ERF_HUMAN
ID ERF_HUMAN Reviewed; 548 AA.
AC P50548; B2RAP1; B7Z4R0; Q59G38; Q9UPI7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=ETS domain-containing transcription factor ERF;
DE AltName: Full=Ets2 repressor factor;
DE AltName: Full=PE-2;
GN Name=ERF;
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), PHOSPHORYLATION AT THR-526, AND
RP MUTAGENESIS OF THR-526.
RX PubMed=7588608; DOI=10.1002/j.1460-2075.1995.tb00160.x;
RA Sgouras D.N., Athanasiou M.A., Beal G.J. Jr., Fisher R.J., Blair D.G.,
RA Mavrothalassitis G.J.;
RT "ERF: an ETS domain protein with strong transcriptional repressor activity,
RT can suppress ets-associated tumorigenesis and is regulated by
RT phosphorylation during cell cycle and mitogenic stimulation.";
RL EMBO J. 14:4781-4793(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Heart;
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=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Duodenum;
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 PROTEIN SEQUENCE OF 102-110; 206-218; 313-347; 377-386; 402-426 AND
RP 515-528, PHOSPHORYLATION AT SER-327, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=9192842; DOI=10.1006/geno.1997.4730;
RA de Castro C.M., Rabe S.M., Langdon S.D., Fleenor D.E., Slentz-Kesler K.,
RA Ahmed M.N., Qumsiyeh M.B., Kaufman R.E.;
RT "Genomic structure and chromosomal localization of the novel ETS factor,
RT PE-2 (ERF).";
RL Genomics 42:227-235(1997).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; THR-7; SER-20; SER-185;
RP SER-327; SER-431; SER-435; THR-441; SER-444; SER-531 AND SER-548, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-444 AND THR-526, AND
RP IDENTIFICATION BY 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 [12]
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-185; SER-327;
RP THR-526; SER-531 AND SER-532, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-465 AND LYS-512, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-465; LYS-481 AND LYS-512, AND
RP IDENTIFICATION BY MASS 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 [17]
RP VARIANTS CRS4 GLN-65 AND CYS-86.
RX PubMed=23354439; DOI=10.1038/ng.2539;
RA Twigg S.R., Vorgia E., McGowan S.J., Peraki I., Fenwick A.L., Sharma V.P.,
RA Allegra M., Zaragkoulias A., Sadighi Akha E., Knight S.J., Lord H.,
RA Lester T., Izatt L., Lampe A.K., Mohammed S.N., Stewart F.J., Verloes A.,
RA Wilson L.C., Healy C., Sharpe P.T., Hammond P., Hughes J., Taylor S.,
RA Johnson D., Wall S.A., Mavrothalassitis G., Wilkie A.O.;
RT "Reduced dosage of ERF causes complex craniosynostosis in humans and mice
RT and links ERK1/2 signaling to regulation of osteogenesis.";
RL Nat. Genet. 45:308-313(2013).
RN [18]
RP INVOLVEMENT IN CHYTS, AND VARIANT CHYTS CYS-89.
RX PubMed=27738187; DOI=10.1136/jmedgenet-2016-104143;
RG DDD Study;
RA Balasubramanian M., Lord H., Levesque S., Guturu H., Thuriot F., Sillon G.,
RA Wenger A.M., Sureka D.L., Lester T., Johnson D.S., Bowen J., Calhoun A.R.,
RA Viskochil D.H., Bejerano G., Bernstein J.A., Chitayat D.;
RT "Chitayat syndrome: hyperphalangism, characteristic facies, hallux valgus
RT and bronchomalacia results from a recurrent c.266A>G p.(Tyr89Cys) variant
RT in the ERF gene.";
RL J. Med. Genet. 54:157-165(2017).
CC -!- FUNCTION: Potent transcriptional repressor that binds to the H1 element
CC of the Ets2 promoter. May regulate other genes involved in cellular
CC proliferation. Required for extraembryonic ectoderm differentiation,
CC ectoplacental cone cavity closure, and chorioallantoic attachment (By
CC similarity). May be important for regulating trophoblast stem cell
CC differentiation (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P50548; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-8465203, EBI-348259;
CC P50548; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-8465203, EBI-16439278;
CC P50548; Q08117-2: TLE5; NbExp=3; IntAct=EBI-8465203, EBI-11741437;
CC P50548; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-8465203, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50548-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50548-2; Sequence=VSP_055487;
CC -!- TISSUE SPECIFICITY: Highest levels in testis, ovary, pancreas, and
CC heart. {ECO:0000269|PubMed:9192842}.
CC -!- PTM: Phosphorylated by multiple kinases including MAPK1/ERK2 at THR-
CC 526. Phosphorylation regulates the activity of ERF.
CC {ECO:0000269|PubMed:7588608, ECO:0000269|Ref.7}.
CC -!- DISEASE: Craniosynostosis 4 (CRS4) [MIM:600775]: A primary abnormality
CC of skull growth involving premature fusion of one or more cranial
CC sutures. The growth velocity of the skull often cannot match that of
CC the developing brain resulting in an abnormal head shape and, in some
CC cases, increased intracranial pressure, which must be treated promptly
CC to avoid permanent neurodevelopmental disability.
CC {ECO:0000269|PubMed:23354439}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Chitayat syndrome (CHYTS) [MIM:617180]: An autosomal dominant
CC syndrome characterized by hyperphalangism, partial syndactyly,
CC bilateral accessory phalanx resulting in shortened index fingers,
CC hallux valgus, brachydactyly, facial anomalies, diffuse bronchomalacia,
CC and respiratory distress at birth and in infancy.
CC {ECO:0000269|PubMed:27738187}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92508.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; U15655; AAA86686.1; -; mRNA.
DR EMBL; AK297666; BAH12646.1; -; mRNA.
DR EMBL; AK314278; BAG36938.1; -; mRNA.
DR EMBL; AB209271; BAD92508.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AC006486; AAD11987.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57116.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57118.1; -; Genomic_DNA.
DR EMBL; BC022231; AAH22231.1; -; mRNA.
DR CCDS; CCDS12600.1; -. [P50548-1]
DR CCDS; CCDS77308.1; -. [P50548-2]
DR PIR; S59133; S59133.
DR RefSeq; NP_001287964.1; NM_001301035.1. [P50548-2]
DR RefSeq; NP_001295331.1; NM_001308402.1. [P50548-2]
DR RefSeq; NP_001299585.1; NM_001312656.1. [P50548-2]
DR RefSeq; NP_006485.2; NM_006494.3. [P50548-1]
DR RefSeq; XP_016881957.1; XM_017026468.1. [P50548-2]
DR RefSeq; XP_016881958.1; XM_017026469.1. [P50548-2]
DR PDB; 7JSA; X-ray; 2.85 A; J=22-140.
DR PDB; 7JSL; X-ray; 4.51 A; E/H/J/L=22-140.
DR PDBsum; 7JSA; -.
DR PDBsum; 7JSL; -.
DR AlphaFoldDB; P50548; -.
DR SMR; P50548; -.
DR BioGRID; 108388; 140.
DR IntAct; P50548; 27.
DR MINT; P50548; -.
DR STRING; 9606.ENSP00000222329; -.
DR iPTMnet; P50548; -.
DR PhosphoSitePlus; P50548; -.
DR BioMuta; ERF; -.
DR DMDM; 50403684; -.
DR EPD; P50548; -.
DR jPOST; P50548; -.
DR MassIVE; P50548; -.
DR MaxQB; P50548; -.
DR PaxDb; P50548; -.
DR PeptideAtlas; P50548; -.
DR PRIDE; P50548; -.
DR ProteomicsDB; 56243; -. [P50548-1]
DR ProteomicsDB; 6624; -.
DR Antibodypedia; 30909; 337 antibodies from 25 providers.
DR DNASU; 2077; -.
DR Ensembl; ENST00000222329.9; ENSP00000222329.3; ENSG00000105722.10. [P50548-1]
DR Ensembl; ENST00000440177.6; ENSP00000388173.2; ENSG00000105722.10. [P50548-2]
DR GeneID; 2077; -.
DR KEGG; hsa:2077; -.
DR MANE-Select; ENST00000222329.9; ENSP00000222329.3; NM_006494.4; NP_006485.2.
DR UCSC; uc002ote.5; human. [P50548-1]
DR CTD; 2077; -.
DR DisGeNET; 2077; -.
DR GeneCards; ERF; -.
DR HGNC; HGNC:3444; ERF.
DR HPA; ENSG00000105722; Low tissue specificity.
DR MalaCards; ERF; -.
DR MIM; 600775; phenotype.
DR MIM; 611888; gene.
DR MIM; 617180; phenotype.
DR neXtProt; NX_P50548; -.
DR OpenTargets; ENSG00000105722; -.
DR Orphanet; 207; Crouzon syndrome.
DR Orphanet; 35093; Non-syndromic sagittal craniosynostosis.
DR PharmGKB; PA27857; -.
DR VEuPathDB; HostDB:ENSG00000105722; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000157292; -.
DR HOGENOM; CLU_023454_0_0_1; -.
DR InParanoid; P50548; -.
DR OMA; QRDCSAS; -.
DR PhylomeDB; P50548; -.
DR TreeFam; TF351065; -.
DR PathwayCommons; P50548; -.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR SignaLink; P50548; -.
DR SIGNOR; P50548; -.
DR BioGRID-ORCS; 2077; 19 hits in 1113 CRISPR screens.
DR ChiTaRS; ERF; human.
DR GeneWiki; ERF_(gene); -.
DR GenomeRNAi; 2077; -.
DR Pharos; P50548; Tbio.
DR PRO; PR:P50548; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P50548; protein.
DR Bgee; ENSG00000105722; Expressed in right uterine tube and 156 other tissues.
DR ExpressionAtlas; P50548; baseline and differential.
DR Genevisible; P50548; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR032925; ERF.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF31; PTHR11849:SF31; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Craniosynostosis;
KW Direct protein sequencing; Disease variant; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..548
FT /note="ETS domain-containing transcription factor ERF"
FT /id="PRO_0000204101"
FT DNA_BIND 27..107
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 130..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 526
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:7588608,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055487"
FT VARIANT 65
FT /note="R -> Q (in CRS4; dbSNP:rs587777009)"
FT /evidence="ECO:0000269|PubMed:23354439"
FT /id="VAR_070098"
FT VARIANT 86
FT /note="R -> C (in CRS4; dbSNP:rs587777008)"
FT /evidence="ECO:0000269|PubMed:23354439"
FT /id="VAR_070099"
FT VARIANT 89
FT /note="Y -> C (in CHYTS; dbSNP:rs886041001)"
FT /evidence="ECO:0000269|PubMed:27738187"
FT /id="VAR_078043"
FT VARIANT 205
FT /note="R -> H (in dbSNP:rs1053655)"
FT /id="VAR_048947"
FT MUTAGEN 526
FT /note="T->A: Loss of a phosphorylation site."
FT /evidence="ECO:0000269|PubMed:7588608"
FT CONFLICT 381
FT /note="P -> R (in Ref. 1; AAA86686)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="G -> A (in Ref. 1; AAA86686)"
FT /evidence="ECO:0000305"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:7JSA"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:7JSA"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:7JSA"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7JSA"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:7JSA"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:7JSA"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:7JSA"
FT TURN 87..92
FT /evidence="ECO:0007829|PDB:7JSA"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:7JSA"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:7JSA"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:7JSA"
SQ SEQUENCE 548 AA; 58703 MW; 01242339B8D328ED CRC64;
MKTPADTGFA FPDWAYKPES SPGSRQIQLW HFILELLRKE EYQGVIAWQG DYGEFVIKDP
DEVARLWGVR KCKPQMNYDK LSRALRYYYN KRILHKTKGK RFTYKFNFNK LVLVNYPFID
VGLAGGAVPQ SAPPVPSGGS HFRFPPSTPS EVLSPTEDPR SPPACSSSSS SLFSAVVARR
LGRGSVSDCS DGTSELEEPL GEDPRARPPG PPDLGAFRGP PLARLPHDPG VFRVYPRPRG
GPEPLSPFPV SPLAGPGSLL PPQLSPALPM TPTHLAYTPS PTLSPMYPSG GGGPSGSGGG
SHFSFSPEDM KRYLQAHTQS VYNYHLSPRA FLHYPGLVVP QPQRPDKCPL PPMAPETPPV
PSSASSSSSS SSSPFKFKLQ PPPLGRRQRA AGEKAVAGAD KSGGSAGGLA EGAGALAPPP
PPPQIKVEPI SEGESEEVEV TDISDEDEED GEVFKTPRAP PAPPKPEPGE APGASQCMPL
KLRFKRRWSE DCRLEGGGGP AGGFEDEGED KKVRGEGPGE AGGPLTPRRV SSDLQHATAQ
LSLEHRDS
