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Etoposide-induced protein 2.4 homolog (p53-induced gene 8 protein)

 EI24_HUMAN              Reviewed;         340 AA.
O14681; A8K7D6; B4DKL6; Q9BUQ1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 4.
28-FEB-2018, entry version 137.
RecName: Full=Etoposide-induced protein 2.4 homolog;
AltName: Full=p53-induced gene 8 protein;
Name=EI24; Synonyms=PIG8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION BY TP53.
TISSUE=Colon cancer;
PubMed=9305847; DOI=10.1038/38525;
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
"A model for p53-induced apoptosis.";
Nature 389:300-306(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
POSSIBLE INVOLVEMENT IN BREAST CANCER, AND VARIANTS GLY-30; TRP-195;
ASP-196; TYR-197; HIS-199 AND ALA-319.
PubMed=11753653; DOI=10.1038/sj.onc.1204993;
Gentile M., Ahnstrom M., Schon F., Wingren S.;
"Candidate tumour suppressor genes at 11q23-q24 in breast cancer:
evidence of alterations in PIG8, a gene involved in p53-induced
apoptosis.";
Oncogene 20:7753-7760(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND SER-330, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
SUBCELLULAR LOCATION, AND POSSIBLE INVOLVEMENT IN CERVICAL CANCER.
PubMed=21154811; DOI=10.1002/ijc.25849;
Mazumder ' Indra ' D., Mitra S., Singh R.K., Dutta S., Roy A.,
Mondal R.K., Basu P.S., Roychoudhury S., Panda C.K.;
"Inactivation of CHEK1 and EI24 are associated with the development of
invasive cervical carcinoma: Clinical and prognostic implications.";
Int. J. Cancer 129:1859-1871(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Acts as a negative growth regulator via p53-mediated
apoptosis pathway. Regulates formation of degradative
autolysosomes during autophagy (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with BCL2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000269|PubMed:21154811}; Multi-pass membrane protein
{ECO:0000269|PubMed:21154811}. Cytoplasm
{ECO:0000269|PubMed:21154811}. Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14681-1; Sequence=Displayed;
Name=2;
IsoId=O14681-3; Sequence=VSP_055466;
Note=No experimental confirmation available.;
-!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:9305847}.
-!- DISEASE: Note=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.
-!- SIMILARITY: Belongs to the EI24 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC39531.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF010313; AAC39531.2; ALT_INIT; mRNA.
EMBL; AK291951; BAF84640.1; -; mRNA.
EMBL; AK296620; BAG59228.1; -; mRNA.
EMBL; AK315841; BAF98732.1; -; mRNA.
EMBL; CH471065; EAW67641.1; -; Genomic_DNA.
EMBL; BC002390; AAH02390.1; -; mRNA.
CCDS; CCDS73410.1; -. [O14681-1]
CCDS; CCDS76493.1; -. [O14681-3]
RefSeq; NP_001277064.1; NM_001290135.1. [O14681-3]
RefSeq; NP_004870.3; NM_004879.4. [O14681-1]
RefSeq; XP_011541371.1; XM_011543069.1. [O14681-1]
UniGene; Hs.643514; -.
ProteinModelPortal; O14681; -.
BioGrid; 114914; 4.
IntAct; O14681; 10.
MINT; O14681; -.
STRING; 9606.ENSP00000278903; -.
TCDB; 2.A.121.3.1; the sulfate transporter (cysz) family.
iPTMnet; O14681; -.
PhosphoSitePlus; O14681; -.
BioMuta; EI24; -.
EPD; O14681; -.
MaxQB; O14681; -.
PaxDb; O14681; -.
PeptideAtlas; O14681; -.
PRIDE; O14681; -.
DNASU; 9538; -.
Ensembl; ENST00000278903; ENSP00000278903; ENSG00000149547. [O14681-1]
Ensembl; ENST00000534546; ENSP00000479943; ENSG00000149547. [O14681-3]
Ensembl; ENST00000620753; ENSP00000484510; ENSG00000149547. [O14681-1]
GeneID; 9538; -.
KEGG; hsa:9538; -.
UCSC; uc031yiu.2; human. [O14681-1]
CTD; 9538; -.
DisGeNET; 9538; -.
EuPathDB; HostDB:ENSG00000149547.14; -.
GeneCards; EI24; -.
H-InvDB; HIX0010241; -.
HGNC; HGNC:13276; EI24.
HPA; HPA047165; -.
HPA; HPA051029; -.
MIM; 605170; gene.
neXtProt; NX_O14681; -.
OpenTargets; ENSG00000149547; -.
PharmGKB; PA134937367; -.
eggNOG; KOG3966; Eukaryota.
eggNOG; ENOG410XRPU; LUCA.
GeneTree; ENSGT00390000018633; -.
HOGENOM; HOG000293197; -.
HOVERGEN; HBG001857; -.
InParanoid; O14681; -.
KO; K10134; -.
OMA; VMIGIGE; -.
OrthoDB; EOG091G0E3F; -.
PhylomeDB; O14681; -.
TreeFam; TF314441; -.
ChiTaRS; EI24; human.
GeneWiki; EI24; -.
GenomeRNAi; 9538; -.
PRO; PR:O14681; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149547; -.
CleanEx; HS_EI24; -.
ExpressionAtlas; O14681; baseline and differential.
Genevisible; O14681; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
GO; GO:0030308; P:negative regulation of cell growth; IDA:MGI.
InterPro; IPR009890; EI24.
PANTHER; PTHR21389; PTHR21389; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Autophagy;
Complete proteome; Cytoplasm; Disease mutation; Endoplasmic reticulum;
Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 340 Etoposide-induced protein 2.4 homolog.
/FTId=PRO_0000086945.
TRANSMEM 77 97 Helical. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TRANSMEM 179 199 Helical. {ECO:0000255}.
TRANSMEM 238 255 Helical. {ECO:0000255}.
TRANSMEM 257 277 Helical. {ECO:0000255}.
COMPBIAS 41 44 Poly-Arg.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:Q4KM77}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:Q4KM77}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000250|UniProtKB:Q61070}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 15 28 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055466.
VARIANT 30 30 D -> G (in some patients with early onset
breast cancer).
{ECO:0000269|PubMed:11753653}.
/FTId=VAR_065459.
VARIANT 195 195 P -> W (in some patients with early onset
breast cancer; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:11753653}.
/FTId=VAR_065460.
VARIANT 196 196 I -> D (in some patients with early onset
breast cancer; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:11753653}.
/FTId=VAR_065461.
VARIANT 197 197 H -> Y (in some patients with early onset
breast cancer).
{ECO:0000269|PubMed:11753653}.
/FTId=VAR_065462.
VARIANT 199 199 V -> H (in some patients with early onset
breast cancer; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:11753653}.
/FTId=VAR_065463.
VARIANT 319 319 T -> A (in some patients with early onset
breast cancer; dbSNP:rs375652371).
{ECO:0000269|PubMed:11753653}.
/FTId=VAR_065464.
CONFLICT 54 54 A -> P (in Ref. 1; AAC39531).
{ECO:0000305}.
CONFLICT 119 119 E -> G (in Ref. 1; AAC39531).
{ECO:0000305}.
CONFLICT 129 129 L -> V (in Ref. 1; AAC39531).
{ECO:0000305}.
CONFLICT 132 132 L -> V (in Ref. 2; BAF84640).
{ECO:0000305}.
CONFLICT 254 254 A -> S (in Ref. 2; BAG59228).
{ECO:0000305}.
SEQUENCE 340 AA; 38965 MW; 928DB15D9B34146E CRC64;
MADSVKTFLQ DLARGIKDSI WGICTISKLD ARIQQKREEQ RRRRASSVLA QRRAQSIERK
QESEPRIVSR IFQCCAWNGG VFWFSLLLFY RVFIPVLQSV TARIIGDPSL HGDVWSWLEF
FLTSIFSALW VLPLFVLSKV VNAIWFQDIA DLAFEVSGRK PHPFPSVSKI IADMLFNLLL
QALFLIQGMF VSLFPIHLVG QLVSLLHMSL LYSLYCFEYR WFNKGIEMHQ RLSNIERNWP
YYFGFGLPLA FLTAMQSSYI ISGCLFSILF PLFIISANEA KTPGKAYLFQ LRLFSLVVFL
SNRLFHKTVY LQSALSSSTS AEKFPSPHPS PAKLKATAGH


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