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 24-JAN-2024, entry version 157. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ELL AND RP 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, INDUCTION, RP 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 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT 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 project: RT 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 polymerase RT 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 BY RP 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., 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 [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 elongation CC activity (By similarity). Acts as a transcriptional transactivator of CC ELL and ELL2 elongation activities. Potent inducer of apoptosis in CC prostatic and non-prostatic cell lines. Inhibits prostate tumor growth CC in vivo. {ECO:0000250, ECO:0000269|PubMed:12446457, CC ECO:0000269|PubMed:12907652, ECO:0000269|PubMed:16006523}. CC -!- SUBUNIT: Isoform 1 and isoform 2 interact with TCEA1 (By similarity). CC Component of the super elongation complex (SEC), at least composed of CC EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and CC ELL (ELL, ELL2 or ELL3). Interacts with ELL and ELL2. {ECO:0000250, CC ECO:0000269|PubMed:12446457, ECO:0000269|PubMed:22195968}. CC -!- INTERACTION: CC Q96CJ1; Q8N7W2-2: BEND7; NbExp=5; IntAct=EBI-1245604, EBI-10181188; CC Q96CJ1; Q13490: BIRC2; NbExp=3; IntAct=EBI-1245604, EBI-514538; CC Q96CJ1; Q16665: HIF1A; NbExp=3; IntAct=EBI-1245604, EBI-447269; CC Q96CJ1; P61289: PSME3; NbExp=3; IntAct=EBI-1245604, EBI-355546; CC Q96CJ1; Q15560: TCEA2; NbExp=3; IntAct=EBI-1245604, EBI-710310; CC Q96CJ1; P0C1Z6: TFPT; NbExp=4; IntAct=EBI-1245604, EBI-1245626; CC Q96CJ1; P36406: TRIM23; NbExp=3; IntAct=EBI-1245604, EBI-740098; CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12446457, CC 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, skeletal CC muscle, kidney, pancreas, spleen, prostate, testis, small intestine, CC colon, adrenal, bone marrow, lymph node, spinal gland, stomach, CC 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_016862350.1; XM_017006861.1. [Q96CJ1-2] DR RefSeq; XP_016862351.1; XM_017006862.1. DR AlphaFoldDB; Q96CJ1; -. DR SMR; Q96CJ1; -. DR BioGRID; 120943; 37. DR CORUM; Q96CJ1; -. DR IntAct; Q96CJ1; 26. DR MINT; Q96CJ1; -. DR STRING; 9606.ENSP00000273668; -. DR iPTMnet; Q96CJ1; -. DR PhosphoSitePlus; Q96CJ1; -. DR BioMuta; EAF2; -. DR DMDM; 73919269; -. DR jPOST; Q96CJ1; -. DR MassIVE; Q96CJ1; -. DR MaxQB; Q96CJ1; -. DR PaxDb; 9606-ENSP00000273668; -. DR PeptideAtlas; Q96CJ1; -. DR ProteomicsDB; 76189; -. [Q96CJ1-1] DR ProteomicsDB; 76190; -. [Q96CJ1-2] DR Antibodypedia; 1994; 205 antibodies from 31 providers. DR DNASU; 55840; -. DR Ensembl; ENST00000273668.7; ENSP00000273668.2; ENSG00000145088.9. [Q96CJ1-1] DR GeneID; 55840; -. DR KEGG; hsa:55840; -. DR MANE-Select; ENST00000273668.7; ENSP00000273668.2; NM_018456.6; NP_060926.2. DR UCSC; uc003een.4; human. [Q96CJ1-1] DR AGR; HGNC:23115; -. DR CTD; 55840; -. DR DisGeNET; 55840; -. DR GeneCards; EAF2; -. DR HGNC; HGNC:23115; EAF2. DR HPA; ENSG00000145088; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 607659; gene. DR neXtProt; NX_Q96CJ1; -. DR OpenTargets; ENSG00000145088; -. DR PharmGKB; PA128394690; -. DR VEuPathDB; HostDB:ENSG00000145088; -. DR eggNOG; KOG4795; Eukaryota. DR GeneTree; ENSGT00390000017724; -. DR HOGENOM; CLU_025755_1_0_1; -. DR InParanoid; Q96CJ1; -. DR OMA; CAFHTIR; -. DR OrthoDB; 318263at2759; -. DR PhylomeDB; Q96CJ1; -. DR TreeFam; TF320864; -. DR PathwayCommons; Q96CJ1; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR SignaLink; Q96CJ1; -. DR SIGNOR; Q96CJ1; -. DR BioGRID-ORCS; 55840; 14 hits in 1172 CRISPR screens. DR ChiTaRS; EAF2; human. DR GeneWiki; EAF2; -. DR GenomeRNAi; 55840; -. DR Pharos; Q96CJ1; Tbio. DR PRO; PR:Q96CJ1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q96CJ1; Protein. DR Bgee; ENSG00000145088; Expressed in bone marrow cell and 157 other cell types or tissues. DR ExpressionAtlas; Q96CJ1; baseline and differential. DR Genevisible; Q96CJ1; HS. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032783; C:super elongation complex; IEA:InterPro. DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB. DR GO; GO:0003711; F:transcription elongation factor activity; IMP:ARUK-UCL. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. 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 by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0034243; P:regulation of transcription elongation by RNA polymerase II; IMP:ARUK-UCL. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central. DR InterPro; IPR027093; EAF_fam. DR InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N. DR PANTHER; PTHR15970:SF7; ELL-ASSOCIATED FACTOR 2; 1. DR PANTHER; PTHR15970; ELL-ASSOCIATED FACTOR EAF; 1. DR Pfam; PF09816; EAF; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Apoptosis; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..260 FT /note="ELL-associated factor 2" FT /id="PRO_0000130337" FT REGION 17..104 FT /note="Necessary for interaction with ELL" FT /evidence="ECO:0000269|PubMed:12446457" FT REGION 116..154 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 177..260 FT /note="Necessary for transactivation activity" FT REGION 246..260 FT /note="Necessary for interaction with TCEA1 and FT transactivation activity" FT /evidence="ECO:0000250" FT COMPBIAS 116..141 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 171..192 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..130 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11042152" FT /id="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 //