EAF1_MOUSE
ID EAF1_MOUSE Reviewed; 268 AA.
AC Q9D4C5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ELL-associated factor 1;
GN Name=Eaf1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Retina, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK016628; BAB30346.2; -; mRNA.
DR EMBL; AK044181; BAC31806.1; -; mRNA.
DR EMBL; AK044737; BAC32058.1; -; mRNA.
DR EMBL; BC079658; AAH79658.1; -; mRNA.
DR CCDS; CCDS26914.1; -.
DR RefSeq; NP_083208.1; NM_028932.4.
DR AlphaFoldDB; Q9D4C5; -.
DR SMR; Q9D4C5; -.
DR STRING; 10090.ENSMUSP00000022446; -.
DR iPTMnet; Q9D4C5; -.
DR PhosphoSitePlus; Q9D4C5; -.
DR EPD; Q9D4C5; -.
DR jPOST; Q9D4C5; -.
DR MaxQB; Q9D4C5; -.
DR PaxDb; Q9D4C5; -.
DR PeptideAtlas; Q9D4C5; -.
DR PRIDE; Q9D4C5; -.
DR ProteomicsDB; 277665; -.
DR Antibodypedia; 26754; 131 antibodies from 21 providers.
DR Ensembl; ENSMUST00000022446; ENSMUSP00000022446; ENSMUSG00000021890.
DR GeneID; 74427; -.
DR KEGG; mmu:74427; -.
DR UCSC; uc007sxt.2; mouse.
DR CTD; 85403; -.
DR MGI; MGI:1921677; Eaf1.
DR VEuPathDB; HostDB:ENSMUSG00000021890; -.
DR eggNOG; KOG4795; Eukaryota.
DR GeneTree; ENSGT00390000017724; -.
DR HOGENOM; CLU_025755_0_0_1; -.
DR InParanoid; Q9D4C5; -.
DR OMA; YHKECVL; -.
DR OrthoDB; 1269479at2759; -.
DR PhylomeDB; Q9D4C5; -.
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; 74427; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Eaf1; mouse.
DR PRO; PR:Q9D4C5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D4C5; protein.
DR Bgee; ENSMUSG00000021890; Expressed in epithelium of lens and 223 other tissues.
DR Genevisible; Q9D4C5; MM.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO: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:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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; 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; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..268
FT /note="ELL-associated factor 1"
FT /id="PRO_0000130335"
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..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..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:0007744|PubMed:21183079"
SQ SEQUENCE 268 AA; 28967 MW; 02ACBA8F33200C20 CRC64;
MNGTANPLLD REEHCLRLGE SFEKRPRASF HTIRYDFKPA SIDTSCEGEL QVGKGDEVTI
TLPHIPGSTP PMTVFKGNKR PYQKDCVLII NHDTGEYVLE KLSSSIQVKK TRAEGSSKIQ
ARMEQQPARP PQPSQPPPPP PPMPFRAPTK PPAGPKTSPL KDNPSPEPQL DDIKRELRAE
VDIIEQMSSS SGSSSSDSES SSGSDDDSSS SAGEDNGPAS PPQPSHQQPY NSRPAVANGT
SRPQGSSQLM NTLRNDLQLS ESGSDSDD
