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   24-JAN-2024, entry version 150.
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   SwissPalm; O08856; -.
DR   EPD; O08856; -.
DR   jPOST; O08856; -.
DR   MaxQB; O08856; -.
DR   PaxDb; 10090-ENSMUSP00000091163; -.
DR   PeptideAtlas; O08856; -.
DR   ProteomicsDB; 275526; -.
DR   Pumba; O08856; -.
DR   Antibodypedia; 15081; 468 antibodies from 33 providers.
DR   DNASU; 13716; -.
DR   Ensembl; ENSMUST00000093454.8; ENSMUSP00000091163.7; ENSMUSG00000070002.8.
DR   GeneID; 13716; -.
DR   KEGG; mmu:13716; -.
DR   UCSC; uc009mau.1; mouse.
DR   AGR; MGI:109377; -.
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; CQPQNSG; -.
DR   OrthoDB; 2910197at2759; -.
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 82 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 203 other cell types or tissues.
DR   ExpressionAtlas; O08856; baseline and differential.
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 by RNA polymerase II; 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 by RNA polymerase II; IEA:InterPro.
DR   Gene3D; 6.10.140.340; -; 1.
DR   Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR   InterPro; IPR042065; E3_ELL-like.
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; OCCLUDIN AND RNA POLYMERASE II ELONGATION FACTOR ELL; 1.
DR   PANTHER; PTHR23288:SF9; RNA POLYMERASE II ELONGATION FACTOR ELL; 1.
DR   Pfam; PF10390; ELL; 1.
DR   Pfam; PF07303; Occludin_ELL; 1.
DR   SUPFAM; SSF144292; occludin/ELL-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51980; OCEL; 1.
DR   Genevisible; O08856; MM.
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;
FT                   AAH14816/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
//