COE1_HUMAN
ID COE1_HUMAN Reviewed; 591 AA.
AC Q9UH73; Q8IW11;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Transcription factor COE1;
DE Short=O/E-1;
DE Short=OE-1;
DE AltName: Full=Early B-cell factor;
GN Name=EBF1; Synonyms=COE1, EBF;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-591 (ISOFORM 1).
RX PubMed=10942392;
RA Gisler R., Jacobsen S.E., Sigvardsson M.;
RT "Cloning of human early B-cell factor and identification of target genes
RT suggest a conserved role in B-cell development in man and mouse.";
RL Blood 96:1457-1464(2000).
RN [3]
RP INTERACTION WITH ZNF521.
RX PubMed=14630787; DOI=10.1182/blood-2003-07-2388;
RA Bond H.M., Mesuraca M., Carbone E., Bonelli P., Agosti V., Amodio N.,
RA De Rosa G., Di Nicola M., Gianni A.M., Moore M.A., Hata A., Grieco M.,
RA Morrone G., Venuta S.;
RT "Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse
RT Evi3, is highly expressed in primitive human hematopoietic cells.";
RL Blood 103:2062-2070(2004).
RN [4]
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-16, 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 [7]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=26819314; DOI=10.1128/jvi.03227-15;
RA Murata T., Noda C., Narita Y., Watanabe T., Yoshida M., Ashio K., Sato Y.,
RA Goshima F., Kanda T., Yoshiyama H., Tsurumi T., Kimura H.;
RT "Induction of Epstein-Barr Virus Oncoprotein LMP1 by Transcription Factors
RT AP-2 and Early B Cell Factor.";
RL J. Virol. 90:3873-3889(2016).
RN [8]
RP FUNCTION, INTERACTION WITH CNOT3, AND MUTAGENESIS OF HIS-240.
RX PubMed=27807034; DOI=10.1101/gad.285452.116;
RA Yang C.Y., Ramamoorthy S., Boller S., Rosenbaum M., Rodriguez Gil A.,
RA Mittler G., Imai Y., Kuba K., Grosschedl R.;
RT "Interaction of CCR4-NOT with EBF1 regulates gene-specific transcription
RT and mRNA stability in B lymphopoiesis.";
RL Genes Dev. 30:2310-2324(2016).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR VIRUS
RP PROTEIN EBNA2 (MICROBIAL INFECTION).
RX PubMed=28968461; DOI=10.1371/journal.ppat.1006664;
RA Glaser L.V., Rieger S., Thumann S., Beer S., Kuklik-Roos C., Martin D.E.,
RA Maier K.C., Harth-Hertle M.L., Gruening B., Backofen R., Krebs S., Blum H.,
RA Zimmer R., Erhard F., Kempkes B.;
RT "EBF1 binds to EBNA2 and promotes the assembly of EBNA2 chromatin complexes
RT in B cells.";
RL PLoS Pathog. 13:e1006664-e1006664(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 10-351 IN COMPLEX WITH ZINC IONS,
RP AND SUBUNIT.
RX PubMed=20592035; DOI=10.1074/jbc.c110.150482;
RA Siponen M.I., Wisniewska M., Lehtio L., Johansson I., Svensson L.,
RA Raszewski G., Nilsson L., Sigvardsson M., Berglund H.;
RT "Structural determination of functional domains in early B-cell factor
RT (EBF) family of transcription factors reveals similarities to Rel DNA-
RT binding proteins and a novel dimerization motif.";
RL J. Biol. Chem. 285:25875-25879(2010).
CC -!- FUNCTION: Key pioneer transcription factor of B-cell specification and
CC commitment (PubMed:27807034). Recognizes variations of the palindromic
CC sequence 5'-ATTCCCNNGGGAATT-3'. Operates in a transcription factor
CC network to activate B-cell-specific genes and repress genes associated
CC with alternative cell fates. For instance, positively regulates many B-
CC cell specific genes including BCR or CD40 while repressing genes that
CC direct cells into alternative lineages, including GATA3 and TCF7 for
CC the T-cell lineage. In addition to its role during lymphopoiesis,
CC controls the thermogenic gene program in adipocytes during development
CC and in response to environmental cold (By similarity).
CC {ECO:0000250|UniProtKB:Q07802, ECO:0000269|PubMed:27807034}.
CC -!- FUNCTION: (Microbial infection) Acts as a chromatin anchor for Epstein-
CC Barr virus EBNA2 to mediate the assembly of EBNA2 chromatin complexes
CC in B-cells (PubMed:28968461). In addition, binds to the viral LMP1
CC proximal promoter and promotes its expression during latency
CC (PubMed:26819314). {ECO:0000269|PubMed:26819314,
CC ECO:0000269|PubMed:28968461}.
CC -!- SUBUNIT: Homodimer (PubMed:20592035). Interacts with ZNF423 and ZNF521,
CC leading to prevent EBF1 to bind DNA and activate target genes
CC (PubMed:14630787). Interacts with CCR4-NOT component CNOT3
CC (PubMed:14630787). {ECO:0000269|PubMed:14630787,
CC ECO:0000269|PubMed:20592035}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-barr virus
CC protein EBNA2. {ECO:0000269|PubMed:28968461}.
CC -!- INTERACTION:
CC Q9UH73; Q8N5M1: ATPAF2; NbExp=10; IntAct=EBI-765426, EBI-1166928;
CC Q9UH73; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-765426, EBI-10172004;
CC Q9UH73; P78424: POU6F2; NbExp=3; IntAct=EBI-765426, EBI-12029004;
CC Q9UH73; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-765426, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UH73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UH73-2; Sequence=VSP_012304, VSP_012305;
CC -!- SIMILARITY: Belongs to the COE family. {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; BC038805; AAH38805.1; -; mRNA.
DR EMBL; BC041178; AAH41178.1; -; mRNA.
DR EMBL; AF208502; AAF19643.1; -; mRNA.
DR CCDS; CCDS4343.1; -. [Q9UH73-1]
DR CCDS; CCDS78081.1; -. [Q9UH73-2]
DR RefSeq; NP_076870.1; NM_024007.4. [Q9UH73-1]
DR RefSeq; NP_874367.1; NM_182708.2. [Q9UH73-2]
DR PDB; 3LYR; X-ray; 2.51 A; A=10-250.
DR PDB; 3MQI; X-ray; 2.30 A; A/B/C=258-351.
DR PDBsum; 3LYR; -.
DR PDBsum; 3MQI; -.
DR AlphaFoldDB; Q9UH73; -.
DR SMR; Q9UH73; -.
DR BioGRID; 108211; 13.
DR IntAct; Q9UH73; 7.
DR STRING; 9606.ENSP00000322898; -.
DR iPTMnet; Q9UH73; -.
DR PhosphoSitePlus; Q9UH73; -.
DR SwissPalm; Q9UH73; -.
DR BioMuta; EBF1; -.
DR DMDM; 47117917; -.
DR EPD; Q9UH73; -.
DR jPOST; Q9UH73; -.
DR MassIVE; Q9UH73; -.
DR MaxQB; Q9UH73; -.
DR PaxDb; Q9UH73; -.
DR PeptideAtlas; Q9UH73; -.
DR PRIDE; Q9UH73; -.
DR ProteomicsDB; 84280; -. [Q9UH73-1]
DR ProteomicsDB; 84281; -. [Q9UH73-2]
DR Antibodypedia; 28482; 188 antibodies from 30 providers.
DR DNASU; 1879; -.
DR Ensembl; ENST00000313708.11; ENSP00000322898.6; ENSG00000164330.17. [Q9UH73-1]
DR Ensembl; ENST00000380654.8; ENSP00000370029.4; ENSG00000164330.17. [Q9UH73-2]
DR GeneID; 1879; -.
DR KEGG; hsa:1879; -.
DR MANE-Select; ENST00000313708.11; ENSP00000322898.6; NM_024007.5; NP_076870.1.
DR UCSC; uc003lxl.7; human. [Q9UH73-1]
DR CTD; 1879; -.
DR DisGeNET; 1879; -.
DR GeneCards; EBF1; -.
DR HGNC; HGNC:3126; EBF1.
DR HPA; ENSG00000164330; Tissue enhanced (adipose).
DR MIM; 164343; gene.
DR neXtProt; NX_Q9UH73; -.
DR OpenTargets; ENSG00000164330; -.
DR PharmGKB; PA162384225; -.
DR VEuPathDB; HostDB:ENSG00000164330; -.
DR eggNOG; KOG3836; Eukaryota.
DR GeneTree; ENSGT00950000182859; -.
DR InParanoid; Q9UH73; -.
DR OMA; DDLFLHR; -.
DR OrthoDB; 817293at2759; -.
DR PhylomeDB; Q9UH73; -.
DR TreeFam; TF313391; -.
DR PathwayCommons; Q9UH73; -.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-9752946; Expression and translocation of olfactory receptors.
DR SignaLink; Q9UH73; -.
DR SIGNOR; Q9UH73; -.
DR BioGRID-ORCS; 1879; 19 hits in 1090 CRISPR screens.
DR ChiTaRS; EBF1; human.
DR EvolutionaryTrace; Q9UH73; -.
DR GeneWiki; EBF1; -.
DR GenomeRNAi; 1879; -.
DR Pharos; Q9UH73; Tbio.
DR PRO; PR:Q9UH73; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UH73; protein.
DR Bgee; ENSG00000164330; Expressed in synovial joint and 187 other tissues.
DR ExpressionAtlas; Q9UH73; baseline and differential.
DR Genevisible; Q9UH73; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd11606; COE_DBD; 1.
DR CDD; cd01175; IPT_COE; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.3180; -; 1.
DR InterPro; IPR032200; COE_DBD.
DR InterPro; IPR038173; COE_DBD_sf.
DR InterPro; IPR032201; COE_HLH.
DR InterPro; IPR038006; COE_IPT.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR003523; Transcription_factor_COE.
DR InterPro; IPR018350; Transcription_factor_COE_CS.
DR PANTHER; PTHR10747; PTHR10747; 1.
DR Pfam; PF16422; COE1_DBD; 1.
DR Pfam; PF16423; COE1_HLH; 1.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS01345; COE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..591
FT /note="Transcription factor COE1"
FT /id="PRO_0000107825"
FT DOMAIN 262..345
FT /note="IPT/TIG"
FT ZN_FING 151..170
FT /note="C5-type"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..66
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT REGION 197..204
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT REGION 236..239
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT REGION 457..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 163
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT SITE 172
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 162..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012304"
FT VAR_SEQ 252..259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012305"
FT MUTAGEN 240
FT /note="H->A: Impaired EBF1-mediated cell differentiation
FT and gene expression mostly without changing EBF1
FT occupancy."
FT /evidence="ECO:0000269|PubMed:27807034"
FT CONFLICT 112
FT /note="L -> I (in Ref. 2; AAF19643)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="N -> S (in Ref. 2; AAF19643)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..229
FT /note="VS -> AP (in Ref. 2; AAF19643)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..306
FT /note="IT -> TG (in Ref. 2; AAF19643)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> S (in Ref. 2; AAF19643)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="L -> R (in Ref. 2; AAF19643)"
FT /evidence="ECO:0000305"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3LYR"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:3LYR"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:3LYR"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3LYR"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:3LYR"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3LYR"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3LYR"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:3LYR"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3LYR"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3LYR"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:3MQI"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:3MQI"
SQ SEQUENCE 591 AA; 64464 MW; E47797B6FC1E5071 CRC64;
MFGIQESIQR SGSSMKEEPL GSGMNAVRTW MQGAGVLDAN TAAQSGVGLA RAHFEKQPPS
NLRKSNFFHF VLALYDRQGQ PVEIERTAFV GFVEKEKEAN SEKTNNGIHY RLQLLYSNGI
RTEQDFYVRL IDSMTKQAIV YEGQDKNPEM CRVLLTHEIM CSRCCDKKSC GNRNETPSDP
VIIDRFFLKF FLKCNQNCLK NAGNPRDMRR FQVVVSTTVN VDGHVLAVSD NMFVHNNSKH
GRRARRLDPS EGTPSYLEHA TPCIKAISPS EGWTTGGATV IIIGDNFFDG LQVIFGTMLV
WSELITPHAI RVQTPPRHIP GVVEVTLSYK SKQFCKGTPG RFIYTALNEP TIDYGFQRLQ
KVIPRHPGDP ERLPKEVILK RAADLVEALY GMPHNNQEII LKRAADIAEA LYSVPRNHNQ
LPALANTSVH AGMMGVNSFS GQLAVNVSEA SQATNQGFTR NSSSVSPHGY VPSTTPQQTN
YNSVTTSMNG YGSAAMSNLG GSPTFLNGSA ANSPYAIVPS SPTMASSTSL PSNCSSSSGI
FSFSPANMVS AVKQKSAFAP VVRPQTSPPP TCTSTNGNSL QAISGMIVPP M
