MN1_MOUSE
ID MN1_MOUSE Reviewed; 1297 AA.
AC D3YWE6;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Transcriptional activator MN1 {ECO:0000305};
GN Name=Mn1 {ECO:0000312|MGI:MGI:1261813};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
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 [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15870292; DOI=10.1128/mcb.25.10.4229-4236.2005;
RA Meester-Smoor M.A., Vermeij M., van Helmond M.J., Molijn A.C.,
RA van Wely K.H., Hekman A.C., Vermey-Keers C., Riegman P.H., Zwarthoff E.C.;
RT "Targeted disruption of the Mn1 oncogene results in severe defects in
RT development of membranous bones of the cranial skeleton.";
RL Mol. Cell. Biol. 25:4229-4236(2005).
RN [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18948418; DOI=10.1242/dev.025304;
RA Liu W., Lan Y., Pauws E., Meester-Smoor M.A., Stanier P., Zwarthoff E.C.,
RA Jiang R.;
RT "The Mn1 transcription factor acts upstream of Tbx22 and preferentially
RT regulates posterior palate growth in mice.";
RL Development 135:3959-3968(2008).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY CALCITROL.
RX PubMed=19386590; DOI=10.1074/jbc.m109.001354;
RA Zhang X., Dowd D.R., Moore M.C., Kranenburg T.A., Meester-Smoor M.A.,
RA Zwarthoff E.C., MacDonald P.N.;
RT "Meningioma 1 is required for appropriate osteoblast proliferation,
RT motility, differentiation, and function.";
RL J. Biol. Chem. 284:18174-18183(2009).
CC -!- FUNCTION: Transcriptional activator which specifically regulates
CC expression of TBX22 in the posterior region of the developing palate
CC (PubMed:18948418). Required during later stages of palate development
CC for normal growth and medial fusion of the palatal shelves
CC (PubMed:18948418). Promotes maturation and normal function of calvarial
CC osteoblasts, including expression of the osteoclastogenic cytokine
CC TNFSF11/RANKL (PubMed:19386590). Necessary for normal development of
CC the membranous bones of the skull (PubMed:15870292). May play a role in
CC tumor suppression (By similarity). {ECO:0000250|UniProtKB:Q10571,
CC ECO:0000269|PubMed:15870292, ECO:0000269|PubMed:18948418,
CC ECO:0000269|PubMed:19386590}.
CC -!- SUBUNIT: Interacts with PBX1, PKNOX1, ZBTB24, E2F7, RING1.
CC {ECO:0000250|UniProtKB:Q10571}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q10571}.
CC -!- TISSUE SPECIFICITY: Detected in brain, heart, tibia, and calvarial
CC osteoclasts. {ECO:0000269|PubMed:19386590}.
CC -!- DEVELOPMENTAL STAGE: Detected in the midbrain, hindbrain and
CC craniofacial mesenchyme at 9.5 dpc. At 10.5 dpc and 11.5 dpc, strong
CC expression is detected in the brain, frontonasal processes, maxillary
CC processes, mandibular processes, the second brachial arch, and also in
CC somites and limb buds. In the developing palatal shelves from 12.5 dpc-
CC 14.5 dpc, shows graded expression with highest levels in the posterior
CC and middle regions and very low levels in the anterior region.
CC {ECO:0000269|PubMed:18948418}.
CC -!- INDUCTION: By calcitrol (1,25-dihydroxyvitamin D3).
CC {ECO:0000269|PubMed:19386590}.
CC -!- DISRUPTION PHENOTYPE: Lethality occurs at or shortly after birth,
CC associated with cleft secondary palate (PubMed:15870292). Skulls at
CC late embryonic stages show multiple abnormalities including complete
CC loss of alisphenoid, squamosal and vomer bones, and poorly developed
CC presphenoid and basisphenoid bones (PubMed:15870292). Other parts of
CC the skeleton are not affected (PubMed:15870292). Early palate
CC development is normal but later the palatal shelves fail to grow and
CC elevate towards the midline, associated with both impaired cell
CC division and apoptosis (PubMed:18948418). {ECO:0000269|PubMed:15870292,
CC ECO:0000269|PubMed:18948418}.
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DR EMBL; AC122226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39214.1; -.
DR RefSeq; NP_001074704.1; NM_001081235.1.
DR AlphaFoldDB; D3YWE6; -.
DR STRING; 10090.ENSMUSP00000092034; -.
DR iPTMnet; D3YWE6; -.
DR PhosphoSitePlus; D3YWE6; -.
DR PaxDb; D3YWE6; -.
DR PRIDE; D3YWE6; -.
DR ProteomicsDB; 291376; -.
DR Antibodypedia; 309; 164 antibodies from 28 providers.
DR Ensembl; ENSMUST00000094463; ENSMUSP00000092034; ENSMUSG00000070576.
DR GeneID; 433938; -.
DR KEGG; mmu:433938; -.
DR UCSC; uc008yse.1; mouse.
DR CTD; 4330; -.
DR MGI; MGI:1261813; Mn1.
DR VEuPathDB; HostDB:ENSMUSG00000070576; -.
DR eggNOG; ENOG502QVWY; Eukaryota.
DR GeneTree; ENSGT00390000001777; -.
DR HOGENOM; CLU_009075_0_0_1; -.
DR InParanoid; D3YWE6; -.
DR OMA; AWFSGPH; -.
DR OrthoDB; 923694at2759; -.
DR PhylomeDB; D3YWE6; -.
DR TreeFam; TF331780; -.
DR BioGRID-ORCS; 433938; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Mn1; mouse.
DR PRO; PR:D3YWE6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; D3YWE6; protein.
DR Bgee; ENSMUSG00000070576; Expressed in ganglionic eminence and 200 other tissues.
DR Genevisible; D3YWE6; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001957; P:intramembranous ossification; IMP:MGI.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISO:MGI.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; ISO:MGI.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR037644; MN1.
DR PANTHER; PTHR15821; PTHR15821; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Tumor suppressor.
FT CHAIN 1..1297
FT /note="Transcriptional activator MN1"
FT /id="PRO_0000435338"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q10571"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10571"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10571"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10571"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10571"
SQ SEQUENCE 1297 AA; 134072 MW; 41130654703FF053 CRC64;
MFGLDQFEPQ INSRHAGQGE GNFNEAGLSM NAHFKAPAFH AGPPTGPVDP AISALGEPPI
LGLNMEPYGF HARSHSELHA GGLQAQPVHG FFGGQQPHHS HPGGHHPHQH HPHFGGNFGG
PDPGASCLHG GRLLGYGGAA GGLGSQPPFA ESYEHMAESQ GPEGFGPQRP GNLPDFHSSG
TSGHAVPAPC LPLDQSPNRA ASFHGLSASS GSDSHSLEPR RVTNQGAVDS LEYNYPSEPP
SGHFDMFSPS DSEGQLPHYA AGRQVPGGAF PGASAMPRAS GMVGLSKMHS QPPQPPPQQQ
QPQHGVFFER FGGARKMPVG LEPAVGSRHP LMQPPQQAPP PPQQPPPQQQ PPPPGLLVRQ
NSCPPALPRP QQGEAGTPSG GLQDGGPMLP SQHAQFEYPI HRLENRSMHP YSEPVFSMQH
PPPQQAPNQR LQHFDAPPYM NVAKRPRFDF PGSAGVDRCA SWNGSMHNGT LDNQLSPSAY
PGLPGEFTPP VPDSFSSGPP LQHPGPDHQS LQQQQQQQQQ QQQQQQQQQQ QQQQQQQRQN
AALMIKQMAS RNQQQRLRQP NLAQLGHPGD VGQGGLVHGG SVGGLAQTNF EREGGSAGAG
RLSGFEQQAP HLAQESAWFP GPHPPGDLLP RRMGGAGLPT DCGPHDPALA PPPAPGGSGV
LFRGSLQEPL RMPGEGHVPA LASPGLQFGG SLAGLGQLQS PGAGVGLPNA PSERRPPPPD
FPAPALGGQP GFPFGSGSRQ ATPHSAPGVN SPPSAGSGSS GAGGGAYPPQ PDFQPSQRNS
ASKLGALSLG SFNKPSSKDN LFGQSCLAAL STACQNMIAS LGAPNLNVTF NKKNPPEGKR
KLSQNEPDSA VAAGNPGSDY FPGGTTPGAP GPGGPSGTSG GGSKASGPPN PPIQGDSTSL
SPNYTLESTS GNDGKPVPGG SGRGRGRRKR DSGHVSPGTF FDKYSTAPDS GGAPGVSPGQ
QQAPGSAAGG SSVNEARGPT PHEKALTSPS WGKGAELLLG DQPDLMASLD STAKSDGSSP
HVGEFASDEV STSYANEDEV SSSSDNTTAL AKASRSPLVT SSPKLPPRGV GAGEHTPKAS
ALGLGILSTS TSTPDSYGGG VGTGHPGTPG LEQVRTPTSS SGAQPPDEIH PLEILQAQIQ
LQRQQFSISE DQPLGLKGSK KAECAVGASG AQNGDSELGS CCSEAVKSAM STIDLDSLMA
EHSTTWYMPP DKALVDGGDE DKTLAPWEKA KSQNPNNKEA HDHPTNKASA TQPGSHLQCL
TVHCTDGDPK ARTSVPTWRS LHSDISNRFG TFVAALT
