ID ELK4_MOUSE Reviewed; 430 AA. AC P41158; A6H693; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 160. DE RecName: Full=ETS domain-containing protein Elk-4; DE AltName: Full=Serum response factor accessory protein 1; DE Short=SAP-1; DE Short=SRF accessory protein 1; GN Name=Elk4; Synonyms=Sap1; 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 [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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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). CC -!- FUNCTION: Involved in both transcriptional activation and repression. CC Interaction with SIRT7 leads to recruitment and stabilization of SIRT7 CC at promoters, followed by deacetylation of histone H3 at 'Lys-18' CC (H3K18Ac) and subsequent transcription repression. Forms a ternary CC complex with the serum response factor (SRF). Requires DNA-bound SRF CC for ternary complex formation and makes extensive DNA contacts to the CC 5'side of SRF, but does not bind DNA autonomously (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with SIRT7. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Lung and liver. CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}. 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; Z36885; CAA85358.1; -; mRNA. DR EMBL; CH466520; EDL39692.1; -; Genomic_DNA. DR EMBL; BC144844; AAI44845.1; -; mRNA. DR EMBL; BC145795; AAI45796.1; -; mRNA. DR CCDS; CCDS35704.1; -. DR PIR; I48755; I48755. DR RefSeq; NP_031949.2; NM_007923.2. DR RefSeq; XP_006529189.1; XM_006529126.3. DR RefSeq; XP_006529190.1; XM_006529127.3. DR RefSeq; XP_006529191.1; XM_006529128.3. DR RefSeq; XP_006529192.1; XM_006529129.3. DR RefSeq; XP_006529193.1; XM_006529130.3. DR AlphaFoldDB; P41158; -. DR SMR; P41158; -. DR BioGRID; 199431; 1. DR STRING; 10090.ENSMUSP00000083743; -. DR iPTMnet; P41158; -. DR PhosphoSitePlus; P41158; -. DR EPD; P41158; -. DR MaxQB; P41158; -. DR PaxDb; 10090-ENSMUSP00000083743; -. DR ProteomicsDB; 275741; -. DR Antibodypedia; 20682; 160 antibodies from 26 providers. DR DNASU; 13714; -. DR Ensembl; ENSMUST00000027696.10; ENSMUSP00000027696.4; ENSMUSG00000026436.16. DR Ensembl; ENSMUST00000086556.12; ENSMUSP00000083743.6; ENSMUSG00000026436.16. DR GeneID; 13714; -. DR KEGG; mmu:13714; -. DR UCSC; uc007cob.1; mouse. DR AGR; MGI:102853; -. DR CTD; 2005; -. DR MGI; MGI:102853; Elk4. DR VEuPathDB; HostDB:ENSMUSG00000026436; -. DR eggNOG; KOG3806; Eukaryota. DR GeneTree; ENSGT00940000158900; -. DR HOGENOM; CLU_036905_1_0_1; -. DR InParanoid; P41158; -. DR OMA; GDPEMPG; -. DR OrthoDB; 4237692at2759; -. DR PhylomeDB; P41158; -. DR TreeFam; TF317732; -. DR BioGRID-ORCS; 13714; 3 hits in 83 CRISPR screens. DR ChiTaRS; Elk4; mouse. DR PRO; PR:P41158; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P41158; Protein. DR Bgee; ENSMUSG00000026436; Expressed in saccule of membranous labyrinth and 256 other cell types or tissues. DR ExpressionAtlas; P41158; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. 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:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; ETS; 1. DR PANTHER; PTHR11849:SF21; ETS DOMAIN-CONTAINING PROTEIN ELK-4; 1. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. DR Genevisible; P41158; MM. PE 2: Evidence at transcript level; KW Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome; KW Repressor; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..430 FT /note="ETS domain-containing protein Elk-4" FT /id="PRO_0000204100" FT DNA_BIND 5..85 FT /note="ETS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237" FT REGION 116..138 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 245..279 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 292..325 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 250..271 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..318 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 166 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P28324" FT CONFLICT 99 FT /note="G -> A (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 206 FT /note="F -> C (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 228 FT /note="S -> F (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 307 FT /note="P -> A (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="L -> S (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 395 FT /note="T -> M (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="F -> L (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 415 FT /note="D -> E (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 419 FT /note="T -> L (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" FT CONFLICT 426 FT /note="D -> R (in Ref. 1; CAA85358)" FT /evidence="ECO:0000305" SQ SEQUENCE 430 AA; 46826 MW; 76CF28AB7627AB5F CRC64; MDSAITLWQF LLQLLQEPQN EHMICWTSNN GEFKLLQAEE VARLWGIRKN KPNMNYDKLS RALRYYYVKN IIKKVNGQKF VYKFVSYPEI LKMDPLTVGR IEGDCEALNS IETSSSKDVE YGGKERPPQP GAKTSSRNDY IHSGLYSSFT LNSLNTSNKK LFKSIKIENP AEKLAEKKAQ EPTPSVIKFV TTPAKKPPIE PVAAAFATSP SLSPSSEETI QALETLVSPT LPSLETPASI SILATTFNPT PPVPSTPLPL KEPPRTPSPP LSSNPDIDTD IESVASQPME LPENLSLEPK NEDSALPEKD KTNNSSRSKK PKGLELTPAL VVTGSDPSPL GILSPSLPTA SLTPALFSQT PILLTPSPLL SSIHFWSTLS PFAPLSPARL QGANTLFQFP SVLNSHGPFT LSGLDGPSTP GPFSPDLQKT //