ELK3_MOUSE
ID ELK3_MOUSE Reviewed; 409 AA.
AC P41971; P97747; Q62346; Q8BWH1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=ETS domain-containing protein Elk-3;
DE AltName: Full=ETS-related protein ERP;
DE AltName: Full=ETS-related protein NET;
GN Name=Elk3; Synonyms=Erp, Net;
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 [MRNA].
RC TISSUE=Embryo;
RX PubMed=7958835; DOI=10.1101/gad.8.13.1502;
RA Giovane A., Pintzas A., Maira S.-M., Sobieszczuk P., Wasylyk B.;
RT "Net, a new ets transcription factor that is activated by Ras.";
RL Genes Dev. 8:1502-1513(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=7909357; DOI=10.1128/mcb.14.5.3292-3309.1994;
RA Lopez M., Oettgen P., Akbarali Y., Dendorfer U., Libermann T.A.;
RT "ERP, a new member of the ets transcription factor/oncoprotein family:
RT cloning, characterization, and differential expression during B-lymphocyte
RT development.";
RL Mol. Cell. Biol. 14:3292-3309(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8892757; DOI=10.1089/dna.1996.15.855;
RA Nozaki M., Onishi Y., Kanno N., Ono Y., Fujimura Y.;
RT "Molecular cloning of Elk-3, a new member of the Ets family expressed
RT during mouse embryogenesis and analysis of its transcriptional repression
RT activity.";
RL DNA Cell Biol. 15:855-862(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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).
CC -!- FUNCTION: May be a negative regulator of transcription, but can
CC activate transcription when coexpressed with Ras, Src or Mos. Forms a
CC ternary complex with the serum response factor and the ETS and SRF
CC motifs of the Fos serum response element.
CC -!- SUBUNIT: Interacts with CTBP1.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Heart, liver, lung, kidney and muscle.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; Z32815; CAA83676.1; -; mRNA.
DR EMBL; L19953; AAA19872.1; -; mRNA.
DR EMBL; S82864; AAB46893.1; -; mRNA.
DR EMBL; AK052546; BAC35034.1; -; mRNA.
DR CCDS; CCDS24124.1; -.
DR PIR; I48680; I48680.
DR RefSeq; NP_001309194.1; NM_001322265.1.
DR RefSeq; NP_001309197.1; NM_001322268.1.
DR RefSeq; NP_038536.2; NM_013508.2.
DR AlphaFoldDB; P41971; -.
DR SMR; P41971; -.
DR BioGRID; 199430; 1.
DR ELM; P41971; -.
DR STRING; 10090.ENSMUSP00000008542; -.
DR iPTMnet; P41971; -.
DR PhosphoSitePlus; P41971; -.
DR EPD; P41971; -.
DR MaxQB; P41971; -.
DR PaxDb; P41971; -.
DR PRIDE; P41971; -.
DR ProteomicsDB; 275524; -.
DR Antibodypedia; 898; 394 antibodies from 27 providers.
DR DNASU; 13713; -.
DR Ensembl; ENSMUST00000008542; ENSMUSP00000008542; ENSMUSG00000008398.
DR GeneID; 13713; -.
DR KEGG; mmu:13713; -.
DR UCSC; uc011xlt.1; mouse.
DR CTD; 2004; -.
DR MGI; MGI:101762; Elk3.
DR VEuPathDB; HostDB:ENSMUSG00000008398; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000157129; -.
DR HOGENOM; CLU_036905_1_0_1; -.
DR InParanoid; P41971; -.
DR OMA; DKHITRP; -.
DR OrthoDB; 981551at2759; -.
DR PhylomeDB; P41971; -.
DR TreeFam; TF317732; -.
DR BioGRID-ORCS; 13713; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Elk3; mouse.
DR PRO; PR:P41971; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P41971; protein.
DR Bgee; ENSMUSG00000008398; Expressed in brain blood vessel and 289 other tissues.
DR ExpressionAtlas; P41971; baseline and differential.
DR Genevisible; P41971; MM.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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:0032422; F:purine-rich negative regulatory element binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045944; P:positive 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:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR Gene3D; 1.10.10.10; -; 1.
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 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 2: Evidence at transcript level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..409
FT /note="ETS domain-containing protein Elk-3"
FT /id="PRO_0000204098"
FT DNA_BIND 5..85
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 235..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..279
FT /note="CTBP-binding motif"
FT COMPBIAS 235..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41970"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41970"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41970"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41970"
FT CONFLICT 152
FT /note="Q -> E (in Ref. 1; CAA83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> M (in Ref. 1; CAA83676 and 2; AAA19872)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="I -> V (in Ref. 1; CAA83676, 2; AAA19872 and 3;
FT AAB46893)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="A -> V (in Ref. 1; CAA83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="D -> E (in Ref. 1; CAA83676, 2; AAA19872 and 3;
FT AAB46893)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> T (in Ref. 3; AAB46893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44414 MW; 7F6B5D1626C62ABA CRC64;
MESAITLWQF LLHLLLDQKH EHLICWTSND GEFKLLKAEE VAKLWGLRKN KTNMNYDKLS
RALRYYYDKN IIKKVIGQKF VYKFVSFPDI LKMDPHAVEI SRESLLLQDG DCKVSPEGRE
VHRHGLSSLK SASRNEYLHS GLYSSFTINS LQNAPEAFKA IKTEKLEEPC DDSPPVEEVR
TVIRFVTNKT DKHITRPVVS LPSTSETAAA AASAFLASSV SAKISSLMLP NAASISSASP
SSSRSPSLSP DSPLPSEHRS LFLEAACHDS DSLEPLNLSS GSKTKSPSLP PKGKKPKGLE
ISAPQLLLSG TDIGSIALNS PALPSGSLTP AFFTAQTPSG LFLASSPLLP SIHFWSSLSP
VAPLSPARLQ GPNTLFQFPT LLNGHMPVPL PSLDRAPSPV LLSPSSQKS
