ELK4_MOUSE
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 03-AUG-2022, entry version 153.
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}.
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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; P41158; -.
DR PRIDE; P41158; -.
DR ProteomicsDB; 275741; -.
DR Antibodypedia; 20682; 144 antibodies from 25 providers.
DR DNASU; 13714; -.
DR Ensembl; ENSMUST00000027696; ENSMUSP00000027696; ENSMUSG00000026436.
DR Ensembl; ENSMUST00000086556; ENSMUSP00000083743; ENSMUSG00000026436.
DR GeneID; 13714; -.
DR KEGG; mmu:13714; -.
DR UCSC; uc007cob.1; mouse.
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; NCGKEKS; -.
DR OrthoDB; 981551at2759; -.
DR PhylomeDB; P41158; -.
DR TreeFam; TF317732; -.
DR BioGRID-ORCS; 13714; 2 hits in 78 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 253 other tissues.
DR ExpressionAtlas; P41158; baseline and differential.
DR Genevisible; P41158; MM.
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:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
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; -; 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; 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
