SHANK1

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SH3 and multiple ankyrin repeat domains 1
File:PBB Protein SHANK1 image.jpg
PDB rendering based on 1q3o.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SHANK1 ; SPANK-1; SSTRIP; synamon
External IDs Template:OMIM5 Template:MGI HomoloGene22949
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

SH3 and multiple ankyrin repeat domains 1, also known as SHANK1, is a human gene.[1]


References

  1. "Entrez Gene: SHANK1 SH3 and multiple ankyrin repeat domains 1".

Further reading

  • Sheng M, Kim E (2000). "The Shank family of scaffold proteins". J. Cell. Sci. 113 ( Pt 11): 1851–6. PMID 10806096.
  • Naisbitt S, Kim E, Tu JC; et al. (1999). "Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin". Neuron. 23 (3): 569–82. PMID 10433268.
  • Tu JC, Xiao B, Naisbitt S; et al. (1999). "Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins". Neuron. 23 (3): 583–92. PMID 10433269.
  • Zitzer H, Hönck HH, Bächner D; et al. (2000). "Somatostatin receptor interacting protein defines a novel family of multidomain proteins present in human and rodent brain". J. Biol. Chem. 274 (46): 32997–3001. PMID 10551867.
  • Tobaben S, Südhof TC, Stahl B (2000). "The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family". J. Biol. Chem. 275 (46): 36204–10. doi:10.1074/jbc.M006448200. PMID 10958799.
  • Kreienkamp HJ, Zitzer H, Gundelfinger ED; et al. (2000). "The calcium-independent receptor for alpha-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins". J. Biol. Chem. 275 (42): 32387–90. doi:10.1074/jbc.C000490200. PMID 10964907.
  • Kreienkamp HJ, Zitzer H, Richter D (2001). "Identification of proteins interacting with the rat somatostatin receptor subtype 2". J. Physiol. Paris. 94 (3–4): 193–8. PMID 11087996.
  • Lim S, Sala C, Yoon J; et al. (2001). "Sharpin, a novel postsynaptic density protein that directly interacts with the shank family of proteins". Mol. Cell. Neurosci. 17 (2): 385–97. doi:10.1006/mcne.2000.0940. PMID 11178875.
  • Böckers TM, Mameza MG, Kreutz MR; et al. (2001). "Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin". J. Biol. Chem. 276 (43): 40104–12. doi:10.1074/jbc.M102454200. PMID 11509555.
  • Okamoto PM, Gamby C, Wells D; et al. (2002). "Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton". J. Biol. Chem. 276 (51): 48458–65. doi:10.1074/jbc.M104927200. PMID 11583995.
  • Soltau M, Richter D, Kreienkamp HJ (2003). "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42". Mol. Cell. Neurosci. 21 (4): 575–83. PMID 12504591.
  • Park E, Na M, Choi J; et al. (2003). "The Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the beta PIX guanine nucleotide exchange factor for Rac1 and Cdc42". J. Biol. Chem. 278 (21): 19220–9. doi:10.1074/jbc.M301052200. PMID 12626503.
  • Daigo Y, Takayama I, Ward SM; et al. (2004). "Novel human and mouse genes encoding a shank-interacting protein and its upregulation in gastric fundus of W/WV mouse". J. Gastroenterol. Hepatol. 18 (6): 712–8. PMID 12753155.
  • Im YJ, Lee JH, Park SH; et al. (2004). "Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization". J. Biol. Chem. 278 (48): 48099–104. doi:10.1074/jbc.M306919200. PMID 12954649.
  • Suzuki T, Li W, Zhang JP; et al. (2005). "A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins". Eur. J. Neurosci. 21 (2): 339–50. doi:10.1111/j.1460-9568.2005.03856.x. PMID 15673434.
  • Fieulaine S, Juillan-Binard C, Serero A; et al. (2006). "The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms". J. Biol. Chem. 280 (51): 42315–24. doi:10.1074/jbc.M507155200. PMID 16192279.

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