SHANK1

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SH3 and multiple ankyrin repeat domains 1
Protein SHANK1 PDB 1q3o.png
PDB rendering based on 1q3o.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SHANK1 ; SPANK-1; SSTRIP; synamon
External IDs OMIM604999 MGI3613677 HomoloGene22949 GeneCards: SHANK1 Gene
Orthologs
Species Human Mouse
Entrez 50944 243961
Ensembl ENSG00000161681 ENSMUSG00000038738
UniProt Q9Y566 D3YZU1
RefSeq (mRNA) NM_016148 NM_001034115
RefSeq (protein) NP_057232 NP_001029287
Location (UCSC) Chr 19:
50.66 – 50.72 Mb
Chr 7:
44.31 – 44.36 Mb
PubMed search [1] [2]

SH3 and multiple ankyrin repeat domains protein 1 is a protein that in humans is encoded by the SHANK1 gene.[1][2]


Interactions[edit]

SHANK1 has been shown to interact with SPTAN1,[3] BAIAP2,[4] ARHGEF7,[5] DNM2[6] and Somatostatin receptor 2.[1]

References[edit]

  1. ^ a b Zitzer H, Honck HH, Bachner D, Richter D, Kreienkamp HJ (January 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. doi:10.1074/jbc.274.46.32997. PMID 10551867. 
  2. ^ "Entrez Gene: SHANK1 SH3 and multiple ankyrin repeat domains 1". 
  3. ^ Böckers, T M; Mameza M G; Kreutz M R; Bockmann J; Weise C; Buck F; Richter D; Gundelfinger E D; Kreienkamp H J (October 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. (United States) 276 (43): 40104–12. doi:10.1074/jbc.M102454200. ISSN 0021-9258. PMID 11509555. 
  4. ^ Soltau, Michaela; Richter Dietmar; Kreienkamp Hans-Jürgen (Dec 2002). "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42". Mol. Cell. Neurosci. (United States) 21 (4): 575–83. doi:10.1006/mcne.2002.1201. ISSN 1044-7431. PMID 12504591. 
  5. ^ Park, Eunhye; Na Moonseok; Choi Jeonghoon; Kim Seho; Lee Jae-Ran; Yoon Jiyoung; Park Dongeun; Sheng Morgan; Kim Eunjoon (May 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. (United States) 278 (21): 19220–9. doi:10.1074/jbc.M301052200. ISSN 0021-9258. PMID 12626503. 
  6. ^ Okamoto, P M; Gamby C; Wells D; Fallon J; Vallee R B (Dec 2001). "Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton". J. Biol. Chem. (United States) 276 (51): 48458–65. doi:10.1074/jbc.M104927200. ISSN 0021-9258. PMC 2715172. PMID 11583995. 

Further reading[edit]

  • Sheng M, Kim E (2000). "The Shank family of scaffold proteins.". J. Cell. Sci. 113 (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. doi:10.1016/S0896-6273(00)80809-0. 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. doi:10.1016/S0896-6273(00)80810-7. PMID 10433269. 
  • 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. doi:10.1016/S0928-4257(00)00204-7. 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. PMC 2715172. 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. doi:10.1006/mcne.2002.1201. 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. doi:10.1046/j.1440-1746.2003.03046.x. 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.