ID EAF2_HUMAN Reviewed; 260 AA. AC Q96CJ1; Q9NZ82; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 06-JUL-2016, entry version 115. DE RecName: Full=ELL-associated factor 2; DE AltName: Full=Testosterone-regulated apoptosis inducer and tumor suppressor protein; GN Name=EAF2; Synonyms=TRAITS; ORFNames=BM-040; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ELL RP AND ELL2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Bone marrow; RX PubMed=12446457; DOI=10.1182/blood-2002-06-1664; RA Simone F., Luo R.T., Polak P.E., Kaberlein J.J., Thirman M.J.; RT "ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with RT alternative ELL binding properties."; RL Blood 101:2355-2362(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN APOPTOSIS, RP INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12907652; RA Xiao W., Zhang Q., Jiang F., Pins M., Kozlowski J.M., Wang Z.; RT "Suppression of prostate tumor growth by U19, a novel testosterone- RT regulated apoptosis inducer."; RL Cancer Res. 63:4698-4704(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-cell; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION. RX PubMed=16006523; DOI=10.1073/pnas.0503017102; RA Kong S.E., Banks C.A., Shilatifard A., Conaway J.W., Conaway R.C.; RT "ELL-associated factors 1 and 2 are positive regulators of RNA RT polymerase II elongation factor ELL."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10094-10098(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-154, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] RP IDENTIFICATION IN THE SEC 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., RA Washburn M.P., Eissenberg J.C., Shilatifard A.; RT "The little elongation complex regulates small nuclear RNA RT transcription."; RL Mol. Cell 44:954-965(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-154, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Acts as a transcriptional transactivator of TCEA1 CC elongation activity (By similarity). Acts as a transcriptional CC transactivator of ELL and ELL2 elongation activities. Potent CC inducer of apoptosis in prostatic and non-prostatic cell lines. CC Inhibits prostate tumor growth in vivo. {ECO:0000250, CC ECO:0000269|PubMed:12446457, ECO:0000269|PubMed:12907652, CC ECO:0000269|PubMed:16006523}. CC -!- SUBUNIT: Isoform 1 and isoform 2 interact with TCEA1 (By CC similarity). Component of the super elongation complex (SEC), at CC least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), CC the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL CC and ELL2. {ECO:0000250, ECO:0000269|PubMed:12446457, CC ECO:0000269|PubMed:22195968}. CC -!- INTERACTION: CC Q8N7W2-2:BEND7; NbExp=3; IntAct=EBI-1245604, EBI-10181188; CC Q13490:BIRC2; NbExp=3; IntAct=EBI-1245604, EBI-514538; CC Q16665:HIF1A; NbExp=3; IntAct=EBI-1245604, EBI-447269; CC P0C1Z6:TFPT; NbExp=4; IntAct=EBI-1245604, EBI-1245626; CC P36406:TRIM23; NbExp=3; IntAct=EBI-1245604, EBI-740098; CC -!- SUBCELLULAR LOCATION: Nucleus speckle CC {ECO:0000269|PubMed:12446457, ECO:0000269|PubMed:12907652}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96CJ1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96CJ1-2; Sequence=VSP_015310; CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, CC skeletal muscle, kidney, pancreas, spleen, prostate, testis, small CC intestine, colon, adrenal, bone marrow, lymph node, spinal gland, CC stomach, thyroid, trachea, thymus, liver and leukocytes. CC {ECO:0000269|PubMed:12446457, ECO:0000269|PubMed:12907652}. CC -!- INDUCTION: By androgen. {ECO:0000269|PubMed:12907652}. CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF517829; AAO63811.1; -; mRNA. DR EMBL; AY049020; AAL12223.1; -; mRNA. DR EMBL; AF217516; AAF67627.1; -; mRNA. DR EMBL; BC014209; AAH14209.1; -; mRNA. DR CCDS; CCDS3006.1; -. [Q96CJ1-1] DR RefSeq; NP_001306970.1; NM_001320041.1. [Q96CJ1-2] DR RefSeq; NP_060926.2; NM_018456.5. [Q96CJ1-1] DR RefSeq; XP_011511288.1; XM_011512986.1. [Q96CJ1-2] DR UniGene; Hs.477325; -. DR ProteinModelPortal; Q96CJ1; -. DR BioGrid; 120943; 16. DR IntAct; Q96CJ1; 11. DR STRING; 9606.ENSP00000273668; -. DR iPTMnet; Q96CJ1; -. DR PhosphoSite; Q96CJ1; -. DR BioMuta; EAF2; -. DR DMDM; 73919269; -. DR EPD; Q96CJ1; -. DR MaxQB; Q96CJ1; -. DR PaxDb; Q96CJ1; -. DR PeptideAtlas; Q96CJ1; -. DR PRIDE; Q96CJ1; -. DR DNASU; 55840; -. DR Ensembl; ENST00000273668; ENSP00000273668; ENSG00000145088. [Q96CJ1-1] DR GeneID; 55840; -. DR KEGG; hsa:55840; -. DR UCSC; uc003een.4; human. [Q96CJ1-1] DR CTD; 55840; -. DR GeneCards; EAF2; -. DR HGNC; HGNC:23115; EAF2. DR HPA; HPA008411; -. DR MIM; 607659; gene. DR neXtProt; NX_Q96CJ1; -. DR PharmGKB; PA128394690; -. DR eggNOG; KOG4795; Eukaryota. DR eggNOG; ENOG4111KQJ; LUCA. DR GeneTree; ENSGT00390000017724; -. DR HOGENOM; HOG000070137; -. DR HOVERGEN; HBG054898; -. DR InParanoid; Q96CJ1; -. DR KO; K15186; -. DR PhylomeDB; Q96CJ1; -. DR TreeFam; TF320864; -. DR SIGNOR; Q96CJ1; -. DR GeneWiki; EAF2; -. DR GenomeRNAi; 55840; -. DR PRO; PR:Q96CJ1; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; Q96CJ1; -. DR CleanEx; HS_EAF2; -. DR ExpressionAtlas; Q96CJ1; baseline and differential. DR Genevisible; Q96CJ1; HS. DR GO; GO:0032783; C:ELL-EAF complex; IEA:InterPro. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl. DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB. DR InterPro; IPR027093; EAF_fam. DR InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N. DR PANTHER; PTHR15970; PTHR15970; 1. DR Pfam; PF09816; EAF; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Apoptosis; Complete proteome; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 260 ELL-associated factor 2. FT /FTId=PRO_0000130337. FT REGION 17 104 Necessary for interaction with ELL. FT REGION 177 260 Necessary for transactivation activity. FT REGION 246 260 Necessary for interaction with TCEA1 and FT transactivation activity. {ECO:0000250}. FT COMPBIAS 126 130 Poly-Gln. FT COMPBIAS 174 207 Ser-rich. FT MOD_RES 146 146 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 151 151 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 154 154 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:23186163}. FT VAR_SEQ 1 130 Missing (in isoform 2). FT {ECO:0000303|PubMed:11042152}. FT /FTId=VSP_015310. SQ SEQUENCE 260 AA; 28792 MW; 2CDCE96FA387C799 CRC64; MNSAAGFSHL DRRERVLKLG ESFEKQPRCA FHTVRYDFKP ASIDTSSEGY LEVGEGEQVT ITLPNIEGST PPVTVFKGSK KPYLKECILI INHDTGECRL EKLSSNITVK KTRVEGSSKI QYRKEQQQQQ MWNSARTPNL VKHSPSEDKM SPASPIDDIE RELKAEASLM DQMSSCDSSS DSKSSSSSSS EDSSSDSEDE DCKSSTSDTG NCVSGHPTMT QYRIPDIDAS HNRFRDNSGL LMNTLRNDLQ LSESGSDSDD //