ID EAPP_HUMAN Reviewed; 285 AA. AC Q56P03; Q9BVF4; Q9NWV5; Q9NZ86; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 4. DT 27-MAR-2024, entry version 147. DE RecName: Full=E2F-associated phosphoprotein; DE Short=EAPP; GN Name=EAPP; Synonyms=C14orf11; ORFNames=BM-036; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=15820313; DOI=10.1016/j.ygeno.2005.01.010; RA Kamnasaran D., Chen C.-P., Devriendt K., Mehta L., Cox D.W.; RT "Defining a holoprosencephaly locus on human chromosome 14q13 and RT characterization of potential candidate genes."; RL Genomics 85:608-621(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH E2F1; E2F2 AND E2F3, AND RP VARIANT GLU-168. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-168. RC TISSUE=Cervix; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-17; SER-109 AND SER-111, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; SER-109 AND SER-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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. CC {ECO:0000269|PubMed:15716352}. 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 -!- INTERACTION: CC Q56P03; Q13895: BYSL; NbExp=3; IntAct=EBI-748732, EBI-358049; CC Q56P03; O95379: TNFAIP8; NbExp=3; IntAct=EBI-748732, EBI-1049336; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in heart, CC placenta, skeletal muscle and pancreas. Lower levels in brain, lung and CC kidney. In the brain, expressed in all regions with high levels in the CC cerebellum and cerebral cortex. Expressed in COS1 and transformed skin CC fibroblasts. {ECO:0000269|PubMed:15716352, CC ECO:0000269|PubMed:15820313}. CC -!- DEVELOPMENTAL STAGE: During the cell cycle, expression disappears CC during mitosis. CC -!- SEQUENCE CAUTION: CC Sequence=AAF67623.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAO17041.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAO17042.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY157300; AAO17041.1; ALT_FRAME; mRNA. DR EMBL; AY157301; AAO17042.1; ALT_FRAME; mRNA. DR EMBL; AY869694; AAX63200.1; -; mRNA. DR EMBL; AF217512; AAF67623.1; ALT_FRAME; mRNA. DR EMBL; AK000585; BAA91271.1; -; mRNA. DR EMBL; AL445363; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001245; AAH01245.1; -; mRNA. DR CCDS; CCDS41941.1; -. DR RefSeq; NP_001305845.1; NM_001318916.1. DR RefSeq; NP_060923.2; NM_018453.3. DR AlphaFoldDB; Q56P03; -. DR BioGRID; 120941; 77. DR IntAct; Q56P03; 24. DR STRING; 9606.ENSP00000250454; -. DR iPTMnet; Q56P03; -. DR PhosphoSitePlus; Q56P03; -. DR BioMuta; EAPP; -. DR DMDM; 296439474; -. DR EPD; Q56P03; -. DR jPOST; Q56P03; -. DR MassIVE; Q56P03; -. DR MaxQB; Q56P03; -. DR PaxDb; 9606-ENSP00000250454; -. DR PeptideAtlas; Q56P03; -. DR ProteomicsDB; 62582; -. DR Pumba; Q56P03; -. DR Antibodypedia; 128; 150 antibodies from 26 providers. DR DNASU; 55837; -. DR Ensembl; ENST00000250454.8; ENSP00000250454.3; ENSG00000129518.10. DR GeneID; 55837; -. DR KEGG; hsa:55837; -. DR MANE-Select; ENST00000250454.8; ENSP00000250454.3; NM_018453.4; NP_060923.2. DR UCSC; uc001wsd.2; human. DR AGR; HGNC:19312; -. DR CTD; 55837; -. DR DisGeNET; 55837; -. DR GeneCards; EAPP; -. DR HGNC; HGNC:19312; EAPP. DR HPA; ENSG00000129518; Low tissue specificity. DR MIM; 609486; gene. DR neXtProt; NX_Q56P03; -. DR OpenTargets; ENSG00000129518; -. DR PharmGKB; PA162384208; -. DR VEuPathDB; HostDB:ENSG00000129518; -. DR eggNOG; KOG3395; Eukaryota. DR GeneTree; ENSGT00390000001332; -. DR InParanoid; Q56P03; -. DR OMA; CFVNKEE; -. DR OrthoDB; 69653at2759; -. DR PhylomeDB; Q56P03; -. DR TreeFam; TF328497; -. DR PathwayCommons; Q56P03; -. DR SignaLink; Q56P03; -. DR SIGNOR; Q56P03; -. DR BioGRID-ORCS; 55837; 276 hits in 1155 CRISPR screens. DR ChiTaRS; EAPP; human. DR GeneWiki; EAPP; -. DR GenomeRNAi; 55837; -. DR Pharos; Q56P03; Tbio. DR PRO; PR:Q56P03; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q56P03; Protein. DR Bgee; ENSG00000129518; Expressed in calcaneal tendon and 210 other cell types or tissues. DR ExpressionAtlas; Q56P03; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0034244; P:negative regulation of transcription elongation by RNA polymerase II; IDA:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA: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; Q56P03; HS. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..285 FT /note="E2F-associated phosphoprotein" FT /id="PRO_0000086904" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 48..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 118..144 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 COMPBIAS 74..95 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..144 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 37 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 109 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 111 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT VARIANT 168 FT /note="Q -> E (in dbSNP:rs17352411)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15716352" FT /id="VAR_031915" FT CONFLICT 3 FT /note="R -> L (in Ref. 2; AAX63200)" FT /evidence="ECO:0000305" FT CONFLICT 52 FT /note="E -> G (in Ref. 4; BAA91271)" FT /evidence="ECO:0000305" FT CONFLICT 239 FT /note="R -> Q (in Ref. 2; AAX63200 and 6; AAH01245)" FT /evidence="ECO:0000305" SQ SEQUENCE 285 AA; 32762 MW; 1C0691602FFB516A CRC64; MNRLPDDYDP YAVEEPSDEE PALSSSEDEV DVLLHGTPDQ KRKLIRECLT GESESSSEDE FEKEMEAELN STMKTMEDKL SSLGTGSSSG NGKVATAPTR YYDDIYFDSD SEDEDRAVQV TKKKKKKQHK IPTNDELLYD PEKDNRDQAW VDAQRRGYHG LGPQRSRQQQ PVPNSDAVLN CPACMTTLCL DCQRHESYKT QYRAMFVMNC SINKEEVLRY KASENRKKRR VHKKMRSNRE DAAEKAETDV EEIYHPVMCT ECSTEVAVYD KDEVFHFFNV LASHS //