EAF1_PONAB
ID EAF1_PONAB Reviewed; 268 AA.
AC Q5RAM8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=ELL-associated factor 1;
GN Name=EAF1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2
CC elongation activities. {ECO:0000250}.
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96JC9}.
CC Nucleus, Cajal body {ECO:0000250|UniProtKB:Q96JC9}.
CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000305}.
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DR EMBL; CR858987; CAH91182.1; -; mRNA.
DR RefSeq; NP_001124559.1; NM_001131087.1.
DR AlphaFoldDB; Q5RAM8; -.
DR SMR; Q5RAM8; -.
DR STRING; 9601.ENSPPYP00000015761; -.
DR GeneID; 100169731; -.
DR KEGG; pon:100169731; -.
DR CTD; 85403; -.
DR eggNOG; KOG4795; Eukaryota.
DR HOGENOM; CLU_025755_0_0_1; -.
DR InParanoid; Q5RAM8; -.
DR OrthoDB; 1269479at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0032783; C:super elongation complex; IEA:InterPro.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR027093; EAF_fam.
DR InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N.
DR PANTHER; PTHR15970; PTHR15970; 1.
DR Pfam; PF09816; EAF; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..268
FT /note="ELL-associated factor 1"
FT /id="PRO_0000130336"
FT REGION 106..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..262
FT /note="Necessary for transactivation activity"
FT /evidence="ECO:0000250"
FT COMPBIAS 106..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JC9"
SQ SEQUENCE 268 AA; 29042 MW; 0D78B586AABB0FA4 CRC64;
MNGTANPLLD REEHCLRLGE SFEKRPRASF HTIRYDFKPA SIDTSCEGEL QVGKGDEVTI
TLPHIPGSTP PMTVFKGNKR PYQKDCVLII NHDTGEYVLE KLSSSIQVKK TRAEGSSKIQ
ARMEQQPTRP PQTSQPPPPP PPMPFRAPTK PPVGPKTSPL KDNPSPEPQL DDIKRELRAE
VDIIEQMSSS SGSSSSDSES SSGSDDDSSS SGGEDNGPAS PPQPSHQQPY NSRPAVANGT
SRPQGSNQLM NTLRNDLQLS ESGSDSDD