ELL2_MOUSE
ID ELL2_MOUSE Reviewed; 639 AA.
AC Q3UKU1; E9QPE1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=RNA polymerase II elongation factor ELL2;
GN Name=Ell2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 [2]
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 [3]
RP FUNCTION.
RX PubMed=19749764; DOI=10.1038/ni.1786;
RA Martincic K., Alkan S.A., Cheatle A., Borghesi L., Milcarek C.;
RT "Transcription elongation factor ELL2 directs immunoglobulin secretion in
RT plasma cells by stimulating altered RNA processing.";
RL Nat. Immunol. 10:1102-1109(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=21832080; DOI=10.1074/jbc.m111.272096;
RA Milcarek C., Albring M., Langer C., Park K.S.;
RT "The eleven-nineteen lysine-rich leukemia gene (ELL2) influences the
RT histone H3 protein modifications accompanying the shift to secretory
RT immunoglobulin heavy chain mRNA production.";
RL J. Biol. Chem. 286:33795-33803(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. Component of the little
CC elongation complex (LEC), a complex required to regulate small nuclear
CC RNA (snRNA) gene transcription by RNA polymerase II and III (By
CC similarity). Plays a role in immunoglobulin secretion in plasma cells:
CC directs efficient alternative mRNA processing, influencing both
CC proximal poly(A) site choice and exon skipping, as well as
CC immunoglobulin heavy chain (IgH) alternative processing. Probably acts
CC by regulating histone modifications accompanying transition from
CC membrane-specific to secretory IgH mRNA expression. {ECO:0000250,
CC ECO:0000269|PubMed:19749764, ECO:0000269|PubMed:21832080}.
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 AFF4; the interaction is direct and leads
CC to stabilize ELL2 and prevent ELL2 ubiquitination. Interacts with EAF1
CC and EAF2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Ubiquitinated by SIAH1, leading to its degradation by the
CC proteasome. Interaction with AFF4 stabilizes ELL2 and prevents ELL2
CC ubiquitination (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; AK145868; BAE26710.1; -; mRNA.
DR EMBL; CT025556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36734.1; -.
DR RefSeq; NP_620403.2; NM_138953.2.
DR AlphaFoldDB; Q3UKU1; -.
DR SMR; Q3UKU1; -.
DR IntAct; Q3UKU1; 1.
DR STRING; 10090.ENSMUSP00000001583; -.
DR iPTMnet; Q3UKU1; -.
DR PhosphoSitePlus; Q3UKU1; -.
DR PaxDb; Q3UKU1; -.
DR PRIDE; Q3UKU1; -.
DR ProteomicsDB; 275525; -.
DR Antibodypedia; 13079; 183 antibodies from 30 providers.
DR DNASU; 192657; -.
DR Ensembl; ENSMUST00000001583; ENSMUSP00000001583; ENSMUSG00000001542.
DR GeneID; 192657; -.
DR KEGG; mmu:192657; -.
DR UCSC; uc007rfu.1; mouse.
DR CTD; 22936; -.
DR MGI; MGI:2183438; Ell2.
DR VEuPathDB; HostDB:ENSMUSG00000001542; -.
DR eggNOG; KOG4796; Eukaryota.
DR GeneTree; ENSGT00940000154828; -.
DR HOGENOM; CLU_021268_0_0_1; -.
DR InParanoid; Q3UKU1; -.
DR OMA; SCGRVTQ; -.
DR OrthoDB; 335949at2759; -.
DR PhylomeDB; Q3UKU1; -.
DR TreeFam; TF326161; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 192657; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ell2; mouse.
DR PRO; PR:Q3UKU1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UKU1; protein.
DR Bgee; ENSMUSG00000001542; Expressed in seminal vesicle and 257 other tissues.
DR ExpressionAtlas; Q3UKU1; baseline and differential.
DR Genevisible; Q3UKU1; MM.
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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR Gene3D; 1.10.10.2670; -; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR031179; ELL2.
DR InterPro; IPR019464; ELL_N.
DR InterPro; IPR010844; Occludin_ELL.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23288; PTHR23288; 2.
DR PANTHER; PTHR23288:SF36; PTHR23288:SF36; 2.
DR Pfam; PF10390; ELL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..639
FT /note="RNA polymerase II elongation factor ELL2"
FT /id="PRO_0000322974"
FT DOMAIN 525..635
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 175..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00472"
FT CONFLICT 286
FT /note="V -> E (in Ref. 1; BAE26710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 72125 MW; D97846C943AC12FB CRC64;
MAAGGAAGLR EEQRYGLACG RLGQDNITVL HVKLTETAIR ALETYQSHKN LIPFRPSIQF
QGLQGLMKIP KNDPFNEVQN FNFYLSNVGR DNPQGSFDCI QQTLSSSGAS QLNCLGFIQD
KITVCATNDS YQMTRERMTQ AEEESRNRST KVIKPGGPYV GKRVQIRKAP QAISDTVPER
KRSTPMNPAN TIRKMHSGNS VSQRPYRDRV IHLLALKAYK KPELLARLQK DGVNQKDKNS
LGAILQQVAN LNPKDLSYTL KDYVFKELQR DWPGYSETDR QTLDLVLSRK LNPSQNASTS
RSESPLCSSK DAASSPQKRP LDSDFIDPLM NKKARISHLT NRVPPTLNGY LNPTSEKSCA
GLLPPPAAAA IPTLSPLPST HLPVSNPPQT VNSNSNSPST PEGLGTQDLP VDSFSQNGSI
FEDQQEKYTS RTCLETLPPS SALLKCPKPM EEEHPVSHKK SKKKSKKHKE KDQIKKLDIE
TMEEKEEDLQ REETAKLSNA SPNPNEGVKE GCTASMEPSS ALELPDYLIK YIAIVSYEQR
QNYKDDFNAE YDEYRALHAR METVARRFIK LDAQRKRLSP GSKEYQNVHE EVLQEYQKIK
QSSPNYHEEK YRCEYLHNKL AHIKRLIGEF DQQQAESWH
