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Homeobox protein Meis1 (Myeloid ecotropic viral integration site 1)

 MEIS1_MOUSE             Reviewed;         390 AA.
Q60954; B1ARH5; Q5SVC8; Q60955; Q8CIL0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
28-MAR-2018, entry version 150.
RecName: Full=Homeobox protein Meis1;
AltName: Full=Myeloid ecotropic viral integration site 1;
Name=Meis1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=7565694; DOI=10.1128/MCB.15.10.5434;
Moskow J.J., Bullrich F., Huebner K., Daar I.O., Buchberg A.M.;
"Meis1, a PBX1-related homeobox gene involved in myeloid leukemia in
BXH-2 mice.";
Mol. Cell. Biol. 15:5434-5443(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH PBX1.
PubMed=9315626; DOI=10.1128/MCB.17.10.5679;
Chang C.-P., Jacobs Y., Nakamura T., Jenkins N.A., Copeland N.G.,
Cleary M.L.;
"Meis proteins are major in vivo DNA binding partners for wild-type
but not chimeric Pbx proteins.";
Mol. Cell. Biol. 17:5679-5687(1997).
[6]
INTERACTION WITH PBX1, AND MUTAGENESIS OF TRP-213.
PubMed=9525891; DOI=10.1074/jbc.273.14.7941;
Bischof L.J., Kagawa N., Moskow J.J., Takahashi Y., Iwamatsu A.,
Buchberg A.M., Waterman M.R.;
"Members of the Meis1 and Pbx homeodomain protein families
cooperatively bind a cAMP-responsive sequence (CRS1) from bovine
CYP17.";
J. Biol. Chem. 273:7941-7948(1998).
[7]
INTERACTION WITH HOXA9; PBX1 AND PBX2, AND SUBCELLULAR LOCATION.
PubMed=10082572; DOI=10.1128/MCB.19.4.3051;
Shen W.-F., Rozenfeld S., Kwong A., Koemueves L.G., Lawrence H.J.,
Largman C.;
"HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells.";
Mol. Cell. Biol. 19:3051-3061(1999).
[8]
INTERACTION WITH PBX1; HOXD4; HOXD9 AND HOXD10, AND MUTAGENESIS OF
ASN-321.
PubMed=10523646; DOI=10.1128/MCB.19.11.7577;
Shanmugam K., Green N.C., Rambaldi I., Saragovi H.U.,
Featherstone M.S.;
"PBX and MEIS as non-DNA-binding partners in trimeric complexes with
HOX proteins.";
Mol. Cell. Biol. 19:7577-7588(1999).
[9]
FUNCTION.
PubMed=12183364; DOI=10.1101/gad.1007602;
Zhang X., Friedman A., Heaney S., Purcell P., Maas R.L.;
"Meis homeoproteins directly regulate Pax6 during vertebrate lens
morphogenesis.";
Genes Dev. 16:2097-2107(2002).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=15882575; DOI=10.1016/j.ydbio.2005.01.004;
Azcoitia V., Aracil M., Martinez-A C., Torres M.;
"The homeodomain protein Meis1 is essential for definitive
hematopoiesis and vascular patterning in the mouse embryo.";
Dev. Biol. 280:307-320(2005).
[11]
TRANSCRIPTIONAL ACTIVATION DOMAIN.
PubMed=15654074; DOI=10.1074/jbc.M413963200;
Huang H., Rastegar M., Bodner C., Goh S.-L., Rambaldi I.,
Featherstone M.;
"MEIS C termini harbor transcriptional activation domains that respond
to cell signaling.";
J. Biol. Chem. 280:10119-10127(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
TISSUE SPECIFICITY.
PubMed=21059917; DOI=10.1073/pnas.1007001107;
Liu J., Wang Y., Birnbaum M.J., Stoffers D.A.;
"Three-amino-acid-loop-extension homeodomain factor Meis3 regulates
cell survival via PDK1.";
Proc. Natl. Acad. Sci. U.S.A. 107:20494-20499(2010).
-!- FUNCTION: Acts as a transcriptional regulator of PAX6. Also acts
as a transcriptional activator of PF4 in complex with PBX1 or
PBX2. Required for hematopoiesis, megakaryocyte lineage
development and vascular patterning. May function as a cofactor
for HOXA7 and HOXA9 in the induction of myeloid leukemias.
{ECO:0000269|PubMed:12183364, ECO:0000269|PubMed:15882575}.
-!- SUBUNIT: Interacts with the N-terminal region of PBX1 to form a
heterodimer which binds DNA including a cAMP-responsive sequence
in CYP17. Also forms heterodimers with PBX2. Forms heterotrimers
with PBX1 or PBX2 and a number of HOX proteins including HOXA9,
HOXD4 and HOXD9 where it acts as a non-DNA-binding partner. Also
forms heterotrimers with PBX1 and HOX proteins including HOXD9 and
HOXD10 where PBX1 is the non-DNA-binding partner.
{ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:10523646,
ECO:0000269|PubMed:9315626, ECO:0000269|PubMed:9525891}.
-!- INTERACTION:
Q62424:Hoxa13; NbExp=3; IntAct=EBI-445723, EBI-925160;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00108, ECO:0000269|PubMed:10082572,
ECO:0000269|PubMed:15882575}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Meis1A;
IsoId=Q60954-1; Sequence=Displayed;
Name=2; Synonyms=Meis1B;
IsoId=Q60954-2; Sequence=VSP_002240;
Name=3;
IsoId=Q60954-3; Sequence=VSP_017056;
-!- TISSUE SPECIFICITY: Expressed at high levels in the lung with
lower levels detected in the heart and brain. Expressed in
pancreatic islets (beta-cells and non-beta-cells)
(PubMed:21059917). {ECO:0000269|PubMed:21059917}.
-!- DEVELOPMENTAL STAGE: Expressed at high levels in all stages of
embryonic development analyzed (7 days to 17 days).
-!- INDUCTION: Expression is coactivated by retroviral integration in
BXH-2 murine myeloid leukemias.
-!- DISEASE: Note=Meis1 serves as a site of viral integration in 15%
of the tumors arising in BXH-2 mice that develop myeloid leukemia
as a result of the expression of an ecotropic murine leukemia
virus. {ECO:0000269|PubMed:7565694}.
-!- DISRUPTION PHENOTYPE: Mice die between embryonic days 11.5 and
14.5, showing internal hemorrhage, liver hypoplasia and anemia.
{ECO:0000269|PubMed:15882575}.
-!- SIMILARITY: Belongs to the TALE/MEIS homeobox family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U33629; AAA85508.1; -; mRNA.
EMBL; U33630; AAA85509.1; -; mRNA.
EMBL; AK132298; BAE21088.1; -; mRNA.
EMBL; AK140748; BAE24465.1; -; mRNA.
EMBL; AL603984; CAI24096.1; -; Genomic_DNA.
EMBL; AL645570; CAI24096.1; JOINED; Genomic_DNA.
EMBL; AL603984; CAI24097.1; -; Genomic_DNA.
EMBL; AL645570; CAI24097.1; JOINED; Genomic_DNA.
EMBL; AL645570; CAI25394.1; -; Genomic_DNA.
EMBL; AL603984; CAI25394.1; JOINED; Genomic_DNA.
EMBL; AL645570; CAI25395.1; -; Genomic_DNA.
EMBL; AL603984; CAI25395.1; JOINED; Genomic_DNA.
EMBL; BC023689; AAH23689.1; -; mRNA.
CCDS; CCDS24453.1; -. [Q60954-2]
CCDS; CCDS56760.1; -. [Q60954-1]
RefSeq; NP_001180200.1; NM_001193271.1. [Q60954-1]
RefSeq; NP_034919.1; NM_010789.3. [Q60954-2]
UniGene; Mm.356578; -.
UniGene; Mm.445192; -.
ProteinModelPortal; Q60954; -.
SMR; Q60954; -.
BioGrid; 201386; 11.
CORUM; Q60954; -.
IntAct; Q60954; 14.
MINT; Q60954; -.
STRING; 10090.ENSMUSP00000099942; -.
iPTMnet; Q60954; -.
PhosphoSitePlus; Q60954; -.
PaxDb; Q60954; -.
PRIDE; Q60954; -.
Ensembl; ENSMUST00000068264; ENSMUSP00000069277; ENSMUSG00000020160. [Q60954-1]
Ensembl; ENSMUST00000144988; ENSMUSP00000134969; ENSMUSG00000020160. [Q60954-3]
Ensembl; ENSMUST00000185131; ENSMUSP00000139219; ENSMUSG00000020160. [Q60954-2]
GeneID; 17268; -.
KEGG; mmu:17268; -.
UCSC; uc007icl.2; mouse. [Q60954-2]
UCSC; uc007icm.2; mouse. [Q60954-1]
UCSC; uc007icn.2; mouse. [Q60954-3]
CTD; 4211; -.
MGI; MGI:104717; Meis1.
eggNOG; KOG0773; Eukaryota.
eggNOG; ENOG410XPMQ; LUCA.
GeneTree; ENSGT00550000074260; -.
HOGENOM; HOG000253923; -.
HOVERGEN; HBG055193; -.
InParanoid; Q60954; -.
KO; K15613; -.
OMA; VSQGAPY; -.
OrthoDB; EOG091G0KDP; -.
PhylomeDB; Q60954; -.
TreeFam; TF318093; -.
ChiTaRS; Meis1; mouse.
PRO; PR:Q60954; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020160; -.
CleanEx; MM_MEIS1; -.
ExpressionAtlas; Q60954; baseline and differential.
Genevisible; Q60954; MM.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
CDD; cd00086; homeodomain; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR008422; Homeobox_KN_domain.
InterPro; IPR032453; PKNOX/Meis_N.
Pfam; PF05920; Homeobox_KN; 1.
Pfam; PF16493; Meis_PKNOX_N; 1.
SMART; SM00389; HOX; 1.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome;
Developmental protein; DNA-binding; Homeobox; Nucleus; Proto-oncogene;
Reference proteome; Transcription.
CHAIN 1 390 Homeobox protein Meis1.
/FTId=PRO_0000049106.
DNA_BIND 272 334 Homeobox; TALE-type.
{ECO:0000255|PROSITE-ProRule:PRU00108}.
REGION 335 390 Required for transcriptional activation.
COMPBIAS 194 240 Ser/Thr-rich.
COMPBIAS 242 269 Asp/Glu-rich (acidic).
COMPBIAS 262 269 Poly-Asp.
VAR_SEQ 342 390 VSQGTPYNPDGQPMGGFVMDGQQHMGIRAPGPMSGMGMNMG
MEGQWHYM -> GKSPLVTVFKSGKRKASSSHSPGGLLPGK
(in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_017056.
VAR_SEQ 373 390 PMSGMGMNMGMEGQWHYM -> LQSMPGEYVARGGPMGVSM
GQPSYTQAQMPPHPAQLRHGPPMHTYIPGHPHHPAVMMHGG
QPHPGMPMSASSPSVLNTGDPTMSAQVMDIHAQ (in
isoform 2). {ECO:0000303|PubMed:7565694}.
/FTId=VSP_002240.
MUTAGEN 213 213 W->A: No effect on cooperative binding
with PBX1 to CYP17.
{ECO:0000269|PubMed:9525891}.
MUTAGEN 321 321 N->S: Loss of binding to other proteins.
{ECO:0000269|PubMed:10523646}.
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


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