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Protein

Max dimerization protein 1

Gene

Mxd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor. MAD binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MAD thus antagonizes MYC transcriptional activity by competing for MAX.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Max dimerization protein 1
Short name:
Max dimerizer 1
Alternative name(s):
Protein MAD
Gene namesi
Name:Mxd1
Synonyms:Mad, Mad1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96908. Mxd1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Max dimerization protein 1PRO_0000127265Add
BLAST

Post-translational modificationi

Ubiquitinated by BIRC2/c-IAP1, leading to its subsequent degradation by the proteasome.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiP50538.
PRIDEiP50538.

PTM databases

PhosphoSiteiP50538.

Expressioni

Developmental stagei

Expressed during neural and epidermal differentiation. Primarily expressed in growth-arrested differentiating cells. In the spinal cord at embryonic day 10.5, a strong expressesion seen in the differentiating cells of the intermediate zone at the ventral part of the neural tube and weakly in the ventricular zone. At 11.5 and 12.5 dpc, highly expressed in the intermediate zone and at reduced levels in the ventricular zone that mostly persists in the dorsal part of the neural tube. At 14.5 dpc, expressed throughout the spinal cord. In the developing epidermis at 14.5 dpc, found in the dorsal lateral epidermis. At 17.5 dpc expressed in the cell cycle arrested, differentiating cells of the suprabasal malphigian layer.1 Publication

Gene expression databases

CleanExiMM_MXD1.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with RNF17.1 Publication

Protein-protein interaction databases

DIPiDIP-864N.
STRINGi10090.ENSMUSP00000001184.

Structurei

3D structure databases

ProteinModelPortaliP50538.
SMRiP50538. Positions 56-134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 10753bHLHPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi21 – 4828Nuclear localization signalSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IPD6. Eukaryota.
ENOG4111X99. LUCA.
HOGENOMiHOG000247060.
HOVERGENiHBG006314.
InParanoidiP50538.
PhylomeDBiP50538.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50538-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATAVGMNIQ LLLEAADYLE RREREAEHGY ASMLPYSKDR DAFKRRNKPK
60 70 80 90 100
KNSTSSRSTH NEMEKNRRAH LRLCLEKLKG LVPLGPESSR HTTLSLLTKA
110 120 130 140 150
KLHIKKLEDC DRKAVHQIDQ LQREQRHLKR RLEKLGAERT RMDSVGSVVS
160 170 180 190 200
SERSDSDREE LDVDVDVDVD VDVEGTDYLN GDLGWSSSVS DSDERGSMQS
210 220
LGSDEGYSSA TVKRAKLQDG HKAGLGL
Length:227
Mass (Da):25,562
Last modified:November 1, 1997 - v2
Checksum:i92736F1C72E419FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141E → A in AAB00682 (PubMed:7667316).Curated
Sequence conflicti160 – 1601Missing in CAA58168 (PubMed:7896882).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38926 mRNA. Translation: AAB00682.1.
U20614 mRNA. Translation: AAA62310.1.
X83106 mRNA. Translation: CAA58168.1.
CCDSiCCDS51835.1.
PIRiA57074. S51642.
UniGeneiMm.279580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38926 mRNA. Translation: AAB00682.1.
U20614 mRNA. Translation: AAA62310.1.
X83106 mRNA. Translation: CAA58168.1.
CCDSiCCDS51835.1.
PIRiA57074. S51642.
UniGeneiMm.279580.

3D structure databases

ProteinModelPortaliP50538.
SMRiP50538. Positions 56-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-864N.
STRINGi10090.ENSMUSP00000001184.

PTM databases

PhosphoSiteiP50538.

Proteomic databases

PaxDbiP50538.
PRIDEiP50538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:96908. Mxd1.

Phylogenomic databases

eggNOGiENOG410IPD6. Eukaryota.
ENOG4111X99. LUCA.
HOGENOMiHOG000247060.
HOVERGENiHBG006314.
InParanoidiP50538.
PhylomeDBiP50538.

Miscellaneous databases

PROiP50538.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MXD1.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Contrasting roles for Myc and Mad proteins in cellular growth and differentiation."
    Chin L., Schreiber-Agus N., Pellicer I., Chen K., Lee H.W., Dudast M., Cordon-Cardo C., DePinho R.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:8488-8492(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Sequential expression of the MAD family of transcriptional repressors during differentiation and development."
    Queva C., Hurlin P.J., Foley K.P., Eisenman R.N.
    Oncogene 16:967-977(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Sv.
  3. "Expression of the mad gene during cell differentiation in vivo and its inhibition of cell growth in vitro."
    Vaestrik I., Kaipainen A., Penttilae T.-L., Lymboussakis A., Alitalo R., Parvinen M., Alitalo K.
    J. Cell Biol. 128:1197-1208(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation."
    Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N.
    EMBO J. 14:5646-5659(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  5. "Mmip-2, a novel RING finger protein that interacts with mad members of the Myc oncoprotein network."
    Yin X.-Y., Gupta K., Prochownik E.V.
    Oncogene 18:6621-6634(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF17.

Entry informationi

Entry nameiMAD1_MOUSE
AccessioniPrimary (citable) accession number: P50538
Secondary accession number(s): Q60798, Q61825
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.