ELK1_MOUSE
ID ELK1_MOUSE Reviewed; 429 AA.
AC P41969; Q3V1M9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ETS domain-containing protein Elk-1;
GN Name=Elk1 {ECO:0000312|MGI:MGI:101833};
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 STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=8863747; DOI=10.1016/0378-1119(96)00357-5;
RA Grevin D., Ung S., Denhez F., Dehem M., Quatannens B., Begue A.,
RA Stehelin D., Martin P.;
RT "Structure and organization of the mouse elk1 gene.";
RL Gene 174:185-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-224.
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).
CC -!- FUNCTION: Transcription factor that binds to purine-rich DNA sequences.
CC Forms a ternary complex with SRF and the ETS and SRF motifs of the
CC serum response element (SRE) on the promoter region of immediate early
CC genes such as FOS and IER2 (By similarity). Induces target gene
CC transcription upon JNK-signaling pathway stimulation (By similarity).
CC {ECO:0000250|UniProtKB:A4GTP4, ECO:0000250|UniProtKB:P19419}.
CC -!- SUBUNIT: Interacts in its sumoylated form with PIAS2/PIASX which
CC enhances its transcriptional activator activity. Interacts with MAD2L2;
CC the interaction is direct and promotes phosphorylation by the kinases
CC MAPK8 and/or MAPK9. Interacts with POU1F1.
CC {ECO:0000250|UniProtKB:P19419}.
CC -!- INTERACTION:
CC P41969; P30275: Ckmt1; NbExp=2; IntAct=EBI-15576110, EBI-773103;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, and to a
CC lesser extent in the heart, liver and muscle.
CC -!- PTM: Sumoylation represses transcriptional activator activity as it
CC results in recruitment of HDAC2 to target gene promoters which leads to
CC decreased histone acetylation and reduced transactivator activity. It
CC also regulates nuclear retention (By similarity).
CC {ECO:0000250|UniProtKB:P19419}.
CC -!- PTM: On mitogenic stimulation, phosphorylated on C-terminal serine and
CC threonine residues by MAPK1 but also MAPK8 and/or MAPK9.
CC Phosphorylation leads to loss of sumoylation and restores
CC transcriptional activator activity. Phosphorylated and activated by
CC CaMK4, MAPK11, MAPK12 and MAPK14 (By similarity). Upon bFGF stimulus,
CC phosphorylated by PAK1 (By similarity). {ECO:0000250|UniProtKB:A4GTP4,
CC ECO:0000250|UniProtKB:P19419}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; X87257; CAA60715.1; -; mRNA.
DR EMBL; AK132354; BAE21121.1; -; mRNA.
DR EMBL; AL671853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466625; EDL00733.1; -; Genomic_DNA.
DR EMBL; Z36939; CAA85391.1; -; mRNA.
DR CCDS; CCDS30048.1; -.
DR PIR; JC4965; JC4965.
DR RefSeq; NP_031948.4; NM_007922.5.
DR AlphaFoldDB; P41969; -.
DR SMR; P41969; -.
DR BioGRID; 199429; 5.
DR DIP; DIP-61141N; -.
DR IntAct; P41969; 1.
DR STRING; 10090.ENSMUSP00000009550; -.
DR iPTMnet; P41969; -.
DR PhosphoSitePlus; P41969; -.
DR MaxQB; P41969; -.
DR PaxDb; P41969; -.
DR PRIDE; P41969; -.
DR ProteomicsDB; 275523; -.
DR Antibodypedia; 3538; 1311 antibodies from 49 providers.
DR DNASU; 13712; -.
DR Ensembl; ENSMUST00000009550; ENSMUSP00000009550; ENSMUSG00000009406.
DR GeneID; 13712; -.
DR KEGG; mmu:13712; -.
DR UCSC; uc009suc.2; mouse.
DR CTD; 2002; -.
DR MGI; MGI:101833; Elk1.
DR VEuPathDB; HostDB:ENSMUSG00000009406; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000157571; -.
DR HOGENOM; CLU_036905_0_0_1; -.
DR InParanoid; P41969; -.
DR OMA; NTAQVCG; -.
DR OrthoDB; 981551at2759; -.
DR PhylomeDB; P41969; -.
DR TreeFam; TF317732; -.
DR BioGRID-ORCS; 13712; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Elk1; mouse.
DR PRO; PR:P41969; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P41969; protein.
DR Bgee; ENSMUSG00000009406; Expressed in rostral migratory stream and 240 other tissues.
DR Genevisible; P41969; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO: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:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0071396; P:cellular response to lipid; ISO:MGI.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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:0071774; P:response to fibroblast growth factor; ISS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; ISO:MGI.
DR DisProt; DP01578; -.
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 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..429
FT /note="ETS domain-containing protein Elk-1"
FT /id="PRO_0000204096"
FT DNA_BIND 5..86
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 119..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..400
FT /note="Sufficient for interaction with MAD2L2"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT COMPBIAS 168..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 337
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 354
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 364
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 369
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 384
FT /note="Phosphoserine; by MAPK1 and MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 390
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 418
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 423
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT CONFLICT 133
FT /note="P -> T (in Ref. 5; CAA85391)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="V -> A (in Ref. 1; CAA60715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 45271 MW; 2E1C5B80790C6DA7 CRC64;
MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK NKTNMNYDKL
SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP PQPEVSVTSA IAMAPATVHA
GPGDTATGKP GTPKGAGMTG QGGLARSSRN EYMRSGLYST FTIQSLQPQP QPPIPPRPAS
VLPNTTPAGV PAPASGSRST SPNPLEACLE AEEAGLPLQV ILTPPEAPNQ KSEELSLDPS
FGHPQPPEVK VEGPKEELEA ARAGGFSSEA VKAEPEVSAS EGLLARLPAI LTENTAQVCG
LSTSTTEITQ PQKGRKPRDL ELPLSPSLLG GQGPERTPGS GTSSGLQAPG PALTPSLLPT
HTLTPVLLTP SSLPPSIHFW STLSPIAPRS PAKLSFQFPS SGSAQVHIPS ISVDGLSTPV
VLSPGPQKP
