EAPP_HUMAN
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 03-AUG-2022, entry version 138.
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};
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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; 70.
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; Q56P03; -.
DR PeptideAtlas; Q56P03; -.
DR PRIDE; Q56P03; -.
DR ProteomicsDB; 62582; -.
DR Antibodypedia; 128; 134 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 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; MEGTWAP; -.
DR OrthoDB; 1484224at2759; -.
DR PhylomeDB; Q56P03; -.
DR TreeFam; TF328497; -.
DR PathwayCommons; Q56P03; -.
DR SignaLink; Q56P03; -.
DR SIGNOR; Q56P03; -.
DR BioGRID-ORCS; 55837; 270 hits in 1078 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 208 other tissues.
DR ExpressionAtlas; Q56P03; baseline and differential.
DR Genevisible; Q56P03; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; 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 from RNA polymerase II promoter; IDA:MGI.
DR InterPro; IPR019370; E2F-assoc_phosphoprotein.
DR PANTHER; PTHR15967; PTHR15967; 1.
DR Pfam; PF10238; Eapp_C; 1.
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
