EAF2_MOUSE
ID EAF2_MOUSE Reviewed; 262 AA.
AC Q91ZD6; Q7TN80; Q99KD2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ELL-associated factor 2;
DE AltName: Full=Ehrlich S-II transcriptional activator factor;
DE AltName: Full=Testosterone-regulated apoptosis inducer and tumor suppressor protein;
GN Name=Eaf2; Synonyms=Festa, Traits;
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 [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=14517999; DOI=10.1002/dvdy.10367;
RA Li M., Wu X., Zhuang F., Jiang S., Jiang M., Liu Y.-H.;
RT "Expression of murine ELL-associated factor 2 (Eaf2) is developmentally
RT regulated.";
RL Dev. Dyn. 228:273-280(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ROLE IN TCEA1-TRANSCRIPTION
RP ACTIVATION, INTERACTION WITH TCEA1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=12761297; DOI=10.1093/jb/mvg065;
RA Saso K., Ito T., Natori S., Sekimizu K.;
RT "Identification of a novel tissue-specific transcriptional activator FESTA
RT as a protein that interacts with the transcription elongation factor S-
RT II.";
RL J. Biochem. 133:493-500(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2
CC elongation activities (By similarity). Acts as a transcriptional
CC transactivator of TCEA1 elongation activity. {ECO:0000250,
CC ECO:0000269|PubMed:12761297}.
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). Interacts with ELL and ELL2 (By
CC similarity). Isoform 1 and isoform 2 interact with TCEA1. {ECO:0000250,
CC ECO:0000269|PubMed:12761297}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96CJ1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=FESTA-L;
CC IsoId=Q91ZD6-1; Sequence=Displayed;
CC Name=2; Synonyms=FESTA-S;
CC IsoId=Q91ZD6-2; Sequence=VSP_015311;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in ovary, uterus, mammary
CC glands, brain, spleen, liver, lung, thymus, kidney, skeletal muscle,
CC skin and testis. Isoform 2 is expressed in kidney.
CC {ECO:0000269|PubMed:12761297, ECO:0000269|PubMed:14517999}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain and spinal cord at 10 dpc.
CC Expressed in brain, spinal cord, cranial and spinal ganglia, lens,
CC retina, cochlea, olfactory epithelium and pituitary at 12 dpc.
CC Expressed in intestine, bladder endothelium, retinal ganglion cells,
CC nephrons, bronchial epithelium, secretory epithelium of submandibular
CC glands, tubular epithelium of the epididymis, ectodermal invaginations
CC of mammary buds and vibrissae follicles, incisors and molars at 15 dpc.
CC {ECO:0000269|PubMed:14517999}.
CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04721.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC77525.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY049021; AAL12224.1; -; mRNA.
DR EMBL; AY034479; AAK59701.1; -; mRNA.
DR EMBL; AB081298; BAC77525.1; ALT_INIT; mRNA.
DR EMBL; BC004721; AAH04721.1; ALT_INIT; mRNA.
DR EMBL; BC056626; AAH56626.1; -; mRNA.
DR CCDS; CCDS37335.1; -. [Q91ZD6-2]
DR CCDS; CCDS49843.1; -. [Q91ZD6-1]
DR RefSeq; NP_001106872.1; NM_001113401.1. [Q91ZD6-1]
DR RefSeq; NP_001106876.1; NM_001113405.1. [Q91ZD6-2]
DR RefSeq; NP_598872.1; NM_134111.2. [Q91ZD6-2]
DR RefSeq; XP_006521746.1; XM_006521683.1. [Q91ZD6-2]
DR RefSeq; XP_006521747.1; XM_006521684.3. [Q91ZD6-2]
DR RefSeq; XP_006521748.1; XM_006521685.3. [Q91ZD6-2]
DR RefSeq; XP_006521749.1; XM_006521686.2.
DR AlphaFoldDB; Q91ZD6; -.
DR SMR; Q91ZD6; -.
DR BioGRID; 223046; 1.
DR IntAct; Q91ZD6; 1.
DR STRING; 10090.ENSMUSP00000110477; -.
DR iPTMnet; Q91ZD6; -.
DR PhosphoSitePlus; Q91ZD6; -.
DR MaxQB; Q91ZD6; -.
DR PaxDb; Q91ZD6; -.
DR PRIDE; Q91ZD6; -.
DR ProteomicsDB; 277434; -. [Q91ZD6-1]
DR ProteomicsDB; 277435; -. [Q91ZD6-2]
DR Antibodypedia; 1994; 187 antibodies from 31 providers.
DR DNASU; 106389; -.
DR Ensembl; ENSMUST00000075946; ENSMUSP00000075331; ENSMUSG00000022838. [Q91ZD6-2]
DR Ensembl; ENSMUST00000114825; ENSMUSP00000110473; ENSMUSG00000022838. [Q91ZD6-2]
DR Ensembl; ENSMUST00000114829; ENSMUSP00000110477; ENSMUSG00000022838. [Q91ZD6-1]
DR GeneID; 106389; -.
DR KEGG; mmu:106389; -.
DR UCSC; uc007zcx.1; mouse. [Q91ZD6-1]
DR CTD; 55840; -.
DR MGI; MGI:2146616; Eaf2.
DR VEuPathDB; HostDB:ENSMUSG00000022838; -.
DR eggNOG; KOG4795; Eukaryota.
DR GeneTree; ENSGT00390000017724; -.
DR HOGENOM; CLU_1885121_0_0_1; -.
DR InParanoid; Q91ZD6; -.
DR OMA; TMSAMPQ; -.
DR OrthoDB; 1269479at2759; -.
DR PhylomeDB; Q91ZD6; -.
DR TreeFam; TF320864; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 106389; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Eaf2; mouse.
DR PRO; PR:Q91ZD6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q91ZD6; protein.
DR Bgee; ENSMUSG00000022838; Expressed in female urethra and 137 other tissues.
DR ExpressionAtlas; Q91ZD6; baseline and differential.
DR Genevisible; Q91ZD6; MM.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032783; C:super elongation complex; IEA:InterPro.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0003711; F:transcription elongation regulator activity; ISO:MGI.
DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:MGI.
DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
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; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..262
FT /note="ELL-associated factor 2"
FT /id="PRO_0000130338"
FT REGION 17..104
FT /note="Necessary for interaction with ELL"
FT /evidence="ECO:0000250"
FT REGION 170..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..262
FT /note="Necessary for transactivation activity"
FT /evidence="ECO:0000250"
FT REGION 248..262
FT /note="Necessary for interaction with TCEA1 and
FT transactivation activity"
FT /evidence="ECO:0000269|PubMed:12761297"
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:0000250|UniProtKB:Q96CJ1"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CJ1"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CJ1"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12761297,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015311"
SQ SEQUENCE 262 AA; 29187 MW; 5D072D84816B766A CRC64;
MSGPAGLAYL DRRERVLKLG ESFEKQPRCA FHTVRYDFKP ASIDTSCEGN LEVGKGEQVT
ITLPNIEGST PPVTVFKGSK RPYLKECILI INHDTGECRL EKLSSNITVK KTRVEGSSRI
QYRLEQQQQQ MWNLPRTSNL VQHSPSEEKM SPTSLMDDIE RELKAEASLM DQMSSCDSSS
DSKSSSSSSS EDSSSDSEDD DQFSPLGPRK YSSEHPSMSA GPQYRTSEAD ATCHRLQDHS
TLLMSTLRSD LQLSESESDS ED
