ZZEF1_HUMAN
ID ZZEF1_HUMAN Reviewed; 2961 AA.
AC O43149; A7MBM5; Q6NXG0; Q6ZRA1; Q6ZSF4; Q9NVB9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 6.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger ZZ-type and EF-hand domain-containing protein 1 {ECO:0000305};
GN Name=ZZEF1 {ECO:0000312|HGNC:HGNC:29027}; Synonyms=KIAA0399;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-1972;
RP VAL-2014 AND GLN-2369.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1614-2961 (ISOFORM 2), AND VARIANT ALA-30.
RC TISSUE=Teratocarcinoma, and Thalamus;
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-1972;
RP VAL-2014 AND GLN-2369.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15519529; DOI=10.1016/j.ejca.2004.08.005;
RA Cvekl A. Jr., Zavadil J., Birshtein B.K., Grotzer M.A., Cvekl A.;
RT "Analysis of transcripts from 17p13.3 in medulloblastoma suggests ROX/MNT
RT as a potential tumour suppressor gene.";
RL Eur. J. Cancer 40:2525-2532(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1518, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1475, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2667, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [13]
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-1537; SER-1540 AND
RP SER-2444, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=24223779; DOI=10.1371/journal.pone.0078235;
RA Moriya K., Nagatoshi K., Noriyasu Y., Okamura T., Takamitsu E., Suzuki T.,
RA Utsumi T.;
RT "Protein N-myristoylation plays a critical role in the endoplasmic
RT reticulum morphological change induced by overexpression of protein
RT Lunapark, an integral membrane protein of the endoplasmic reticulum.";
RL PLoS ONE 8:E78235-E78235(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1512 AND THR-1523, AND
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 [18]
RP FUNCTION, INTERACTION WITH KLF6; KLF9 AND HISTONES H3K4ME3 AND H3K4AC, AND
RP MUTAGENESIS OF ASP-1833 AND ASP-1853.
RX PubMed=33227311; DOI=10.1016/j.jmb.2020.11.021;
RA Yu Y., Tencer A., Xuan H., Kutateladze T.G., Shi X.;
RT "ZZEF1 is a Histone Reader and Transcriptional Coregulator of Krueppel-Like
RT Factors.";
RL J. Mol. Biol. 433:166722-166722(2021).
CC -!- FUNCTION: Histone H3 reader which may act as a transcriptional
CC coactivator for KLF6 and KLF9 transcription factors.
CC {ECO:0000269|PubMed:33227311}.
CC -!- SUBUNIT: Interacts with KLF6 and KLF9 (PubMed:33227311). Interacts via
CC (ZZ-type 2 zinc finger) with histone H3 trimethylated at 'Lys-4'
CC (H3K4me3) and histone H3 acetylated at 'Lys-4' (H3K4ac)
CC (PubMed:33227311). {ECO:0000269|PubMed:33227311}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43149-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43149-2; Sequence=VSP_042268, VSP_042269, VSP_042270;
CC Name=3;
CC IsoId=O43149-3; Sequence=VSP_036989, VSP_025870, VSP_025871;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in cerebellum.
CC {ECO:0000269|PubMed:15519529}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23695.4; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91834.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB007859; BAA23695.4; ALT_INIT; mRNA.
DR EMBL; AK001683; BAA91834.1; ALT_INIT; mRNA.
DR EMBL; AK127482; BAC86999.1; -; mRNA.
DR EMBL; AC067815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067099; AAH67099.1; -; mRNA.
DR EMBL; BC151836; AAI51837.1; -; mRNA.
DR CCDS; CCDS11043.1; -. [O43149-1]
DR PIR; T00048; T00048.
DR RefSeq; NP_055928.3; NM_015113.3. [O43149-1]
DR SMR; O43149; -.
DR BioGRID; 116757; 138.
DR ELM; O43149; -.
DR IntAct; O43149; 57.
DR MINT; O43149; -.
DR STRING; 9606.ENSP00000371051; -.
DR GlyGen; O43149; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O43149; -.
DR MetOSite; O43149; -.
DR PhosphoSitePlus; O43149; -.
DR BioMuta; ZZEF1; -.
DR EPD; O43149; -.
DR jPOST; O43149; -.
DR MassIVE; O43149; -.
DR MaxQB; O43149; -.
DR PaxDb; O43149; -.
DR PeptideAtlas; O43149; -.
DR PRIDE; O43149; -.
DR ProteomicsDB; 48767; -. [O43149-1]
DR ProteomicsDB; 48768; -. [O43149-2]
DR ProteomicsDB; 48769; -. [O43149-3]
DR Antibodypedia; 23205; 33 antibodies from 9 providers.
DR DNASU; 23140; -.
DR Ensembl; ENST00000381638.7; ENSP00000371051.2; ENSG00000074755.15. [O43149-1]
DR GeneID; 23140; -.
DR KEGG; hsa:23140; -.
DR MANE-Select; ENST00000381638.7; ENSP00000371051.2; NM_015113.4; NP_055928.3.
DR UCSC; uc002fxe.4; human. [O43149-1]
DR CTD; 23140; -.
DR DisGeNET; 23140; -.
DR GeneCards; ZZEF1; -.
DR HGNC; HGNC:29027; ZZEF1.
DR HPA; ENSG00000074755; Low tissue specificity.
DR MIM; 619459; gene.
DR neXtProt; NX_O43149; -.
DR OpenTargets; ENSG00000074755; -.
DR PharmGKB; PA134938508; -.
DR VEuPathDB; HostDB:ENSG00000074755; -.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000155045; -.
DR HOGENOM; CLU_000703_0_0_1; -.
DR InParanoid; O43149; -.
DR OMA; MMNVTEQ; -.
DR OrthoDB; 6958at2759; -.
DR PhylomeDB; O43149; -.
DR TreeFam; TF331572; -.
DR PathwayCommons; O43149; -.
DR SignaLink; O43149; -.
DR BioGRID-ORCS; 23140; 5 hits in 1080 CRISPR screens.
DR ChiTaRS; ZZEF1; human.
DR GenomeRNAi; 23140; -.
DR Pharos; O43149; Tdark.
DR PRO; PR:O43149; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43149; protein.
DR Bgee; ENSG00000074755; Expressed in jejunal mucosa and 201 other tissues.
DR ExpressionAtlas; O43149; baseline and differential.
DR Genevisible; O43149; HS.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0140566; F:histone reader activity; IMP:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR CDD; cd02343; ZZ_EF; 1.
DR Gene3D; 3.30.60.90; -; 2.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR InterPro; IPR040099; ZZEF1.
DR InterPro; IPR041986; ZZEF1_ZZ.
DR PANTHER; PTHR22772:SF4; PTHR22772:SF4; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF00569; ZZ; 2.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Lipoprotein; Metal-binding;
KW Myristate; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..2961
FT /note="Zinc finger ZZ-type and EF-hand domain-containing
FT protein 1"
FT /id="PRO_0000289000"
FT DOMAIN 111..146
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 226..405
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT ZN_FING 1778..1833
FT /note="ZZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1827..1882
FT /note="ZZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2426..2455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2005..2029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1783
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1786
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1797
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1800
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1806
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1809
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1832
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1835
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1846
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1849
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1855
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1858
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1872
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSH7"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1512
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSH7"
FT MOD_RES 1523
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2667
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681,
FT ECO:0000269|PubMed:24223779"
FT VAR_SEQ 1..1686
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042268"
FT VAR_SEQ 882
FT /note="M -> MK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036989"
FT VAR_SEQ 1079..1084
FT /note="LDVETW -> VTRVST (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025870"
FT VAR_SEQ 1085..2961
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025871"
FT VAR_SEQ 2405..2424
FT /note="ILSIMLYSSKKEINALAEHG -> VRDERDSCSSFLVQMCWPRS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042269"
FT VAR_SEQ 2425..2961
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042270"
FT VARIANT 30
FT /note="V -> A (in dbSNP:rs1454121)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_032551"
FT VARIANT 1021
FT /note="I -> V (in dbSNP:rs16953687)"
FT /id="VAR_032552"
FT VARIANT 1437
FT /note="S -> A (in dbSNP:rs4790555)"
FT /id="VAR_032553"
FT VARIANT 1972
FT /note="L -> P (in dbSNP:rs781852)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9455477"
FT /id="VAR_032554"
FT VARIANT 2014
FT /note="I -> V (in dbSNP:rs781831)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9455477"
FT /id="VAR_032555"
FT VARIANT 2051
FT /note="P -> S (in dbSNP:rs1006954)"
FT /id="VAR_032556"
FT VARIANT 2301
FT /note="Y -> H (in dbSNP:rs34357158)"
FT /id="VAR_032557"
FT VARIANT 2303
FT /note="L -> P (in dbSNP:rs35638819)"
FT /id="VAR_032558"
FT VARIANT 2369
FT /note="E -> Q (in dbSNP:rs711177)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9455477"
FT /id="VAR_032559"
FT VARIANT 2421
FT /note="A -> T (in dbSNP:rs781861)"
FT /id="VAR_032560"
FT MUTAGEN 1833
FT /note="D->A: Loss of histone H3 binding."
FT /evidence="ECO:0000269|PubMed:33227311"
FT MUTAGEN 1853
FT /note="D->A: Loss of histone H3 binding."
FT /evidence="ECO:0000269|PubMed:33227311"
FT CONFLICT 959
FT /note="V -> A (in Ref. 1; BAA23695 and 5; AAI51837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1929
FT /note="R -> H (in Ref. 3; BAA91834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2961 AA; 331075 MW; 0DB2EB72C16BC168 CRC64;
MGNAPSHSSE DEAAAAGGEG WGPHQDWAAV SGTTPGPGVA APALPPAAAL LEPARLREAA
AALLPTPPCE SLVSRHRGAL FRWLEERLGR GEESVTLEQF RELLEARGAG CSSEQFEEAF
AQFDAEGDGT VDAENMLEAL KNSSGANLQG ELSHIIRQLQ ACSLVPGFTD IFSESKEGLD
IHSSMILRFL HRNRLSSAVM PYPMLEHCNN MCTMRSSVLK ESLDQLVQKE KESPGDLTRS
PEMDKLKSVA KCYAYIETSS NSADIDKMTN GETSSYWQSD GSACSHWIRL KMKPDVVLRH
LSIAVAATDQ SYMPQQVTVA VGRNASDLQE VRDVHIPSNV TGYVTLLENA NVSQLYVQIN
IKRCLSDGCD TRIHGLRAVG FQRVKKSGVS VSDASAIWYW SLLTSLVTAS METNPAFVQT
VLHNTQKALR HMPPLSLSPG STDFSTFLSP NVLEEVDSFL IRITSCCSTP EVELTLLAFA
LARGSVAKVM SSLCTITDHL DTQYDASSLI LSMASVRQNL LLKYGKPLQL TLQACDVKGK
EDKSGPENLL VEPWTRDGFL TETGKTRAST IFSTGTESAF QVTQIRIMVR RGGIGAQCGL
VFAYNSSSDK FCAEEHFKRF EKYDKWKLQE LRQFVKSRIG CSSDDLGEDD PIGWFELEEE
WDEADVKLQQ CRVAKYLMVK FLCTRQESAE RLGVQGLTIS GYLRPARAEA EQSVTCAHCR
KDTEESVCGA TLLLRTLQFI QQLAHDLVQQ KESGLKYKSF LDFAGLDLQI FWNFYSKLKQ
NPREECVSAQ TLLLQLLQSC FSVLQGDVLA ASEEEKAPIQ SPKGVEAAKE LYTHLCDVVD
KVDGDSVPME ILKQEVRNTL LNGAAIFFPN RQTRRNHLFT MMNVTEQEHK QSLQLTFRSL
CTYFSDKDPG GLLLLPEKND LAKMNISEVL AVMDTLVSVA ARECELLMLS GAPGEVGSVL
FSLFWSVQGS LLSWCYLQLK STDSGAKDLA VDLIEKYVGQ FLASMRAILE SLFSQYSGKT
IVERLCNSVF SMAARQLVIF LLDFCTLDIP HCVLLREFSV LTELLKKLCS GPEGGLRKLD
VETWQQEQPV VLHTWTKESA HNYENNCHEV SVFVSPGATY FEVEFDDRCE TEKRYDYLEF
TDARGRKTRY DTKVGTDKWP KKVTFKAGPR LQFLFHSDSS HNEWGYKFTV TACGLPDVAV
SWGLDLQLLV SRLMGRLASQ CMALKSVRQL GSNMVVPQAK MALVLSSPLW KPVFRHQVCP
ELELEASWPT HPHRNSKEVK NIPDDPCRHF LLDFAQSEPA QNFCGPYSEL FKGFIQACRK
QAPKTDIVAG STIDQAVNAT FAALVYRTPD LYEKLQKYVN SGGKIALSEE FAQVYSLADG
IRIWMLEMKQ KSLMSLGNEA EEKHSSEATE VNPESLAKEC IEKSLLLLKF LPTGISSKES
CEKLETADET SHLQPLNKRQ RTSSVVEEHF QASVSPTEAA PPATGDQSPG LGTQPKLPSS
SGLPAADVSP ATAEEPLSPS TPTRRPPFTR GRLRLLSFRS MEEARLVPTV KEKYPVLKDV
MDFIKDQSLS HRSVVKVLSL RKAQAQSILE VLKITQHCAE SLGQPHCFHP PFILFLLELL
TCQKDFTNYF GHLEGCGADL HKEIRDTYYQ LVLFLVKAVK GFSSLNDRSL LPALSCVQTA
LLHLLDMGWE PNDLAFFVDI QLPDLLMKMS QENISVHDSV ISQWSEEDEL ADAKQNSEWM
DECQDGMFEA WYEKIAQEDP EKQRKMHMFI ARYCDLLNVD ISCDGCDEIA PWHRYRCLQC
SDMDLCKTCF LGGVKPEGHG DDHEMVNMEF TCDHCQGLII GRRMNCNVCD DFDLCYGCYA
AKKYSYGHLP THSITAHPMV TIRISDRQRL IQPYIHNYSW LLFAALALYS AHLASAEDVD
GEKLDPQTRS SATTLRSQCM QLVGDCLMKA HQGKGLKALA LLGVLPDGDS SLEDQALPVT
VPTGASEEQL EKKAVQGAEL SEAGNGKRAV HEEIRPVDFK QRNKADKGVS LSKDPSCQTQ
ISDSPADASP PTGLPDAEDS EVSSQKPIEE KAVTPSPEQV FAECSQKRIL GLLAAMLPPL
KSGPTVPLID LEHVLPLMFQ VVISNAGHLN ETYHLTLGLL GQLIIRLLPA EVDAAVIKVL
SAKHNLFAAG DSSIVPDGWK TTHLLFSLGA VCLDSRVGLD WACSMAEILR SLNSAPLWRD
VIATFTDHCI KQLPFQLKHT NIFTLLVLVG FPQVLCVGTR CVYMDNANEP HNVIILKHFT
EKNRAVIVDV KTRKRKTVKD YQLVQKGGGQ ECGDSRAQLS QYSQHFAFIA SHLLQSSMDS
HCPEAVEATW VLSLALKGLY KTLKAHGFEE IRATFLQTDL LKLLVKKCSK GTGFSKTWLL
RDLEILSIML YSSKKEINAL AEHGDLELDE RGDREEEVER PVSSPGDPEQ KKLDPLEGLD
EPTRICFLMA HDALNAPLHI LRAIYELQMK KTDYFFLEVQ KRFDGDELTT DERIRSLAQR
WQPSKSLRLE EQSAKAVDTD MIILPCLSRP ARCDQATAES NPVTQKLISS TESELQQSYA
KQRRSKSAAL LHKELNCKSK RAVRDYLFRV NEATAVLYAR HVLASLLAEW PSHVPVSEDI
LELSGPAHMT YILDMFMQLE EKHEWEKILQ KVLQGCREDM LGTMALAACQ FMEEPGMEVQ
VRESKHPYNN NTNFEDKVHI PGAIYLSIKF DSQCNTEEGC DELAMSSSSD FQQDRHSFSG
SQQKWKDFEL PGDTLYYRFT SDMSNTEWGY RFTVTAGHLG RFQTGFEILK QMLSEERVVP
HLPLAKIWEW LVGVACRQTG HQRLKAIHLL LRIVRCCGHS DLCDLALLKP LWQLFTHMEY
GLFEDVTQPG ILLPLHRALT ELFFVTENRA QELGVLQDYL LALTTDDHLL RCAAQALQNI
AAISLAINYP NKATRLWNVE C
