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Protein

E2F-associated phosphoprotein

Gene

Eapp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May play an important role in the fine-tuning of both major E2F1 activities, the regulation of the cell-cycle and the induction of apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression (By similarity).By similarity

GO - Biological processi

  1. negative regulation of transcription elongation from RNA polymerase II promoter Source: MGI
  2. positive regulation of cell proliferation Source: MGI
  3. positive regulation of transcription elongation from RNA polymerase II promoter Source: MGI
  4. regulation of transcription elongation from RNA polymerase II promoter Source: GO_Central
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
E2F-associated phosphoprotein
Short name:
EAPP
Gene namesi
Name:Eapp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1913516. Eapp.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. Golgi apparatus Source: MGI
  3. nucleoplasm Source: MGI
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281E2F-associated phosphoproteinPRO_0000086905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei37 – 371PhosphothreonineBy similarity
Modified residuei109 – 1091PhosphoserineBy similarity
Modified residuei111 – 1111PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5BU09.
PRIDEiQ5BU09.

PTM databases

PhosphoSiteiQ5BU09.

Expressioni

Gene expression databases

BgeeiQ5BU09.
CleanExiMM_EAPP.
ExpressionAtlasiQ5BU09. baseline and differential.
GenevestigatoriQ5BU09.

Interactioni

Subunit structurei

Interacts with E2F1. The C-terminal half binds the N-terminal of E2F1. Also interacts with E2F2 and E2F3, but not E2F4.1 Publication

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi120 – 1256Poly-Lys

Phylogenomic databases

eggNOGiNOG250977.
GeneTreeiENSGT00390000001332.
HOGENOMiHOG000068005.
HOVERGENiHBG054593.
InParanoidiQ5BU09.
OMAiRGHKKMR.
OrthoDBiEOG7SR4ND.
PhylomeDBiQ5BU09.
TreeFamiTF328497.

Family and domain databases

InterProiIPR019370. E2F-assoc_phosphoprotein.
[Graphical view]
PfamiPF10238. Eapp_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5BU09-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNRLQDDYDP YAVEEPSDEE PALSSSEDEL DVLLHGTPDQ KRKLIRECLT
60 70 80 90 100
GESESSSEDE FEKEMEAELN STMKTMEDQL SSLGTGSSSG VAKVGGVTEK
110 120 130 140 150
FYDEIYFDSD SEDEDKTVTK KKKKKQHRIP TNDELLYDPE KDNRDQAWVD
160 170 180 190 200
AKRRGYHAFG LQRPRQKQQP VPNSDAVLNC PACMTTLCLD CQRHESYKTQ
210 220 230 240 250
YRAMFVMNCS INREEVLRYK NPENRRKRRS AKKMRSNPED PAEREAEEIY
260 270 280
HPVMCTECST EVAVYDKDEV FHFFNVLASH S
Length:281
Mass (Da):32,494
Last modified:August 30, 2005 - v2
Checksum:i269C664CA3E3C401
GO
Isoform 2 (identifier: Q5BU09-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     156-193: Missing.

Note: No experimental confirmation available.

Show »
Length:243
Mass (Da):28,208
Checksum:i5701DEB71ABCEC22
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161K → R in AAX20161 (PubMed:15716352).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei156 – 19338Missing in isoform 2. 1 PublicationVSP_015331Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY882557 mRNA. Translation: AAX20161.1.
AK007442 mRNA. Translation: BAB25042.1.
AK012800 mRNA. Translation: BAB28479.1.
BC037622 mRNA. Translation: AAH37622.1.
CCDSiCCDS25910.1. [Q5BU09-1]
RefSeqiNP_079732.1. NM_025456.3. [Q5BU09-1]
XP_006516205.1. XM_006516142.2. [Q5BU09-1]
UniGeneiMm.156440.

Genome annotation databases

EnsembliENSMUST00000110713; ENSMUSP00000106341; ENSMUSG00000054302. [Q5BU09-2]
ENSMUST00000161592; ENSMUSP00000123698; ENSMUSG00000054302. [Q5BU09-1]
ENSMUST00000163433; ENSMUSP00000130251; ENSMUSG00000054302. [Q5BU09-1]
GeneIDi66266.
KEGGimmu:66266.
UCSCiuc007nnu.1. mouse. [Q5BU09-1]
uc011ylx.1. mouse. [Q5BU09-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY882557 mRNA. Translation: AAX20161.1.
AK007442 mRNA. Translation: BAB25042.1.
AK012800 mRNA. Translation: BAB28479.1.
BC037622 mRNA. Translation: AAH37622.1.
CCDSiCCDS25910.1. [Q5BU09-1]
RefSeqiNP_079732.1. NM_025456.3. [Q5BU09-1]
XP_006516205.1. XM_006516142.2. [Q5BU09-1]
UniGeneiMm.156440.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ5BU09.

Proteomic databases

MaxQBiQ5BU09.
PRIDEiQ5BU09.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110713; ENSMUSP00000106341; ENSMUSG00000054302. [Q5BU09-2]
ENSMUST00000161592; ENSMUSP00000123698; ENSMUSG00000054302. [Q5BU09-1]
ENSMUST00000163433; ENSMUSP00000130251; ENSMUSG00000054302. [Q5BU09-1]
GeneIDi66266.
KEGGimmu:66266.
UCSCiuc007nnu.1. mouse. [Q5BU09-1]
uc011ylx.1. mouse. [Q5BU09-2]

Organism-specific databases

CTDi55837.
MGIiMGI:1913516. Eapp.

Phylogenomic databases

eggNOGiNOG250977.
GeneTreeiENSGT00390000001332.
HOGENOMiHOG000068005.
HOVERGENiHBG054593.
InParanoidiQ5BU09.
OMAiRGHKKMR.
OrthoDBiEOG7SR4ND.
PhylomeDBiQ5BU09.
TreeFamiTF328497.

Miscellaneous databases

NextBioi321143.
PROiQ5BU09.
SOURCEiSearch...

Gene expression databases

BgeeiQ5BU09.
CleanExiMM_EAPP.
ExpressionAtlasiQ5BU09. baseline and differential.
GenevestigatoriQ5BU09.

Family and domain databases

InterProiIPR019370. E2F-assoc_phosphoprotein.
[Graphical view]
PfamiPF10238. Eapp_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EAPP, a novel E2F binding protein that modulates E2F-dependent transcription."
    Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L., Rotheneder H.
    Mol. Biol. Cell 16:2181-2190(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH E2F1; E2F2 AND E2F3.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Pancreas.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N-3.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiEAPP_MOUSE
AccessioniPrimary (citable) accession number: Q5BU09
Secondary accession number(s): Q9CZB5, Q9D914
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: April 1, 2015
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.