MIER1_MOUSE
ID MIER1_MOUSE Reviewed; 511 AA.
AC Q5UAK0; A1L3P9; B1AY29; B1AY34; Q5UAK1; Q5UAK2; Q5UAK3; Q6ZPL6; Q9D402;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Mesoderm induction early response protein 1;
DE Short=Early response 1;
DE Short=Er1;
DE Short=Mi-er1;
GN Name=Mier1; Synonyms=Kiaa1610;
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] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP AND FUNCTION.
RX PubMed=16147882; DOI=10.1080/10425170500069783;
RA Thorne L.B., Grant A.L., Paterno G.D., Gillespie L.L.;
RT "Cloning and characterization of the mouse ortholog of mi-er1.";
RL DNA Seq. 16:237-240(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, 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-159; SER-165; SER-376;
RP SER-482 AND SER-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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: Transcriptional repressor regulating the expression of a
CC number of genes including SP1 target genes. Probably functions through
CC recruitment of HDAC1 a histone deacetylase involved in chromatin
CC silencing. {ECO:0000269|PubMed:16147882}.
CC -!- SUBUNIT: Interacts with HDAC1. Part of a complex containing at least
CC CDYL, MIER1, MIER2, HDAC1 and HDAC2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=3; Synonyms=N3 beta;
CC IsoId=Q5UAK0-3; Sequence=Displayed;
CC Name=1; Synonyms=N4 beta;
CC IsoId=Q5UAK0-1; Sequence=VSP_042454;
CC Name=2; Synonyms=N1 beta;
CC IsoId=Q5UAK0-2; Sequence=VSP_016175;
CC Name=4; Synonyms=N2 beta;
CC IsoId=Q5UAK0-4; Sequence=VSP_016177;
CC Name=5;
CC IsoId=Q5UAK0-5; Sequence=VSP_016174;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is only expressed
CC in testis. {ECO:0000269|PubMed:16147882}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98215.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY769435; AAV37181.1; -; mRNA.
DR EMBL; AY769436; AAV37182.1; -; mRNA.
DR EMBL; AY769437; AAV37183.1; -; mRNA.
DR EMBL; AY769438; AAV37184.1; -; mRNA.
DR EMBL; AK129405; BAC98215.1; ALT_INIT; mRNA.
DR EMBL; AK016915; BAB30493.1; -; mRNA.
DR EMBL; AL844176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130227; AAI30228.1; -; mRNA.
DR CCDS; CCDS18408.1; -. [Q5UAK0-2]
DR CCDS; CCDS38825.1; -. [Q5UAK0-3]
DR CCDS; CCDS71432.1; -. [Q5UAK0-1]
DR RefSeq; NP_001034170.1; NM_001039081.2. [Q5UAK0-3]
DR RefSeq; NP_001273150.1; NM_001286221.1. [Q5UAK0-1]
DR RefSeq; NP_001273151.1; NM_001286222.1. [Q5UAK0-2]
DR RefSeq; NP_001273152.1; NM_001286223.1. [Q5UAK0-4]
DR RefSeq; NP_081972.2; NM_027696.3. [Q5UAK0-2]
DR RefSeq; XP_006503464.1; XM_006503401.3. [Q5UAK0-2]
DR RefSeq; XP_006503465.1; XM_006503402.1. [Q5UAK0-2]
DR AlphaFoldDB; Q5UAK0; -.
DR BioGRID; 214509; 4.
DR STRING; 10090.ENSMUSP00000102470; -.
DR iPTMnet; Q5UAK0; -.
DR PhosphoSitePlus; Q5UAK0; -.
DR EPD; Q5UAK0; -.
DR jPOST; Q5UAK0; -.
DR MaxQB; Q5UAK0; -.
DR PaxDb; Q5UAK0; -.
DR PeptideAtlas; Q5UAK0; -.
DR PRIDE; Q5UAK0; -.
DR ProteomicsDB; 292326; -. [Q5UAK0-3]
DR ProteomicsDB; 292327; -. [Q5UAK0-1]
DR ProteomicsDB; 292328; -. [Q5UAK0-2]
DR ProteomicsDB; 292329; -. [Q5UAK0-4]
DR ProteomicsDB; 292330; -. [Q5UAK0-5]
DR Antibodypedia; 9204; 111 antibodies from 20 providers.
DR DNASU; 71148; -.
DR Ensembl; ENSMUST00000030247; ENSMUSP00000030247; ENSMUSG00000028522. [Q5UAK0-2]
DR Ensembl; ENSMUST00000097945; ENSMUSP00000095558; ENSMUSG00000028522. [Q5UAK0-1]
DR Ensembl; ENSMUST00000106855; ENSMUSP00000102468; ENSMUSG00000028522. [Q5UAK0-5]
DR Ensembl; ENSMUST00000106857; ENSMUSP00000102470; ENSMUSG00000028522. [Q5UAK0-3]
DR Ensembl; ENSMUST00000106858; ENSMUSP00000102471; ENSMUSG00000028522. [Q5UAK0-2]
DR GeneID; 71148; -.
DR KEGG; mmu:71148; -.
DR UCSC; uc008txd.2; mouse. [Q5UAK0-2]
DR UCSC; uc008txf.2; mouse. [Q5UAK0-4]
DR UCSC; uc008txi.2; mouse. [Q5UAK0-3]
DR UCSC; uc012dhr.2; mouse. [Q5UAK0-1]
DR CTD; 57708; -.
DR MGI; MGI:1918398; Mier1.
DR VEuPathDB; HostDB:ENSMUSG00000028522; -.
DR eggNOG; KOG4329; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR HOGENOM; CLU_027202_1_0_1; -.
DR InParanoid; Q5UAK0; -.
DR OMA; TIDHMDA; -.
DR OrthoDB; 1062529at2759; -.
DR TreeFam; TF106453; -.
DR BioGRID-ORCS; 71148; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Mier1; mouse.
DR PRO; PR:Q5UAK0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q5UAK0; protein.
DR Bgee; ENSMUSG00000028522; Expressed in humerus cartilage element and 222 other tissues.
DR ExpressionAtlas; Q5UAK0; baseline and differential.
DR Genevisible; Q5UAK0; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR040138; MIER/MTA.
DR InterPro; IPR031169; MIER1.
DR InterPro; IPR045787; MIER1/3_C.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR PANTHER; PTHR10865; PTHR10865; 1.
DR PANTHER; PTHR10865:SF24; PTHR10865:SF24; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF19426; MIER1_beta_C; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..511
FT /note="Mesoderm induction early response protein 1"
FT /id="PRO_0000197142"
FT DOMAIN 179..277
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 282..334
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 154
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT VAR_SEQ 1..181
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016174"
FT VAR_SEQ 1..11
FT /note="MAEPSVESSSP -> MCIRCLCLIGLQTVSGFFSCQITSHLLSLQVQGEYKC
FT GLLCENTSLLIANVRRKVS (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:16147882"
FT /id="VSP_042454"
FT VAR_SEQ 1..3
FT /note="MAE -> MFMFNWFTDCLWILFLSNYK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16147882"
FT /id="VSP_016175"
FT VAR_SEQ 1..3
FT /note="MAE -> ML (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16147882"
FT /id="VSP_016177"
SQ SEQUENCE 511 AA; 57908 MW; 144FBD1A575A557F CRC64;
MAEPSVESSS PGGSATSEDH EFDPSADMLV HDFDDERTLE EEEMMEGETN FSSEIEDLAR
EGDMPIHELL SLYGYDSTVR LPEEEEEEEE EEEGEDDEDA DNDDNSGCSG ENKEENIKDS
SGQEDETQSS NDDPSQSVTS QDAQEIIRPR RCKYFDTNSE IEEESEEDED YIPSEDWKKE
IMVGSMFQAE IPVGVCRYKE NEKVYENDDQ LLWDPECLPE EKVVVFLKDA SRRTGDEKGV
EAIPEGSHIK DNEQALYELV KCSFDTEEAL RRLRFNVKAA REELSVWTEE ECRNFEQGLK
AYGKDFHLIQ ANKVRTRSVG ECVAFYYMWK KSERYDFFAQ QTRFGKKKYN LHPGVTDYMD
RLLDESESAA SSRAPSPPPT ASNSSNSQSE KEDGAVSSRN QNGVSSNGPG EILNKEEVKV
EGLHVNGPTG GNKKPLLTDM DTNGYEANNL TTDPKLAHMT ARNENDFDEK NERPAKRRRI
NSSGKESPGS SEFFQEAVSH GKFEEHENTN D
