Afadin

Afadin is a protein that in humans is encoded by the AFDN gene.[5]

AFDN
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAFDN, AF6, MLL-AF6, MLLT4, myeloid/lymphoid or mixed-lineage leukemia; translocated to, 4, afadin, adherens junction formation factor, l-afadin
External IDsOMIM: 159559 MGI: 1314653 HomoloGene: 21202 GeneCards: AFDN
Gene location (Human)
Chr.Chromosome 6 (human)[1]
Band6q27Start167,826,922 bp[1]
End167,972,023 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

4301

17356

Ensembl

ENSG00000130396

ENSMUSG00000068036

UniProt

P55196

Q9QZQ1

RefSeq (mRNA)

NM_010806

RefSeq (protein)

NP_034936

Location (UCSC)Chr 6: 167.83 – 167.97 MbChr 17: 13.76 – 13.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

Afadin is a Ras (see HRAS; MIM 190020) target that regulates cell–cell adhesions downstream of Ras activation. It is fused with MLL (MIM 159555) in leukemias caused by t(6;11) translocations (Taya et al., 1998).[supplied by OMIM][6]

Interactions

Afadin has been shown to interact with:

gollark: That sure is a thing of some kind.
gollark: As they say, there is no escape.
gollark: Rescheduled to 2022.
gollark: (not February 30th; this does not, in fact, exist, under any circumstances. DO NOT believe any claims of its existence. Immediately cease contact with anyone who tells you it exists. The 30th of February does not, and in fact by definition cannot, occur. There is no 30/02. It is not real. Avert your gaze. IT IS NOT REAL.)
gollark: They hide a lot of things, actually.

References

  1. GRCh38: Ensembl release 89: ENSG00000130396 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000068036 - 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. Prasad R, Gu Y, Alder H, Nakamura T, Canaani O, Saito H, Huebner K, Gale RP, Nowell PC, Kuriyama K (Dec 1993). "Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation". Cancer Research. 53 (23): 5624–8. PMID 8242616.
  6. "Entrez Gene: MLLT4 myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4".
  7. Radziwill G, Erdmann RA, Margelisch U, Moelling K (Jul 2003). "The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain". Molecular and Cellular Biology. 23 (13): 4663–72. doi:10.1128/mcb.23.13.4663-4672.2003. PMC 164848. PMID 12808105.
  8. Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K (Aug 1998). "PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor". Proceedings of the National Academy of Sciences of the United States of America. 95 (17): 9779–84. doi:10.1073/pnas.95.17.9779. PMC 21413. PMID 9707552.
  9. Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
  10. Boettner B, Govek EE, Cross J, Van Aelst L (Aug 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 9064–9. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
  11. Yamamoto T, Harada N, Kawano Y, Taya S, Kaibuchi K (May 1999). "In vivo interaction of AF-6 with activated Ras and ZO-1". Biochemical and Biophysical Research Communications. 259 (1): 103–7. doi:10.1006/bbrc.1999.0731. PMID 10334923.
  12. Bégay-Müller V, Ansieau S, Leutz A (Jun 2002). "The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene". FEBS Letters. 521 (1–3): 36–8. doi:10.1016/s0014-5793(02)02814-4. PMID 12067721.
  13. Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y (May 1999). "Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein". The Journal of Cell Biology. 145 (3): 539–49. doi:10.1083/jcb.145.3.539. PMC 2185068. PMID 10225955.
  14. Satoh-Horikawa K, Nakanishi H, Takahashi K, Miyahara M, Nishimura M, Tachibana K, Mizoguchi A, Takai Y (Apr 2000). "Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities". The Journal of Biological Chemistry. 275 (14): 10291–9. doi:10.1074/jbc.275.14.10291. PMID 10744716.
  15. Reymond N, Borg JP, Lecocq E, Adelaide J, Campadelli-Fiume G, Dubreuil P, Lopez M (Sep 2000). "Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadin". Gene. 255 (2): 347–55. doi:10.1016/s0378-1119(00)00316-4. PMID 11024295.
  16. Su L, Hattori M, Moriyama M, Murata N, Harazaki M, Kaibuchi K, Minato N (Apr 2003). "AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1". The Journal of Biological Chemistry. 278 (17): 15232–8. doi:10.1074/jbc.M211888200. PMID 12590145.
  17. Mandai K, Nakanishi H, Satoh A, Takahashi K, Satoh K, Nishioka H, Mizoguchi A, Takai Y (Mar 1999). "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions". The Journal of Cell Biology. 144 (5): 1001–17. doi:10.1083/jcb.144.5.1001. PMC 2148189. PMID 10085297.
  18. Asada M, Irie K, Morimoto K, Yamada A, Ikeda W, Takeuchi M, Takai Y (Feb 2003). "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". The Journal of Biological Chemistry. 278 (6): 4103–11. doi:10.1074/jbc.M209832200. PMID 12446711.
  19. Taya S, Yamamoto T, Kanai-Azuma M, Wood SA, Kaibuchi K (Dec 1999). "The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin". Genes to Cells. 4 (12): 757–67. doi:10.1046/j.1365-2443.1999.00297.x. PMID 10620020.
  20. Taya S, Yamamoto T, Kano K, Kawano Y, Iwamatsu A, Tsuchiya T, Tanaka K, Kanai-Azuma M, Wood SA, Mattick JS, Kaibuchi K (Aug 1998). "The Ras target AF-6 is a substrate of the fam deubiquitinating enzyme". The Journal of Cell Biology. 142 (4): 1053–62. doi:10.1083/jcb.142.4.1053. PMC 2132865. PMID 9722616.

Further reading

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