SH3PXD2A

SH3PXD2A

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2DNU, 2EGA, 2EGC, 2EKH

Identifiers

SH3PXD2A, FISH, SH3MD1, TKS5, SH3 and PX domains 2A

External IDs

MGI: 1298393 HomoloGene: 7317 GeneCards: SH3PXD2A

Gene ontology
Molecular function	• protein binding • superoxide-generating NADPH oxidase activator activity • phosphatidylinositol binding
Cellular component	• cytoplasm • podosome • cell junction • cell projection
Biological process	• osteoclast fusion • superoxide metabolic process • reactive oxygen species metabolic process • positive regulation of catalytic activity • oxidation-reduction process • podosome assembly
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse


9644


14218


ENSG00000107957


ENSMUSG00000053617


Q5TCZ1


O89032

RefSeq (mRNA)


NM_014631


NM_001164717 NM_008018 NM_177833

RefSeq (protein)


NP_055446.2


NP_001158189.1 NP_032044.2

Location (UCSC)

Chr 10: 103.59 – 103.86 Mb

Chr 19: 47.26 – 47.46 Mb

PubMed search

^[1]

^[2]

View/Edit Human

View/Edit Mouse

SH3 and PX domain-containing protein 2A is a protein that in humans is encoded by the SH3PXD2A gene.^[3]^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Lock P, Abram CL, Gibson T, Courtneidge SA (Sep 1998). "A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate". EMBO J. 17 (15): 4346–57. doi:10.1093/emboj/17.15.4346. PMC 1170768. PMID 9687503.
↑ "Entrez Gene: SH3PXD2A SH3 and PX domains 2A".

Further reading

Ishikawa K, Nagase T, Nakajima D, et al. (1998). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 4 (5): 307–13. doi:10.1093/dnares/4.5.307. PMID 9455477.
Abram CL, Seals DF, Pass I, et al. (2003). "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells.". J. Biol. Chem. 278 (19): 16844–51. doi:10.1074/jbc.M300267200. PMID 12615925.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10.". Nature. 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.
Seals DF, Azucena EF, Pass I, et al. (2005). "The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells.". Cancer Cell. 7 (2): 155–65. doi:10.1016/j.ccr.2005.01.006. PMID 15710328.
Malinin NL, Wright S, Seubert P, et al. (2005). "Amyloid-beta neurotoxicity is mediated by FISH adapter protein and ADAM12 metalloprotease activity.". Proc. Natl. Acad. Sci. U.S.A. 102 (8): 3058–63. doi:10.1073/pnas.0408237102. PMC 549444. PMID 15710903.
Harold D, Jehu L, Turic D, et al. (2007). "Interaction between the ADAM12 and SH3MD1 genes may confer susceptibility to late-onset Alzheimer's disease.". Am. J. Med. Genet. B Neuropsychiatr. Genet. 144 (4): 448–52. doi:10.1002/ajmg.b.30456. PMID 17440933.

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