ID ERF_HUMAN STANDARD; PRT; 548 AA. AC P50548; Q9UPI7; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-MAR-2002 (Rel. 41, Last annotation update) DE ETS-domain transcription factor ERF (Ets2 repressor factor). GN ERF. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RA Lamerdin J.E., McCready P.M., Skowronski E., Viswanathan V., RA Burkhart-Schultz K., Gordon L., Dias J., Ramirez M., Stilwagen S., RA Phan H., Velasco N., Do L., Regala W., Terry A., Garnes J., RA Danganan L., Erler A., Christensen M., Georgescu A., Avila J., Liu S., RA Attix C., Andreise T., Trankheim M., Amico-Keller G., Coefield J., RA Duarte S., Lucas S., Bruce R., Thomas P., Quan G., Kronmiller B., RA Arellano A., Sanders C., Ow D., Nolan M., Trong S., Kobayashi A., RA Olsen A.S., Carrano A.V.; RT "Sequence analysis of a 3.2 Mb region in 19q13.2 between CYP2F1 and RT D19S178."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: POTENT TRANSCRIPTIONAL REPRESSOR THAT BINDS TO THE H1 CC ELEMENT OF THE ETS2 PROMOTER. MAY REGULATE OTHER GENES INVOLVED CC IN CELLULAR PROLIFERATION. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- PTM: PHOSPHORYLATED BY MULTIPLE KINASES INCLUDING PROBABLY ERK2. CC PHOSPHORYLATION REGULATES THE ACTIVITY OF ERF. CC -!- SIMILARITY: BELONGS TO THE ETS FAMILY. 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; -. DR EMBL; AC006486; AAD11987.1; -. DR HSSP; Q01543; 1FLI. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS. 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. KW Transcription regulation; Repressor; DNA-binding; Nuclear protein; KW Phosphorylation. FT DNA_BIND 27 107 ETS-DOMAIN. FT DOMAIN 166 171 POLY-SER. FT DOMAIN 290 293 POLY-GLY. FT DOMAIN 362 373 POLY-SER. FT DOMAIN 418 423 POLY-PRO. FT DOMAIN 496 499 POLY-GLY. FT MOD_RES 526 526 PHOSPHORYLATION (BY MAPK1). FT MUTAGEN 526 526 T->A: LOSS OF A PHOSPHORYLATION SITE. FT CONFLICT 381 381 R -> P (IN REF. 2). FT CONFLICT 398 398 A -> G (IN REF. 2). SQ SEQUENCE 548 AA; 58776 MW; C93A155394B1EEDD 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 RPPLGRRQRA AGEKAVAAAD KSGGSAGGLA EGAGALAPPP PPPQIKVEPI SEGESEEVEV TDISDEDEED GEVFKTPRAP PAPPKPEPGE APGASQCMPL KLRFKRRWSE DCRLEGGGGP AGGFEDEGED KKVRGEGPGE AGGPLTPRRV SSDLQHATAQ LSLEHRDS //