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O14681 (EI24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Etoposide-induced protein 2.4 homolog
Alternative name(s):
p53-induced gene 8 protein
Gene names
Name:EI24
Synonyms:PIG8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy By similarity.

Subunit structure

Interacts with BCL2 By similarity.

Subcellular location

Nucleus membrane; Multi-pass membrane protein. Cytoplasm. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.12.

Induction

By p53/TP53. Ref.1

Involvement in disease

EI24 is on a chromosomal region frequently deleted in solid tumors, and it is thought to play a role in breast and cervical cancer. Particularly, expression analysis of EI24 in cancerous tissues shows that EI24 loss is associated with tumor invasiveness.

Sequence similarities

Belongs to the EI24 family.

Sequence caution

The sequence AAC39531.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 340339Etoposide-induced protein 2.4 homolog
PRO_0000086945

Regions

Transmembrane77 – 9721Helical; Potential
Transmembrane117 – 13721Helical; Potential
Transmembrane179 – 19921Helical; Potential
Transmembrane238 – 25518Helical; Potential
Transmembrane257 – 27721Helical; Potential
Compositional bias41 – 444Poly-Arg

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue561Phosphoserine Ref.6 Ref.10
Modified residue3261Phosphoserine Ref.7 Ref.8
Modified residue3301Phosphoserine Ref.8

Natural variations

Natural variant301D → G in some patients with early onset breast cancer. Ref.5
VAR_065459
Natural variant1951P → W in some patients with early onset breast cancer; requires 2 nucleotide substitutions. Ref.5
VAR_065460
Natural variant1961I → D in some patients with early onset breast cancer; requires 2 nucleotide substitutions. Ref.5
VAR_065461
Natural variant1971H → Y in some patients with early onset breast cancer. Ref.5
VAR_065462
Natural variant1991V → H in some patients with early onset breast cancer; requires 2 nucleotide substitutions. Ref.5
VAR_065463
Natural variant3191T → A in some patients with early onset breast cancer. Ref.5
VAR_065464

Experimental info

Sequence conflict541A → P in AAC39531. Ref.1
Sequence conflict1191E → G in AAC39531. Ref.1
Sequence conflict1291L → V in AAC39531. Ref.1
Sequence conflict1321L → V in BAF84640. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O14681 [UniParc].

Last modified May 5, 2009. Version 4.
Checksum: 928DB15D9B34146E

FASTA34038,965
        10         20         30         40         50         60 
MADSVKTFLQ DLARGIKDSI WGICTISKLD ARIQQKREEQ RRRRASSVLA QRRAQSIERK 

        70         80         90        100        110        120 
QESEPRIVSR IFQCCAWNGG VFWFSLLLFY RVFIPVLQSV TARIIGDPSL HGDVWSWLEF 

       130        140        150        160        170        180 
FLTSIFSALW VLPLFVLSKV VNAIWFQDIA DLAFEVSGRK PHPFPSVSKI IADMLFNLLL 

       190        200        210        220        230        240 
QALFLIQGMF VSLFPIHLVG QLVSLLHMSL LYSLYCFEYR WFNKGIEMHQ RLSNIERNWP 

       250        260        270        280        290        300 
YYFGFGLPLA FLTAMQSSYI ISGCLFSILF PLFIISANEA KTPGKAYLFQ LRLFSLVVFL 

       310        320        330        340 
SNRLFHKTVY LQSALSSSTS AEKFPSPHPS PAKLKATAGH 

« Hide

References

« Hide 'large scale' references
[1]"A model for p53-induced apoptosis."
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.
Nature 389:300-306(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY TP53.
Tissue: Colon cancer.
[2]"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].
Tissue: Synovium.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Lung.
[5]"Candidate tumour suppressor genes at 11q23-q24 in breast cancer: evidence of alterations in PIG8, a gene involved in p53-induced apoptosis."
Gentile M., Ahnstrom M., Schon F., Wingren S.
Oncogene 20:7753-7760(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN BREAST CANCER, VARIANTS GLY-30; TRP-195; ASP-196; TYR-197; HIS-199 AND ALA-319.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-326 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Inactivation of CHEK1 and EI24 are associated with the development of invasive cervical carcinoma: Clinical and prognostic implications."
Mazumder ' Indra ' D., Mitra S., Singh R.K., Dutta S., Roy A., Mondal R.K., Basu P.S., Roychoudhury S., Panda C.K.
Int. J. Cancer 129:1859-1871(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, POSSIBLE INVOLVEMENT IN CERVICAL CANCER.
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF010313 mRNA. Translation: AAC39531.2. Different initiation.
AK291951 mRNA. Translation: BAF84640.1.
AK315841 mRNA. Translation: BAF98732.1.
CH471065 Genomic DNA. Translation: EAW67641.1.
BC002390 mRNA. Translation: AAH02390.1.
RefSeqNP_001007278.1. NM_001007277.1.
NP_004870.3. NM_004879.3.
UniGeneHs.643514.

3D structure databases

ProteinModelPortalO14681.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114914. 2 interactions.
IntActO14681. 2 interactions.
STRING9606.ENSP00000278903.

Protein family/group databases

TCDB9.B.7.3.1. the putative sulfate transporter (cysz) family.

PTM databases

PhosphoSiteO14681.

Proteomic databases

PaxDbO14681.
PRIDEO14681.

Protocols and materials databases

DNASU9538.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278903; ENSP00000278903; ENSG00000149547.
GeneID9538.
KEGGhsa:9538.
UCSCuc001qca.3. human.

Organism-specific databases

CTD9538.
GeneCardsGC11P125441.
H-InvDBHIX0010241.
HGNCHGNC:13276. EI24.
HPAHPA047165.
MIM605170. gene.
neXtProtNX_O14681.
PharmGKBPA134937367.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266932.
HOGENOMHOG000293197.
HOVERGENHBG001857.
InParanoidO14681.
KOK10134.
PhylomeDBO14681.
TreeFamTF314441.

Gene expression databases

ArrayExpressO14681.
BgeeO14681.
CleanExHS_EI24.
GenevestigatorO14681.

Family and domain databases

InterProIPR009890. EI24.
[Graphical view]
PANTHERPTHR21389. PTHR21389. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEI24. human.
GeneWikiEI24.
GenomeRNAi9538.
NextBio35764.
PROO14681.
SOURCESearch...

Entry information

Entry nameEI24_HUMAN
AccessionPrimary (citable) accession number: O14681
Secondary accession number(s): A8K7D6, Q9BUQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 109 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

SIMILARITY comments

Index of protein domains and families

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 11

Human chromosome 11: entries, gene names and cross-references to MIM