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MXD1

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
Not to be confused withMothers against decapentaplegic.
MXD1
Available structures
PDBOrtholog search:PDBeRCSB
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
Band2p13.3Start69,897,688bp[1]
End69,942,945bp[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 cMStart86,624,024bp[2]
End86,646,143bp[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
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[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

MAD protein is aprotein that in humans is encoded by theMXD1gene.[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

[edit]

MXD1 has been shown tointeract withHistone deacetylase 2,[7][8]SMC3,[9]MLX,[10][11]SIN3A[12][13][14] andMAX.[9][15][16][17]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000059728Ensembl, May 2017
  2. ^abcGRCm38: 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. ^ab"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. ^abGupta, 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

[edit]

External links

[edit]
  • Overview of all the structural information available in thePDB forUniProt:Q05195 (Max dimerization protein 1) at thePDBe-KB.
PDB gallery
  • 1nlw: Crystal structure of Mad-Max recognizing DNA
    1nlw: Crystal structure of Mad-Max recognizing DNA
(1) Basic domains
(1.1) Basicleucine 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
(3.1)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
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