MEIS1_MOUSE
ID MEIS1_MOUSE Reviewed; 390 AA.
AC Q60954; B1ARH5; Q5SVC8; Q60955; Q8CIL0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Homeobox protein Meis1;
DE AltName: Full=Myeloid ecotropic viral integration site 1;
GN Name=Meis1;
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 AND 2).
RX PubMed=7565694; DOI=10.1128/mcb.15.10.5434;
RA Moskow J.J., Bullrich F., Huebner K., Daar I.O., Buchberg A.M.;
RT "Meis1, a PBX1-related homeobox gene involved in myeloid leukemia in BXH-2
RT mice.";
RL Mol. Cell. Biol. 15:5434-5443(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP INTERACTION WITH PBX1.
RX PubMed=9315626; DOI=10.1128/mcb.17.10.5679;
RA Chang C.-P., Jacobs Y., Nakamura T., Jenkins N.A., Copeland N.G.,
RA Cleary M.L.;
RT "Meis proteins are major in vivo DNA binding partners for wild-type but not
RT chimeric Pbx proteins.";
RL Mol. Cell. Biol. 17:5679-5687(1997).
RN [6]
RP INTERACTION WITH PBX1, AND MUTAGENESIS OF TRP-213.
RX PubMed=9525891; DOI=10.1074/jbc.273.14.7941;
RA Bischof L.J., Kagawa N., Moskow J.J., Takahashi Y., Iwamatsu A.,
RA Buchberg A.M., Waterman M.R.;
RT "Members of the Meis1 and Pbx homeodomain protein families cooperatively
RT bind a cAMP-responsive sequence (CRS1) from bovine CYP17.";
RL J. Biol. Chem. 273:7941-7948(1998).
RN [7]
RP INTERACTION WITH HOXA9; PBX1 AND PBX2, AND SUBCELLULAR LOCATION.
RX PubMed=10082572; DOI=10.1128/mcb.19.4.3051;
RA Shen W.-F., Rozenfeld S., Kwong A., Koemueves L.G., Lawrence H.J.,
RA Largman C.;
RT "HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells.";
RL Mol. Cell. Biol. 19:3051-3061(1999).
RN [8]
RP INTERACTION WITH PBX1; HOXD4; HOXD9 AND HOXD10, AND MUTAGENESIS OF ASN-321.
RX PubMed=10523646; DOI=10.1128/mcb.19.11.7577;
RA Shanmugam K., Green N.C., Rambaldi I., Saragovi H.U., Featherstone M.S.;
RT "PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX
RT proteins.";
RL Mol. Cell. Biol. 19:7577-7588(1999).
RN [9]
RP FUNCTION.
RX PubMed=12183364; DOI=10.1101/gad.1007602;
RA Zhang X., Friedman A., Heaney S., Purcell P., Maas R.L.;
RT "Meis homeoproteins directly regulate Pax6 during vertebrate lens
RT morphogenesis.";
RL Genes Dev. 16:2097-2107(2002).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15882575; DOI=10.1016/j.ydbio.2005.01.004;
RA Azcoitia V., Aracil M., Martinez-A C., Torres M.;
RT "The homeodomain protein Meis1 is essential for definitive hematopoiesis
RT and vascular patterning in the mouse embryo.";
RL Dev. Biol. 280:307-320(2005).
RN [11]
RP TRANSCRIPTIONAL ACTIVATION DOMAIN.
RX PubMed=15654074; DOI=10.1074/jbc.m413963200;
RA Huang H., Rastegar M., Bodner C., Goh S.-L., Rambaldi I., Featherstone M.;
RT "MEIS C termini harbor transcriptional activation domains that respond to
RT cell signaling.";
RL J. Biol. Chem. 280:10119-10127(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=21059917; DOI=10.1073/pnas.1007001107;
RA Liu J., Wang Y., Birnbaum M.J., Stoffers D.A.;
RT "Three-amino-acid-loop-extension homeodomain factor Meis3 regulates cell
RT survival via PDK1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20494-20499(2010).
CC -!- FUNCTION: Acts as a transcriptional regulator of PAX6. Also acts as a
CC transcriptional activator of PF4 in complex with PBX1 or PBX2. Required
CC for hematopoiesis, megakaryocyte lineage development and vascular
CC patterning. May function as a cofactor for HOXA7 and HOXA9 in the
CC induction of myeloid leukemias. {ECO:0000269|PubMed:12183364,
CC ECO:0000269|PubMed:15882575}.
CC -!- SUBUNIT: Interacts with the N-terminal region of PBX1 to form a
CC heterodimer which binds DNA including a cAMP-responsive sequence in
CC CYP17. Also forms heterodimers with PBX2. Forms heterotrimers with PBX1
CC or PBX2 and a number of HOX proteins including HOXA9, HOXD4 and HOXD9
CC where it acts as a non-DNA-binding partner. Also forms heterotrimers
CC with PBX1 and HOX proteins including HOXD9 and HOXD10 where PBX1 is the
CC non-DNA-binding partner. Heterodimer with DLX3. Heterodimer with HOXB13
CC (By similarity). {ECO:0000250|UniProtKB:O00470,
CC ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:10523646,
CC ECO:0000269|PubMed:9315626, ECO:0000269|PubMed:9525891}.
CC -!- INTERACTION:
CC Q60954-2; Q62424: Hoxa13; NbExp=3; IntAct=EBI-445723, EBI-925160;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:15882575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Meis1A;
CC IsoId=Q60954-1; Sequence=Displayed;
CC Name=2; Synonyms=Meis1B;
CC IsoId=Q60954-2; Sequence=VSP_002240;
CC Name=3;
CC IsoId=Q60954-3; Sequence=VSP_017056;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the lung with lower
CC levels detected in the heart and brain. Expressed in pancreatic islets
CC (beta-cells and non-beta-cells) (PubMed:21059917).
CC {ECO:0000269|PubMed:21059917}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in all stages of
CC embryonic development analyzed (7 days to 17 days).
CC -!- INDUCTION: Expression is coactivated by retroviral integration in BXH-2
CC murine myeloid leukemias.
CC -!- DISEASE: Note=Meis1 serves as a site of viral integration in 15% of the
CC tumors arising in BXH-2 mice that develop myeloid leukemia as a result
CC of the expression of an ecotropic murine leukemia virus.
CC {ECO:0000269|PubMed:7565694}.
CC -!- DISRUPTION PHENOTYPE: Mice die between embryonic days 11.5 and 14.5,
CC showing internal hemorrhage, liver hypoplasia and anemia.
CC {ECO:0000269|PubMed:15882575}.
CC -!- SIMILARITY: Belongs to the TALE/MEIS homeobox family. {ECO:0000305}.
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DR EMBL; U33629; AAA85508.1; -; mRNA.
DR EMBL; U33630; AAA85509.1; -; mRNA.
DR EMBL; AK132298; BAE21088.1; -; mRNA.
DR EMBL; AK140748; BAE24465.1; -; mRNA.
DR EMBL; AL603984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023689; AAH23689.1; -; mRNA.
DR CCDS; CCDS24453.1; -. [Q60954-2]
DR CCDS; CCDS56760.1; -. [Q60954-1]
DR RefSeq; NP_001180200.1; NM_001193271.1. [Q60954-1]
DR RefSeq; NP_034919.1; NM_010789.3. [Q60954-2]
DR AlphaFoldDB; Q60954; -.
DR SMR; Q60954; -.
DR BioGRID; 201386; 11.
DR CORUM; Q60954; -.
DR IntAct; Q60954; 17.
DR MINT; Q60954; -.
DR STRING; 10090.ENSMUSP00000139219; -.
DR iPTMnet; Q60954; -.
DR PhosphoSitePlus; Q60954; -.
DR MaxQB; Q60954; -.
DR PaxDb; Q60954; -.
DR PRIDE; Q60954; -.
DR ProteomicsDB; 295876; -. [Q60954-1]
DR ProteomicsDB; 295877; -. [Q60954-2]
DR ProteomicsDB; 295878; -. [Q60954-3]
DR Antibodypedia; 3157; 332 antibodies from 41 providers.
DR DNASU; 17268; -.
DR Ensembl; ENSMUST00000068264; ENSMUSP00000069277; ENSMUSG00000020160. [Q60954-1]
DR Ensembl; ENSMUST00000144988; ENSMUSP00000134969; ENSMUSG00000020160. [Q60954-3]
DR Ensembl; ENSMUST00000185131; ENSMUSP00000139219; ENSMUSG00000020160. [Q60954-2]
DR GeneID; 17268; -.
DR KEGG; mmu:17268; -.
DR UCSC; uc007icl.2; mouse. [Q60954-2]
DR UCSC; uc007icm.2; mouse. [Q60954-1]
DR UCSC; uc007icn.2; mouse. [Q60954-3]
DR CTD; 4211; -.
DR MGI; MGI:104717; Meis1.
DR VEuPathDB; HostDB:ENSMUSG00000020160; -.
DR eggNOG; KOG0773; Eukaryota.
DR GeneTree; ENSGT00940000156327; -.
DR InParanoid; Q60954; -.
DR OMA; YLEVWIS; -.
DR OrthoDB; 1126341at2759; -.
DR PhylomeDB; Q60954; -.
DR TreeFam; TF318093; -.
DR BioGRID-ORCS; 17268; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Meis1; mouse.
DR PRO; PR:Q60954; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60954; protein.
DR Bgee; ENSMUSG00000020160; Expressed in ureter smooth muscle and 261 other tissues.
DR ExpressionAtlas; Q60954; baseline and differential.
DR Genevisible; Q60954; MM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IBA:GO_Central.
DR GO; GO:0001654; P:eye development; IBA:GO_Central.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR InterPro; IPR032453; PKNOX/Meis_N.
DR Pfam; PF05920; Homeobox_KN; 1.
DR Pfam; PF16493; Meis_PKNOX_N; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; DNA-binding;
KW Homeobox; Nucleus; Proto-oncogene; Reference proteome; Transcription.
FT CHAIN 1..390
FT /note="Homeobox protein Meis1"
FT /id="PRO_0000049106"
FT DOMAIN 108..192
FT /note="MEIS N-terminal"
FT /evidence="ECO:0000255"
FT DNA_BIND 272..334
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 190..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..329
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:O00470"
FT REGION 335..390
FT /note="Required for transcriptional activation"
FT COMPBIAS 223..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 342..390
FT /note="VSQGTPYNPDGQPMGGFVMDGQQHMGIRAPGPMSGMGMNMGMEGQWHYM ->
FT GKSPLVTVFKSGKRKASSSHSPGGLLPGK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017056"
FT VAR_SEQ 373..390
FT /note="PMSGMGMNMGMEGQWHYM -> LQSMPGEYVARGGPMGVSMGQPSYTQAQMP
FT PHPAQLRHGPPMHTYIPGHPHHPAVMMHGGQPHPGMPMSASSPSVLNTGDPTMSAQVMD
FT IHAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7565694"
FT /id="VSP_002240"
FT MUTAGEN 213
FT /note="W->A: No effect on cooperative binding with PBX1 to
FT CYP17."
FT /evidence="ECO:0000269|PubMed:9525891"
FT MUTAGEN 321
FT /note="N->S: Loss of binding to other proteins."
FT /evidence="ECO:0000269|PubMed:10523646"
SQ SEQUENCE 390 AA; 43002 MW; E0C32B5CE25E1E2C CRC64;
MAQRYDDLPH YGGMDGVGIP STMYGDPHAA RSMQPVHHLN HGPPLHSHQY PHTAHTNAMA
PSMGSSVNDA LKRDKDAIYG HPLFPLLALI FEKCELATCT PREPGVAGGD VCSSESFNED
IAVFAKQIRA EKPLFSSNPE LDNLMIQAIQ VLRFHLLELE KVHELCDNFC HRYISCLKGK
MPIDLVIDDR EGGSKSDSED VTRSANLTDQ PSWNRDHDDT ASTRSGGTPG PSSGGHTSHS
GDNSSEQGDG LDNSVASPST GDDDDPDKDK KRHKKRGIFP KVATNIMRAW LFQHLTHPYP
SEEQKKQLAQ DTGLTILQVN NWFINARRRI VQPMIDQSNR AVSQGTPYNP DGQPMGGFVM
DGQQHMGIRA PGPMSGMGMN MGMEGQWHYM
