(data stored in SCRATCH zone)

SWISSPROT: MSX1_MOUSE

ID   MSX1_MOUSE              Reviewed;         303 AA.
AC   P13297; Q91W75; Q9ERF6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 4.
DT   07-SEP-2016, entry version 164.
DE   RecName: Full=Homeobox protein MSX-1;
DE   AltName: Full=Homeobox protein Hox-7;
DE   AltName: Full=Hox-7.1;
DE   AltName: Full=Msh homeobox 1-like protein;
GN   Name=Msx1; Synonyms=Hox7, Hox7.1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=2565278; DOI=10.1101/gad.3.1.26;
RA   Hill R.E., Jones P.F., Rees A.R., Sime C.M., Justice M.J.,
RA   Copeland N.G., Jenkins N.A., Graham E., Davidson D.R.;
RT   "A new family of mouse homeo box-containing genes: molecular
RT   structure, chromosomal location, and developmental expression of Hox-
RT   7.1.";
RL   Genes Dev. 3:26-37(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=1682128;
RA   Monaghan A.P., Davidson D.R., Sime C., Graham E., Baldock R.,
RA   Bhattacharya S.S., Hill R.E.;
RT   "The Msh-like homeobox genes define domains in the developing
RT   vertebrate eye.";
RL   Development 112:1053-1061(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RA   Wu X.B., Liu Y.-H.;
RT   "Isolation of a mouse homeodomain protein MSX1 cDNA variant.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-256.
RX   PubMed=2565810;
RA   Robert B., Sassoon D., Jacq B., Gehring W.J., Buckingham M.;
RT   "Hox-7, a mouse homeobox gene with a novel pattern of expression
RT   during embryogenesis.";
RL   EMBO J. 8:91-100(1989).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 171-231.
RX   PubMed=1673109; DOI=10.1016/0378-1119(91)90182-B;
RA   Holland P.W.H.;
RT   "Cloning and evolutionary analysis of msh-like homeobox genes from
RT   mouse, zebrafish and ascidian.";
RL   Gene 98:253-257(1991).
RN   [9]
RP   FUNCTION.
RX   PubMed=1677742; DOI=10.1038/352429a0;
RA   Davidson D.R., Crawley A., Hill R.E., Tickle C.;
RT   "Position-dependent expression of two related homeobox genes in
RT   developing vertebrate limbs.";
RL   Nature 352:429-431(1991).
RN   [10]
RP   FUNCTION.
RX   PubMed=7823952;
RA   Catron K.M., Zhang H., Marshall S.C., Inostroza J.A., Wilson J.M.,
RA   Abate C.;
RT   "Transcriptional repression by Msx-1 does not require homeodomain DNA-
RT   binding sites.";
RL   Mol. Cell. Biol. 15:861-871(1995).
RN   [11]
RP   SUMOYLATION AT LYS-15 AND LYS-133, AND MUTAGENESIS OF LYS-15; LYS-53;
RP   LYS-72; LYS-125; LYS-133 AND LYS-139.
RX   PubMed=16678795; DOI=10.1016/j.bbrc.2006.03.232;
RA   Gupta V., Bei M.;
RT   "Modification of Msx1 by SUMO-1.";
RL   Biochem. Biophys. Res. Commun. 345:74-77(2006).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 173-230 IN COMPLEX WITH DNA.
RX   PubMed=11580277; DOI=10.1021/bi0108148;
RA   Hovde S., Abate-Shen C., Geiger J.H.;
RT   "Crystal structure of the Msx-1 homeodomain/DNA complex.";
RL   Biochemistry 40:12013-12021(2001).
CC   -!- FUNCTION: Acts as a transcriptional repressor. May play a role in
CC       limb-pattern formation. Acts in cranofacial development and
CC       specifically in odontogenesis. {ECO:0000269|PubMed:1677742,
CC       ECO:0000269|PubMed:7823952}.
CC   -!- INTERACTION:
CC       P43276:Hist1h1b; NbExp=3; IntAct=EBI-903969, EBI-903960;
CC       P25233:Ndn; NbExp=2; IntAct=EBI-903969, EBI-1801080;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Sumoylated by PIAS1, desumoylated by SENP1.
CC       {ECO:0000269|PubMed:16678795}.
CC   -!- SIMILARITY: Belongs to the Msh homeobox family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16426.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAA32871.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAA32871.1; Type=Frameshift; Positions=252; Evidence={ECO:0000305};
DR   EMBL; X14759; CAA32871.1; ALT_SEQ; mRNA.
DR   EMBL; X59251; CAA41944.1; -; mRNA.
DR   EMBL; AF308572; AAG32466.1; -; mRNA.
DR   EMBL; AC114671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466524; EDL37531.1; -; Genomic_DNA.
DR   EMBL; BC016426; AAH16426.1; ALT_INIT; mRNA.
DR   EMBL; X14457; CAA32626.1; -; Genomic_DNA.
DR   EMBL; M38575; AAA37823.1; -; Genomic_DNA.
DR   CCDS; CCDS19249.1; -.
DR   PIR; PS0411; PS0411.
DR   PIR; S03636; S03636.
DR   PIR; S18813; S18813.
DR   RefSeq; NP_034965.2; NM_010835.2.
DR   UniGene; Mm.256509; -.
DR   PDB; 1IG7; X-ray; 2.20 A; A=173-230.
DR   PDBsum; 1IG7; -.
DR   ProteinModelPortal; P13297; -.
DR   SMR; P13297; 173-230.
DR   BioGrid; 201536; 12.
DR   IntAct; P13297; 5.
DR   STRING; 10090.ENSMUSP00000058354; -.
DR   iPTMnet; P13297; -.
DR   PhosphoSite; P13297; -.
DR   PaxDb; P13297; -.
DR   PRIDE; P13297; -.
DR   Ensembl; ENSMUST00000063116; ENSMUSP00000058354; ENSMUSG00000048450.
DR   GeneID; 17701; -.
DR   KEGG; mmu:17701; -.
DR   UCSC; uc008xfw.1; mouse.
DR   CTD; 4487; -.
DR   MGI; MGI:97168; Msx1.
DR   eggNOG; KOG0492; Eukaryota.
DR   eggNOG; ENOG410YT2J; LUCA.
DR   GeneTree; ENSGT00840000129671; -.
DR   HOGENOM; HOG000231922; -.
DR   HOVERGEN; HBG005205; -.
DR   InParanoid; P13297; -.
DR   KO; K09341; -.
DR   OMA; EKQERTP; -.
DR   OrthoDB; EOG091G0P1V; -.
DR   PhylomeDB; P13297; -.
DR   TreeFam; TF350699; -.
DR   EvolutionaryTrace; P13297; -.
DR   PRO; PR:P13297; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000048450; -.
DR   CleanEx; MM_MSX1; -.
DR   Genevisible; P13297; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IGI:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
DR   GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
DR   GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
DR   GO; GO:0090427; P:activation of meiosis; IGI:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR   GO; GO:0061312; P:BMP signaling pathway involved in heart development; IGI:MGI.
DR   GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR   GO; GO:0060536; P:cartilage morphogenesis; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; ISO:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IGI:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IGI:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR   GO; GO:0035880; P:embryonic nail plate morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IGI:MGI.
DR   GO; GO:0060325; P:face morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0061180; P:mammary gland epithelium development; IGI:MGI.
DR   GO; GO:0010463; P:mesenchymal cell proliferation; IMP:UniProtKB.
DR   GO; GO:0030901; P:midbrain development; IMP:MGI.
DR   GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
DR   GO; GO:0007517; P:muscle organ development; IPI:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
DR   GO; GO:0051154; P:negative regulation of striated muscle cell differentiation; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR   GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IGI:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0042476; P:odontogenesis; IMP:UniProtKB.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:BHF-UCL.
DR   GO; GO:0060021; P:palate development; IMP:MGI.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IGI:MGI.
DR   GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR   GO; GO:2001055; P:positive regulation of mesenchymal cell apoptotic process; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0034504; P:protein localization to nucleus; ISO:MGI.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   GO; GO:0042481; P:regulation of odontogenesis; IGI:MGI.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IGI:MGI.
DR   GO; GO:0048863; P:stem cell differentiation; IGI:MGI.
DR   Gene3D; 1.10.10.60; -; 1.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR020479; Homeobox_metazoa.
DR   InterPro; IPR009057; Homeodomain-like.
DR   Pfam; PF00046; Homeobox; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P13297.
DR   SWISS-2DPAGE; P13297.
KW   3D-structure; Complete proteome; Developmental protein; DNA-binding;
KW   Homeobox; Isopeptide bond; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    303       Homeobox protein MSX-1.
FT                                /FTId=PRO_0000049091.
FT   DNA_BIND    172    231       Homeobox. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00108}.
FT   CROSSLNK     15     15       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    133    133       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   MUTAGEN      15     15       K->R: Abolishes sumoylation.
FT                                {ECO:0000269|PubMed:16678795}.
FT   MUTAGEN      53     53       K->R: Sumoylated.
FT                                {ECO:0000269|PubMed:16678795}.
FT   MUTAGEN      72     72       K->R: Sumoylated.
FT                                {ECO:0000269|PubMed:16678795}.
FT   MUTAGEN     125    125       K->R: Sumoylated.
FT                                {ECO:0000269|PubMed:16678795}.
FT   MUTAGEN     133    133       K->R: Abolishes sumoylation.
FT                                {ECO:0000269|PubMed:16678795}.
FT   MUTAGEN     139    139       K->R: Sumoylated.
FT                                {ECO:0000269|PubMed:16678795}.
FT   CONFLICT    263    266       Missing (in Ref. 2; CAA41944).
FT                                {ECO:0000305}.
FT   HELIX       181    193       {ECO:0000244|PDB:1IG7}.
FT   HELIX       199    208       {ECO:0000244|PDB:1IG7}.
FT   HELIX       213    229       {ECO:0000244|PDB:1IG7}.
SQ   SEQUENCE   303 AA;  31672 MW;  8E07FF038AEF0EDF CRC64;
     MAPAAAMTSL PLGVKVEDSA FAKPAGGGVG QAPGAAAATA TAMGTDEEGA KPKVPASLLP
     FSVEALMADH RKPGAKESVL VASEGAQAAG GSVQHLGTRP GSLGAPDAPS SPRPLGHFSV
     GGLLKLPEDA LVKAESPEKL DRTPWMQSPR FSPPPARRLS PPACTLRKHK TNRKPRTPFT
     TAQLLALERK FRQKQYLSIA ERAEFSSSLS LTETQVKIWF QNRRAKAKRL QEAELEKLKM
     AAKPMLPPAA FGLSFPLGGP AAVAAAAGAS LYSASGPFQR AALPVAPVGL YTAHVGYSMY
     HLT
//

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