SHANK1

From Wikipedia, the free encyclopedia


SH3 and multiple ankyrin repeat domains 1
PDB rendering based on 1q3o.
Available structures: 1q3o, 1q3p
Identifiers
Symbol(s) SHANK1; SPANK-1; SSTRIP; synamon
External IDs OMIM: 604999 MGI: 3613677 HomoloGene: 22949
Orthologs
Human Mouse
Entrez 50944 243961
Ensembl n/a ENSMUSG00000038738
Refseq NM_016148 (mRNA)
NP_057232 (protein)		 XM_001001982 (mRNA)
XP_001001982 (protein)
Location n/a Chr 7: 44.18 - 44.22 Mb
Pubmed search [1] [2]

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


[edit] References

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

[edit] 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. 
 This protein-related article is a stub. You can help Wikipedia by expanding it.