ID   MIER1_HUMAN             Reviewed;         536 AA.
AC   Q8N108; Q5T104; Q6AHY8; Q86TB4; Q8N156; Q8N161; Q8NC37; Q8NES4;
AC   Q8NES5; Q8NES6; Q8WWG2; Q9HCG2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   05-OCT-2010, entry version 75.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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   MEDLINE=22226629; 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.,
RA   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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8).
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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-223 (ISOFORM 3).
RC   TISSUE=Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-536.
RX   MEDLINE=20450683; 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.
RT   XVIII. The complete sequences of 100 new cDNA clones from brain which
RT   code for large proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [7]
RP   FUNCTION, INTERACTION WITH HDAC1, AND MUTAGENESIS OF TRP-238 AND
RP   251-PHE--LEU-252.
RX   MEDLINE=22371506; 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   [8]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99033003; 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
RT   in breast tumours and tumour-derived cell lines.";
RL   Gene 222:77-82(1998).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-190; SER-401;
RP   THR-405 AND SER-407, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASS
RP   SPECTROMETRY.
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix adenocarcinoma;
RX   PubMed=16565220; DOI=10.1073/pnas.0507066103;
RA   Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
RT   "Phosphoproteome analysis of the human mitotic spindle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-179; SER-184; SER-190;
RP   SER-507 AND SER-512, AND MASS SPECTROMETRY.
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-184 AND SER-190, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-190, AND
RP   MASS SPECTROMETRY.
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).
CC   -!- FUNCTION: Transcriptional repressor of a number of genes including
CC       Sp1 target genes.
CC   -!- SUBUNIT: Interacts with HDAC1.
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=N1-beta;
CC         IsoId=Q8N108-1; Sequence=Displayed;
CC         Note=Found in the nucleus;
CC       Name=2; Synonyms=N2-beta;
CC         IsoId=Q8N108-2; Sequence=VSP_016167;
CC         Note=Found in the nucleus;
CC       Name=3; Synonyms=N3-beta;
CC         IsoId=Q8N108-3; Sequence=VSP_016168;
CC         Note=Found in the nucleus;
CC       Name=4; Synonyms=N1-alpha;
CC         IsoId=Q8N108-4; Sequence=VSP_016172, VSP_016173;
CC         Note=Found in the cytoplasm;
CC       Name=5; Synonyms=N2-alpha;
CC         IsoId=Q8N108-5; Sequence=VSP_016167, VSP_016172, VSP_016173;
CC         Note=Found in the cytoplasm;
CC       Name=6; Synonyms=N3-alpha;
CC         IsoId=Q8N108-6; Sequence=VSP_016168, VSP_016172, VSP_016173;
CC         Note=Found in the cytoplasm;
CC       Name=7;
CC         IsoId=Q8N108-7; Sequence=VSP_016166;
CC         Note=No experimental confirmation available;
CC       Name=8;
CC         IsoId=Q8N108-8; Sequence=VSP_016170;
CC         Note=No experimental confirmation available;
CC       Name=9;
CC         IsoId=Q8N108-9; Sequence=VSP_016168, VSP_016171;
CC         Note=No experimental confirmation available;
CC       Name=10;
CC         IsoId=Q8N108-10; Sequence=VSP_016169;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, but at very low
CC       levels. However, consistent level of expression are observed in
CC       heart, testis, thyroid, ovary and adrenal gland. Transcripts are
CC       up-regulated in breast carcinoma cell lines and tumor.
CC   -!- SIMILARITY: Contains 1 ELM2 domain.
CC   -!- SIMILARITY: Contains 1 SANT domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH17423.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 224;
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DR   EMBL; AF515446; AAM76040.1; -; mRNA.
DR   EMBL; AF515447; AAM76041.1; -; mRNA.
DR   EMBL; AF515448; AAM76042.1; -; mRNA.
DR   EMBL; AY124186; AAM97499.1; -; mRNA.
DR   EMBL; AY124187; AAM97500.1; -; mRNA.
DR   EMBL; AY124188; AAM97501.1; -; mRNA.
DR   EMBL; AY124189; AAM97502.1; -; mRNA.
DR   EMBL; AY124190; AAM97503.1; -; mRNA.
DR   EMBL; AY124191; AAM97504.1; -; mRNA.
DR   EMBL; AY124192; AAM97505.1; -; mRNA.
DR   EMBL; AY124193; AAM97506.1; -; mRNA.
DR   EMBL; AY124194; AAM97507.1; -; mRNA.
DR   EMBL; AK074990; BAC11339.1; -; mRNA.
DR   EMBL; CR627441; CAH10526.1; -; mRNA.
DR   EMBL; AL831987; CAD89921.1; -; mRNA.
DR   EMBL; AL139216; CAI18875.1; -; Genomic_DNA.
DR   EMBL; AL500525; CAI18875.1; JOINED; Genomic_DNA.
DR   EMBL; AL139216; CAI18878.1; -; Genomic_DNA.
DR   EMBL; AL500525; CAI18878.1; JOINED; Genomic_DNA.
DR   EMBL; AL139216; CAI18879.1; -; Genomic_DNA.
DR   EMBL; AL500525; CAI18879.1; JOINED; Genomic_DNA.
DR   EMBL; AL500525; CAI23429.1; -; Genomic_DNA.
DR   EMBL; AL139216; CAI23429.1; JOINED; Genomic_DNA.
DR   EMBL; AL500525; CAI23431.1; -; Genomic_DNA.
DR   EMBL; AL139216; CAI23431.1; JOINED; Genomic_DNA.
DR   EMBL; AL500525; CAI23432.1; -; Genomic_DNA.
DR   EMBL; AL139216; CAI23432.1; JOINED; Genomic_DNA.
DR   EMBL; BC017423; AAH17423.1; ALT_SEQ; mRNA.
DR   EMBL; AB046830; BAB13436.1; -; mRNA.
DR   IPI; IPI00477825; -.
DR   IPI; IPI00478280; -.
DR   IPI; IPI00479032; -.
DR   IPI; IPI00640919; -.
DR   IPI; IPI00646985; -.
DR   IPI; IPI00655630; -.
DR   IPI; IPI00655783; -.
DR   IPI; IPI00655845; -.
DR   IPI; IPI00656079; -.
DR   IPI; IPI00656089; -.
DR   RefSeq; NP_001071169.1; -.
DR   RefSeq; NP_001071170.2; -.
DR   RefSeq; NP_001071171.2; -.
DR   RefSeq; NP_001071172.1; -.
DR   RefSeq; NP_001139582.1; -.
DR   RefSeq; NP_001139584.1; -.
DR   RefSeq; NP_065999.2; -.
DR   UniGene; Hs.605432; -.
DR   ProteinModelPortal; Q8N108; -.
DR   SMR; Q8N108; 303-370.
DR   MINT; MINT-4534304; -.
DR   STRING; Q8N108; -.
DR   PhosphoSite; Q8N108; -.
DR   PRIDE; Q8N108; -.
DR   Ensembl; ENST00000439314; ENSP00000401288; ENSG00000198160.
DR   GeneID; 57708; -.
DR   UCSC; uc001ddd.1; human.
DR   CTD; 57708; -.
DR   GeneCards; GC01P067390; -.
DR   HGNC; HGNC:29657; MIER1.
DR   HPA; HPA019589; -.
DR   PharmGKB; PA142671456; -.
DR   HOVERGEN; HBG052923; -.
DR   OMA; HTDMDTN; -.
DR   NextBio; 64594; -.
DR   ArrayExpress; Q8N108; -.
DR   Bgee; Q8N108; -.
DR   CleanEx; HS_MIER1; -.
DR   Genevestigator; Q8N108; -.
DR   GermOnline; ENSG00000198160; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-k...; IMP:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000949; ELM2.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   Pfam; PF01448; ELM2; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    536       Mesoderm induction early response protein
FT                                1.
FT                                /FTId=PRO_0000197141.
FT   DOMAIN      204    302       ELM2.
FT   DOMAIN      307    359       SANT.
FT   REGION      179    283       Interaction with HDAC1.
FT   COMPBIAS     60    205       Glu-rich.
FT   MOD_RES     146    146       Phosphoserine.
FT   MOD_RES     179    179       Phosphotyrosine.
FT   MOD_RES     184    184       Phosphoserine.
FT   MOD_RES     190    190       Phosphoserine.
FT   MOD_RES     397    397       Phosphoserine.
FT   MOD_RES     401    401       Phosphoserine.
FT   MOD_RES     405    405       Phosphothreonine.
FT   MOD_RES     407    407       Phosphoserine.
FT   MOD_RES     507    507       Phosphoserine.
FT   MOD_RES     512    512       Phosphoserine.
FT   VAR_SEQ       1     51       Missing (in isoform 7).
FT                                /FTId=VSP_016166.
FT   VAR_SEQ       1     27       MLKMCIRCLCLIGLQTVCGLFSCQITQ -> ML (in
FT                                isoform 2 and isoform 5).
FT                                /FTId=VSP_016167.
FT   VAR_SEQ       1     27       MLKMCIRCLCLIGLQTVCGLFSCQITQ -> MAE (in
FT                                isoform 3, isoform 6 and isoform 9).
FT                                /FTId=VSP_016168.
FT   VAR_SEQ       1     26       MLKMCIRCLCLIGLQTVCGLFSCQIT -> MFMFNWFTDCL
FT                                WTLFLSNY (in isoform 10).
FT                                /FTId=VSP_016169.
FT   VAR_SEQ       1      3       Missing (in isoform 8).
FT                                /FTId=VSP_016170.
FT   VAR_SEQ     229    536       VYENDDQLLWDPEYLPEDKVIIFLKDASRRTGDEKGVEAIP
FT                                EGSHIKDNEQALYELVKCNFDTEEALRRLRFNVKAAREELS
FT                                VWTEEECRNFEQGLKAYGKDFHLIQANKVRTRSVGECVAFY
FT                                YMWKKSERYDFFAQQTRFGKKKYNLHPGVTDYMDRLLDESE
FT                                SAASSRAPSPPPTASNSSNSQSEKEDGTVSTANQNGVSSNG
FT                                PGEILNKEEVKVEGLHINGPTGGNKKPLHADMDTNGYETDN
FT                                LTTDPKLAHMTARNENDFDEKSERPAKRRRVNSNGKESPGS
FT                                SEFFQEAVSHGKFEELENTDD -> APGPTTAVSYMSVKCV
FT                                DARKNHHKTKWFVPWGPNHCDKIRDIEEAIPREIEANDIVF
FT                                SVHIPLPHMEMSPWFQFMLFILQLDIAFKLNNQIRENAEVS
FT                                MDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEG
FT                                RYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGE
FT                                IKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRI
FT                                TMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWML
FT                                LFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQ
FT                                VGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDIGTELAM
FT                                AFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKV
FT                                RWLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVTEGHWK
FT                                WGGVTVQVNSAFFTGIYGMWNLYVFALMFLYAPSHKNYGED
FT                                QSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE
FT                                (in isoform 9).
FT                                /FTId=VSP_016171.
FT   VAR_SEQ     436    457       EILNKEEVKVEGLHINGPTGGN -> ILQMLLPVHFSAISS
FT                                RANAFLK (in isoform 4, isoform 5 and
FT                                isoform 6).
FT                                /FTId=VSP_016172.
FT   VAR_SEQ     458    536       Missing (in isoform 4, isoform 5 and
FT                                isoform 6).
FT                                /FTId=VSP_016173.
FT   MUTAGEN     238    238       W->A: Loss of transcriptional repression
FT                                and HDAC1 recruitment activity.
FT   MUTAGEN     251    252       FL->AA: Loss of transcriptional
FT                                repression and HDAC1 recruitment
FT                                activity.
FT   CONFLICT    166    166       Q -> H (in Ref. 3; CAH10526).
FT   CONFLICT    180    180       F -> S (in Ref. 2; BAC11339).
FT   CONFLICT    261    261       D -> G (in Ref. 3; CAH10526).
SQ   SEQUENCE   536 AA;  60654 MW;  87EA6E915E36709B CRC64;
     MLKMCIRCLC LIGLQTVCGL FSCQITQPSV ESSSPGGSAT SDDHEFDPSA DMLVHDFDDE
     RTLEEEEMME GETNFSSEIE DLAREGDMPI HELLSLYGYG STVRLPEEDE EEEEEEEEGE
     DDEDADNDDN SGCSGENKEE NIKDSSGQED ETQSSNDDPS QSVASQDAQE IIRPRRCKYF
     DTNSEVEEES EEDEDYIPSE DWKKEIMVGS MFQAEIPVGI CRYKENEKVY ENDDQLLWDP
     EYLPEDKVII FLKDASRRTG DEKGVEAIPE GSHIKDNEQA LYELVKCNFD TEEALRRLRF
     NVKAAREELS VWTEEECRNF EQGLKAYGKD FHLIQANKVR TRSVGECVAF YYMWKKSERY
     DFFAQQTRFG KKKYNLHPGV TDYMDRLLDE SESAASSRAP SPPPTASNSS NSQSEKEDGT
     VSTANQNGVS SNGPGEILNK EEVKVEGLHI NGPTGGNKKP LHADMDTNGY ETDNLTTDPK
     LAHMTARNEN DFDEKSERPA KRRRVNSNGK ESPGSSEFFQ EAVSHGKFEE LENTDD
//