ELL3_HUMAN
ID ELL3_HUMAN Reviewed; 397 AA.
AC Q9HB65; B3KQ66; B3KX08; Q6I9Z7; Q9H634;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=RNA polymerase II elongation factor ELL3;
GN Name=ELL3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAG13463.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10882741; DOI=10.1074/jbc.m005175200;
RA Miller T., Williams K., Johnstone R.W., Shilatifard A.;
RT "Identification, cloning, expression, and biochemical characterization of
RT the testis-specific RNA polymerase II elongation factor ELL3.";
RL J. Biol. Chem. 275:32052-32056(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Small intestine {ECO:0000312|EMBL:BAB15432.1}, Testis, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung {ECO:0000312|EMBL:AAH19293.1};
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 [7]
RP FUNCTION, IDENTIFICATION IN THE SEC COMPLEX, AND IDENTIFICATION IN THE LEC
RP COMPLEX.
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).
RN [8]
RP REVIEW ON THE SUPER ELONGATION COMPLEX.
RX PubMed=22895430; DOI=10.1038/nrm3417;
RA Luo Z., Lin C., Shilatifard A.;
RT "The super elongation complex (SEC) family in transcriptional control.";
RL Nat. Rev. Mol. Cell Biol. 13:543-547(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 Does not only bind to enhancer regions of active genes, but also marks
CC the enhancers that are in a poised or inactive state in ES cells and is
CC required for establishing proper RNA polymerase II occupancy at
CC developmentally regulated genes in a cohesin-dependent manner. Probably
CC required for priming developmentally regulated genes for later
CC recruitment of the super elongation complex (SEC), for transcriptional
CC activation during differentiation. Required for recruitment of P-TEFb
CC within SEC during differentiation. Probably preloaded on germ cell
CC chromatin, suggesting that it may prime gene activation by marking
CC enhancers as early as in the germ cells. Promoting epithelial-
CC mesenchymal transition (EMT) (By similarity). Elongation factor
CC component of the super elongation complex (SEC), a complex required to
CC increase the catalytic rate of RNA polymerase II transcription by
CC suppressing transient pausing by the polymerase at multiple sites along
CC the DNA. 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:10882741, ECO:0000269|PubMed:22195968}.
CC -!- SUBUNIT: Interacts with AFF4 (By similarity). Component of the super
CC elongation complex (SEC), at least composed of EAF1, EAF2, CDK9,
CC MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or
CC ELL3). Component of the little elongation complex (LEC), at least
CC composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2.
CC {ECO:0000250, ECO:0000269|PubMed:22195968}.
CC -!- INTERACTION:
CC Q9HB65; Q96JC9: EAF1; NbExp=5; IntAct=EBI-715224, EBI-769261;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10882741}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HB65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HB65-2; Sequence=VSP_045937;
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:10882741}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; AF276512; AAG13463.1; -; mRNA.
DR EMBL; AK026290; BAB15432.1; -; mRNA.
DR EMBL; AK057528; BAG51928.1; -; mRNA.
DR EMBL; AK126384; BAG54320.1; -; mRNA.
DR EMBL; CR457358; CAG33639.1; -; mRNA.
DR EMBL; AC018512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77238.1; -; Genomic_DNA.
DR EMBL; BC006548; AAH06548.1; -; mRNA.
DR EMBL; BC019293; AAH19293.1; -; mRNA.
DR CCDS; CCDS10102.1; -. [Q9HB65-1]
DR RefSeq; NP_079441.1; NM_025165.2. [Q9HB65-1]
DR AlphaFoldDB; Q9HB65; -.
DR SMR; Q9HB65; -.
DR BioGRID; 123198; 23.
DR CORUM; Q9HB65; -.
DR IntAct; Q9HB65; 19.
DR STRING; 9606.ENSP00000320346; -.
DR iPTMnet; Q9HB65; -.
DR PhosphoSitePlus; Q9HB65; -.
DR BioMuta; ELL3; -.
DR DMDM; 48428154; -.
DR EPD; Q9HB65; -.
DR jPOST; Q9HB65; -.
DR MassIVE; Q9HB65; -.
DR MaxQB; Q9HB65; -.
DR PaxDb; Q9HB65; -.
DR PeptideAtlas; Q9HB65; -.
DR PRIDE; Q9HB65; -.
DR ProteomicsDB; 81498; -. [Q9HB65-1]
DR Antibodypedia; 24110; 128 antibodies from 21 providers.
DR DNASU; 80237; -.
DR Ensembl; ENST00000319359.8; ENSP00000320346.3; ENSG00000128886.12. [Q9HB65-1]
DR GeneID; 80237; -.
DR KEGG; hsa:80237; -.
DR MANE-Select; ENST00000319359.8; ENSP00000320346.3; NM_025165.3; NP_079441.1.
DR UCSC; uc001zsw.2; human. [Q9HB65-1]
DR CTD; 80237; -.
DR DisGeNET; 80237; -.
DR GeneCards; ELL3; -.
DR HGNC; HGNC:23113; ELL3.
DR HPA; ENSG00000128886; Tissue enhanced (lymphoid tissue, skin).
DR MIM; 609885; gene.
DR neXtProt; NX_Q9HB65; -.
DR PharmGKB; PA128394728; -.
DR VEuPathDB; HostDB:ENSG00000128886; -.
DR eggNOG; KOG4796; Eukaryota.
DR GeneTree; ENSGT00940000161615; -.
DR HOGENOM; CLU_692530_0_0_1; -.
DR InParanoid; Q9HB65; -.
DR OMA; RLHCLGP; -.
DR OrthoDB; 335949at2759; -.
DR PhylomeDB; Q9HB65; -.
DR TreeFam; TF337345; -.
DR PathwayCommons; Q9HB65; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q9HB65; -.
DR BioGRID-ORCS; 80237; 25 hits in 1081 CRISPR screens.
DR GenomeRNAi; 80237; -.
DR Pharos; Q9HB65; Tbio.
DR PRO; PR:Q9HB65; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9HB65; protein.
DR Bgee; ENSG00000128886; Expressed in duodenum and 97 other tissues.
DR ExpressionAtlas; Q9HB65; baseline and differential.
DR Genevisible; Q9HB65; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
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 Alternative splicing; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..397
FT /note="RNA polymerase II elongation factor ELL3"
FT /id="PRO_0000146736"
FT DOMAIN 285..395
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 164..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..56
FT /note="MEELQEPLRGQLRLCFTQAARTSLLLLRLNDAALRALQECQRQQVRPVIAFQ
FT GHRG -> MGLTVSFHPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045937"
FT VARIANT 11
FT /note="Q -> E (in dbSNP:rs2277531)"
FT /id="VAR_018992"
FT VARIANT 140
FT /note="W -> R (in dbSNP:rs35454865)"
FT /id="VAR_053074"
FT CONFLICT 5
FT /note="Q -> H (in Ref. 1; AAG13463)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="S -> P (in Ref. 2; BAG54320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 45361 MW; 9DC16B3D6E184FA7 CRC64;
MEELQEPLRG QLRLCFTQAA RTSLLLLRLN DAALRALQEC QRQQVRPVIA FQGHRGYLRL
PGPGWSCLFS FIVSQCCQEG AGGSLDLVCQ RFLRSGPNSL HCLGSLRERL IIWAAMDSIP
APSSVQGHNL TEDARHPESW QNTGGYSEGD AVSQPQMALE EVSVSDPLAS NQGQSLPGSS
REHMAQWEVR SQTHVPNREP VQALPSSASR KRLDKKRSVP VATVELEEKR FRTLPLVPSP
LQGLTNQDLQ EGEDWEQEDE DMDPRLEHSS SVQEDSESPS PEDIPDYLLQ YRAIHSAEQQ
HAYEQDFETD YAEYRILHAR VGTASQRFIE LGAEIKRVRR GTPEYKVLED KIIQEYKKFR
KQYPSYREEK RRCEYLHQKL SHIKGLILEF EEKNRGS
