ELL_MOUSE
ID ELL_MOUSE Reviewed; 602 AA.
AC O08856; Q3TXY9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=RNA polymerase II elongation factor ELL;
DE AltName: Full=Eleven-nineteen lysine-rich leukemia protein;
GN Name=Ell;
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].
RX PubMed=9037066; DOI=10.1073/pnas.94.4.1408;
RA Thirman M.J., Diskin E.B., Bin S.S., Ip H.S., Miller J.M., Simon M.C.;
RT "Developmental analysis and subcellular localization of the murine
RT homologue of ELL.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1408-1413(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
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 [5]
RP FUNCTION.
RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA Eissenberg J.C., Shilatifard A.;
RT "The little elongation complex regulates small nuclear RNA transcription.";
RL Mol. Cell 44:954-965(2011).
CC -!- FUNCTION: Elongation factor component of the super elongation complex
CC (SEC), a complex required to increase the catalytic rate of RNA
CC polymerase II transcription by suppressing transient pausing by the
CC polymerase at multiple sites along the DNA. Specifically required for
CC stimulating the elongation step of RNA polymerase II- and III-dependent
CC snRNA gene transcription. ELL also plays an early role before its
CC assembly into in the SEC complex by stabilizing RNA polymerase II
CC recruitment/initiation and entry into the pause site. Required to
CC stabilize the pre-initiation complex and early elongation. Specifically
CC required for stimulating the elongation step of RNA polymerase II- and
CC III-dependent snRNA gene transcription (By similarity). Elongation
CC factor component of the little elongation complex (LEC), a complex
CC required to regulate small nuclear RNA (snRNA) gene transcription by
CC RNA polymerase II and III (PubMed:22195968). {ECO:0000250,
CC ECO:0000269|PubMed:22195968}.
CC -!- SUBUNIT: 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). Component of the little elongation
CC complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8,
CC ICE1 and ICE2. Interacts with ICE1 (via N-terminus domain). Interacts
CC with ICE2. Interacts with AFF4; the interaction is direct. Interacts
CC with EAF1 and EAF2 (By similarity). Interacts with USPL1 (By
CC similarity). {ECO:0000250|UniProtKB:P55199}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55199}. Nucleus
CC speckle {ECO:0000250|UniProtKB:P55199}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:P55199}. Note=Colocalizes with EAF2 to nuclear
CC speckles. Colocalizes with coilin in subnuclear cajal and histone locus
CC bodies. Translocates in the LEC complex to cajal and histone locus
CC bodies at snRNA genes in a ICE1-dependent manner. Associates to
CC transcriptionally active chromatin at snRNA genes (By similarity).
CC {ECO:0000250|UniProtKB:P55199}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; U80227; AAC53150.1; -; mRNA.
DR EMBL; AK159027; BAE34775.1; -; mRNA.
DR EMBL; CH466569; EDL28843.1; -; Genomic_DNA.
DR EMBL; BC014816; AAH14816.1; -; mRNA.
DR EMBL; BC024894; AAH24894.1; -; mRNA.
DR CCDS; CCDS22372.1; -.
DR RefSeq; NP_031950.2; NM_007924.2.
DR AlphaFoldDB; O08856; -.
DR SMR; O08856; -.
DR BioGRID; 199432; 5.
DR IntAct; O08856; 6.
DR MINT; O08856; -.
DR STRING; 10090.ENSMUSP00000091163; -.
DR iPTMnet; O08856; -.
DR PhosphoSitePlus; O08856; -.
DR EPD; O08856; -.
DR jPOST; O08856; -.
DR MaxQB; O08856; -.
DR PaxDb; O08856; -.
DR PeptideAtlas; O08856; -.
DR PRIDE; O08856; -.
DR ProteomicsDB; 275526; -.
DR Antibodypedia; 15081; 399 antibodies from 33 providers.
DR DNASU; 13716; -.
DR Ensembl; ENSMUST00000093454; ENSMUSP00000091163; ENSMUSG00000070002.
DR GeneID; 13716; -.
DR KEGG; mmu:13716; -.
DR UCSC; uc009mau.1; mouse.
DR CTD; 8178; -.
DR MGI; MGI:109377; Ell.
DR VEuPathDB; HostDB:ENSMUSG00000070002; -.
DR eggNOG; KOG4796; Eukaryota.
DR GeneTree; ENSGT00940000155914; -.
DR HOGENOM; CLU_021268_0_0_1; -.
DR InParanoid; O08856; -.
DR OMA; THNGRDC; -.
DR OrthoDB; 335949at2759; -.
DR PhylomeDB; O08856; -.
DR TreeFam; TF326161; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 13716; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Ell; mouse.
DR PRO; PR:O08856; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O08856; protein.
DR Bgee; ENSMUSG00000070002; Expressed in ileal epithelium and 199 other tissues.
DR ExpressionAtlas; O08856; baseline and differential.
DR Genevisible; O08856; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0035363; C:histone locus body; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR Gene3D; 1.10.10.2670; -; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR031184; ELL.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR019464; ELL_N.
DR InterPro; IPR010844; Occludin_ELL.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23288; PTHR23288; 1.
DR PANTHER; PTHR23288:SF9; PTHR23288:SF9; 1.
DR Pfam; PF10390; ELL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55199"
FT CHAIN 2..602
FT /note="RNA polymerase II elongation factor ELL"
FT /id="PRO_0000146734"
FT DOMAIN 488..598
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 292..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P55199"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55199"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55199"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55199"
FT CONFLICT 103
FT /note="Y -> H (in Ref. 1; AAC53150 and 4; AAH14816/
FT AAH24894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 67146 MW; DECAD56CF19ABF4B CRC64;
MAALKEARSY GLSCGRVSDG SRVSVFHVKL TDSALKAFES YRAHQDSVSL RPSIRFEGSQ
GHISIPQPDC PEEVRAFSFY LSNIGRDSPQ GSFDCIQQYV SSYGDVHLDC LGSIQDKVTV
CATDDSYQKA RQSMAQAEEE TRSRSAIVIK AGGRYMGKKV QFRKPAPGAA DAVPSRKRAT
PINLASAIRK SSGSGASSVV QRPFRDRVLH LLALRPYRKA ELLLRLQKDG LTQADKDTLD
SLLQQVASVN PKDGTCTLQD CMYKSLQKDW PGYSEGDRQL LKRMLMRKLC QPQNATTDSS
PPREHGRSAS PSQKRPTDFI DPLASKKPRI SHFTQRAQPT LNGKLGAPNG HETLLPAPGP
TPSDTLSSSH LPPRLEPPRT HDPLADVSND LGHSTQDYKH QEATPAPAPH LGLPLLTDFP
QAEQPTSSSH THSRPKKKSK KHKDKERPPE ERPPAPQPDA PTAPALPPDA PGLNGACDNE
PTSSSETPDY LLKYPAISSS EQRQSYKNDF NAEYSEYRSL HARIEQITRR FTQLDAQLRQ
LSQGSDEYET TRGQILQEYR KIKKTNTNYS CEKRRCEYLH RKLAHIKRLI AEYDQRQLQA
WP
