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Q5BU09 (EAPP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E2F-associated phosphoprotein

Short name=EAPP
Gene names
Name:Eapp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5BU09-1)

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.
Isoform 2 (identifier: Q5BU09-2)

The sequence of this isoform differs from the canonical sequence as follows:
     156-193: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281E2F-associated phosphoprotein
PRO_0000086905

Regions

Compositional bias120 – 1256Poly-Lys

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue171Phosphoserine By similarity
Modified residue1091Phosphoserine By similarity
Modified residue1111Phosphoserine By similarity

Natural variations

Alternative sequence156 – 19338Missing in isoform 2.
VSP_015331

Experimental info

Sequence conflict1161K → R in AAX20161. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 269C664CA3E3C401

FASTA28132,494
        10         20         30         40         50         60 
MNRLQDDYDP YAVEEPSDEE PALSSSEDEL DVLLHGTPDQ KRKLIRECLT GESESSSEDE 

        70         80         90        100        110        120 
FEKEMEAELN STMKTMEDQL SSLGTGSSSG VAKVGGVTEK FYDEIYFDSD SEDEDKTVTK 

       130        140        150        160        170        180 
KKKKKQHRIP TNDELLYDPE KDNRDQAWVD AKRRGYHAFG LQRPRQKQQP VPNSDAVLNC 

       190        200        210        220        230        240 
PACMTTLCLD CQRHESYKTQ YRAMFVMNCS INREEVLRYK NPENRRKRRS AKKMRSNPED 

       250        260        270        280 
PAEREAEEIY HPVMCTECST EVAVYDKDEV FHFFNVLASH S 

« Hide

Isoform 2 [UniParc].

Checksum: 5701DEB71ABCEC22
Show »

FASTA24328,208

References

« Hide 'large scale' references
[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(2005) [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. expand/collapse author list , 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(2005) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N-3.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY882557 mRNA. Translation: AAX20161.1.
AK007442 mRNA. Translation: BAB25042.1.
AK012800 mRNA. Translation: BAB28479.1.
BC037622 mRNA. Translation: AAH37622.1.
CCDSCCDS25910.1. [Q5BU09-1]
RefSeqNP_079732.1. NM_025456.3. [Q5BU09-1]
XP_006516205.1. XM_006516142.1. [Q5BU09-1]
UniGeneMm.156440.

3D structure databases

ProteinModelPortalQ5BU09.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ5BU09.

Proteomic databases

MaxQBQ5BU09.
PRIDEQ5BU09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000110713; ENSMUSP00000106341; ENSMUSG00000054302. [Q5BU09-2]
ENSMUST00000161592; ENSMUSP00000123698; ENSMUSG00000054302. [Q5BU09-1]
ENSMUST00000163433; ENSMUSP00000130251; ENSMUSG00000054302. [Q5BU09-1]
GeneID66266.
KEGGmmu:66266.
UCSCuc007nnu.1. mouse. [Q5BU09-1]
uc011ylx.1. mouse. [Q5BU09-2]

Organism-specific databases

CTD55837.
MGIMGI:1913516. Eapp.

Phylogenomic databases

eggNOGNOG250977.
GeneTreeENSGT00390000001332.
HOGENOMHOG000068005.
HOVERGENHBG054593.
InParanoidQ5BU09.
OMARGHKKMR.
OrthoDBEOG7SR4ND.
PhylomeDBQ5BU09.
TreeFamTF328497.

Gene expression databases

ArrayExpressQ5BU09.
BgeeQ5BU09.
CleanExMM_EAPP.
GenevestigatorQ5BU09.

Family and domain databases

InterProIPR019370. E2F-assoc_phosphoprotein.
[Graphical view]
PfamPF10238. Eapp_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio321143.
PROQ5BU09.
SOURCESearch...

Entry information

Entry nameEAPP_MOUSE
AccessionPrimary (citable) accession number: Q5BU09
Secondary accession number(s): Q9CZB5, Q9D914
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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