EAF2_HUMAN
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 03-AUG-2022, entry version 149.
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}.
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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. [Q96CJ1-2]
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; Q96CJ1; -.
DR PeptideAtlas; Q96CJ1; -.
DR PRIDE; Q96CJ1; -.
DR ProteomicsDB; 76189; -. [Q96CJ1-1]
DR ProteomicsDB; 76190; -. [Q96CJ1-2]
DR Antibodypedia; 1994; 187 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 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; TMSAMPQ; -.
DR OrthoDB; 1269479at2759; -.
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 1095 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 155 other 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 regulator 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:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IMP:ARUK-UCL.
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; 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
