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MXD1

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Protein-coding gene in the species Homo sapiens Not to be confused with Mothers against decapentaplegic.
MXD1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1E91, 1G1E, 1NLW, 1PD7, 1S5Q

Identifiers
AliasesMXD1, BHLHC58, MAD, MAD1, MAX dimerization protein 1
External IDsOMIM: 600021; MGI: 96908; HomoloGene: 1767; GeneCards: MXD1; OMA:MXD1 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)
Chromosome 2 (human)Genomic location for MXD1Genomic location for MXD1
Band2p13.3Start69,897,688 bp
End69,942,945 bp
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)
Chromosome 6 (mouse)Genomic location for MXD1Genomic location for MXD1
Band6 D1|6 37.75 cMStart86,624,024 bp
End86,646,143 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • mucosa of pharynx

  • oocyte

  • secondary oocyte

  • amniotic fluid

  • blood

  • oral cavity

  • jejunal mucosa

  • mucosa of colon

  • mucosa of sigmoid colon
Top expressed in
  • granulocyte

  • left colon

  • blood

  • retinal pigment epithelium

  • duodenum

  • ciliary body

  • secondary oocyte

  • epithelium of stomach

  • jejunum

  • conjunctival fornix
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4084

17119

Ensembl

ENSG00000059728

ENSMUSG00000001156

UniProt

Q05195

P50538

RefSeq (mRNA)

NM_002357
NM_001202513
NM_001202514

NM_010751

RefSeq (protein)

NP_001189442
NP_001189443
NP_002348

n/a

Location (UCSC)Chr 2: 69.9 – 69.94 MbChr 6: 86.62 – 86.65 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

MAD protein is a protein that in humans is encoded by the MXD1 gene.

MAD-MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acts as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor.

Interactions

MXD1 has been shown to interact with Histone deacetylase 2, SMC3, MLX, SIN3A and MAX.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000059728Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000001156Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Shapiro DN, Valentine V, Eagle L, Yin X, Morris SW, Prochownik EV (February 1995). "Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-q25". Genomics. 23 (1): 282–5. doi:10.1006/geno.1994.1496. PMID 7829091.
  6. ^ "Entrez Gene: MXD1 MAX dimerization protein 1".
  7. Laherty, C D; Yang W M; Sun J M; Davie J R; Seto E; Eisenman R N (May 1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. 89 (3). UNITED STATES: 349–56. doi:10.1016/S0092-8674(00)80215-9. ISSN 0092-8674. PMID 9150134. S2CID 13490886.
  8. Spronk, C A; Tessari M; Kaan A M; Jansen J F; Vermeulen M; Stunnenberg H G; Vuister G W (December 2000). "The Mad1-Sin3B interaction involves a novel helical fold". Nat. Struct. Biol. 7 (12). UNITED STATES: 1100–4. doi:10.1038/81944. hdl:2066/79474. ISSN 1072-8368. PMID 11101889. S2CID 12451972.
  9. ^ Gupta, K; Anand G; Yin X; Grove L; Prochownik E V (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9). ENGLAND: 1149–59. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857.
  10. Cairo, S; Merla G; Urbinati F; Ballabio A; Reymond A (March 2001). "WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network". Hum. Mol. Genet. 10 (6). England: 617–27. doi:10.1093/hmg/10.6.617. ISSN 0964-6906. PMID 11230181.
  11. Meroni, G; Cairo S; Merla G; Messali S; Brent R; Ballabio A; Reymond A (July 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene. 19 (29). ENGLAND: 3266–77. doi:10.1038/sj.onc.1203634. ISSN 0950-9232. PMID 10918583.
  12. Swanson, Kurt A; Knoepfler Paul S; Huang Kai; Kang Richard S; Cowley Shaun M; Laherty Carol D; Eisenman Robert N; Radhakrishnan Ishwar (August 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nat. Struct. Mol. Biol. 11 (8). United States: 738–46. doi:10.1038/nsmb798. ISSN 1545-9993. PMID 15235594. S2CID 44324333.
  13. Brubaker, K; Cowley S M; Huang K; Loo L; Yochum G S; Ayer D E; Eisenman R N; Radhakrishnan I (November 2000). "Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex". Cell. 103 (4). UNITED STATES: 655–65. doi:10.1016/S0092-8674(00)00168-9. ISSN 0092-8674. PMID 11106735. S2CID 17476603.
  14. Ayer, D E; Lawrence Q A; Eisenman R N (March 1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. 80 (5). UNITED STATES: 767–76. doi:10.1016/0092-8674(95)90355-0. ISSN 0092-8674. PMID 7889570. S2CID 8749951.
  15. Lee, Clement M; Onésime Djamila; Reddy C Damodara; Dhanasekaran N; Reddy E Premkumar (October 2002). "JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors". Proc. Natl. Acad. Sci. U.S.A. 99 (22). United States: 14189–94. Bibcode:2002PNAS...9914189L. doi:10.1073/pnas.232310199. ISSN 0027-8424. PMC 137859. PMID 12391307.
  16. Ayer, D E; Kretzner L; Eisenman R N (January 1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell. 72 (2). UNITED STATES: 211–22. doi:10.1016/0092-8674(93)90661-9. ISSN 0092-8674. PMID 8425218. S2CID 13317223.
  17. Nair, Satish K; Burley Stephen K (January 2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell. 112 (2). United States: 193–205. doi:10.1016/S0092-8674(02)01284-9. ISSN 0092-8674. PMID 12553908. S2CID 16142388.

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: Q05195 (Max dimerization protein 1) at the PDBe-KB.
PDB gallery
  • 1nlw: Crystal structure of Mad-Max recognizing DNA 1nlw: Crystal structure of Mad-Max recognizing DNA
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies
Category: