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Radiation-inducible immediate-early gene IEX-1 (Differentiation-dependent gene 2 protein) (Protein DIF-2) (Immediate early protein GLY96) (Immediate early response 3 protein) (PACAP-responsive gene 1 protein) (Protein PRG1)

 IEX1_HUMAN              Reviewed;         156 AA.
P46695; Q5SU30; Q92691; Q93044;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
27-SEP-2017, entry version 145.
RecName: Full=Radiation-inducible immediate-early gene IEX-1;
AltName: Full=Differentiation-dependent gene 2 protein;
Short=Protein DIF-2;
AltName: Full=Immediate early protein GLY96;
AltName: Full=Immediate early response 3 protein;
AltName: Full=PACAP-responsive gene 1 protein;
Short=Protein PRG1;
Name=IER3; Synonyms=DIF2, IEX1, PRG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-127.
TISSUE=Placenta;
PubMed=8603392;
Kondratyev A.D., Chung K.-N., Jung M.O.;
"Identification and characterization of a radiation-inducible
glycosylated human early-response gene.";
Cancer Res. 56:1498-1502(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-127.
PubMed=8653710;
Schaefer H., Trauzold A., Siegel E.G., Folsch U.R., Schmidt W.E.;
"PRG1: a novel early-response gene transcriptionally induced by
pituitary adenylate cyclase activating polypeptide in a pancreatic
carcinoma cell line.";
Cancer Res. 56:2641-2648(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-127.
PubMed=9196025; DOI=10.1006/bbrc.1997.6715;
Pietzsch A., Buechler C., Aslanidis C., Schmitz G.;
"Identification and characterization of a novel monocyte/macrophage
differentiation-dependent gene that is responsive to
lipopolysaccharide, ceramide, and lysophosphatidylcholine.";
Biochem. Biophys. Res. Commun. 235:4-9(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-127.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-127.
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-127.
TISSUE=Cervix, and Skin;
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).
[8]
PHOSPHORYLATION AT THR-18; THR-123 AND SER-126, INTERACTION WITH
MAPK1/ERK2, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=12356731; DOI=10.1093/emboj/cdf488;
Garcia J., Ye Y., Arranz V., Letourneux C., Pezeron G., Porteu F.;
"IEX-1: a new ERK substrate involved in both ERK survival activity and
ERK activation.";
EMBO J. 21:5151-5163(2002).
[9]
FUNCTION, AND INTERACTION WITH PPP2R5C AND PPP2CA.
PubMed=16456541; DOI=10.1038/sj.emboj.7600980;
Letourneux C., Rocher G., Porteu F.;
"B56-containing PP2A dephosphorylate ERK and their activity is
controlled by the early gene IEX-1 and ERK.";
EMBO J. 25:727-738(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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).
[11]
FUNCTION, AND INDUCTION BY NUPR1.
PubMed=22565310; DOI=10.1172/JCI60144;
Hamidi T., Algul H., Cano C.E., Sandi M.J., Molejon M.I., Riemann M.,
Calvo E.L., Lomberk G., Dagorn J.C., Weih F., Urrutia R., Schmid R.M.,
Iovanna J.L.;
"Nuclear protein 1 promotes pancreatic cancer development and protects
cells from stress by inhibiting apoptosis.";
J. Clin. Invest. 122:2092-2103(2012).
-!- FUNCTION: May play a role in the ERK signaling pathway by
inhibiting the dephosphorylation of ERK by phosphatase PP2A-
PPP2R5C holoenzyme. Acts also as an ERK downstream effector
mediating survival. As a member of the NUPR1/RELB/IER3 survival
pathway, may provide pancreatic ductal adenocarcinoma with
remarkable resistance to cell stress, such as starvation or
gemcitabine treatment. {ECO:0000269|PubMed:12356731,
ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:22565310}.
-!- SUBUNIT: Interacts with the PPP2R5C-PP2A holoenzyme and ERK
kinases; regulates ERK dephosphorylation.
{ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:16456541}.
-!- INTERACTION:
P49069:CAMLG; NbExp=2; IntAct=EBI-1748945, EBI-1748958;
P67775:PPP2CA; NbExp=2; IntAct=EBI-1748945, EBI-712311;
Q15173:PPP2R5B; NbExp=4; IntAct=EBI-1748945, EBI-1369497;
Q13362:PPP2R5C; NbExp=2; IntAct=EBI-1748945, EBI-1266156;
Q04206:RELA; NbExp=6; IntAct=EBI-1748945, EBI-73886;
O43765:SGTA; NbExp=4; IntAct=EBI-1748945, EBI-347996;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12356731};
Single-pass type II membrane protein
{ECO:0000269|PubMed:12356731}.
-!- INDUCTION: By radiation, 12-O-tetradecanoyl phorbol-13 acetate
(TPA), okadaic acid, TNF and NUPR1. {ECO:0000269|PubMed:22565310}.
-!- PTM: Phosphorylated at Thr-18, Thr-123 and Ser-126 by MAPK1/ERK2
and probably MAPK3/ERK1. Upon phosphorylation by MAPK1/ERK2 and
MAPK3/ERK1, acquires the ability to inhibit cell death induced by
various stimuli. {ECO:0000269|PubMed:12356731}.
-!- PTM: Glycosylated.
-!- SIMILARITY: Belongs to the IER3 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IER3ID40919ch6p21.html";
-----------------------------------------------------------------------
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EMBL; S81914; AAB36278.1; -; mRNA.
EMBL; X96438; CAA65304.1; -; Genomic_DNA.
EMBL; Y14551; CAA74886.1; -; mRNA.
EMBL; BT006703; AAP35349.1; -; mRNA.
EMBL; BA000025; BAB63319.1; -; Genomic_DNA.
EMBL; AL662797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000844; AAH00844.1; -; mRNA.
EMBL; BC005080; AAH05080.1; -; mRNA.
CCDS; CCDS4689.1; -.
PIR; JC5537; JC5537.
RefSeq; NP_003888.2; NM_003897.3.
UniGene; Hs.730861; -.
UniGene; Hs.76095; -.
ProteinModelPortal; P46695; -.
BioGrid; 114390; 10.
IntAct; P46695; 13.
MINT; MINT-2835388; -.
STRING; 9606.ENSP00000259874; -.
iPTMnet; P46695; -.
PhosphoSitePlus; P46695; -.
BioMuta; IER3; -.
DMDM; 317373569; -.
PaxDb; P46695; -.
PeptideAtlas; P46695; -.
PRIDE; P46695; -.
DNASU; 8870; -.
Ensembl; ENST00000259874; ENSP00000259874; ENSG00000137331.
Ensembl; ENST00000383560; ENSP00000373054; ENSG00000206478.
Ensembl; ENST00000416884; ENSP00000406245; ENSG00000227231.
Ensembl; ENST00000435856; ENSP00000412283; ENSG00000235030.
Ensembl; ENST00000439190; ENSP00000397956; ENSG00000237155.
Ensembl; ENST00000450236; ENSP00000398139; ENSG00000230128.
GeneID; 8870; -.
KEGG; hsa:8870; -.
UCSC; uc003nrn.4; human.
CTD; 8870; -.
DisGeNET; 8870; -.
EuPathDB; HostDB:ENSG00000137331.11; -.
GeneCards; IER3; -.
HGNC; HGNC:5392; IER3.
HPA; HPA043847; -.
MIM; 602996; gene.
neXtProt; NX_P46695; -.
OpenTargets; ENSG00000137331; -.
PharmGKB; PA29639; -.
eggNOG; ENOG410IZ8Q; Eukaryota.
eggNOG; ENOG410Z2E4; LUCA.
GeneTree; ENSGT00390000003213; -.
HOGENOM; HOG000113001; -.
HOVERGEN; HBG000172; -.
InParanoid; P46695; -.
OMA; FCQILMA; -.
OrthoDB; EOG091G0UO1; -.
PhylomeDB; P46695; -.
TreeFam; TF338252; -.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SIGNOR; P46695; -.
ChiTaRS; IER3; human.
GeneWiki; IER3; -.
GenomeRNAi; 8870; -.
PRO; PR:P46695; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000137331; -.
CleanEx; HS_IER3; -.
ExpressionAtlas; P46695; baseline and differential.
Genevisible; P46695; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:0010941; P:regulation of cell death; IBA:GO_Central.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:MGI.
InterPro; IPR024829; IEX-1.
PANTHER; PTHR16915; PTHR16915; 1.
PRINTS; PR02100; GENEIEX1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 156 Radiation-inducible immediate-early gene
IEX-1.
/FTId=PRO_0000084159.
TOPO_DOM 1 82 Cytoplasmic. {ECO:0000255}.
TRANSMEM 83 99 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 100 156 Extracellular. {ECO:0000255}.
MOD_RES 18 18 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:12356731}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 123 123 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:12356731}.
MOD_RES 126 126 Phosphoserine; by MAPK1.
{ECO:0000269|PubMed:12356731}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 127 127 A -> P (in dbSNP:rs3094124).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8603392,
ECO:0000269|PubMed:8653710,
ECO:0000269|PubMed:9196025,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_058496.
CONFLICT 54 54 A -> G (in Ref. 1; AAB36278).
{ECO:0000305}.
CONFLICT 106 106 P -> R (in Ref. 1; AAB36278).
{ECO:0000305}.
SEQUENCE 156 AA; 16903 MW; 83C06116C81B8341 CRC64;
MCHSRSCHPT MTILQAPTPA PSTIPGPRRG SGPEIFTFDP LPEPAAAPAG RPSASRGHRK
RSRRVLYPRV VRRQLPVEEP NPAKRLLFLL LTIVFCQILM AEEGVPAPLP PEDAPNAASL
APTPVSAVLE PFNLTSEPSD YALDLSTFLQ QHPAAF


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