EAF2_RAT
ID EAF2_RAT Reviewed; 262 AA.
AC Q811X5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ELL-associated factor 2;
DE AltName: Full=Testosterone-regulated apoptosis inducer and tumor suppressor protein;
GN Name=Eaf2; Synonyms=Traits;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION IN APOPTOSIS.
RC STRAIN=Sprague-Dawley;
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).
CC -!- FUNCTION: Acts as a transcriptional transactivator of ELL, ELL2 and
CC TCEA1 elongation activities (By similarity). Potent inducer of
CC apoptosis in prostatic and non-prostatic cell lines. {ECO:0000250,
CC ECO:0000269|PubMed:12907652}.
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, ELL2 and TCEA1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96CJ1}.
CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000305}.
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DR EMBL; AY049022; AAL12225.1; -; mRNA.
DR RefSeq; NP_742044.1; NM_172047.1.
DR AlphaFoldDB; Q811X5; -.
DR SMR; Q811X5; -.
DR STRING; 10116.ENSRNOP00000003208; -.
DR CarbonylDB; Q811X5; -.
DR PhosphoSitePlus; Q811X5; -.
DR PaxDb; Q811X5; -.
DR Ensembl; ENSRNOT00000003208; ENSRNOP00000003208; ENSRNOG00000002350.
DR GeneID; 266787; -.
DR KEGG; rno:266787; -.
DR UCSC; RGD:628879; rat.
DR CTD; 55840; -.
DR RGD; 628879; Eaf2.
DR eggNOG; KOG4795; Eukaryota.
DR GeneTree; ENSGT00390000017724; -.
DR HOGENOM; CLU_025755_1_0_1; -.
DR InParanoid; Q811X5; -.
DR OMA; TMSAMPQ; -.
DR OrthoDB; 1269479at2759; -.
DR PhylomeDB; Q811X5; -.
DR TreeFam; TF320864; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q811X5; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000002350; Expressed in spleen and 11 other tissues.
DR Genevisible; Q811X5; RN.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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:RGD.
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; ISO:RGD.
DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; ISO:RGD.
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; Apoptosis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..262
FT /note="ELL-associated factor 2"
FT /id="PRO_0000130339"
FT REGION 17..104
FT /note="Necessary for interaction with ELL"
FT /evidence="ECO:0000250"
FT REGION 124..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..232
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:0000250"
FT COMPBIAS 124..151
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 COMPBIAS 209..232
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"
SQ SEQUENCE 262 AA; 28933 MW; FD34BA01DC8D26CC CRC64;
MNGPAGLAYL DRRERILKLG ESFEKQPRCA FHTVRYDFKP ASVDASCEGN LEVGKGEQVT
ITLPNIEGST PPVTVFKGSK RPYLKECILI INHDTGECRL EKLSSNITVK KTRGEGSSKI
QCRLEQQQQQ MWNPPRTSNL VQHSPSEDKL SPTSLMDDIE RELKAEASLM DQMSSCDSSS
DSRSSSSSSS EDSSSDSEDD DRSSPSGPRR YSSEHPSVSA GPQYRTSDAD TTCNRLYDNS
ALLMSTLRSD LQLSESDSDS ED