ID   EAPP_MOUSE              Reviewed;         281 AA.
AC   Q5BU09; Q9CZB5; Q9D914;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=E2F-associated phosphoprotein;
DE            Short=EAPP;
GN   Name=Eapp;
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), AND INTERACTION WITH E2F1; E2F2 AND
RP   E2F3.
RX   PubMed=15716352; DOI=10.1091/mbc.e04-11-0975;
RA   Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L.,
RA   Rotheneder H.;
RT   "EAPP, a novel E2F binding protein that modulates E2F-dependent
RT   transcription.";
RL   Mol. Biol. Cell 16:2181-2190(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   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: May play an important role in the fine-tuning of both major
CC       E2F1 activities, the regulation of the cell-cycle and the induction of
CC       apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with E2F1. The C-terminal half binds the N-terminal
CC       of E2F1. Also interacts with E2F2 and E2F3, but not E2F4.
CC       {ECO:0000269|PubMed:15716352}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5BU09-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5BU09-2; Sequence=VSP_015331;
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DR   EMBL; AY882557; AAX20161.1; -; mRNA.
DR   EMBL; AK007442; BAB25042.1; -; mRNA.
DR   EMBL; AK012800; BAB28479.1; -; mRNA.
DR   EMBL; BC037622; AAH37622.1; -; mRNA.
DR   CCDS; CCDS25910.1; -. [Q5BU09-1]
DR   CCDS; CCDS88337.1; -. [Q5BU09-2]
DR   RefSeq; NP_001318091.1; NM_001331162.1. [Q5BU09-2]
DR   RefSeq; NP_079732.1; NM_025456.4. [Q5BU09-1]
DR   RefSeq; XP_006516205.1; XM_006516142.3. [Q5BU09-1]
DR   AlphaFoldDB; Q5BU09; -.
DR   STRING; 10090.ENSMUSP00000123698; -.
DR   iPTMnet; Q5BU09; -.
DR   PhosphoSitePlus; Q5BU09; -.
DR   EPD; Q5BU09; -.
DR   MaxQB; Q5BU09; -.
DR   PaxDb; 10090-ENSMUSP00000123698; -.
DR   ProteomicsDB; 277710; -. [Q5BU09-1]
DR   ProteomicsDB; 277711; -. [Q5BU09-2]
DR   Pumba; Q5BU09; -.
DR   Antibodypedia; 128; 150 antibodies from 26 providers.
DR   DNASU; 66266; -.
DR   Ensembl; ENSMUST00000110713.10; ENSMUSP00000106341.4; ENSMUSG00000054302.16. [Q5BU09-2]
DR   Ensembl; ENSMUST00000161592.8; ENSMUSP00000123698.2; ENSMUSG00000054302.16. [Q5BU09-1]
DR   Ensembl; ENSMUST00000163433.8; ENSMUSP00000130251.2; ENSMUSG00000054302.16. [Q5BU09-1]
DR   GeneID; 66266; -.
DR   KEGG; mmu:66266; -.
DR   UCSC; uc007nnu.1; mouse. [Q5BU09-1]
DR   UCSC; uc011ylx.1; mouse. [Q5BU09-2]
DR   AGR; MGI:1913516; -.
DR   CTD; 55837; -.
DR   MGI; MGI:1913516; Eapp.
DR   VEuPathDB; HostDB:ENSMUSG00000054302; -.
DR   eggNOG; KOG3395; Eukaryota.
DR   GeneTree; ENSGT00390000001332; -.
DR   HOGENOM; CLU_075202_0_0_1; -.
DR   InParanoid; Q5BU09; -.
DR   OMA; CFVNKEE; -.
DR   OrthoDB; 69653at2759; -.
DR   PhylomeDB; Q5BU09; -.
DR   TreeFam; TF328497; -.
DR   BioGRID-ORCS; 66266; 18 hits in 75 CRISPR screens.
DR   ChiTaRS; Eapp; mouse.
DR   PRO; PR:Q5BU09; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q5BU09; Protein.
DR   Bgee; ENSMUSG00000054302; Expressed in interventricular septum and 257 other cell types or tissues.
DR   ExpressionAtlas; Q5BU09; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0034244; P:negative regulation of transcription elongation by RNA polymerase II; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; ISO:MGI.
DR   InterPro; IPR019370; E2F-assoc_phosphoprotein.
DR   PANTHER; PTHR15967:SF0; E2F-ASSOCIATED PHOSPHOPROTEIN; 1.
DR   PANTHER; PTHR15967; UNCHARACTERIZED; 1.
DR   Pfam; PF10238; Eapp_C; 1.
DR   Genevisible; Q5BU09; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..281
FT                   /note="E2F-associated phosphoprotein"
FT                   /id="PRO_0000086905"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q56P03"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q56P03"
FT   MOD_RES         37
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q56P03"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         156..193
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015331"
FT   CONFLICT        116
FT                   /note="K -> R (in Ref. 1; AAX20161)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  32494 MW;  269C664CA3E3C401 CRC64;
     MNRLQDDYDP YAVEEPSDEE PALSSSEDEL DVLLHGTPDQ KRKLIRECLT GESESSSEDE
     FEKEMEAELN STMKTMEDQL SSLGTGSSSG VAKVGGVTEK FYDEIYFDSD SEDEDKTVTK
     KKKKKQHRIP TNDELLYDPE KDNRDQAWVD AKRRGYHAFG LQRPRQKQQP VPNSDAVLNC
     PACMTTLCLD CQRHESYKTQ YRAMFVMNCS INREEVLRYK NPENRRKRRS AKKMRSNPED
     PAEREAEEIY HPVMCTECST EVAVYDKDEV FHFFNVLASH S
//