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 02-JUN-2021, entry version 187. 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}; 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; 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 SMR; P50548; -. DR BioGRID; 108388; 49. DR IntAct; P50548; 25. 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; 323 antibodies. DR DNASU; 2077; -. DR Ensembl; ENST00000222329; ENSP00000222329; ENSG00000105722. [P50548-1] DR Ensembl; ENST00000440177; ENSP00000388173; ENSG00000105722. [P50548-2] DR GeneID; 2077; -. DR KEGG; hsa:2077; -. 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 disease. DR Orphanet; 3267; Familial lambdoid synostosis. DR Orphanet; 2343; Isolated cloverleaf skull syndrome. DR Orphanet; 35093; Isolated scaphocephaly. DR PharmGKB; PA27857; -. DR VEuPathDB; HostDB:ENSG00000105722.9; -. DR eggNOG; KOG3806; Eukaryota. DR GeneTree; ENSGT00940000157292; -. DR HOGENOM; CLU_023454_0_0_1; -. DR InParanoid; P50548; -. DR OMA; PGVAQCM; -. DR PhylomeDB; P50548; -. DR TreeFam; TF351065; -. DR PathwayCommons; P50548; -. DR Reactome; R-HSA-2559585; Oncogene Induced Senescence. DR SIGNOR; P50548; -. DR BioGRID-ORCS; 2077; 11 hits in 1019 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 left lobe of thyroid gland and 202 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; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. 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 //