ERF_MOUSE
ID ERF_MOUSE Reviewed; 551 AA.
AC P70459; Q3TXK4; Q6P544; Q7TSJ1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=ETS domain-containing transcription factor ERF;
GN Name=Erf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9136988; DOI=10.1038/sj.onc.1200965;
RA Liu D., Pavlopoulos E., Modi W., Moschonas N., Mavrothalassitis G.J.;
RT "ERF: genomic organization, chromosomal localization and promoter analysis
RT of the human and mouse genes.";
RL Oncogene 14:1445-1451(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Jaw;
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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17502352; DOI=10.1128/mcb.02237-06;
RA Papadaki C., Alexiou M., Cecena G., Verykokakis M., Bilitou A., Cross J.C.,
RA Oshima R.G., Mavrothalassitis G.;
RT "Transcriptional repressor erf determines extraembryonic ectoderm
RT differentiation.";
RL Mol. Cell. Biol. 27:5201-5213(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY.
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).
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 (By similarity). Required for extraembryonic ectoderm
CC differentiation, ectoplacental cone cavity closure, and chorioallantoic
CC attachment. May be important for regulating trophoblast stem cell
CC differentiation. {ECO:0000250, ECO:0000269|PubMed:17502352}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed along the osteogenic margins of the
CC developing calvarial bones, in a similar distribution to that observed
CC for the master osteogenic regulator RUNX2.
CC {ECO:0000269|PubMed:23354439}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development and
CC adulthood. In the developing placenta, after 7.5 dpc expression is
CC restricted to the extraembryonic ectoderm, and after 9.5 dpc to
CC subpopulation of labyrinth cells. {ECO:0000269|PubMed:17502352}.
CC -!- PTM: Phosphorylated by multiple kinases including MAPK1/ERK2 at THR-
CC 529. Phosphorylation regulates the activity of ERF (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice fail to undergo chorioallantoic attachment
CC and labyrinth development and die in utero due to severe placenta
CC defects. {ECO:0000269|PubMed:17502352}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53045.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH59176.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U58533; AAC09474.1; -; Genomic_DNA.
DR EMBL; U58534; AAC09474.1; JOINED; Genomic_DNA.
DR EMBL; AK159225; BAE34912.1; -; mRNA.
DR EMBL; CH466593; EDL24284.1; -; Genomic_DNA.
DR EMBL; BC053045; AAH53045.1; ALT_INIT; mRNA.
DR EMBL; BC059176; AAH59176.1; ALT_INIT; mRNA.
DR EMBL; BC063092; AAH63092.1; -; mRNA.
DR CCDS; CCDS20978.1; -.
DR RefSeq; NP_034285.3; NM_010155.3.
DR AlphaFoldDB; P70459; -.
DR SMR; P70459; -.
DR BioGRID; 199503; 1.
DR STRING; 10090.ENSMUSP00000041912; -.
DR iPTMnet; P70459; -.
DR PhosphoSitePlus; P70459; -.
DR jPOST; P70459; -.
DR MaxQB; P70459; -.
DR PaxDb; P70459; -.
DR PeptideAtlas; P70459; -.
DR PRIDE; P70459; -.
DR ProteomicsDB; 275940; -.
DR DNASU; 13875; -.
DR GeneID; 13875; -.
DR KEGG; mmu:13875; -.
DR UCSC; uc009frz.2; mouse.
DR CTD; 2077; -.
DR MGI; MGI:109637; Erf.
DR eggNOG; KOG3806; Eukaryota.
DR InParanoid; P70459; -.
DR OrthoDB; 677533at2759; -.
DR PhylomeDB; P70459; -.
DR TreeFam; TF351065; -.
DR Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR BioGRID-ORCS; 13875; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Erf; mouse.
DR PRO; PR:P70459; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70459; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
DR GO; GO:0010668; P:ectodermal cell differentiation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
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 DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..551
FT /note="ETS domain-containing transcription factor ERF"
FT /id="PRO_0000204102"
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..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..551
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 240..256
FT /note="Pro 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 436..452
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 529
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50548"
FT CONFLICT 68
FT /note="G -> V (in Ref. 4; AAH63092)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="P -> S (in Ref. 4; AAH59176/AAH53045)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="P -> L (in Ref. 2; BAE34912, 3; EDL24284 and 4;
FT AAH59176/AAH53045/AAH63092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 59050 MW; 5AC1B72FB2743FE5 CRC64;
MKTPADTGFA FPDWAYKPES SPGSRQIQLW HFILELLRKE EYQGVIAWQG DYGEFVIKDP
DEVARLWGVR KCKPQMNYDK LSRALRYYYN KRILHKTKGK RFTYKFNFNK LVLVNYPFID
MGLAGGAVPQ SAPPVPSGGS HFRFPPSTPS EVLSPTEDPR SPPACSSSSS SLFSAVVARR
LGRGSVSDCS DGTSELEEPL GEDPRARPPG PPELGAFRGP PLARLPHDPG VFRVYPRPRG
GPEPLSPFPV SPLAGPGSLL PPQLSPALPM TPTHLAYTPS PTLSPMYPSG GGGPSGSGGG
SHFSFSPEDM KRYLQAHTQS VYNYHLSPRA FLHYPGLVVP QPQRPDKCPL PPMAPETPPV
PSSASSSSSS SSSPFKFKLQ PPPLGRRQRA AGEKAPGGTD KSSGGSGSGG LAEGAGAVAP
PPPPPQIKVE PISEGESEEV EVTDISDEDE EDGEVFKTPR APPAPPKPEP GEAPGVAQCM
PLKLRFKRRW SEDCRLEGGG CLSGGPEDEG EDKKVRGDVG PGESGGPLTP RRVSSDLQHA
TAQLSLEHRD S
