MXD4

Protein-coding gene in the species Homo sapiens
MXD4
Identifiers
AliasesMXD4, MAD4, MST149, MSTP149, bHLHc12, MAX dimerization protein 4
External IDsMGI: 104991; HomoloGene: 4712; GeneCards: MXD4; OMA:MXD4 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for MXD4
Genomic location for MXD4
Band4p16.3Start2,247,432 bp[1]
End2,262,109 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for MXD4
Genomic location for MXD4
Band5 B2|5 17.84 cMStart34,331,227 bp[2]
End34,345,064 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • anterior pituitary

  • right lung

  • tibial nerve

  • ascending aorta

  • right coronary artery

  • right lobe of thyroid gland

  • left coronary artery

  • left lobe of thyroid gland

  • spleen

  • right uterine tube
Top expressed in
  • ascending aorta

  • aortic valve

  • Paneth cell

  • fossa

  • left lung lobe

  • calvaria

  • thymus

  • femur

  • body of femur

  • utricle
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • protein binding
  • protein dimerization activity
  • transcription corepressor activity
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • nucleus
Biological process
  • regulation of transcription, DNA-templated
  • negative regulation of transcription by RNA polymerase II
  • transcription, DNA-templated
  • negative regulation of cell population proliferation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10608

17122

Ensembl

ENSG00000123933

ENSMUSG00000037235

UniProt

Q14582

Q60948

RefSeq (mRNA)

NM_006454

NM_010753

RefSeq (protein)

NP_006445

n/a

Location (UCSC)Chr 4: 2.25 – 2.26 MbChr 5: 34.33 – 34.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Max-interacting transcriptional repressor MAD4 is a protein that in humans is encoded by the MXD4 gene.[5][6]

Function

This gene is a member of the MAD gene family . The MAD genes encode basic helix-loop-helix-leucine zipper proteins that heterodimerize with MAX protein, forming a transcriptional repression complex. The MAD proteins compete for MAX binding with MYC, which heterodimerizes with MAX forming a transcriptional activation complex. Studies in rodents suggest that the MAD genes are tumor suppressors and contribute to the regulation of cell growth in differentiating tissues.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123933 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037235 – 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. ^ Hurlin PJ, Quéva C, Koskinen PJ, Steingrímsson E, Ayer DE, Copeland NG, Jenkins NA, Eisenman RN (November 1995). "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation". The EMBO Journal. 14 (22): 5646–59. doi:10.1002/j.1460-2075.1995.tb00252.x. PMC 394680. PMID 8521822.
  6. ^ a b "Entrez Gene: MXD4 MAX dimerization protein 4".

Further reading

  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Marcotte R, Chen JM, Huard S, Wang E (December 2005). "c-Myc creates an activation loop by transcriptionally repressing its own functional inhibitor, hMad4, in young fibroblasts, a loop lost in replicatively senescent fibroblasts". Journal of Cellular Biochemistry. 96 (5): 1071–85. doi:10.1002/jcb.20503. PMID 16167342. S2CID 8251961.
  • Pope SN, Lee IR (February 2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". The Journal of Steroid Biochemistry and Molecular Biology. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967. S2CID 9746088.
  • Jiang DJ, Yu HX, Hexige SY, Guo ZK, Wang X, Ma LJ, Chen Z, Zhao SY, Yu L (July 2004). "Human liver specific transcriptional factor TCP10L binds to MAD4". Journal of Biochemistry and Molecular Biology. 37 (4): 402–7. doi:10.5483/bmbrep.2004.37.4.402. PMID 15469726.
  • Kime L, Wright SC (February 2003). "Mad4 is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc". The Biochemical Journal. 370 (Pt 1): 291–8. doi:10.1042/BJ20021679. PMC 1223147. PMID 12418961.
  • 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". Human Molecular Genetics. 10 (6): 617–27. doi:10.1093/hmg/10.6.617. PMID 11230181.
  • Billin AN, Eilers AL, Queva C, Ayer DE (December 1999). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". The Journal of Biological Chemistry. 274 (51): 36344–50. doi:10.1074/jbc.274.51.36344. PMID 10593926.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

  • 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
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