EI24_MOUSE
ID EI24_MOUSE Reviewed; 340 AA.
AC Q61070; Q3T9X1; Q3TVX9; Q3UGS7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Etoposide-induced protein 2.4;
DE AltName: Full=p53-induced gene 8 protein;
GN Name=Ei24; Synonyms=Pig8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Fibroblast;
RX PubMed=8649819;
RA Lehar S.M., Nacht M., Jacks T., Vater C.A., Chittenden T., Guild B.C.;
RT "Identification and cloning of EI24, a gene induced by p53 in etoposide-
RT treated cells.";
RL Oncogene 12:1181-1187(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX PubMed=10594026; DOI=10.1128/mcb.20.1.233-241.2000;
RA Gu Z., Flemington C., Chittenden T., Zambetti G.P.;
RT "ei24, a p53 response gene involved in growth suppression and apoptosis.";
RL Mol. Cell. Biol. 20:233-241(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, INTERACTION WITH BCL2, AND SUBCELLULAR LOCATION.
RX PubMed=15781622; DOI=10.1158/0008-5472.can-04-3377;
RA Zhao X., Ayer R.E., Davis S.L., Ames S.J., Florence B., Torchinsky C.,
RA Liou J.S., Shen L., Spanjaard R.A.;
RT "Apoptosis factor EI24/PIG8 is a novel endoplasmic reticulum-localized Bcl-
RT 2-binding protein which is associated with suppression of breast cancer
RT invasiveness.";
RL Cancer Res. 65:2125-2129(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-326 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a negative growth regulator via p53-mediated
CC apoptosis pathway. Regulates formation of degradative autolysosomes
CC during autophagy (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10594026, ECO:0000269|PubMed:15781622}.
CC -!- SUBUNIT: Interacts with BCL2. {ECO:0000269|PubMed:15781622}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:15781622}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:15781622}.
CC -!- TISSUE SPECIFICITY: Found in all the examined tissues. High expression
CC was found in liver, skeletal muscle, pancreas, kidney heart and to a
CC lesser extent in brain, placenta and lung.
CC -!- INDUCTION: By etoposide treatment, induction requires p53. Etoposide
CC induces DNA damage in cells by inhibiting DNA topoisomerase II, and
CC ultimately causes apoptotic cell death. {ECO:0000269|PubMed:10594026,
CC ECO:0000269|PubMed:8649819}.
CC -!- SIMILARITY: Belongs to the EI24 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52483.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE28130.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE35489.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE42899.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U41751; AAC52483.2; ALT_INIT; mRNA.
DR EMBL; AK147776; BAE28130.1; ALT_INIT; mRNA.
DR EMBL; AK159927; BAE35489.1; ALT_INIT; mRNA.
DR EMBL; AK172233; BAE42899.1; ALT_INIT; mRNA.
DR CCDS; CCDS22973.2; -.
DR RefSeq; NP_001186423.1; NM_001199494.1.
DR RefSeq; NP_031941.1; NM_007915.5.
DR AlphaFoldDB; Q61070; -.
DR BioGRID; 199410; 2.
DR STRING; 10090.ENSMUSP00000132270; -.
DR iPTMnet; Q61070; -.
DR PhosphoSitePlus; Q61070; -.
DR EPD; Q61070; -.
DR jPOST; Q61070; -.
DR MaxQB; Q61070; -.
DR PaxDb; Q61070; -.
DR PeptideAtlas; Q61070; -.
DR PRIDE; Q61070; -.
DR ProteomicsDB; 277838; -.
DR Antibodypedia; 32951; 177 antibodies from 31 providers.
DR DNASU; 13663; -.
DR Ensembl; ENSMUST00000163192; ENSMUSP00000132270; ENSMUSG00000062762.
DR Ensembl; ENSMUST00000238932; ENSMUSP00000159090; ENSMUSG00000062762.
DR GeneID; 13663; -.
DR KEGG; mmu:13663; -.
DR UCSC; uc009oua.2; mouse.
DR CTD; 9538; -.
DR MGI; MGI:108090; Ei24.
DR VEuPathDB; HostDB:ENSMUSG00000062762; -.
DR eggNOG; KOG3966; Eukaryota.
DR GeneTree; ENSGT00390000018633; -.
DR InParanoid; Q61070; -.
DR OMA; QCCALNG; -.
DR OrthoDB; 889537at2759; -.
DR PhylomeDB; Q61070; -.
DR TreeFam; TF314441; -.
DR BioGRID-ORCS; 13663; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Ei24; mouse.
DR PRO; PR:Q61070; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q61070; protein.
DR Bgee; ENSMUSG00000062762; Expressed in cleaving embryo and 254 other tissues.
DR ExpressionAtlas; Q61070; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IMP:MGI.
DR GO; GO:0071494; P:cellular response to UV-C; IGI:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:MGI.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IDA:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR InterPro; IPR009890; EI24.
DR PANTHER; PTHR21389; PTHR21389; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Autophagy; Cytoplasm; Endoplasmic reticulum;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14681"
FT CHAIN 2..340
FT /note="Etoposide-induced protein 2.4"
FT /id="PRO_0000086946"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 52..115
FT /note="Interaction with BH3 domain of BCL2"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O14681"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KM77"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KM77"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 78
FT /note="N -> D (in Ref. 3; BAE28130)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="I -> F (in Ref. 3; BAE35489)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="S -> P (in Ref. 3; BAE42899)"
FT /evidence="ECO:0000305"
SQ 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
