MXD1

Protein-coding gene in the species Homo sapiens
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)[1]
Chromosome 2 (human)
Genomic location for MXD1
Genomic location for MXD1
Band2p13.3Start69,897,688 bp[1]
End69,942,945 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for MXD1
Genomic location for MXD1
Band6 D1|6 37.75 cMStart86,624,024 bp[2]
End86,646,143 bp[2]
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
  • DNA-binding transcription factor activity
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • DNA binding
  • DNA-binding transcription repressor activity, RNA polymerase II-specific
  • protein binding
  • transcription coregulator activity
  • protein dimerization activity
  • transcription corepressor activity
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • nucleus
  • nucleoplasm
  • mitochondrion
  • cytosol
Biological process
  • multicellular organism development
  • cell population proliferation
  • regulation of transcription, DNA-templated
  • negative regulation of transcription by RNA polymerase II
  • transcription, DNA-templated
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[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

MAD protein is a protein that in humans is encoded by the MXD1 gene.[5][6]

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.[6]

Interactions

MXD1 has been shown to interact with Histone deacetylase 2,[7][8] SMC3,[9] MLX,[10][11] SIN3A[12][13][14] and MAX.[9][15][16][17]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000059728 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001156 – Ensembl, 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. ^ a b "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. ISSN 1072-8368. PMID 11101889. S2CID 12451972.
  9. ^ a b 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

  • Grandori C, Cowley SM, James LP, Eisenman RN (2001). "The Myc/Max/Mad network and the transcriptional control of cell behavior". Annu. Rev. Cell Dev. Biol. 16 (1): 653–99. doi:10.1146/annurev.cellbio.16.1.653. PMID 11031250.
  • Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network". Gene. 277 (1–2): 1–14. doi:10.1016/S0378-1119(01)00697-7. PMID 11602341.
  • Ayer DE, Lawrence QA, Eisenman RN (1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. PMID 7889570. S2CID 8749951.
  • Edelhoff S, Ayer DE, Zervos AS, et al. (1994). "Mapping of two genes encoding members of a distinct subfamily of MAX interacting proteins: MAD to human chromosome 2 and mouse chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome 19". Oncogene. 9 (2): 665–8. PMID 8290278.
  • Ayer DE, Kretzner L, Eisenman RN (1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell. 72 (2): 211–22. doi:10.1016/0092-8674(93)90661-9. PMID 8425218. S2CID 13317223.
  • Hassig CA, Fleischer TC, Billin AN, et al. (1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133. S2CID 14233219.
  • Laherty CD, Yang WM, Sun JM, et al. (1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. PMID 9150134. S2CID 13490886.
  • Gupta K, Anand G, Yin X, et al. (1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
  • FitzGerald MJ, Arsura M, Bellas RE, et al. (1999). "Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc". Oncogene. 18 (15): 2489–98. doi:10.1038/sj.onc.1202611. PMID 10229200.
  • Khan MM, Nomura T, Kim H, et al. (2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Mol. Cell. 7 (6): 1233–43. doi:10.1016/S1097-2765(01)00257-X. PMID 11430826.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Nikiforov MA, Popov N, Kotenko I, et al. (2003). "The Mad and Myc basic domains are functionally equivalent". J. Biol. Chem. 278 (13): 11094–9. doi:10.1074/jbc.M212298200. PMID 12538578.
  • Nair SK, Burley SK (2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell. 112 (2): 193–205. doi:10.1016/S0092-8674(02)01284-9. PMID 12553908. S2CID 16142388.
  • Siegel PM, Shu W, Massagué J (2003). "Mad upregulation and Id2 repression accompany transforming growth factor (TGF)-beta-mediated epithelial cell growth suppression". J. Biol. Chem. 278 (37): 35444–50. doi:10.1074/jbc.M301413200. PMID 12824180.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
  • Zada AA, Pulikkan JA, Bararia D, et al. (2007). "Proteomic discovery of Max as a novel interacting partner of C/EBPalpha: a Myc/Max/Mad link". Leukemia. 20 (12): 2137–46. doi:10.1038/sj.leu.2404438. PMID 17082780.

External links

  • Overview of all the structural information available in the PDB for UniProt: Q05195 (Max dimerization protein 1) at the PDBe-KB.
  • v
  • t
  • e
  • 1nlw: Crystal structure of Mad-Max recognizing DNA
    1nlw: Crystal structure of Mad-Max recognizing DNA
  • v
  • t
  • e
(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