ELL3_RAT
ID ELL3_RAT Reviewed; 387 AA.
AC Q5XFX8;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=RNA polymerase II elongation factor ELL3;
GN Name=Ell3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AFF4. Component of the super elongation complex
CC (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or
CC AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Component of the
CC little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or
CC ELL3), ZC3H8, ICE1 and ICE2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; AC097745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC084693; AAH84693.1; -; mRNA.
DR RefSeq; NP_001011957.1; NM_001011957.1.
DR AlphaFoldDB; Q5XFX8; -.
DR SMR; Q5XFX8; -.
DR STRING; 10116.ENSRNOP00000031619; -.
DR iPTMnet; Q5XFX8; -.
DR PhosphoSitePlus; Q5XFX8; -.
DR PaxDb; Q5XFX8; -.
DR PRIDE; Q5XFX8; -.
DR GeneID; 296102; -.
DR KEGG; rno:296102; -.
DR UCSC; RGD:1309917; rat.
DR CTD; 80237; -.
DR RGD; 1309917; Ell3.
DR VEuPathDB; HostDB:ENSRNOG00000022868; -.
DR eggNOG; KOG4796; Eukaryota.
DR HOGENOM; CLU_692530_0_0_1; -.
DR InParanoid; Q5XFX8; -.
DR OMA; RLHCLGP; -.
DR OrthoDB; 335949at2759; -.
DR PhylomeDB; Q5XFX8; -.
DR TreeFam; TF337345; -.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:Q5XFX8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000022868; Expressed in spleen and 19 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; ISO:RGD.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; ISO:RGD.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISO:RGD.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS: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; ISS:UniProtKB.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:RGD.
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..387
FT /note="RNA polymerase II elongation factor ELL3"
FT /id="PRO_0000421767"
FT DOMAIN 275..385
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 127..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 387 AA; 43803 MW; 9A2BCF8A71DA4920 CRC64;
MEGTQEALSG KMRLLFTPAA RTSLLMLRLN EAALRALQEC QQQQVRPVIA FQGQRGYLRL
PGPGWSCLFS FIVSQCGQEG GGLDLVYQRL GRSGPNCLHC LGSLRERLTI WAAMDTIPAP
LLAQEHLTEG TRESESWQDS EDEPEGHPQM ALQEVSDPLA SNHEQSLPGS SSEPMAQWEV
RNHTYLSNRE PDQPLPSSAS QKRLDKKRSA PITTEEPEEK RPRALPLASS PLQGLSNQDS
PEEQDWGQDA DGDSRLEQSL SVQSASESPS PEEVPDYLLQ YSTIHSAEQQ QAYEQDFETD
YAEYRILHAR VGAASQRFTE LGAEIKRLQR GTPEHKVLED KIVQEYKKFR KRYPSYSEEK
RRCEYLHEKL SHIKGLILEF EEKNRGS
