ID ERF_HUMAN Reviewed; 548 AA. AC P50548; B2RAP1; Q59G38; Q9UPI7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 23-MAR-2010, entry version 93. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF THR-526. RX MEDLINE=96030784; PubMed=7588608; 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 RT activity, can suppress ets-associated tumorigenesis and is regulated RT by phosphorylation during cell cycle and mitogenic stimulation."; RL EMBO J. 14:4781-4793(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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]. 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., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: 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 MASS 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., RA Slentz-Kesler K., Ahmed M.N., Qumsiyeh M.B., Kaufman R.E.; RT "Genomic structure and chromosomal localization of the novel ETS RT factor, PE-2 (ERF)."; RL Genomics 42:227-235(1997). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-185; SER-187; RP SER-190 AND SER-531, AND MASS SPECTROMETRY. RC TISSUE=Epithelium; 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; 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 RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; THR-7; TYR-16; RP SER-20; SER-21; THR-148; SER-171; SER-185; SER-187; SER-190; SER-327; RP SER-431; SER-435; THR-441; SER-444; THR-526; SER-531 AND SER-548, AND RP MASS SPECTROMETRY. 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-444 AND RP THR-526, AND MASS SPECTROMETRY. RC TISSUE=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). CC -!- FUNCTION: Potent transcriptional repressor that binds to the H1 CC element of the Ets2 promoter. May regulate other genes involved in CC cellular proliferation. Required for extraembryonic ectoderm CC differentiation, ectoplacental cone cavity closure, and CC chorioallantoic attachment (By similarity). May be important for CC regulating trophoblast stem cell differentiation (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Highest levels in testis, ovary, pancreas, and CC heart. CC -!- PTM: Phosphorylated by multiple kinases including probably ERK2. CC Phosphorylation regulates the activity of ERF. CC -!- SIMILARITY: Belongs to the ETS family. CC -!- SIMILARITY: Contains 1 ETS DNA-binding domain. 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; 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; 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; BC022231; AAH22231.1; -; mRNA. DR IPI; IPI00032936; -. DR PIR; S59133; S59133. DR RefSeq; NP_006485.2; -. DR UniGene; Hs.655969; -. DR SMR; P50548; 23-106. DR STRING; P50548; -. DR PhosphoSite; P50548; -. DR PeptideAtlas; P50548; -. DR PRIDE; P50548; -. DR Ensembl; ENST00000222329; ENSP00000222329; ENSG00000105722; Homo sapiens. DR GeneID; 2077; -. DR KEGG; hsa:2077; -. DR UCSC; uc002ote.2; human. DR CTD; 2077; -. DR GeneCards; GC19M047443; -. DR HGNC; HGNC:3444; ERF. DR MIM; 611888; gene. DR PharmGKB; PA27857; -. DR eggNOG; prNOG18306; -. DR HOGENOM; HBG402951; -. DR HOVERGEN; HBG005183; -. DR InParanoid; P50548; -. DR OMA; VVPQPQR; -. DR OrthoDB; EOG91C9FJ; -. DR PhylomeDB; P50548; -. DR NextBio; 8443; -. DR ArrayExpress; P50548; -. DR Bgee; P50548; -. DR CleanEx; HS_ERF; -. DR Genevestigator; P50548; -. DR GermOnline; ENSG00000105722; Homo sapiens. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003706; F:ligand-regulated transcription factor activity; TAS:ProtInc. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc. DR GO; GO:0003700; F:transcription factor activity; IEA:InterPro. DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc. DR GO; GO:0006350; P:cellular transcription; IEA:UniProtKB-KW. DR GO; GO:0006357; P:regulation of transcription from RNA polyme...; TAS:ProtInc. DR InterPro; IPR000418; Ets. DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 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 Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; KW Phosphoprotein; Polymorphism; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 548 ETS domain-containing transcription FT factor ERF. FT /FTId=PRO_0000204101. FT DNA_BIND 27 107 ETS. FT COMPBIAS 166 171 Poly-Ser. FT COMPBIAS 290 293 Poly-Gly. FT COMPBIAS 362 373 Poly-Ser. FT COMPBIAS 418 423 Poly-Pro. FT COMPBIAS 496 499 Poly-Gly. FT MOD_RES 3 3 Phosphothreonine. FT MOD_RES 7 7 Phosphothreonine. FT MOD_RES 16 16 Phosphotyrosine. FT MOD_RES 20 20 Phosphoserine. FT MOD_RES 21 21 Phosphoserine. FT MOD_RES 148 148 Phosphothreonine. FT MOD_RES 171 171 Phosphoserine. FT MOD_RES 185 185 Phosphoserine. FT MOD_RES 187 187 Phosphoserine. FT MOD_RES 190 190 Phosphoserine. FT MOD_RES 327 327 Phosphoserine. FT MOD_RES 431 431 Phosphoserine. FT MOD_RES 435 435 Phosphoserine. FT MOD_RES 441 441 Phosphothreonine. FT MOD_RES 444 444 Phosphoserine. FT MOD_RES 526 526 Phosphothreonine; by MAPK1. FT MOD_RES 531 531 Phosphoserine. FT MOD_RES 548 548 Phosphoserine. FT VARIANT 205 205 R -> H (in dbSNP:rs1053655). FT /FTId=VAR_048947. FT MUTAGEN 526 526 T->A: Loss of a phosphorylation site. FT CONFLICT 381 381 P -> R (in Ref. 1; AAA86686). FT CONFLICT 398 398 G -> A (in Ref. 1; AAA86686). 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 //