ADAM11

ADAM11
Identifiers
AliasesADAM11, MDC, ADAM metallopeptidase domain 11
External IDsMGI: 1098667 HomoloGene: 7614 GeneCards: ADAM11
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17q21.31Start44,759,031 bp[1]
End44,781,846 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

4185

11488

Ensembl

ENSG00000073670

ENSMUSG00000020926

UniProt

O75078

Q9R1V4

RefSeq (mRNA)

NM_002390
NM_001318933

NM_001110778
NM_009613

RefSeq (protein)

NP_001305862
NP_002381

NP_001104248
NP_033743

Location (UCSC)Chr 17: 44.76 – 44.78 MbChr 11: 102.76 – 102.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Disintegrin and metalloproteinase domain-containing protein 11 is an enzyme that in humans is encoded by the ADAM11 gene.[5][6]

This gene encodes a member of the ADAM (a disintegrin and metalloprotease) protein family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This gene represents a candidate tumor suppressor gene for human breast cancer based on its location within a minimal region of chromosome 17q21 previously defined by tumor deletion mapping.[6]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000073670 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020926 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Emi M, Katagiri T, Harada Y, Saito H, Inazawa J, Ito I, Kasumi F, Nakamura Y (Jan 1994). "A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers". Nat Genet. 5 (2): 151–7. doi:10.1038/ng1093-151. PMID 8252040.
  6. 1 2 "Entrez Gene: ADAM11 ADAM metallopeptidase domain 11".

Further reading

  • Wolfsberg TG, Primakoff P, Myles DG, White JM (1995). "ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell- matrix interactions". J. Cell Biol. 131 (2): 275–8. doi:10.1083/jcb.131.2.275. PMC 2199973. PMID 7593158.
  • Katagiri T, Harada Y, Emi M, Nakamura Y (1994). "Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicing". Cytogenet. Cell Genet. 68 (1–2): 39–44. doi:10.1159/000133884. PMID 7956356.
  • Sagane K, Ohya Y, Hasegawa Y, Tanaka I (1998). "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain". Biochem. J. 334 ( Pt 1) (Pt 1): 93–8. PMC 1219666. PMID 9693107.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
  • Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
  • Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.


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