MXI1_MOUSE
ID MXI1_MOUSE Reviewed; 228 AA.
AC P50540;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Max-interacting protein 1;
DE Short=Max interactor 1;
GN Name=Mxi1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=7889571; DOI=10.1016/0092-8674(95)90356-9;
RA Schreiber-Agus N., Chin L., Chen K., Torres R., Rao G., Guida P.,
RA Skoultchi A.I., DePinho R.A.;
RT "An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and
RT interacts with a homolog of the yeast transcriptional repressor SIN3.";
RL Cell 80:777-786(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=7954804;
RA Zervos A.S., Gyuris J., Brent R.;
RT "Mxi1, a protein that specifically interacts with Max to bind Myc-Max
RT recognition sites.";
RL Cell 79:388-388(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RX PubMed=7835718; DOI=10.1016/0378-1119(94)00722-5;
RA Shimizu E., Shirasawa H., Kodama K., Koseki K., Sato T., Simizu B.;
RT "Cloning and sequencing of the murine Mxi1 cDNA.";
RL Gene 152:283-284(1995).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=8521822; DOI=10.1002/j.1460-2075.1995.tb00252.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RT "Mad3 and Mad4: novel Max-interacting transcriptional repressors that
RT suppress c-myc dependent transformation and are expressed during neural and
RT epidermal differentiation.";
RL EMBO J. 14:5646-5659(1995).
RN [5]
RP ERRATUM OF PUBMED:8521822.
RX PubMed=8617250; DOI=10.1002/j.1460-2075.1996.tb00555.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RL EMBO J. 15:2030-2030(1996).
RN [6]
RP INTERACTION WITH SMC3.
RX PubMed=9528857; DOI=10.1038/sj.onc.1201634;
RA Gupta K., Anand G., Yin X.Y., Prochownik E.V.;
RT "Mmip1: a novel leucine zipper protein that reverses the suppressive
RT effects of mad family members on C-myc.";
RL Oncogene 16:1149-1159(1998).
RN [7]
RP INTERACTION WITH RNF17.
RX PubMed=10597267; DOI=10.1038/sj.onc.1203097;
RA Yin X.-Y., Gupta K., Prochownik E.V.;
RT "Mmip-2, a novel RING finger protein that interacts with mad members of the
RT Myc oncoprotein network.";
RL Oncogene 18:6621-6634(1999).
CC -!- FUNCTION: Transcriptional repressor. MXI1 binds with MAX to form a
CC sequence-specific DNA-binding protein complex which recognizes the core
CC sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional
CC activity by competing for MAX. Isoform Short, which lacks a segment,
CC has a much stronger suppressive potential and associates with a SIN3
CC homologous protein.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX. Interacts with SMC3.
CC Interacts with RNF17. {ECO:0000269|PubMed:10597267,
CC ECO:0000269|PubMed:9528857}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P50540-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P50540-2; Sequence=VSP_002141;
CC -!- DEVELOPMENTAL STAGE: Primarily expressed in differentiating cells. Also
CC expressed in the proliferating cells of the developing CNS and the
CC epidermis. In the spinal cord at embryonic day 10.5, expressed in the
CC ventricular zone of the neural tube. Expressed at highest levels in
CC cells accumulating in the intermediate zone. At 11.5 and 12.5 dpc,
CC highly expressed in the intermediate zone and at reduced levels in the
CC ventricular zone that mostly persists in the dorsal part of the neural
CC tube. At 14.5 dpc, expressed throughout the spinal cord. In the
CC developing epidermis at 14.5 dpc, found in the dorsal lateral
CC epidermis. At 17 dpc, expression is restricted not only to the
CC differentiating cells of the epidermis but also to the proliferating
CC cell compartment and expression extends into the first differentiating
CC cell layers, but decreases in the uppermost layers of the epidermis.
CC {ECO:0000269|PubMed:8521822}.
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DR EMBL; L38822; AAA65684.1; -; mRNA.
DR EMBL; L38821; AAA65685.1; -; mRNA.
DR EMBL; U24674; AAA65183.1; -; mRNA.
DR EMBL; U24673; AAA65182.1; -; mRNA.
DR EMBL; D31824; BAA06612.1; -; mRNA.
DR CCDS; CCDS29901.1; -. [P50540-1]
DR CCDS; CCDS38023.1; -. [P50540-2]
DR PIR; A56069; A56069.
DR PIR; JC4050; JC4050.
DR RefSeq; NP_001008543.1; NM_001008543.2. [P50540-2]
DR RefSeq; NP_034977.1; NM_010847.3. [P50540-1]
DR RefSeq; XP_006526801.1; XM_006526738.1.
DR RefSeq; XP_006526802.1; XM_006526739.1. [P50540-2]
DR RefSeq; XP_006526803.1; XM_006526740.1.
DR AlphaFoldDB; P50540; -.
DR SMR; P50540; -.
DR BioGRID; 201630; 8.
DR DIP; DIP-489N; -.
DR IntAct; P50540; 2.
DR STRING; 10090.ENSMUSP00000003870; -.
DR PhosphoSitePlus; P50540; -.
DR PaxDb; P50540; -.
DR PRIDE; P50540; -.
DR ProteomicsDB; 287644; -. [P50540-1]
DR ProteomicsDB; 287645; -. [P50540-2]
DR Antibodypedia; 18346; 253 antibodies from 30 providers.
DR DNASU; 17859; -.
DR Ensembl; ENSMUST00000025998; ENSMUSP00000025998; ENSMUSG00000025025. [P50540-2]
DR Ensembl; ENSMUST00000111737; ENSMUSP00000107366; ENSMUSG00000025025. [P50540-1]
DR Ensembl; ENSMUST00000235201; ENSMUSP00000158401; ENSMUSG00000025025. [P50540-2]
DR Ensembl; ENSMUST00000235880; ENSMUSP00000157790; ENSMUSG00000025025. [P50540-2]
DR Ensembl; ENSMUST00000236973; ENSMUSP00000157400; ENSMUSG00000025025. [P50540-2]
DR GeneID; 17859; -.
DR KEGG; mmu:17859; -.
DR UCSC; uc008hwq.1; mouse. [P50540-1]
DR CTD; 4601; -.
DR MGI; MGI:97245; Mxi1.
DR VEuPathDB; HostDB:ENSMUSG00000025025; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00940000155809; -.
DR HOGENOM; CLU_082604_0_1_1; -.
DR InParanoid; P50540; -.
DR OMA; VEMINIQ; -.
DR PhylomeDB; P50540; -.
DR BioGRID-ORCS; 17859; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Mxi1; mouse.
DR PRO; PR:P50540; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P50540; protein.
DR Bgee; ENSMUSG00000025025; Expressed in blood and 255 other tissues.
DR ExpressionAtlas; P50540; baseline and differential.
DR Genevisible; P50540; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..228
FT /note="Max-interacting protein 1"
FT /id="PRO_0000127286"
FT DOMAIN 67..119
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 30..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7889571,
FT ECO:0000303|PubMed:7954804"
FT /id="VSP_002141"
FT CONFLICT 1..25
FT /note="MERVRMINVQRLLEAAEFLERRERE -> MEKHINTFLQNVQILLEAASYLE
FT QIEKENKK (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 25978 MW; 7B5D4ACAEF97C4F1 CRC64;
MERVRMINVQ RLLEAAEFLE RRERECEHGY ASSFPSMPSP RLQHSKPPRR LSRAQKHSSG
SSNTSTANRS THNELEKNRR AHLRLCLERL KVLIPLGPDC TRHTTLGLLN KAKAHIKKLE
EAERKSQHQL ENLEREQRFL KRRLEQLQGP QEMERIRMDS IGSTISSDRS DSEREEIEVD
VESTEFSHGE ADSVSTTSIS DLDDHSSLQS VGSDEGYSSA SVKLSFAS
