Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q56P03 (EAPP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Synonyms:C14orf11
ORF Names:BM-036
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length285 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. Ref.2

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.2

Subcellular location

Cytoplasm. Nucleus Ref.1 Ref.2.

Tissue specificity

Ubiquitously expressed. Highest levels in heart, placenta, skeletal muscle and pancreas. Lower levels in brain, lung and kidney. In the brain, expressed in all regions with high levels in the cerebellum and cerebral cortex. Expressed in COS1 and transformed skin fibroblasts. Ref.1 Ref.2

Developmental stage

During the cell cycle, expression disappears during mitosis.

Sequence caution

The sequence AAF67623.1 differs from that shown. Reason: Frameshift at positions 178, 189, 198 and 226.

The sequence AAO17041.1 differs from that shown. Reason: Frameshift at positions 178, 189, 198 and 226.

The sequence AAO17042.1 differs from that shown. Reason: Frameshift at positions 178, 189, 198 and 226.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285E2F-associated phosphoprotein
PRO_0000086904

Regions

Compositional bias122 – 1276Poly-Lys

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue171Phosphoserine Ref.9
Modified residue1091Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10
Modified residue1111Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10

Natural variations

Natural variant1681Q → E. Ref.2 Ref.6
Corresponds to variant rs17856038 [ dbSNP | Ensembl ].
VAR_031915

Experimental info

Sequence conflict31R → L in AAX63200. Ref.2
Sequence conflict521E → G in BAA91271. Ref.4
Sequence conflict2391R → Q in AAX63200. Ref.2
Sequence conflict2391R → Q in AAH01245. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q56P03 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: 1C0691602FFB516A

FASTA28532,762
        10         20         30         40         50         60 
MNRLPDDYDP YAVEEPSDEE PALSSSEDEV DVLLHGTPDQ KRKLIRECLT GESESSSEDE 

        70         80         90        100        110        120 
FEKEMEAELN STMKTMEDKL SSLGTGSSSG NGKVATAPTR YYDDIYFDSD SEDEDRAVQV 

       130        140        150        160        170        180 
TKKKKKKQHK IPTNDELLYD PEKDNRDQAW VDAQRRGYHG LGPQRSRQQQ PVPNSDAVLN 

       190        200        210        220        230        240 
CPACMTTLCL DCQRHESYKT QYRAMFVMNC SINKEEVLRY KASENRKKRR VHKKMRSNRE 

       250        260        270        280 
DAAEKAETDV EEIYHPVMCT ECSTEVAVYD KDEVFHFFNV LASHS 

« Hide

References

« Hide 'large scale' references
[1]"Defining a holoprosencephaly locus on human chromosome 14q13 and characterization of potential candidate genes."
Kamnasaran D., Chen C.-P., Devriendt K., Mehta L., Cox D.W.
Genomics 85:608-621(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"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], FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH E2F1; E2F2 AND E2F3, VARIANT GLU-168.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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], VARIANT GLU-168.
Tissue: Cervix.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-109 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY157300 mRNA. Translation: AAO17041.1. Frameshift.
AY157301 mRNA. Translation: AAO17042.1. Frameshift.
AY869694 mRNA. Translation: AAX63200.1.
AF217512 mRNA. Translation: AAF67623.1. Frameshift.
AK000585 mRNA. Translation: BAA91271.1.
AL445363 Genomic DNA. No translation available.
BC001245 mRNA. Translation: AAH01245.1.
CCDSCCDS41941.1.
RefSeqNP_060923.2. NM_018453.3.
UniGeneHs.433269.

3D structure databases

ProteinModelPortalQ56P03.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120941. 6 interactions.
IntActQ56P03. 5 interactions.
MINTMINT-2874613.
STRING9606.ENSP00000250454.

PTM databases

PhosphoSiteQ56P03.

Polymorphism databases

DMDM296439474.

Proteomic databases

MaxQBQ56P03.
PaxDbQ56P03.
PRIDEQ56P03.

Protocols and materials databases

DNASU55837.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250454; ENSP00000250454; ENSG00000129518.
GeneID55837.
KEGGhsa:55837.
UCSCuc001wsd.1. human.

Organism-specific databases

CTD55837.
GeneCardsGC14M034985.
HGNCHGNC:19312. EAPP.
HPAHPA002916.
MIM609486. gene.
neXtProtNX_Q56P03.
PharmGKBPA162384208.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250977.
HOGENOMHOG000068005.
HOVERGENHBG054593.
InParanoidQ56P03.
OMARGHKKMR.
OrthoDBEOG7SR4ND.
PhylomeDBQ56P03.
TreeFamTF328497.

Gene expression databases

ArrayExpressQ56P03.
BgeeQ56P03.
CleanExHS_EAPP.
GenevestigatorQ56P03.

Family and domain databases

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

Other

GeneWikiEAPP.
GenomeRNAi55837.
NextBio61061.
PROQ56P03.
SOURCESearch...

Entry information

Entry nameEAPP_HUMAN
AccessionPrimary (citable) accession number: Q56P03
Secondary accession number(s): Q9BVF4, Q9NWV5, Q9NZ86
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 84 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM