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Protein

E2F-associated phosphoprotein

Gene

EAPP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

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
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
E2F-associated phosphoprotein
Short name:
EAPP
Gene namesi
Name:EAPP
Synonyms:C14orf11
ORF Names:BM-036
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:19312. EAPP.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384208.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285E2F-associated phosphoproteinPRO_0000086904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei17 – 171Phosphoserine1 Publication
Modified residuei37 – 371Phosphothreonine1 Publication
Modified residuei109 – 1091Phosphoserine5 Publications
Modified residuei111 – 1111Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ56P03.
PaxDbiQ56P03.
PRIDEiQ56P03.

PTM databases

PhosphoSiteiQ56P03.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

During the cell cycle, expression disappears during mitosis.

Gene expression databases

BgeeiQ56P03.
CleanExiHS_EAPP.
ExpressionAtlasiQ56P03. baseline and differential.
GenevestigatoriQ56P03.

Organism-specific databases

HPAiHPA002916.

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

Protein-protein interaction databases

BioGridi120941. 18 interactions.
IntActiQ56P03. 5 interactions.
MINTiMINT-2874613.
STRINGi9606.ENSP00000250454.

Structurei

3D structure databases

ProteinModelPortaliQ56P03.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 1276Poly-Lys

Phylogenomic databases

eggNOGiNOG250977.
GeneTreeiENSGT00390000001332.
HOGENOMiHOG000068005.
HOVERGENiHBG054593.
InParanoidiQ56P03.
OMAiRGHKKMR.
OrthoDBiEOG7SR4ND.
PhylomeDBiQ56P03.
TreeFamiTF328497.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q56P03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRLPDDYDP YAVEEPSDEE PALSSSEDEV DVLLHGTPDQ KRKLIRECLT
60 70 80 90 100
GESESSSEDE FEKEMEAELN STMKTMEDKL SSLGTGSSSG NGKVATAPTR
110 120 130 140 150
YYDDIYFDSD SEDEDRAVQV TKKKKKKQHK IPTNDELLYD PEKDNRDQAW
160 170 180 190 200
VDAQRRGYHG LGPQRSRQQQ PVPNSDAVLN CPACMTTLCL DCQRHESYKT
210 220 230 240 250
QYRAMFVMNC SINKEEVLRY KASENRKKRR VHKKMRSNRE DAAEKAETDV
260 270 280
EEIYHPVMCT ECSTEVAVYD KDEVFHFFNV LASHS
Length:285
Mass (Da):32,762
Last modified:May 18, 2010 - v4
Checksum:i1C0691602FFB516A
GO

Sequence cautioni

The sequence AAF67623.1 differs from that shown. Reason: Frameshift at positions 178, 189, 198 and 226. Curated
The sequence AAO17041.1 differs from that shown. Reason: Frameshift at positions 178, 189, 198 and 226. Curated
The sequence AAO17042.1 differs from that shown. Reason: Frameshift at positions 178, 189, 198 and 226. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31R → L in AAX63200 (PubMed:15716352).Curated
Sequence conflicti52 – 521E → G in BAA91271 (PubMed:14702039).Curated
Sequence conflicti239 – 2391R → Q in AAX63200 (PubMed:15716352).Curated
Sequence conflicti239 – 2391R → Q in AAH01245 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681Q → E.2 Publications
Corresponds to variant rs17856038 [ dbSNP | Ensembl ].
VAR_031915

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41941.1.
RefSeqiNP_060923.2. NM_018453.3.
UniGeneiHs.433269.

Genome annotation databases

EnsembliENST00000250454; ENSP00000250454; ENSG00000129518.
GeneIDi55837.
KEGGihsa:55837.
UCSCiuc001wsd.1. human.

Polymorphism databases

DMDMi296439474.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41941.1.
RefSeqiNP_060923.2. NM_018453.3.
UniGeneiHs.433269.

3D structure databases

ProteinModelPortaliQ56P03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120941. 18 interactions.
IntActiQ56P03. 5 interactions.
MINTiMINT-2874613.
STRINGi9606.ENSP00000250454.

PTM databases

PhosphoSiteiQ56P03.

Polymorphism databases

DMDMi296439474.

Proteomic databases

MaxQBiQ56P03.
PaxDbiQ56P03.
PRIDEiQ56P03.

Protocols and materials databases

DNASUi55837.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250454; ENSP00000250454; ENSG00000129518.
GeneIDi55837.
KEGGihsa:55837.
UCSCiuc001wsd.1. human.

Organism-specific databases

CTDi55837.
GeneCardsiGC14M034985.
HGNCiHGNC:19312. EAPP.
HPAiHPA002916.
MIMi609486. gene.
neXtProtiNX_Q56P03.
PharmGKBiPA162384208.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250977.
GeneTreeiENSGT00390000001332.
HOGENOMiHOG000068005.
HOVERGENiHBG054593.
InParanoidiQ56P03.
OMAiRGHKKMR.
OrthoDBiEOG7SR4ND.
PhylomeDBiQ56P03.
TreeFamiTF328497.

Miscellaneous databases

ChiTaRSiEAPP. human.
GeneWikiiEAPP.
GenomeRNAii55837.
NextBioi61061.
PROiQ56P03.
SOURCEiSearch...

Gene expression databases

BgeeiQ56P03.
CleanExiHS_EAPP.
ExpressionAtlasiQ56P03. baseline and differential.
GenevestigatoriQ56P03.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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. 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].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; SER-109 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEAPP_HUMAN
AccessioniPrimary (citable) accession number: Q56P03
Secondary accession number(s): Q9BVF4, Q9NWV5, Q9NZ86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 18, 2010
Last modified: March 4, 2015
This is version 90 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) 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.