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ELL3_MOUSE
ID   ELL3_MOUSE              Reviewed;         395 AA.
AC   Q80VR2; A2ARQ1;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=RNA polymerase II elongation factor ELL3;
GN   Name=Ell3;
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 {ECO:0000312|EMBL:AAH45151.1};
RN   [1]
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   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAH45151.1};
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   [3]
RP   INTERACTION WITH AFF4.
RX   PubMed=20159561; DOI=10.1016/j.molcel.2010.01.026;
RA   Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L.,
RA   Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.;
RT   "AFF4, a component of the ELL/P-TEFb elongation complex and a shared
RT   subunit of MLL chimeras, can link transcription elongation to leukemia.";
RL   Mol. Cell 37:429-437(2010).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22768269; DOI=10.1371/journal.pone.0040293;
RA   Ahn H.J., Cha Y., Moon S.H., Jung J.E., Park K.S.;
RT   "Ell3 enhances differentiation of mouse embryonic stem cells by regulating
RT   epithelial-mesenchymal transition and apoptosis.";
RL   PLoS ONE 7:E40293-E40293(2012).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AFF4.
RX   PubMed=23273992; DOI=10.1016/j.cell.2012.12.015;
RA   Lin C., Garruss A.S., Luo Z., Guo F., Shilatifard A.;
RT   "The RNA Pol II elongation factor Ell3 marks enhancers in ES cells and
RT   primes future gene activation.";
RL   Cell 152:144-156(2013).
CC   -!- FUNCTION: Enhancer-binding elongation factor that specifically binds
CC       enhancers in embryonic stem cells (ES cells), marks them, and is
CC       required for their future activation during stem cell specification.
CC       Elongation factor component of the super elongation complex (SEC), a
CC       complex required to increase the catalytic rate of RNA polymerase II
CC       transcription by suppressing transient pausing by the polymerase at
CC       multiple sites along the DNA. Component of the little elongation
CC       complex (LEC), a complex required to regulate small nuclear RNA (snRNA)
CC       gene transcription by RNA polymerase II and III. Does not only bind to
CC       enhancer regions of active genes, but also marks the enhancers that are
CC       in a poised or inactive state in ES cells and is required for
CC       establishing proper RNA polymerase II occupancy at developmentally
CC       regulated genes in a cohesin-dependent manner. Probably required for
CC       priming developmentally regulated genes for later recruitment of the
CC       super elongation complex (SEC), for transcriptional activation during
CC       differentiation. Required for recruitment of P-TEFb within SEC during
CC       differentiation. Probably preloaded on germ cell chromatin, suggesting
CC       that it may prime gene activation by marking enhancers as early as in
CC       the germ cells. Promoting epithelial-mesenchymal transition (EMT).
CC       {ECO:0000269|PubMed:22768269, ECO:0000269|PubMed:23273992}.
CC   -!- SUBUNIT: Component of the little elongation complex (LEC), at least
CC       composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2 (By
CC       similarity). Component of the super elongation complex (SEC), at least
CC       composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb
CC       complex and ELL (ELL, ELL2 or ELL3). Interacts with AFF4. {ECO:0000250,
CC       ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:23273992}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23273992}.
CC   -!- TISSUE SPECIFICITY: Actively expressed in embryonic stem cells (ES
CC       cells), while it is weakly expressed in differentiated cells.
CC       {ECO:0000269|PubMed:22768269}.
CC   -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR   EMBL; AL845466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC045151; AAH45151.1; -; mRNA.
DR   CCDS; CCDS16644.1; -.
DR   RefSeq; NP_666085.2; NM_145973.2.
DR   AlphaFoldDB; Q80VR2; -.
DR   SMR; Q80VR2; -.
DR   BioGRID; 234639; 2.
DR   STRING; 10090.ENSMUSP00000028679; -.
DR   PhosphoSitePlus; Q80VR2; -.
DR   MaxQB; Q80VR2; -.
DR   PaxDb; Q80VR2; -.
DR   PeptideAtlas; Q80VR2; -.
DR   PRIDE; Q80VR2; -.
DR   ProteomicsDB; 277782; -.
DR   Antibodypedia; 24110; 128 antibodies from 21 providers.
DR   DNASU; 269344; -.
DR   Ensembl; ENSMUST00000028679; ENSMUSP00000028679; ENSMUSG00000027246.
DR   Ensembl; ENSMUST00000116432; ENSMUSP00000112133; ENSMUSG00000027246.
DR   GeneID; 269344; -.
DR   KEGG; mmu:269344; -.
DR   UCSC; uc008lzc.1; mouse.
DR   CTD; 80237; -.
DR   MGI; MGI:2673679; Ell3.
DR   VEuPathDB; HostDB:ENSMUSG00000027246; -.
DR   eggNOG; KOG4796; Eukaryota.
DR   GeneTree; ENSGT00940000161615; -.
DR   HOGENOM; CLU_692530_0_0_1; -.
DR   InParanoid; Q80VR2; -.
DR   OMA; RLHCLGP; -.
DR   OrthoDB; 335949at2759; -.
DR   PhylomeDB; Q80VR2; -.
DR   TreeFam; TF337345; -.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   BioGRID-ORCS; 269344; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Ell3; mouse.
DR   PRO; PR:Q80VR2; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q80VR2; protein.
DR   Bgee; ENSMUSG00000027246; Expressed in spleen and 63 other tissues.
DR   Genevisible; Q80VR2; MM.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0006354; P:DNA-templated transcription, elongation; ISO:MGI.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
DR   GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
DR   GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IDA:MGI.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IDA:MGI.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISO:MGI.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IDA:MGI.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IDA:MGI.
DR   GO; GO:2000648; P:positive regulation of stem cell proliferation; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:0072331; P:signal transduction by p53 class mediator; IDA:MGI.
DR   GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR   GO; GO:0072089; P:stem cell proliferation; IDA:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR   InterPro; IPR031176; ELL/occludin.
DR   InterPro; IPR031175; ELL3.
DR   InterPro; IPR019464; ELL_N.
DR   InterPro; IPR010844; Occludin_ELL.
DR   PANTHER; PTHR23288; PTHR23288; 1.
DR   PANTHER; PTHR23288:SF18; PTHR23288:SF18; 1.
DR   Pfam; PF10390; ELL; 1.
DR   Pfam; PF07303; Occludin_ELL; 1.
DR   PROSITE; PS51980; OCEL; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..395
FT                   /note="RNA polymerase II elongation factor ELL3"
FT                   /id="PRO_0000146737"
FT   DOMAIN          283..393
FT                   /note="OCEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT   REGION          129..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..261
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XFX8"
SQ   SEQUENCE   395 AA;  44762 MW;  9297E95C5AD222EA CRC64;
     MEGTQEALSG KMRLLFTPAA RTSLLMLRLN EAALRALQEC QQQQVRPVIA FQGHRGYLRF
     PGPGWSCLFS FIVSQCGQEG TNGGLDLVYQ RLGRSGPNCL HCLGSLRERL TIWAAMDTIP
     APLLAQEHLT EGTRESESWQ DTGDEPEGHP QLAPDEVSDP LASHHEQSLP GSSSEPMAQW
     EMRNHTYLPS REPDQSLLSP ASQKRLDKKR SAPITTEEPE EKRLRALPLA SSPLQGLANQ
     DSQEGEDWGQ DEDEEGDEDG DSRLEQSLSA PSASESPSPE EVPDYLLQYR AIHSTEQQQA
     YEQDFETDYA EYRILHARVG AASQRFTELG AEIKRLQRGT PEHKVLEDKI VQEYKKFRKR
     YPSYREEKHR CEYLHQKLSH IKGLILEFEE KNRGS
 
 
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