MIER1_HUMAN
ID MIER1_HUMAN Reviewed; 512 AA.
AC Q8N108; C9JFD4; Q08AE0; Q32NC4; Q5T104; Q5TAD1; Q5TAD2; Q5TAD4; Q5TAD5;
AC Q6AHY8; Q86TB4; Q8N156; Q8N161; Q8NC37; Q8NES4; Q8NES5; Q8NES6; Q8WWG2;
AC Q9HCG2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Mesoderm induction early response protein 1;
DE Short=Early response 1;
DE Short=Er1;
DE Short=Mi-er1;
DE Short=hMi-er1;
GN Name=MIER1; Synonyms=KIAA1610;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12242014; DOI=10.1016/s0378-1119(02)00823-5;
RA Paterno G.D., Ding Z., Yew Y.-Y., Nash G.W., Mercer F.C., Gillespie L.L.;
RT "Genomic organization of the human mi-er1 gene and characterization of
RT alternatively spliced isoforms: regulated use of a facultative intron
RT determines subcellular localization.";
RL Gene 295:79-88(2002).
RN [2]
RP SEQUENCE REVISION.
RA Paterno G.D., Ding Z., Lew Y.Y., Nash G.W., Mercer F.C., Gillespie L.L.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-204 (ISOFORMS 1/6).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
RC TISSUE=Retina, and Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8; 9 AND 10), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-199 (ISOFORMS 1/6).
RC TISSUE=Lung, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-512 (ISOFORMS 1/2/3/7).
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [9]
RP FUNCTION, INTERACTION WITH HDAC1, AND MUTAGENESIS OF TRP-214 AND
RP 227-PHE--LEU-228.
RX PubMed=12482978; DOI=10.1128/mcb.23.1.250-258.2003;
RA Ding Z., Gillespie L.L., Paterno G.D.;
RT "Human MI-ER1 alpha and beta function as transcriptional repressors by
RT recruitment of histone deacetylase 1 to their conserved ELM2 domain.";
RL Mol. Cell. Biol. 23:250-258(2003).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=9813250; DOI=10.1016/s0378-1119(98)00473-9;
RA Paterno G.D., Mercer F.C., Chayter J.J., Yang X., Robb J.D.,
RA Gillespie L.L.;
RT "Molecular cloning of human er1 cDNA and its differential expression in
RT breast tumours and tumour-derived cell lines.";
RL Gene 222:77-82(1998).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH CDYL; MIER2; HDAC1 AND HDAC2.
RX PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
RA Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E.,
RA Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.;
RT "CDYL bridges REST and histone methyltransferases for gene repression and
RT suppression of cellular transformation.";
RL Mol. Cell 32:718-726(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155; SER-160; SER-166;
RP SER-483 AND SER-488, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-166; SER-483 AND
RP SER-488, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-367; SER-369;
RP SER-377; THR-448; SER-483; SER-488 AND SER-491, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-377, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-420, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-420, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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:12482978}.
CC -!- SUBUNIT: Interacts with HDAC1. Part of a complex containing at least
CC CDYL, MIER1, MIER2, HDAC1 and HDAC2. {ECO:0000269|PubMed:12482978,
CC ECO:0000269|PubMed:19061646}.
CC -!- INTERACTION:
CC Q8N108; Q13547: HDAC1; NbExp=8; IntAct=EBI-3504940, EBI-301834;
CC Q8N108-14; Q8WVE6: TMEM171; NbExp=3; IntAct=EBI-10264833, EBI-10264837;
CC Q8N108-16; Q15109: AGER; NbExp=3; IntAct=EBI-25830642, EBI-1646426;
CC Q8N108-16; P15311: EZR; NbExp=3; IntAct=EBI-25830642, EBI-1056902;
CC Q8N108-16; Q16512: PKN1; NbExp=3; IntAct=EBI-25830642, EBI-602382;
CC Q8N108-16; P24928: POLR2A; NbExp=3; IntAct=EBI-25830642, EBI-295301;
CC Q8N108-16; Q13148: TARDBP; NbExp=6; IntAct=EBI-25830642, EBI-372899;
CC Q8N108-16; P31930: UQCRC1; NbExp=3; IntAct=EBI-25830642, EBI-1052596;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=N3-beta;
CC IsoId=Q8N108-11; Sequence=Displayed;
CC Name=2; Synonyms=N2-beta;
CC IsoId=Q8N108-12; Sequence=VSP_042450;
CC Name=3; Synonyms=N1-beta;
CC IsoId=Q8N108-13; Sequence=VSP_042451;
CC Name=4; Synonyms=N1-alpha;
CC IsoId=Q8N108-14; Sequence=VSP_042451, VSP_042452, VSP_042453;
CC Name=5; Synonyms=N2-alpha;
CC IsoId=Q8N108-15; Sequence=VSP_042450, VSP_042452, VSP_042453;
CC Name=6; Synonyms=N3-alpha;
CC IsoId=Q8N108-16; Sequence=VSP_042452, VSP_042453;
CC Name=7;
CC IsoId=Q8N108-17; Sequence=VSP_042449;
CC Name=8;
CC IsoId=Q8N108-18; Sequence=VSP_042451, VSP_043218;
CC Name=9;
CC IsoId=Q8N108-19; Sequence=VSP_044343, VSP_044344;
CC Name=10;
CC IsoId=Q8N108-20; Sequence=VSP_042451, VSP_055710, VSP_055711;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, but at very low levels.
CC However, consistent level of expression are observed in heart, testis,
CC thyroid, ovary and adrenal gland. Transcripts are up-regulated in
CC breast carcinoma cell lines and tumor. {ECO:0000269|PubMed:12242014,
CC ECO:0000269|PubMed:9813250}.
CC -!- MISCELLANEOUS: [Isoform 2]: It is uncertain whether Met-1 or Met-55 is
CC the initiator. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: It is uncertain whether Met-1 or Met-55 is
CC the initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17423.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS. Probable cloning artifact due to reverse transcription from RNA internal poly-A tracts.; Evidence={ECO:0000305};
CC Sequence=AAM76041.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM97500.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM97503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM97506.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11339.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. C-terminal is identical to the product of the WLS gene.; Evidence={ECO:0000305};
CC Sequence=CAD89921.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MIER1ID50389ch1p31.html";
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DR EMBL; AF515446; AAM76040.1; -; mRNA.
DR EMBL; AF515447; AAM76041.1; ALT_INIT; mRNA.
DR EMBL; AF515448; AAM76042.2; -; mRNA.
DR EMBL; AY124186; AAM97499.2; -; mRNA.
DR EMBL; AY124187; AAM97500.1; ALT_INIT; mRNA.
DR EMBL; AY124188; AAM97501.1; -; mRNA.
DR EMBL; AY124189; AAM97502.2; -; mRNA.
DR EMBL; AY124190; AAM97503.1; ALT_INIT; mRNA.
DR EMBL; AY124191; AAM97504.1; -; mRNA.
DR EMBL; AY124192; AAM97505.2; -; mRNA.
DR EMBL; AY124193; AAM97506.1; ALT_INIT; mRNA.
DR EMBL; AY124194; AAM97507.1; -; mRNA.
DR EMBL; AK074990; BAC11339.1; ALT_SEQ; mRNA.
DR EMBL; AK302061; BAG63451.1; -; mRNA.
DR EMBL; AL831987; CAD89921.1; ALT_SEQ; mRNA.
DR EMBL; CR627441; CAH10526.1; -; mRNA.
DR EMBL; AL139216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL500525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06505.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06508.1; -; Genomic_DNA.
DR EMBL; BC017423; AAH17423.1; ALT_SEQ; mRNA.
DR EMBL; BC066898; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC108726; AAI08727.1; -; mRNA.
DR EMBL; BC125217; AAI25218.1; -; mRNA.
DR EMBL; BC125218; AAI25219.1; -; mRNA.
DR EMBL; AB046830; BAB13436.1; -; mRNA.
DR CCDS; CCDS41347.1; -. [Q8N108-16]
DR CCDS; CCDS41348.1; -. [Q8N108-11]
DR CCDS; CCDS53325.1; -. [Q8N108-15]
DR CCDS; CCDS53326.1; -. [Q8N108-12]
DR CCDS; CCDS53327.1; -. [Q8N108-14]
DR CCDS; CCDS53328.1; -. [Q8N108-18]
DR CCDS; CCDS53329.1; -. [Q8N108-13]
DR CCDS; CCDS53330.1; -. [Q8N108-19]
DR CCDS; CCDS60163.1; -. [Q8N108-20]
DR RefSeq; NP_001071168.2; NM_001077700.2. [Q8N108-12]
DR RefSeq; NP_001071169.1; NM_001077701.2. [Q8N108-11]
DR RefSeq; NP_001071170.2; NM_001077702.2. [Q8N108-14]
DR RefSeq; NP_001071171.2; NM_001077703.2. [Q8N108-15]
DR RefSeq; NP_001071172.1; NM_001077704.2. [Q8N108-16]
DR RefSeq; NP_001139582.1; NM_001146110.1. [Q8N108-13]
DR RefSeq; NP_001139583.1; NM_001146111.1. [Q8N108-18]
DR RefSeq; NP_001139584.1; NM_001146112.1. [Q8N108-17]
DR RefSeq; NP_001139585.1; NM_001146113.1. [Q8N108-19]
DR RefSeq; NP_001265144.1; NM_001278215.1. [Q8N108-20]
DR RefSeq; NP_065999.2; NM_020948.3. [Q8N108-13]
DR RefSeq; XP_005271133.1; XM_005271076.3. [Q8N108-13]
DR RefSeq; XP_016857413.1; XM_017001924.1. [Q8N108-13]
DR RefSeq; XP_016857414.1; XM_017001925.1. [Q8N108-13]
DR RefSeq; XP_016857415.1; XM_017001926.1. [Q8N108-13]
DR RefSeq; XP_016857416.1; XM_017001927.1.
DR RefSeq; XP_016857417.1; XM_017001928.1.
DR RefSeq; XP_016857420.1; XM_017001931.1. [Q8N108-17]
DR AlphaFoldDB; Q8N108; -.
DR BioGRID; 121732; 70.
DR IntAct; Q8N108; 35.
DR MINT; Q8N108; -.
DR STRING; 9606.ENSP00000383820; -.
DR iPTMnet; Q8N108; -.
DR PhosphoSitePlus; Q8N108; -.
DR BioMuta; MIER1; -.
DR DMDM; 380865399; -.
DR EPD; Q8N108; -.
DR jPOST; Q8N108; -.
DR MassIVE; Q8N108; -.
DR MaxQB; Q8N108; -.
DR PaxDb; Q8N108; -.
DR PeptideAtlas; Q8N108; -.
DR PRIDE; Q8N108; -.
DR ProteomicsDB; 58657; -.
DR ProteomicsDB; 64844; -.
DR ProteomicsDB; 71504; -. [Q8N108-11]
DR ProteomicsDB; 71505; -. [Q8N108-12]
DR ProteomicsDB; 71506; -. [Q8N108-13]
DR ProteomicsDB; 71507; -. [Q8N108-14]
DR ProteomicsDB; 71508; -. [Q8N108-15]
DR ProteomicsDB; 71509; -. [Q8N108-16]
DR ProteomicsDB; 71510; -. [Q8N108-17]
DR ProteomicsDB; 71511; -. [Q8N108-18]
DR Antibodypedia; 9204; 111 antibodies from 20 providers.
DR DNASU; 57708; -.
DR Ensembl; ENST00000355356.3; ENSP00000347514.3; ENSG00000198160.15. [Q8N108-11]
DR Ensembl; ENST00000355977.10; ENSP00000348253.6; ENSG00000198160.15. [Q8N108-19]
DR Ensembl; ENST00000357692.6; ENSP00000350321.2; ENSG00000198160.15. [Q8N108-13]
DR Ensembl; ENST00000371012.6; ENSP00000360051.2; ENSG00000198160.15. [Q8N108-20]
DR Ensembl; ENST00000371014.5; ENSP00000360053.1; ENSG00000198160.15. [Q8N108-15]
DR Ensembl; ENST00000371016.5; ENSP00000360055.1; ENSG00000198160.15. [Q8N108-14]
DR Ensembl; ENST00000371018.7; ENSP00000360057.3; ENSG00000198160.15. [Q8N108-18]
DR Ensembl; ENST00000401041.6; ENSP00000383820.1; ENSG00000198160.15. [Q8N108-12]
DR Ensembl; ENST00000401042.7; ENSP00000383821.3; ENSG00000198160.15. [Q8N108-16]
DR GeneID; 57708; -.
DR KEGG; hsa:57708; -.
DR MANE-Select; ENST00000401041.6; ENSP00000383820.1; NM_001077700.3; NP_001071168.2. [Q8N108-12]
DR UCSC; uc001dda.6; human. [Q8N108-11]
DR CTD; 57708; -.
DR DisGeNET; 57708; -.
DR GeneCards; MIER1; -.
DR HGNC; HGNC:29657; MIER1.
DR HPA; ENSG00000198160; Tissue enhanced (bone).
DR neXtProt; NX_Q8N108; -.
DR OpenTargets; ENSG00000198160; -.
DR PharmGKB; PA142671456; -.
DR VEuPathDB; HostDB:ENSG00000198160; -.
DR eggNOG; KOG4329; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR HOGENOM; CLU_195428_0_0_1; -.
DR InParanoid; Q8N108; -.
DR OMA; TIDHMDA; -.
DR OrthoDB; 1062529at2759; -.
DR TreeFam; TF106453; -.
DR PathwayCommons; Q8N108; -.
DR SignaLink; Q8N108; -.
DR BioGRID-ORCS; 57708; 12 hits in 1085 CRISPR screens.
DR ChiTaRS; MIER1; human.
DR GeneWiki; MIER1; -.
DR GenomeRNAi; 57708; -.
DR Pharos; Q8N108; Tbio.
DR PRO; PR:Q8N108; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N108; protein.
DR Bgee; ENSG00000198160; Expressed in calcaneal tendon and 192 other tissues.
DR Genevisible; Q8N108; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..512
FT /note="Mesoderm induction early response protein 1"
FT /id="PRO_0000197141"
FT DOMAIN 180..278
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 283..335
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..284
FT /note="Interaction with HDAC1"
FT /evidence="ECO:0000269|PubMed:12482978"
FT REGION 366..512
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 82..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..63
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044343"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_042449"
FT VAR_SEQ 1..3
FT /note="MAE -> MDGASSGGGGSSEGGGGSSGSGYGVVARFSQCLAEFRTWLRTNWL
FT RFNADKTDVML (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12242014,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_042450"
FT VAR_SEQ 1..3
FT /note="MAE -> MFMFNWFTDCLWTLFLSNYQ (in isoform 3, isoform
FT 4, isoform 8 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:12242014,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_042451"
FT VAR_SEQ 61..64
FT /note="EGDM -> VNNM (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055710"
FT VAR_SEQ 65..512
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055711"
FT VAR_SEQ 412..512
FT /note="EILNKEEVKVEGLHINGPTGGNKKPLHADMDTNGYETDNLTTDPKLAHMTAR
FT NENDFDEKSERPAKRRRVNSNGKESPGSSEFFQEAVSHGKFEELENTDD -> ILQMLL
FT PVHFSAISSRANAFLK (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044344"
FT VAR_SEQ 412..433
FT /note="EILNKEEVKVEGLHINGPTGGN -> ILQMLLPVHFSAISSRANAFLK (in
FT isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12242014"
FT /id="VSP_042452"
FT VAR_SEQ 432..512
FT /note="GNKKPLHADMDTNGYETDNLTTDPKLAHMTARNENDFDEKSERPAKRRRVNS
FT NGKESPGSSEFFQEAVSHGKFEELENTDD -> ILQMLLPVHFSAISSRANAFLK (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043218"
FT VAR_SEQ 434..512
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12242014"
FT /id="VSP_042453"
FT MUTAGEN 214
FT /note="W->A: Loss of transcriptional repression and HDAC1
FT recruitment activity."
FT /evidence="ECO:0000269|PubMed:12482978"
FT MUTAGEN 227..228
FT /note="FL->AA: Loss of transcriptional repression and HDAC1
FT recruitment activity."
FT /evidence="ECO:0000269|PubMed:12482978"
FT CONFLICT 14
FT /note="S -> P (in Ref. 7; BC066898)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="Q -> H (in Ref. 4; CAH10526)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="F -> S (in Ref. 3; BAC11339)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="D -> G (in Ref. 4; CAH10526)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8N108-12:1
FT /note="M -> L (in Ref. 1; AAM76041/AAM97503/AAM97506)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8N108-15:1
FT /note="M -> L (in Ref. 1; AAM97500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57983 MW; 182C92C7FC5063AD CRC64;
MAEPSVESSS PGGSATSDDH EFDPSADMLV HDFDDERTLE EEEMMEGETN FSSEIEDLAR
EGDMPIHELL SLYGYGSTVR LPEEDEEEEE EEEEGEDDED ADNDDNSGCS GENKEENIKD
SSGQEDETQS SNDDPSQSVA SQDAQEIIRP RRCKYFDTNS EVEEESEEDE DYIPSEDWKK
EIMVGSMFQA EIPVGICRYK ENEKVYENDD QLLWDPEYLP EDKVIIFLKD ASRRTGDEKG
VEAIPEGSHI KDNEQALYEL VKCNFDTEEA LRRLRFNVKA AREELSVWTE EECRNFEQGL
KAYGKDFHLI QANKVRTRSV GECVAFYYMW KKSERYDFFA QQTRFGKKKY NLHPGVTDYM
DRLLDESESA ASSRAPSPPP TASNSSNSQS EKEDGTVSTA NQNGVSSNGP GEILNKEEVK
VEGLHINGPT GGNKKPLHAD MDTNGYETDN LTTDPKLAHM TARNENDFDE KSERPAKRRR
VNSNGKESPG SSEFFQEAVS HGKFEELENT DD
