_SEQ 69..109
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045618"
FT MUTAGEN 218..222
FT /note="LSYLM->ASYAA: In ANP32E-m1; abolished ability to
FT interact with the H2A.Z/H2AZ1-H2B dimer."
FT /evidence="ECO:0000269|PubMed:24463511"
FT MUTAGEN 232..235
FT /note="DDDY->ADAA: In ANP32E-m2; abolished ability to
FT interact with the H2A.Z/H2AZ1-H2B dimer."
FT /evidence="ECO:0000269|PubMed:24463511"
FT CONFLICT 185..186
FT /note="Missing (in Ref. 1; AAL25814 and 2; BAC04505/
FT BAG64448)"
FT /evidence="ECO:0000305"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:4CAY"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4CAY"
SQ SEQUENCE 268 AA; 30692 MW; 99D74AF4B59BF971 CRC64;
MEMKKKINLE LRNRSPEEVT ELVLDNCLCV NGEIEGLNDT FKELEFLSMA NVELSSLARL
PSLNKLRKLE LSDNIISGGL EVLAEKCPNL TYLNLSGNKI KDLSTVEALQ NLKNLKSLDL
FNCEITNLED YRESIFELLQ QITYLDGFDQ EDNEAPDSEE EDDEDGDEDD EEEEENEAGP
PEGYEEEEEE EEEEDEDEDE DEDEAGSELG EGEEEVGLSY LMKEEIQDEE DDDDYVEEGE
EEEEEEEGGL RGEKRKRDAE DDGEEEDD
