MAD1_MOUSE
ID MAD1_MOUSE Reviewed; 227 AA.
AC P50538; Q60798; Q61825;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Max dimerization protein 1;
DE Short=Max dimerizer 1;
DE AltName: Full=Protein MAD;
GN Name=Mxd1; Synonyms=Mad, Mad1;
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].
RC TISSUE=Brain;
RX PubMed=7667316; DOI=10.1073/pnas.92.18.8488;
RA Chin L., Schreiber-Agus N., Pellicer I., Chen K., Lee H.W., Dudast M.,
RA Cordon-Cardo C., DePinho R.A.;
RT "Contrasting roles for Myc and Mad proteins in cellular growth and
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8488-8492(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RX PubMed=9519870; DOI=10.1038/sj.onc.1201611;
RA Queva C., Hurlin P.J., Foley K.P., Eisenman R.N.;
RT "Sequential expression of the MAD family of transcriptional repressors
RT during differentiation and development.";
RL Oncogene 16:967-977(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7896882; DOI=10.1083/jcb.128.6.1197;
RA Vaestrik I., Kaipainen A., Penttilae T.-L., Lymboussakis A., Alitalo R.,
RA Parvinen M., Alitalo K.;
RT "Expression of the mad gene during cell differentiation in vivo and its
RT inhibition of cell growth in vitro.";
RL J. Cell Biol. 128:1197-1208(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 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: Component of a transcriptional repressor complex together
CC with MAX (By similarity). In complex with MAX binds to the core DNA
CC sequence 5'-CAC[GA]TG-3' (By similarity). Antagonizes MYC
CC transcriptional activity by competing with MYC for MAX binding (By
CC similarity). Binds to the TERT promoter and represses telomerase
CC expression, possibly by interfering with MYC binding (By similarity).
CC {ECO:0000250|UniProtKB:Q05195}.
CC -!- SUBUNIT: Heterodimer with MAX; the interaction is required for DNA-
CC binding (By similarity). DNA binding requires dimerization with another
CC bHLH protein; does not form homodimers, and does not bind to DNA in the
CC absence of MAX in vitro (By similarity). Interacts with RNF17
CC (PubMed:10597267). {ECO:0000250|UniProtKB:Q05195,
CC ECO:0000269|PubMed:10597267}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05195}.
CC -!- DEVELOPMENTAL STAGE: Expressed during neural and epidermal
CC differentiation. Primarily expressed in growth-arrested differentiating
CC cells. In the spinal cord at embryonic day 10.5, a strong expressesion
CC seen in the differentiating cells of the intermediate zone at the
CC ventral part of the neural tube and weakly in the ventricular zone. At
CC 11.5 and 12.5 dpc, highly expressed in the intermediate zone and at
CC reduced levels in the ventricular zone that mostly persists in the
CC dorsal part of the neural tube. At 14.5 dpc, expressed throughout the
CC spinal cord. In the developing epidermis at 14.5 dpc, found in the
CC dorsal lateral epidermis. At 17.5 dpc expressed in the cell cycle
CC arrested, differentiating cells of the suprabasal malphigian layer.
CC {ECO:0000269|PubMed:8521822}.
CC -!- PTM: Ubiquitinated by BIRC2/c-IAP1, leading to its subsequent
CC degradation by the proteasome. {ECO:0000250}.
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DR EMBL; L38926; AAB00682.1; -; mRNA.
DR EMBL; U20614; AAA62310.1; -; mRNA.
DR EMBL; X83106; CAA58168.1; -; mRNA.
DR CCDS; CCDS51835.1; -.
DR PIR; A57074; S51642.
DR AlphaFoldDB; P50538; -.
DR SMR; P50538; -.
DR ComplexPortal; CPX-105; Transcriptional repressor Mad-Max complex.
DR CORUM; P50538; -.
DR DIP; DIP-864N; -.
DR STRING; 10090.ENSMUSP00000001184; -.
DR iPTMnet; P50538; -.
DR PhosphoSitePlus; P50538; -.
DR PaxDb; P50538; -.
DR PRIDE; P50538; -.
DR ProteomicsDB; 291998; -.
DR MGI; MGI:96908; Mxd1.
DR eggNOG; KOG2483; Eukaryota.
DR InParanoid; P50538; -.
DR PhylomeDB; P50538; -.
DR ChiTaRS; Mxd1; mouse.
DR PRO; PR:P50538; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P50538; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070443; C:Mad-Max complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; 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; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR040157; MXD1.
DR PANTHER; PTHR11969:SF18; PTHR11969:SF18; 1.
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 DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..227
FT /note="Max dimerization protein 1"
FT /id="PRO_0000127265"
FT DOMAIN 55..107
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 30..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 21..48
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 184..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 14
FT /note="E -> A (in Ref. 1; AAB00682)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="Missing (in Ref. 3; CAA58168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25562 MW; 92736F1C72E419FC CRC64;
MATAVGMNIQ LLLEAADYLE RREREAEHGY ASMLPYSKDR DAFKRRNKPK KNSTSSRSTH
NEMEKNRRAH LRLCLEKLKG LVPLGPESSR HTTLSLLTKA KLHIKKLEDC DRKAVHQIDQ
LQREQRHLKR RLEKLGAERT RMDSVGSVVS SERSDSDREE LDVDVDVDVD VDVEGTDYLN
GDLGWSSSVS DSDERGSMQS LGSDEGYSSA TVKRAKLQDG HKAGLGL
