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

 EI24_MOUSE              Reviewed;         340 AA.
Q61070; Q3T9X1; Q3TVX9; Q3UGS7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
30-AUG-2017, entry version 120.
RecName: Full=Etoposide-induced protein 2.4;
AltName: Full=p53-induced gene 8 protein;
Name=Ei24; Synonyms=Pig8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
TISSUE=Fibroblast;
PubMed=8649819;
Lehar S.M., Nacht M., Jacks T., Vater C.A., Chittenden T., Guild B.C.;
"Identification and cloning of EI24, a gene induced by p53 in
etoposide-treated cells.";
Oncogene 12:1181-1187(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
PubMed=10594026; DOI=10.1128/MCB.20.19.7109-7120.2000;
Gu Z., Flemington C., Chittenden T., Zambetti G.P.;
"ei24, a p53 response gene involved in growth suppression and
apoptosis.";
Mol. Cell. Biol. 20:233-241(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION, INTERACTION WITH BCL2, AND SUBCELLULAR LOCATION.
PubMed=15781622; DOI=10.1158/0008-5472.CAN-04-3377;
Zhao X., Ayer R.E., Davis S.L., Ames S.J., Florence B., Torchinsky C.,
Liou J.S., Shen L., Spanjaard R.A.;
"Apoptosis factor EI24/PIG8 is a novel endoplasmic reticulum-localized
Bcl-2-binding protein which is associated with suppression of breast
cancer invasiveness.";
Cancer Res. 65:2125-2129(2005).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-326 AND
SER-330, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts as a negative growth regulator via p53-mediated
apoptosis pathway. Regulates formation of degradative
autolysosomes during autophagy (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10594026, ECO:0000269|PubMed:15781622}.
-!- SUBUNIT: Interacts with BCL2. {ECO:0000269|PubMed:15781622}.
-!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:15781622};
Multi-pass membrane protein {ECO:0000269|PubMed:15781622}.
-!- TISSUE SPECIFICITY: Found in all the examined tissues. High
expression was found in liver, skeletal muscle, pancreas, kidney
heart and to a lesser extent in brain, placenta and lung.
-!- INDUCTION: By etoposide treatment, induction requires p53.
Etoposide induces DNA damage in cells by inhibiting DNA
topoisomerase II, and ultimately causes apoptotic cell death.
{ECO:0000269|PubMed:10594026, ECO:0000269|PubMed:8649819}.
-!- SIMILARITY: Belongs to the EI24 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC52483.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAE28130.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAE35489.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAE42899.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U41751; AAC52483.2; ALT_INIT; mRNA.
EMBL; AK147776; BAE28130.1; ALT_INIT; mRNA.
EMBL; AK159927; BAE35489.1; ALT_INIT; mRNA.
EMBL; AK172233; BAE42899.1; ALT_INIT; mRNA.
RefSeq; NP_001186423.1; NM_001199494.1.
RefSeq; NP_031941.1; NM_007915.5.
UniGene; Mm.4337; -.
ProteinModelPortal; Q61070; -.
iPTMnet; Q61070; -.
PhosphoSitePlus; Q61070; -.
EPD; Q61070; -.
MaxQB; Q61070; -.
PaxDb; Q61070; -.
PeptideAtlas; Q61070; -.
PRIDE; Q61070; -.
DNASU; 13663; -.
GeneID; 13663; -.
KEGG; mmu:13663; -.
UCSC; uc009oua.2; mouse.
CTD; 9538; -.
MGI; MGI:108090; Ei24.
eggNOG; KOG3966; Eukaryota.
eggNOG; ENOG410XRPU; LUCA.
HOGENOM; HOG000293197; -.
HOVERGEN; HBG001857; -.
InParanoid; Q61070; -.
KO; K10134; -.
PhylomeDB; Q61070; -.
TreeFam; TF314441; -.
ChiTaRS; Ei24; mouse.
PRO; PR:Q61070; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_EI24; -.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0006914; P:autophagy; IMP:MGI.
GO; GO:0071494; P:cellular response to UV-C; IGI:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
GO; GO:0030308; P:negative regulation of cell growth; ISS:MGI.
GO; GO:0042308; P:negative regulation of protein import into nucleus; IDA:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
InterPro; IPR009890; EI24.
PANTHER; PTHR21389; PTHR21389; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Autophagy; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O14681}.
CHAIN 2 340 Etoposide-induced protein 2.4.
/FTId=PRO_0000086946.
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}.
REGION 52 115 Interaction with BH3 domain of BCL2.
COMPBIAS 41 44 Poly-Arg.
COMPBIAS 316 320 Poly-Ser.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O14681}.
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:17208939}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 78 78 N -> D (in Ref. 3; BAE28130).
{ECO:0000305}.
CONFLICT 144 144 I -> F (in Ref. 3; BAE35489).
{ECO:0000305}.
CONFLICT 320 320 S -> P (in Ref. 3; BAE42899).
{ECO:0000305}.
SEQUENCE 340 AA; 38933 MW; AA3B824B2CE330BC CRC64;
MADSVKTFLQ DLGRGIKDSI WGICTISKLD ARIQQKREEQ RRRRASSLLA QRRPQSVERK
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 LQSALSSSSS AEKFPSPHPS PAKLKAAAGH


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