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Homeobox protein Meis2 (Meis1-related protein 1)

 MEIS2_HUMAN             Reviewed;         477 AA.
O14770; A6NJI5; A8MWD5; B3KP98; B3KPQ6; Q96DI2; Q96KI4; Q96KI5;
Q9NRS1; Q9NRS2; Q9NRS3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
28-MAR-2018, entry version 163.
RecName: Full=Homeobox protein Meis2;
AltName: Full=Meis1-related protein 1;
Name=MEIS2; Synonyms=MRG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND FUNCTION.
TISSUE=Brain;
PubMed=10764806; DOI=10.1074/jbc.M908382199;
Yang Y., Hwang C.K., D'Souza U.M., Lee S.-H., Junn E., Mouradian M.M.;
"Three-amino acid extension loop homeodomain proteins Meis2 and TGIF
differentially regulate transcription.";
J. Biol. Chem. 275:20734-20741(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 8).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 7).
TISSUE=Muscle, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 271-477 (ISOFORM 3).
PubMed=9383298; DOI=10.1007/s003359900621;
Smith J.E. Jr., Afonja O., Yee H.T., Inghirami G., Takeshita K.;
"Chromosomal mapping to 15q14 and expression analysis of the human
MEIS2 homeobox gene.";
Mamm. Genome 8:951-952(1997).
[7]
FUNCTION.
PubMed=11279116; DOI=10.1074/jbc.M100678200;
Liu Y., MacDonald R.J., Swift G.H.;
"DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b
trimer and cooperation with a pancreas-specific basic helix-loop-helix
complex.";
J. Biol. Chem. 276:17985-17993(2001).
[8]
DEVELOPMENTAL STAGE.
PubMed=20523026; DOI=10.1159/000297602;
Larsen K.B., Lutterodt M.C., Laursen H., Graem N., Pakkenberg B.,
Mollgard K., Moller M.;
"Spatiotemporal distribution of PAX6 and MEIS2 expression and total
cell numbers in the ganglionic eminence in the early developing human
forebrain.";
Dev. Neurosci. 32:149-162(2010).
[9]
DOMAIN, INTERACTION WITH PBX1, AND MUTAGENESIS OF LEU-85; LEU-88;
94-GLU--GLU-97; ILE-151; LEU-154; 158-LEU-LEU-159; LEU-161 AND
ARG-332.
PubMed=20553494; DOI=10.1111/j.1742-4658.2010.07668.x;
Hyman-Walsh C., Bjerke G.A., Wotton D.;
"An autoinhibitory effect of the homothorax domain of Meis2.";
FEBS J. 277:2584-2597(2010).
[10]
INTERACTION WITH TLX1.
PubMed=19559479; DOI=10.1016/j.leukres.2009.06.003;
Milech N., Gottardo N.G., Ford J., D'Souza D., Greene W.K., Kees U.R.,
Watt P.M.;
"MEIS proteins as partners of the TLX1/HOX11 oncoprotein.";
Leuk. Res. 34:358-363(2010).
[11]
FUNCTION, INTERACTION WITH SP1; SP3 AND KLF4, AND MUTAGENESIS OF
ARG-332.
PubMed=21746878; DOI=10.1128/MCB.01456-10;
Bjerke G.A., Hyman-Walsh C., Wotton D.;
"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1.";
Mol. Cell. Biol. 31:3723-3733(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
INVOLVEMENT IN CPCMR.
PubMed=24678003; DOI=10.1002/ajmg.a.36498;
Johansson S., Berland S., Gradek G.A., Bongers E., de Leeuw N.,
Pfundt R., Fannemel M., Roedningen O., Brendehaug A., Haukanes B.I.,
Hovland R., Helland G., Houge G.;
"Haploinsufficiency of MEIS2 is associated with orofacial clefting and
learning disability.";
Am. J. Med. Genet. A 164A:1622-1626(2014).
[14]
INVOLVEMENT IN CPCMR, AND VARIANT CPCMR ARG-333 DEL.
PubMed=25712757; DOI=10.1002/ajmg.a.36989;
Louw J.J., Corveleyn A., Jia Y., Hens G., Gewillig M., Devriendt K.;
"MEIS2 involvement in cardiac development, cleft palate, and
intellectual disability.";
Am. J. Med. Genet. A 167A:1142-1146(2015).
[15]
INVOLVEMENT IN CPCMR, AND VARIANT CPCMR 204-SER--GLN-477 DEL.
PubMed=27225850; DOI=10.1038/jhg.2016.54;
Fujita A., Isidor B., Piloquet H., Corre P., Okamoto N., Nakashima M.,
Tsurusaki Y., Saitsu H., Miyake N., Matsumoto N.;
"De novo MEIS2 mutation causes syndromic developmental delay with
persistent gastro-esophageal reflux.";
J. Hum. Genet. 61:835-838(2016).
-!- FUNCTION: Involved in transcriptional regulation. Binds to HOX or
PBX proteins to form dimers, or to a DNA-bound dimer of PBX and
HOX proteins and thought to have a role in stabilization of the
homeoprotein-DNA complex. Isoform 3 is required for the activity
of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved
in the transcriptional activation of the ELA1 enhancer; the
complex binds to the enhancer B element and cooperates with the
transcription factor 1 complex (PTF1) bound to the enhancer A
element; MEIS2 is not involved in complex DNA-binding. Probably in
complex with PBX1, is involved in transcriptional regulation by
KLF4. Isoform 3 and isoform 4 can bind to a EPHA8 promoter
sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation
with a PBX protein (such as PBX2) is proposed to be involved in
the transcriptional activation of EPHA8 in the developing
midbrain. May be involved in regulation of myeloid
differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the
activator ACT sequence of the D(1A) dopamine receptor (DRD1)
promoter and activate DRD1 transcription; isoform 5 cannot
activate DRD1 transcription. {ECO:0000269|PubMed:10764806,
ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:21746878}.
-!- SUBUNIT: Isoform 2 interacts with TLX1. Isoform 3 interacts with
HOXA13 and PBX1 isoform PBX1b. Isoform 4 interacts with SP1, SP3
and KLF4. Isoform 4 and isoform 5 interact with PBX1 isoform
PBX1a; the interaction partially relieves MEIS2 autoinhibition.
Isoform 3 also known as MEIS2b is part of a PDX1:PBX1b:Meis2B
complex; Meis2B is recruited by PBX1b and can be replaced by
isoform 4 in a small fraction of complexes. Can form trimeric
complexes including HOXB8 and PBX2 or PBX3.
{ECO:0000269|PubMed:19559479, ECO:0000269|PubMed:20553494,
ECO:0000269|PubMed:21746878}.
-!- INTERACTION:
Q5TZZ9:ANXA1; NbExp=3; IntAct=EBI-2804934, EBI-10181435;
Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-2804934, EBI-946029;
A0A1B0GWI1:CCDC196; NbExp=4; IntAct=EBI-8025850, EBI-10181422;
P03363:gag-pro-pol (xeno); NbExp=3; IntAct=EBI-2804934, EBI-9676133;
Q9BVL2:NUP58; NbExp=4; IntAct=EBI-8025850, EBI-2811583;
O43482:OIP5; NbExp=4; IntAct=EBI-8025850, EBI-536879;
Q9UJX0:OSGIN1; NbExp=3; IntAct=EBI-2804934, EBI-9057006;
P40424:PBX1; NbExp=8; IntAct=EBI-8025850, EBI-301611;
Q9BYU1:PBX4; NbExp=6; IntAct=EBI-8025850, EBI-10302990;
P31314:TLX1; NbExp=4; IntAct=EBI-6390216, EBI-2820655;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00108}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P97367}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=Meis2C;
IsoId=O14770-1; Sequence=Displayed;
Name=2; Synonyms=Meis2A;
IsoId=O14770-2; Sequence=VSP_002245, VSP_002246;
Name=3; Synonyms=Meis2B;
IsoId=O14770-3; Sequence=VSP_002242, VSP_002245, VSP_002246;
Name=4; Synonyms=Meis2D;
IsoId=O14770-4; Sequence=VSP_002242;
Name=5; Synonyms=Meis2E;
IsoId=O14770-5; Sequence=VSP_002243, VSP_002244;
Name=6;
IsoId=O14770-6; Sequence=VSP_043219, VSP_002242, VSP_002245,
VSP_002246;
Name=7;
IsoId=O14770-7; Sequence=VSP_043494, VSP_002242, VSP_002245,
VSP_002246;
Note=No experimental confirmation available.;
Name=8;
IsoId=O14770-8; Sequence=VSP_043494, VSP_002245, VSP_002246;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in various tissues. Expressed at
high level in the lymphoid organs of hematopoietic tissues. Also
expressed in some regions of the brain, such as the putamen.
-!- DEVELOPMENTAL STAGE: Expressed in the proliferative zones of the
fetal neocortex. Expressed at a very high level in the developing
ganglionic eminence and at a more moderate level in the cortical
plate. {ECO:0000269|PubMed:20523026}.
-!- DISEASE: Cleft palate, cardiac defects, and mental retardation
(CPCMR) [MIM:600987]: An autosomal dominant disease characterized
by multiple congenital malformations, mild-to-severe intellectual
disability with poor speech, and delayed psychomotor development.
Congenital malformations include heart defects, cleft lip/palate,
distally-placed thumbs and toes, and cutaneous syndactyly between
the second and third toes. {ECO:0000269|PubMed:24678003,
ECO:0000269|PubMed:25712757, ECO:0000269|PubMed:27225850}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the TALE/MEIS homeobox family.
{ECO:0000305}.
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EMBL; AF178948; AAF81638.1; -; mRNA.
EMBL; AF179896; AAF81639.1; -; mRNA.
EMBL; AF179897; AAF81640.1; -; mRNA.
EMBL; AF179898; AAF81641.1; -; mRNA.
EMBL; AF179899; AAF81642.1; -; mRNA.
EMBL; AK056038; BAG51610.1; -; mRNA.
EMBL; AK056620; BAG51768.1; -; mRNA.
EMBL; AC018563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC069483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC078909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471125; EAW92353.1; -; Genomic_DNA.
EMBL; CH471125; EAW92354.1; -; Genomic_DNA.
EMBL; CH471125; EAW92356.1; -; Genomic_DNA.
EMBL; BC001516; AAH01516.1; -; mRNA.
EMBL; BC001844; AAH01844.3; -; mRNA.
EMBL; BC007202; AAH07202.1; -; mRNA.
EMBL; BC050431; AAH50431.1; -; mRNA.
EMBL; AF017418; AAB70270.1; -; mRNA.
CCDS; CCDS10044.1; -. [O14770-1]
CCDS; CCDS10045.1; -. [O14770-4]
CCDS; CCDS42014.1; -. [O14770-7]
CCDS; CCDS45217.1; -. [O14770-2]
CCDS; CCDS45218.1; -. [O14770-3]
CCDS; CCDS45219.1; -. [O14770-8]
CCDS; CCDS45220.1; -. [O14770-6]
RefSeq; NP_001207411.1; NM_001220482.1. [O14770-4]
RefSeq; NP_002390.1; NM_002399.3. [O14770-7]
RefSeq; NP_733774.1; NM_170674.4. [O14770-3]
RefSeq; NP_733775.1; NM_170675.4. [O14770-1]
RefSeq; NP_733776.1; NM_170676.4. [O14770-4]
RefSeq; NP_733777.1; NM_170677.4. [O14770-2]
RefSeq; NP_758526.1; NM_172315.2. [O14770-8]
RefSeq; NP_758527.1; NM_172316.2. [O14770-6]
RefSeq; XP_016877694.1; XM_017022205.1. [O14770-6]
UniGene; Hs.510989; -.
PDB; 3K2A; X-ray; 1.95 A; A/B=281-345.
PDB; 4XRM; X-ray; 1.60 A; A/B=281-342.
PDB; 5BNG; X-ray; 3.50 A; A/B=283-342.
PDB; 5EG0; X-ray; 3.10 A; A=284-338.
PDBsum; 3K2A; -.
PDBsum; 4XRM; -.
PDBsum; 5BNG; -.
PDBsum; 5EG0; -.
ProteinModelPortal; O14770; -.
SMR; O14770; -.
BioGrid; 110376; 32.
DIP; DIP-61027N; -.
IntAct; O14770; 31.
MINT; O14770; -.
STRING; 9606.ENSP00000453793; -.
iPTMnet; O14770; -.
PhosphoSitePlus; O14770; -.
BioMuta; MEIS2; -.
MaxQB; O14770; -.
PaxDb; O14770; -.
PeptideAtlas; O14770; -.
PRIDE; O14770; -.
DNASU; 4212; -.
Ensembl; ENST00000314177; ENSP00000326296; ENSG00000134138. [O14770-5]
Ensembl; ENST00000338564; ENSP00000341400; ENSG00000134138. [O14770-4]
Ensembl; ENST00000340545; ENSP00000339549; ENSG00000134138. [O14770-7]
Ensembl; ENST00000397620; ENSP00000380745; ENSG00000134138. [O14770-6]
Ensembl; ENST00000397624; ENSP00000380749; ENSG00000134138. [O14770-6]
Ensembl; ENST00000424352; ENSP00000404185; ENSG00000134138. [O14770-2]
Ensembl; ENST00000557796; ENSP00000452693; ENSG00000134138. [O14770-7]
Ensembl; ENST00000559085; ENSP00000453390; ENSG00000134138. [O14770-8]
Ensembl; ENST00000559561; ENSP00000453497; ENSG00000134138. [O14770-3]
Ensembl; ENST00000561208; ENSP00000453793; ENSG00000134138. [O14770-1]
GeneID; 4212; -.
KEGG; hsa:4212; -.
UCSC; uc001zjl.4; human. [O14770-1]
CTD; 4212; -.
DisGeNET; 4212; -.
EuPathDB; HostDB:ENSG00000134138.19; -.
GeneCards; MEIS2; -.
HGNC; HGNC:7001; MEIS2.
HPA; CAB004999; -.
HPA; HPA003256; -.
MalaCards; MEIS2; -.
MIM; 600987; phenotype.
MIM; 601740; gene.
neXtProt; NX_O14770; -.
OpenTargets; ENSG00000134138; -.
Orphanet; 261190; 15q14 microdeletion syndrome.
PharmGKB; PA30741; -.
eggNOG; KOG0773; Eukaryota.
eggNOG; ENOG410XPMQ; LUCA.
GeneTree; ENSGT00550000074260; -.
HOGENOM; HOG000253923; -.
HOVERGEN; HBG055193; -.
InParanoid; O14770; -.
KO; K16670; -.
OMA; PGEYVPQ; -.
OrthoDB; EOG091G0KDP; -.
PhylomeDB; O14770; -.
TreeFam; TF318093; -.
ChiTaRS; MEIS2; human.
EvolutionaryTrace; O14770; -.
GeneWiki; MEIS2; -.
GenomeRNAi; 4212; -.
PRO; PR:O14770; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000134138; -.
CleanEx; HS_MEIS2; -.
ExpressionAtlas; O14770; baseline and differential.
Genevisible; O14770; HS.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003700; F:DNA binding transcription factor activity; NAS:ProtInc.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISM:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003712; F:transcription cofactor activity; ISS:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001654; P:eye development; IEA:Ensembl.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0031016; P:pancreas development; IEA:Ensembl.
GO; GO:0110024; P:positive regulation of cardiac muscle myoblast proliferation; IDA:BHF-UCL.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
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;
3D-structure; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Developmental protein; Disease mutation; DNA-binding;
Homeobox; Mental retardation; Nucleus; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 477 Homeobox protein Meis2.
/FTId=PRO_0000049108.
DNA_BIND 276 338 Homeobox; TALE-type.
{ECO:0000255|PROSITE-ProRule:PRU00108}.
REGION 71 191 Required for interaction with PBX1.
{ECO:0000250}.
REGION 340 477 Transcriptional activation domain.
COMPBIAS 195 244 Ser/Thr-rich.
COMPBIAS 246 273 Asp/Glu-rich (acidic).
COMPBIAS 266 273 Poly-Asp.
VAR_SEQ 1 89 MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNH
GPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAIYG
HPLFPLL -> M (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043219.
VAR_SEQ 1 13 Missing (in isoform 7 and isoform 8).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_043494.
VAR_SEQ 301 302 HP -> VY (in isoform 5).
{ECO:0000303|PubMed:10764806}.
/FTId=VSP_002243.
VAR_SEQ 303 477 Missing (in isoform 5).
{ECO:0000303|PubMed:10764806}.
/FTId=VSP_002244.
VAR_SEQ 346 352 Missing (in isoform 3, isoform 4, isoform
6 and isoform 7).
{ECO:0000303|PubMed:10764806,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9383298}.
/FTId=VSP_002242.
VAR_SEQ 384 401 LQSMPGDYVSQGGPMGMS -> PMSGMGMNMGMDGQWHYM
(in isoform 2, isoform 3, isoform 6,
isoform 7 and isoform 8).
{ECO:0000303|PubMed:10764806,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9383298}.
/FTId=VSP_002245.
VAR_SEQ 402 477 Missing (in isoform 2, isoform 3, isoform
6, isoform 7 and isoform 8).
{ECO:0000303|PubMed:10764806,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9383298}.
/FTId=VSP_002246.
VARIANT 204 477 Missing (in CPCMR).
{ECO:0000269|PubMed:27225850}.
/FTId=VAR_078978.
VARIANT 333 333 Missing (in CPCMR).
{ECO:0000269|PubMed:25712757}.
/FTId=VAR_078979.
MUTAGEN 85 85 L->A: Impairs interaction with PBX1; when
associated with A-88.
{ECO:0000269|PubMed:20553494}.
MUTAGEN 88 88 L->A: Impairs interaction with PBX1; when
associated with A-85. HELIX 285 297.
{ECO:0000269|PubMed:20553494}.
MUTAGEN 94 97 EKCE->NNGT: Impairs interaction with
PBX1. {ECO:0000269|PubMed:20553494}.
MUTAGEN 151 151 I->A: Impairs interaction with PBX1; when
associated with A-154.
{ECO:0000269|PubMed:20553494}.
MUTAGEN 154 154 L->A: Impairs interaction with PBX1; when
associated with A-151.
{ECO:0000269|PubMed:20553494}.
MUTAGEN 158 159 LL->AA: Impairs interaction with PBX1;
when associated with A-161.
{ECO:0000269|PubMed:20553494}.
MUTAGEN 161 161 L->A: Impairs interaction with PBX1; when
associated with 158-A-A-159.
{ECO:0000269|PubMed:20553494}.
MUTAGEN 332 332 R->M: Impairs DNA binding and PBX1-
dependent transcriptional activation. No
effect on interaction with PBX1.
{ECO:0000269|PubMed:20553494,
ECO:0000269|PubMed:21746878}.
HELIX 287 296 {ECO:0000244|PDB:4XRM}.
TURN 298 300 {ECO:0000244|PDB:3K2A}.
HELIX 306 316 {ECO:0000244|PDB:4XRM}.
HELIX 320 333 {ECO:0000244|PDB:4XRM}.
HELIX 335 339 {ECO:0000244|PDB:4XRM}.
SEQUENCE 477 AA; 51790 MW; 94EBD0801A312B24 CRC64;
MAQRYDELPH YGGMDGVGVP ASMYGDPHAP RPIPPVHHLN HGPPLHATQH YGAHAPHPNV
MPASMGSAVN DALKRDKDAI YGHPLFPLLA LVFEKCELAT CTPREPGVAG GDVCSSDSFN
EDIAVFAKQV RAEKPLFSSN PELDNLMIQA IQVLRFHLLE LEKVHELCDN FCHRYISCLK
GKMPIDLVID ERDGSSKSDH EELSGSSTNL ADHNPSSWRD HDDATSTHSA GTPGPSSGGH
ASQSGDNSSE QGDGLDNSVA SPGTGDDDDP DKDKKRQKKR GIFPKVATNI MRAWLFQHLT
HPYPSEEQKK QLAQDTGLTI LQVNNWFINA RRRIVQPMID QSNRAGFLLD PSVSQGAAYS
PEGQPMGSFV LDGQQHMGIR PAGLQSMPGD YVSQGGPMGM SMAQPSYTPP QMTPHPTQLR
HGPPMHSYLP SHPHHPAMMM HGGPPTHPGM TMSAQSPTML NSVDPNVGGQ VMDIHAQ


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