MEIS2_HUMAN
ID MEIS2_HUMAN Reviewed; 477 AA.
AC O14770; A6NJI5; A8MWD5; B3KP98; B3KPQ6; Q96DI2; Q96KI4; Q96KI5; Q9NRS1;
AC Q9NRS2; Q9NRS3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Homeobox protein Meis2;
DE AltName: Full=Meis1-related protein 1;
GN Name=MEIS2; Synonyms=MRG1;
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 AND 5), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10764806; DOI=10.1074/jbc.m908382199;
RA Yang Y., Hwang C.K., D'Souza U.M., Lee S.-H., Junn E., Mouradian M.M.;
RT "Three-amino acid extension loop homeodomain proteins Meis2 and TGIF
RT differentially regulate transcription.";
RL J. Biol. Chem. 275:20734-20741(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 8).
RC TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 7).
RC TISSUE=Muscle, 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 271-477 (ISOFORM 3).
RX PubMed=9383298; DOI=10.1007/s003359900621;
RA Smith J.E. Jr., Afonja O., Yee H.T., Inghirami G., Takeshita K.;
RT "Chromosomal mapping to 15q14 and expression analysis of the human MEIS2
RT homeobox gene.";
RL Mamm. Genome 8:951-952(1997).
RN [7]
RP FUNCTION.
RX PubMed=11279116; DOI=10.1074/jbc.m100678200;
RA Liu Y., MacDonald R.J., Swift G.H.;
RT "DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b trimer
RT and cooperation with a pancreas-specific basic helix-loop-helix complex.";
RL J. Biol. Chem. 276:17985-17993(2001).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=20523026; DOI=10.1159/000297602;
RA Larsen K.B., Lutterodt M.C., Laursen H., Graem N., Pakkenberg B.,
RA Mollgard K., Moller M.;
RT "Spatiotemporal distribution of PAX6 and MEIS2 expression and total cell
RT numbers in the ganglionic eminence in the early developing human
RT forebrain.";
RL Dev. Neurosci. 32:149-162(2010).
RN [9]
RP DOMAIN, INTERACTION WITH PBX1, AND MUTAGENESIS OF LEU-85; LEU-88;
RP 94-GLU--GLU-97; ILE-151; LEU-154; 158-LEU-LEU-159; LEU-161 AND ARG-332.
RX PubMed=20553494; DOI=10.1111/j.1742-4658.2010.07668.x;
RA Hyman-Walsh C., Bjerke G.A., Wotton D.;
RT "An autoinhibitory effect of the homothorax domain of Meis2.";
RL FEBS J. 277:2584-2597(2010).
RN [10]
RP INTERACTION WITH TLX1.
RX PubMed=19559479; DOI=10.1016/j.leukres.2009.06.003;
RA Milech N., Gottardo N.G., Ford J., D'Souza D., Greene W.K., Kees U.R.,
RA Watt P.M.;
RT "MEIS proteins as partners of the TLX1/HOX11 oncoprotein.";
RL Leuk. Res. 34:358-363(2010).
RN [11]
RP FUNCTION, INTERACTION WITH SP1; SP3 AND KLF4, AND MUTAGENESIS OF ARG-332.
RX PubMed=21746878; DOI=10.1128/mcb.01456-10;
RA Bjerke G.A., Hyman-Walsh C., Wotton D.;
RT "Cooperative transcriptional activation by Klf4, Meis2, and Pbx1.";
RL Mol. Cell. Biol. 31:3723-3733(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP INVOLVEMENT IN CPCMR.
RX PubMed=24678003; DOI=10.1002/ajmg.a.36498;
RA Johansson S., Berland S., Gradek G.A., Bongers E., de Leeuw N., Pfundt R.,
RA Fannemel M., Roedningen O., Brendehaug A., Haukanes B.I., Hovland R.,
RA Helland G., Houge G.;
RT "Haploinsufficiency of MEIS2 is associated with orofacial clefting and
RT learning disability.";
RL Am. J. Med. Genet. A 164A:1622-1626(2014).
RN [14] {ECO:0007744|PDB:3K2A}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 281-345.
RA Lam R., Soloveychik M., Battaile K.P., Romanov V., Lam K., Beletskaya I.,
RA Gordon E., Pai E.F., Chirgadze N.Y.;
RT "Crystal structure of the homeobox domain of human homeobox protein
RT Meis2.";
RL Submitted (SEP-2009) to the PDB data bank.
RN [15] {ECO:0007744|PDB:4XRM, ECO:0007744|PDB:5BNG}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 281-342 IN COMPLEX WITH DNA,
RP SUBUNIT, AND DNA-BINDING.
RX PubMed=26550823; DOI=10.1038/nature15518;
RA Jolma A., Yin Y., Nitta K.R., Dave K., Popov A., Taipale M., Enge M.,
RA Kivioja T., Morgunova E., Taipale J.;
RT "DNA-dependent formation of transcription factor pairs alters their binding
RT specificity.";
RL Nature 527:384-388(2015).
RN [16] {ECO:0007744|PDB:5EG0}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 284-338 IN COMPLEX WITH HOXB13
RP AND DNA, SUBUNIT, AND DNA-BINDING.
RA Morgunova E., Yin Y., Jolma A., Popov A., Taipale J.;
RT "Molecular basis of recognition of two distinct DNA sequences by a single
RT transcription factor.";
RL Submitted (OCT-2015) to the PDB data bank.
RN [17]
RP INVOLVEMENT IN CPCMR, AND VARIANT CPCMR ARG-333 DEL.
RX PubMed=25712757; DOI=10.1002/ajmg.a.36989;
RA Louw J.J., Corveleyn A., Jia Y., Hens G., Gewillig M., Devriendt K.;
RT "MEIS2 involvement in cardiac development, cleft palate, and intellectual
RT disability.";
RL Am. J. Med. Genet. A 167A:1142-1146(2015).
RN [18]
RP INVOLVEMENT IN CPCMR, AND VARIANT CPCMR 204-SER--GLN-477 DEL.
RX PubMed=27225850; DOI=10.1038/jhg.2016.54;
RA Fujita A., Isidor B., Piloquet H., Corre P., Okamoto N., Nakashima M.,
RA Tsurusaki Y., Saitsu H., Miyake N., Matsumoto N.;
RT "De novo MEIS2 mutation causes syndromic developmental delay with
RT persistent gastro-esophageal reflux.";
RL J. Hum. Genet. 61:835-838(2016).
CC -!- FUNCTION: Involved in transcriptional regulation. Binds to HOX or PBX
CC proteins to form dimers, or to a DNA-bound dimer of PBX and HOX
CC proteins and thought to have a role in stabilization of the
CC homeoprotein-DNA complex. Isoform 3 is required for the activity of a
CC PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the
CC transcriptional activation of the ELA1 enhancer; the complex binds to
CC the enhancer B element and cooperates with the transcription factor 1
CC complex (PTF1) bound to the enhancer A element; MEIS2 is not involved
CC in complex DNA-binding. Probably in complex with PBX1, is involved in
CC transcriptional regulation by KLF4. Isoform 3 and isoform 4 can bind to
CC a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in
CC cooperation with a PBX protein (such as PBX2) is proposed to be
CC involved in the transcriptional activation of EPHA8 in the developing
CC midbrain. May be involved in regulation of myeloid differentiation. Can
CC bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of
CC the D(1A) dopamine receptor (DRD1) promoter and activate DRD1
CC transcription; isoform 5 cannot activate DRD1 transcription.
CC {ECO:0000269|PubMed:10764806, ECO:0000269|PubMed:11279116,
CC ECO:0000269|PubMed:21746878}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:26550823). Heterodimer with
CC HOXB13 (Ref.16). Isoform 2 interacts with TLX1. Isoform 3 interacts
CC with HOXA13 and PBX1 isoform PBX1b. Isoform 4 interacts with SP1, SP3
CC and KLF4. Isoform 4 and isoform 5 interact with PBX1 isoform PBX1a; the
CC interaction partially relieves MEIS2 autoinhibition. Isoform 3 also
CC known as MEIS2b is part of a PDX1:PBX1b:Meis2B complex; Meis2B is
CC recruited by PBX1b and can be replaced by isoform 4 in a small fraction
CC of complexes. Can form trimeric complexes including HOXB8 and PBX2 or
CC PBX3. {ECO:0000269|PubMed:19559479, ECO:0000269|PubMed:20553494,
CC ECO:0000269|PubMed:21746878, ECO:0000269|PubMed:26550823,
CC ECO:0000269|Ref.16}.
CC -!- INTERACTION:
CC O14770; Q5TZZ9: ANXA1; NbExp=3; IntAct=EBI-2804934, EBI-10181435;
CC O14770; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-2804934, EBI-946029;
CC O14770; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-2804934, EBI-10181422;
CC O14770; Q9UJX0: OSGIN1; NbExp=4; IntAct=EBI-2804934, EBI-9057006;
CC O14770; P03363: gag-pro-pol; Xeno; NbExp=3; IntAct=EBI-2804934, EBI-9676133;
CC O14770-2; P31314: TLX1; NbExp=4; IntAct=EBI-6390216, EBI-2820655;
CC O14770-4; P18825: ADRA2C; NbExp=3; IntAct=EBI-8025850, EBI-12015266;
CC O14770-4; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-8025850, EBI-713602;
CC O14770-4; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-8025850, EBI-953896;
CC O14770-4; Q16568: CARTPT; NbExp=3; IntAct=EBI-8025850, EBI-4314526;
CC O14770-4; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-8025850, EBI-10181422;
CC O14770-4; P78358: CTAG1B; NbExp=3; IntAct=EBI-8025850, EBI-1188472;
CC O14770-4; Q96C01: FAM136A; NbExp=3; IntAct=EBI-8025850, EBI-373319;
CC O14770-4; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-8025850, EBI-11978259;
CC O14770-4; P24592: IGFBP6; NbExp=3; IntAct=EBI-8025850, EBI-947015;
CC O14770-4; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-8025850, EBI-712105;
CC O14770-4; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8025850, EBI-10171774;
CC O14770-4; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-8025850, EBI-1052037;
CC O14770-4; Q3LHN2: KRTAP19-2; NbExp=5; IntAct=EBI-8025850, EBI-12196745;
CC O14770-4; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-8025850, EBI-12805508;
CC O14770-4; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-8025850, EBI-12111050;
CC O14770-4; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-8025850, EBI-11962084;
CC O14770-4; P59942: MCCD1; NbExp=3; IntAct=EBI-8025850, EBI-11987923;
CC O14770-4; P17568: NDUFB7; NbExp=3; IntAct=EBI-8025850, EBI-1246238;
CC O14770-4; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-8025850, EBI-17490746;
CC O14770-4; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-8025850, EBI-2811583;
CC O14770-4; O43482: OIP5; NbExp=3; IntAct=EBI-8025850, EBI-536879;
CC O14770-4; P40424: PBX1; NbExp=9; IntAct=EBI-8025850, EBI-301611;
CC O14770-4; Q9BYU1: PBX4; NbExp=6; IntAct=EBI-8025850, EBI-10302990;
CC O14770-4; Q16633: POU2AF1; NbExp=3; IntAct=EBI-8025850, EBI-943588;
CC O14770-4; P78424: POU6F2; NbExp=3; IntAct=EBI-8025850, EBI-12029004;
CC O14770-4; Q13882: PTK6; NbExp=3; IntAct=EBI-8025850, EBI-1383632;
CC O14770-4; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-8025850, EBI-6257312;
CC O14770-4; P09683: SCT; NbExp=3; IntAct=EBI-8025850, EBI-12844598;
CC O14770-4; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-8025850, EBI-10269322;
CC O14770-4; Q13207: TBX2; NbExp=3; IntAct=EBI-8025850, EBI-2853051;
CC O14770-4; Q9Y5J6: TIMM10B; NbExp=3; IntAct=EBI-8025850, EBI-1200382;
CC O14770-4; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-8025850, EBI-5235829;
CC O14770-4; Q99990: VGLL1; NbExp=3; IntAct=EBI-8025850, EBI-11983165;
CC O14770-7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-25848073, EBI-25882629;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97367}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=Meis2C;
CC IsoId=O14770-1; Sequence=Displayed;
CC Name=2; Synonyms=Meis2A;
CC IsoId=O14770-2; Sequence=VSP_002245, VSP_002246;
CC Name=3; Synonyms=Meis2B;
CC IsoId=O14770-3; Sequence=VSP_002242, VSP_002245, VSP_002246;
CC Name=4; Synonyms=Meis2D;
CC IsoId=O14770-4; Sequence=VSP_002242;
CC Name=5; Synonyms=Meis2E;
CC IsoId=O14770-5; Sequence=VSP_002243, VSP_002244;
CC Name=6;
CC IsoId=O14770-6; Sequence=VSP_043219, VSP_002242, VSP_002245,
CC VSP_002246;
CC Name=7;
CC IsoId=O14770-7; Sequence=VSP_043494, VSP_002242, VSP_002245,
CC VSP_002246;
CC Name=8;
CC IsoId=O14770-8; Sequence=VSP_043494, VSP_002245, VSP_002246;
CC -!- TISSUE SPECIFICITY: Expressed in various tissues. Expressed at high
CC level in the lymphoid organs of hematopoietic tissues. Also expressed
CC in some regions of the brain, such as the putamen.
CC -!- DEVELOPMENTAL STAGE: Expressed in the proliferative zones of the fetal
CC neocortex. Expressed at a very high level in the developing ganglionic
CC eminence and at a more moderate level in the cortical plate.
CC {ECO:0000269|PubMed:20523026}.
CC -!- DISEASE: Cleft palate, cardiac defects, and intellectual disability
CC (CPCMR) [MIM:600987]: An autosomal dominant disease characterized by
CC multiple congenital malformations, mild-to-severe intellectual
CC disability with poor speech, and delayed psychomotor development.
CC Congenital malformations include heart defects, cleft lip/palate,
CC distally-placed thumbs and toes, and cutaneous syndactyly between the
CC second and third toes. {ECO:0000269|PubMed:24678003,
CC ECO:0000269|PubMed:25712757, ECO:0000269|PubMed:27225850}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TALE/MEIS homeobox family. {ECO:0000305}.
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DR EMBL; AF178948; AAF81638.1; -; mRNA.
DR EMBL; AF179896; AAF81639.1; -; mRNA.
DR EMBL; AF179897; AAF81640.1; -; mRNA.
DR EMBL; AF179898; AAF81641.1; -; mRNA.
DR EMBL; AF179899; AAF81642.1; -; mRNA.
DR EMBL; AK056038; BAG51610.1; -; mRNA.
DR EMBL; AK056620; BAG51768.1; -; mRNA.
DR EMBL; AC018563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92353.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92354.1; -; Genomic_DNA.
DR EMBL; CH471125; EAW92356.1; -; Genomic_DNA.
DR EMBL; BC001516; AAH01516.1; -; mRNA.
DR EMBL; BC001844; AAH01844.3; -; mRNA.
DR EMBL; BC007202; AAH07202.1; -; mRNA.
DR EMBL; BC050431; AAH50431.1; -; mRNA.
DR EMBL; AF017418; AAB70270.1; -; mRNA.
DR CCDS; CCDS10044.1; -. [O14770-1]
DR CCDS; CCDS10045.1; -. [O14770-4]
DR CCDS; CCDS42014.1; -. [O14770-7]
DR CCDS; CCDS45217.1; -. [O14770-2]
DR CCDS; CCDS45218.1; -. [O14770-3]
DR CCDS; CCDS45219.1; -. [O14770-8]
DR CCDS; CCDS45220.1; -. [O14770-6]
DR RefSeq; NP_001207411.1; NM_001220482.1. [O14770-4]
DR RefSeq; NP_002390.1; NM_002399.3. [O14770-7]
DR RefSeq; NP_733774.1; NM_170674.4. [O14770-3]
DR RefSeq; NP_733775.1; NM_170675.4. [O14770-1]
DR RefSeq; NP_733776.1; NM_170676.4. [O14770-4]
DR RefSeq; NP_733777.1; NM_170677.4. [O14770-2]
DR RefSeq; NP_758526.1; NM_172315.2. [O14770-8]
DR RefSeq; NP_758527.1; NM_172316.2. [O14770-6]
DR RefSeq; XP_016877694.1; XM_017022205.1. [O14770-6]
DR PDB; 3K2A; X-ray; 1.95 A; A/B=281-345.
DR PDB; 4XRM; X-ray; 1.60 A; A/B=281-342.
DR PDB; 5BNG; X-ray; 3.50 A; A/B=283-342.
DR PDB; 5EG0; X-ray; 3.10 A; A=284-338.
DR PDBsum; 3K2A; -.
DR PDBsum; 4XRM; -.
DR PDBsum; 5BNG; -.
DR PDBsum; 5EG0; -.
DR AlphaFoldDB; O14770; -.
DR SMR; O14770; -.
DR BioGRID; 110376; 84.
DR DIP; DIP-61027N; -.
DR IntAct; O14770; 63.
DR MINT; O14770; -.
DR STRING; 9606.ENSP00000453793; -.
DR GlyGen; O14770; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14770; -.
DR PhosphoSitePlus; O14770; -.
DR BioMuta; MEIS2; -.
DR EPD; O14770; -.
DR jPOST; O14770; -.
DR MassIVE; O14770; -.
DR MaxQB; O14770; -.
DR PaxDb; O14770; -.
DR PeptideAtlas; O14770; -.
DR PRIDE; O14770; -.
DR ProteomicsDB; 48214; -. [O14770-1]
DR ProteomicsDB; 48215; -. [O14770-2]
DR ProteomicsDB; 48216; -. [O14770-3]
DR ProteomicsDB; 48217; -. [O14770-4]
DR ProteomicsDB; 48218; -. [O14770-5]
DR ProteomicsDB; 48219; -. [O14770-6]
DR ProteomicsDB; 48220; -. [O14770-7]
DR ProteomicsDB; 48221; -. [O14770-8]
DR Antibodypedia; 918; 306 antibodies from 36 providers.
DR DNASU; 4212; -.
DR Ensembl; ENST00000314177.12; ENSP00000326296.8; ENSG00000134138.20. [O14770-5]
DR Ensembl; ENST00000338564.9; ENSP00000341400.4; ENSG00000134138.20. [O14770-4]
DR Ensembl; ENST00000340545.9; ENSP00000339549.5; ENSG00000134138.20. [O14770-7]
DR Ensembl; ENST00000397620.6; ENSP00000380745.2; ENSG00000134138.20. [O14770-6]
DR Ensembl; ENST00000397624.7; ENSP00000380749.3; ENSG00000134138.20. [O14770-6]
DR Ensembl; ENST00000424352.6; ENSP00000404185.2; ENSG00000134138.20. [O14770-2]
DR Ensembl; ENST00000557796.6; ENSP00000452693.2; ENSG00000134138.20. [O14770-7]
DR Ensembl; ENST00000559085.5; ENSP00000453390.1; ENSG00000134138.20. [O14770-8]
DR Ensembl; ENST00000559561.5; ENSP00000453497.1; ENSG00000134138.20. [O14770-3]
DR Ensembl; ENST00000561208.6; ENSP00000453793.1; ENSG00000134138.20. [O14770-1]
DR GeneID; 4212; -.
DR KEGG; hsa:4212; -.
DR MANE-Select; ENST00000561208.6; ENSP00000453793.1; NM_170675.5; NP_733775.1.
DR UCSC; uc001zjl.4; human. [O14770-1]
DR CTD; 4212; -.
DR DisGeNET; 4212; -.
DR GeneCards; MEIS2; -.
DR HGNC; HGNC:7001; MEIS2.
DR HPA; ENSG00000134138; Low tissue specificity.
DR MalaCards; MEIS2; -.
DR MIM; 600987; phenotype.
DR MIM; 601740; gene.
DR neXtProt; NX_O14770; -.
DR OpenTargets; ENSG00000134138; -.
DR Orphanet; 261190; 15q14 microdeletion syndrome.
DR PharmGKB; PA30741; -.
DR VEuPathDB; HostDB:ENSG00000134138; -.
DR eggNOG; KOG0773; Eukaryota.
DR GeneTree; ENSGT00940000155643; -.
DR HOGENOM; CLU_023139_0_0_1; -.
DR InParanoid; O14770; -.
DR OMA; QIMDIHA; -.
DR PhylomeDB; O14770; -.
DR TreeFam; TF318093; -.
DR PathwayCommons; O14770; -.
DR SignaLink; O14770; -.
DR SIGNOR; O14770; -.
DR BioGRID-ORCS; 4212; 28 hits in 1106 CRISPR screens.
DR ChiTaRS; MEIS2; human.
DR EvolutionaryTrace; O14770; -.
DR GeneWiki; MEIS2; -.
DR GenomeRNAi; 4212; -.
DR Pharos; O14770; Tbio.
DR PRO; PR:O14770; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O14770; protein.
DR Bgee; ENSG00000134138; Expressed in ventricular zone and 196 other tissues.
DR ExpressionAtlas; O14770; baseline and differential.
DR Genevisible; O14770; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
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; ISA:NTNU_SB.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0009880; P:embryonic pattern specification; IBA:GO_Central.
DR GO; GO:0001654; P:eye development; IBA:GO_Central.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0031016; P:pancreas development; IEA:Ensembl.
DR GO; GO:0110024; P:positive regulation of cardiac muscle myoblast proliferation; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IDA:BHF-UCL.
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:0070848; P:response to growth factor; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
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 3D-structure; Activator; Alternative splicing; Cytoplasm;
KW Developmental protein; Disease variant; DNA-binding; Homeobox;
KW Intellectual disability; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..477
FT /note="Homeobox protein Meis2"
FT /id="PRO_0000049108"
FT DOMAIN 110..193
FT /note="MEIS N-terminal"
FT /evidence="ECO:0000255"
FT DNA_BIND 276..338
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 71..191
FT /note="Required for interaction with PBX1"
FT /evidence="ECO:0000250"
FT REGION 193..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..333
FT /note="Interaction with DNA"
FT /evidence="ECO:0000305|PubMed:26550823, ECO:0000305|Ref.16"
FT REGION 340..477
FT /note="Transcriptional activation domain"
FT COMPBIAS 227..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..89
FT /note="MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYG
FT AHAPHPNVMPASMGSAVNDALKRDKDAIYGHPLFPLL -> M (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043219"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_043494"
FT VAR_SEQ 301..302
FT /note="HP -> VY (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10764806"
FT /id="VSP_002243"
FT VAR_SEQ 303..477
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10764806"
FT /id="VSP_002244"
FT VAR_SEQ 346..352
FT /note="Missing (in isoform 3, isoform 4, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:10764806,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9383298"
FT /id="VSP_002242"
FT VAR_SEQ 384..401
FT /note="LQSMPGDYVSQGGPMGMS -> PMSGMGMNMGMDGQWHYM (in isoform
FT 2, isoform 3, isoform 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10764806,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9383298"
FT /id="VSP_002245"
FT VAR_SEQ 402..477
FT /note="Missing (in isoform 2, isoform 3, isoform 6, isoform
FT 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10764806,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9383298"
FT /id="VSP_002246"
FT VARIANT 204..477
FT /note="Missing (in CPCMR)"
FT /evidence="ECO:0000269|PubMed:27225850"
FT /id="VAR_078978"
FT VARIANT 333
FT /note="Missing (in CPCMR)"
FT /evidence="ECO:0000269|PubMed:25712757"
FT /id="VAR_078979"
FT MUTAGEN 85
FT /note="L->A: Impairs interaction with PBX1; when associated
FT with A-88."
FT /evidence="ECO:0000269|PubMed:20553494"
FT MUTAGEN 88
FT /note="L->A: Impairs interaction with PBX1; when associated
FT with A-85. HELIX 285 297."
FT /evidence="ECO:0000269|PubMed:20553494"
FT MUTAGEN 94..97
FT /note="EKCE->NNGT: Impairs interaction with PBX1."
FT /evidence="ECO:0000269|PubMed:20553494"
FT MUTAGEN 151
FT /note="I->A: Impairs interaction with PBX1; when associated
FT with A-154."
FT /evidence="ECO:0000269|PubMed:20553494"
FT MUTAGEN 154
FT /note="L->A: Impairs interaction with PBX1; when associated
FT with A-151."
FT /evidence="ECO:0000269|PubMed:20553494"
FT MUTAGEN 158..159
FT /note="LL->AA: Impairs interaction with PBX1; when
FT associated with A-161."
FT /evidence="ECO:0000269|PubMed:20553494"
FT MUTAGEN 161
FT /note="L->A: Impairs interaction with PBX1; when associated
FT with 158-A-A-159."
FT /evidence="ECO:0000269|PubMed:20553494"
FT MUTAGEN 332
FT /note="R->M: Impairs DNA binding and PBX1-dependent
FT transcriptional activation. No effect on interaction with
FT PBX1."
FT /evidence="ECO:0000269|PubMed:20553494,
FT ECO:0000269|PubMed:21746878"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:4XRM"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:3K2A"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:4XRM"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:4XRM"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:4XRM"
SQ 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
