IER2_MOUSE
ID IER2_MOUSE Reviewed; 221 AA.
AC P17950; Q3TD12; Q64251; Q8BME8; Q99M25;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Immediate early response gene 2 protein;
DE AltName: Full=CHX1;
DE AltName: Full=Cycloheximide-induced gene protein;
DE AltName: Full=Growth factor-inducible immediate early protein;
DE AltName: Full=Proline-rich-induced protein 92;
DE Short=Pip92;
DE AltName: Full=T-lymphocyte-activated protein;
GN Name=Ier2;
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.
RX PubMed=2308934; DOI=10.1073/pnas.87.5.1753;
RA Coleclough C., Kuhn L., Lefkovits I.;
RT "Regulation of mRNA abundance in activated T lymphocytes: identification of
RT mRNA species affected by the inhibition of protein synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1753-1757(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=2247083; DOI=10.1128/mcb.10.12.6769-6774.1990;
RA Charles C.H., Simske J.S., O'Brien T.P., Lau L.F.;
RT "Pip92: a short-lived, growth factor-inducible protein in BALB/c 3T3 and
RT PC12 cells.";
RL Mol. Cell. Biol. 10:6769-6774(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=8083220; DOI=10.1016/s0021-9258(17)31634-4;
RA Latinkic B.V., Lau L.F.;
RT "Transcriptional activation of the immediate early gene pip92 by serum
RT growth factors requires both Ets and CArG-like elements.";
RL J. Biol. Chem. 269:23163-23170(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Wolffian duct;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: DNA-binding protein that seems to act as a transcription
CC factor (By similarity). Involved in the regulation of neuronal
CC differentiation, acts upon JNK-signaling pathway activation and plays a
CC role in neurite outgrowth in hippocampal cells (By similarity). May
CC mediate with FIBP FGF-signaling in the establishment of laterality in
CC the embryo (By similarity). Promotes cell motility, seems to stimulate
CC tumor metastasis (By similarity). {ECO:0000250|UniProtKB:B7SXM5,
CC ECO:0000250|UniProtKB:Q6P7D3, ECO:0000250|UniProtKB:Q9BTL4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BTL4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BTL4}. Note=Cytoplasmic during quiescence,
CC translocates to the nucleus upon stimulation.
CC {ECO:0000250|UniProtKB:Q9BTL4}.
CC -!- INDUCTION: By growth factors and cycloheximide.
CC {ECO:0000269|PubMed:2247083, ECO:0000269|PubMed:2308934}.
CC -!- SIMILARITY: Belongs to the IER family. {ECO:0000305}.
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DR EMBL; M31042; AAA40059.1; -; mRNA.
DR EMBL; M59821; AAA39931.1; -; mRNA.
DR EMBL; L26490; AAB00120.1; -; Genomic_DNA.
DR EMBL; AK032692; BAC27990.1; -; mRNA.
DR EMBL; AK144601; BAE25960.1; -; mRNA.
DR EMBL; AK170433; BAE41793.1; -; mRNA.
DR EMBL; AC145556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002067; AAH02067.1; -; mRNA.
DR CCDS; CCDS22474.1; -.
DR PIR; A54722; A36370.
DR RefSeq; NP_034629.3; NM_010499.4.
DR AlphaFoldDB; P17950; -.
DR SMR; P17950; -.
DR STRING; 10090.ENSMUSP00000060275; -.
DR iPTMnet; P17950; -.
DR PhosphoSitePlus; P17950; -.
DR PaxDb; P17950; -.
DR PRIDE; P17950; -.
DR ProteomicsDB; 267090; -.
DR Antibodypedia; 13536; 124 antibodies from 22 providers.
DR Ensembl; ENSMUST00000060427; ENSMUSP00000060275; ENSMUSG00000053560.
DR GeneID; 15936; -.
DR KEGG; mmu:15936; -.
DR UCSC; uc009mmr.2; mouse.
DR CTD; 9592; -.
DR MGI; MGI:104815; Ier2.
DR VEuPathDB; HostDB:ENSMUSG00000053560; -.
DR eggNOG; ENOG502S19F; Eukaryota.
DR GeneTree; ENSGT00900000141021; -.
DR HOGENOM; CLU_1234685_0_0_1; -.
DR InParanoid; P17950; -.
DR OMA; MVMRSAR; -.
DR OrthoDB; 1503216at2759; -.
DR PhylomeDB; P17950; -.
DR TreeFam; TF331376; -.
DR BioGRID-ORCS; 15936; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Ier2; mouse.
DR PRO; PR:P17950; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P17950; protein.
DR Bgee; ENSMUSG00000053560; Expressed in granulocyte and 230 other tissues.
DR Genevisible; P17950; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0071774; P:response to fibroblast growth factor; ISS:UniProtKB.
DR InterPro; IPR008653; IER.
DR PANTHER; PTHR15895; PTHR15895; 1.
DR Pfam; PF05760; IER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..221
FT /note="Immediate early response gene 2 protein"
FT /id="PRO_0000190436"
FT REGION 105..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTL4"
FT CONFLICT 27
FT /note="G -> D (in Ref. 1; AAA40059)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="V -> L (in Ref. 1; AAA40059, 2; AAA39931 and 3;
FT AAB00120)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="F -> S (in Ref. 1; AAA40059)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> D (in Ref. 4; BAC27990)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="E -> G (in Ref. 4; BAC27990)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="G -> S (in Ref. 1; AAA40059, 2; AAA39931 and 3;
FT AAB00120)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="L -> F (in Ref. 4; BAC27990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 24459 MW; 661D2E167EC5D081 CRC64;
MEVQKEAQRI MTLSVWKMYH SRMQRGGLRL HRSLQLSLVM RSAREVYLSA KVEAHQPEFP
PSRRALDPRL HPPREAEVAV EVASPEAVQP PEPMDTQEEV LRVQETPALC DPPPARVSRK
RRSSSDLSDG SDAGLVPSKK ARLEEVEGEA TSEVPDRLQL PPAQSEGAFP NLARVLQRRF
SSLLNCGPAV PPPTPPTCEA KPACRPADNM LNVLVRAVVA F
