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Gene Review

SHANK1  -  SH3 and multiple ankyrin repeat domains 1

Homo sapiens

Synonyms: SH3 and multiple ankyrin repeat domains protein 1, SPANK-1, SSTR-interacting protein, SSTRIP, Shank1, ...
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Disease relevance of SHANK1

  • Thus, large genetic increases in body weight of males can be achieved without loss in walking ability by genetic increases in shank width.(ABSTRACT TRUNCATED AT 250 WORDS)[1]
  • Previous work from our laboratory suggested that the trans-acting defect which allows packaging of cellular mRNA mapped to the provirus but did not map to the nucleocapsid region of the gag gene (D.J. Anderson, P. Lee, K. L. Levine, J. Sang, S. A. Shah, O. O. Yang, P. R. Shank, and M. L. Linial, J. Virol. 66:204-216, 1992) [2].
  • They were designed to occlude aneurysms with irregular necks by using the angle and shank portion of a bayonet clip (shank clipping) [3].
  • Exposed poults varied in size as early as day 8 and had significantly decreased weight gains and reduced shank lengths on days 8, 12, 16, and 21 [4].
  • In addition, the presence of local electrical inhomogeneities (encapsulation, edema, coatings) around the electrode shank can substantially influence neural recordings and requires further theoretical and experimental investigation [5].

Psychiatry related information on SHANK1

  • A new method of monitoring physical activity that is able to detect walking upstairs using a miniature gyroscope attached to the shank is presented [6].

High impact information on SHANK1

  • The organization of these terminally redundant sequences appeared identical to that of the 300 base pair (bp) repeats found at the ends of unintegrated linear DNA (Shank et al., 1978) [7].
  • Shank proteins, initially also described as ProSAP proteins, are scaffolding adaptors that have been previously shown to integrate neurotransmitter receptors into the cortical cytoskeleton at postsynaptic densities [8].
  • The proteins of the Homer family bind to proline-rich sequences in group I metabotropic glutamate receptors, inositol trisphosphate receptors, ryanodine receptors, and Shank family proteins [9].
  • Anatomically distinct muscles arise by the progressive segregation of muscle: differentiated myotubes first appear as a pair of dorsal and ventral muscle masses; these masses subdivide into dorsal and ventral thigh, shank and foot muscle masses; and finally these six masses segregate into individual muscles [10].
  • Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization [11].

Chemical compound and disease context of SHANK1


Biological context of SHANK1

  • Novel human and mouse genes encoding a shank-interacting protein and its upregulation in gastric fundus of W/WV mouse [13].
  • Axons of older hosts innervating hindlimbs transplanted from young tadpoles distinguished flexor from extensor limb regions, but failed to distinguish thigh from shank, demonstrating that axons in older animals can respond to at least some guidance cues [14].
  • With one exception, heterosis was not an important source of variation for shank width or shank depth and there was a low level of heterosis for shank length [15].
  • Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin [16].
  • Considering the fact that the ankyrin repeats and the SH3 domain of Shank can be truncated by alternative splicing, these results define Sharpin as a novel PSD protein that may regulate the complexity of the Shank-based protein network in an alternative splicing-dependent manner [17].

Anatomical context of SHANK1

  • Postsynaptic shank antagonizes dendrite branching induced by the leucine-rich repeat protein Densin-180 [18].
  • The N-terminal leucine-rich repeat region, which is not involved in binding shank, targets Densin-180 to the plasma membrane in transfected cells and to the basolateral membrane of epithelial cells [18].
  • One possibility is that the shank degenerates when the hindlimb is transplanted to a different host [14].
  • Shank deceleration was measured by a lightweight accelerometer which was tightly attached over the distal medial tibia [19].
  • Fractionation of rat brain membranes indicated that somatostatin receptor interacting protein is enriched in the postsynaptic density fraction [20].

Associations of SHANK1 with chemical compounds

  • Shank polypeptides contain multiple sites for protein-protein interaction, including ankyrin repeats, an SH3 domain, a PDZ domain, a long proline-rich region, and a SAM domain [21].
  • Our data indicate that the Shank1 and -3 family members provide multiple independent connections between synaptic glutamate receptor complexes and the cytoskeleton [16].
  • Telone C35 (61% 1,3-D and 35% CP) was shank-applied at a depth of 46 cm at a rate of 610 kg ha(-1) [22].
  • Distribution and leaching of methyl iodide in soil following emulated shank and drip application [23].
  • For the NB zirconium oxide, only the Axis 856C consistently produced a significantly smoother (P<.01, P<.0001 and P<.0001, respectively) surface finish on the start, shank, and tip [24].

Physical interactions of SHANK1


Other interactions of SHANK1


Analytical, diagnostic and therapeutic context of SHANK1

  • Incidence of shank vessel injuries, imaging studies required for accurate and expedient diagnosis, determinants influencing the decision for repair or amputation, and details of techniques in surgical intervention are discussed [27].
  • Monolimb refers to a transtibial prosthesis with the prosthetic socket and the shank being molded into one piece of thermoplastic material [28].
  • Discrete subplasmalemmal areas of pronounced ProSAP/Shank immunoreactivity could be demonstrated inside several thymocytes by confocal laser scanning microscopy [29].
  • We used the N-terminal ankyrin repeats of Shank1 and -3 to search for interacting proteins by yeast two-hybrid screening and by affinity chromatography [16].
  • Our study suggests that if the patient's foot does not improve after Fogarty embolectomy, the popliteal artery should be exposed and the catheter directed into the shank arteries using vascular forceps [30].


  1. The influence of genetic increases in shank width on body weight, walking ability, and reproduction of turkeys. Nestor, K.E., Bacon, W.L., Saif, Y.M., Renner, P.A. Poult. Sci. (1985) [Pubmed]
  2. The packaging phenotype of the SE21Q1b provirus is related to high proviral expression and not trans-acting factors. Anderson, D.J., Stone, J., Lum, R., Linial, M.L. J. Virol. (1995) [Pubmed]
  3. Newly designed bayonet clips for complicated aneurysms: technical note. Osawa, M., Obinata, C., Kobayashi, S., Tanaka, Y. Neurosurgery (1995) [Pubmed]
  4. Skeletal lesions associated with a naturally occurring poult enteritis. Perry, R.W., Rowland, G.N., Glisson, J.R., Steffens, W.L., Quinn, J.A. Avian Dis. (1991) [Pubmed]
  5. Model-based analysis of cortical recording with silicon microelectrodes. Moffitt, M.A., McIntyre, C.C. Clinical neurophysiology : official journal of the International Federation of Clinical Neurophysiology. (2005) [Pubmed]
  6. Stair climbing detection during daily physical activity using a miniature gyroscope. Coley, B., Najafi, B., Paraschiv-Ionescu, A., Aminian, K. Gait & posture. (2005) [Pubmed]
  7. Proviruses of avian sarcoma virus are terminally redundant, co-extensive with unintegrated linear DNA and integrated at many sites. Hughes, S.H., Shank, P.R., Spector, D.H., Kung, H.J., Bishop, J.M., Varmus, H.E., Vogt, P.K., Breitman, M.L. Cell (1978) [Pubmed]
  8. The neuronal scaffold protein Shank3 mediates signaling and biological function of the receptor tyrosine kinase Ret in epithelial cells. Schuetz, G., Rosário, M., Grimm, J., Boeckers, T.M., Gundelfinger, E.D., Birchmeier, W. J. Cell Biol. (2004) [Pubmed]
  9. Homer: a link between neural activity and glutamate receptor function. Xiao, B., Tu, J.C., Worley, P.F. Curr. Opin. Neurobiol. (2000) [Pubmed]
  10. Muscle and tendon morphogenesis in the avian hind limb. Kardon, G. Development (1998) [Pubmed]
  11. Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization. Im, Y.J., Lee, J.H., Park, S.H., Park, S.J., Rho, S.H., Kang, G.B., Kim, E., Eom, S.H. J. Biol. Chem. (2003) [Pubmed]
  12. In vivo injection of dipyridamole stimulates the synthesis of prostacyclin-like substances in human varicose veins. Fahr, A., Langer, R., Sziegoleit, W., Beitz, J., Krause, P., Förster, W. Biomed. Biochim. Acta (1984) [Pubmed]
  13. Novel human and mouse genes encoding a shank-interacting protein and its upregulation in gastric fundus of W/WV mouse. Daigo, Y., Takayama, I., Ward, S.M., Sanders, K.M., Fujino, M.A. J. Gastroenterol. Hepatol. (2003) [Pubmed]
  14. Neuromuscular specificity following cross-stage hindlimb transplantation. Farel, P.B., Wray, S.E. Exp. Neurol. (1992) [Pubmed]
  15. Effect of crossing a line selected for increased shank width with two commercial sire lines on performance and walking ability of turkeys. Nestor, K.E., Anderson, J.W. Poult. Sci. (1998) [Pubmed]
  16. Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin. Böckers, T.M., Mameza, M.G., Kreutz, M.R., Bockmann, J., Weise, C., Buck, F., Richter, D., Gundelfinger, E.D., Kreienkamp, H.J. J. Biol. Chem. (2001) [Pubmed]
  17. Sharpin, a novel postsynaptic density protein that directly interacts with the shank family of proteins. Lim, S., Sala, C., Yoon, J., Park, S., Kuroda, S., Sheng, M., Kim, E. Mol. Cell. Neurosci. (2001) [Pubmed]
  18. Postsynaptic shank antagonizes dendrite branching induced by the leucine-rich repeat protein Densin-180. Quitsch, A., Berhörster, K., Liew, C.W., Richter, D., Kreienkamp, H.J. J. Neurosci. (2005) [Pubmed]
  19. The effect of varied stride rate upon shank deceleration in running. Clarke, T.E., Cooper, L.B., Hamill, C.L., Clark, D.E. Journal of sports sciences. (1985) [Pubmed]
  20. Somatostatin receptor interacting protein defines a novel family of multidomain proteins present in human and rodent brain. Zitzer, H., Hönck, H.H., Bächner, D., Richter, D., Kreienkamp, H.J. J. Biol. Chem. (1999) [Pubmed]
  21. The Shank family of scaffold proteins. Sheng, M., Kim, E. J. Cell. Sci. (2000) [Pubmed]
  22. Surface seals reduce 1,3-dichloropropene and chloropicrin emissions in field tests. Gao, S., Trout, T.J. J. Environ. Qual. (2007) [Pubmed]
  23. Distribution and leaching of methyl iodide in soil following emulated shank and drip application. Guo, M., Zheng, W., Papiernik, S.K., Yates, S.R. J. Environ. Qual. (2004) [Pubmed]
  24. Ceramic implant abutments: cutting efficiency and resultant surface finish by diamond rotary cutting instruments. Park, S.W., Driscoll, C.F., Romberg, E.E., Siegel, S., Thompson, G. The Journal of prosthetic dentistry. (2006) [Pubmed]
  25. The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42. Soltau, M., Richter, D., Kreienkamp, H.J. Mol. Cell. Neurosci. (2002) [Pubmed]
  26. Insulin receptor substrate of 53 kDa links postsynaptic shank to PSD-95. Soltau, M., Berhörster, K., Kindler, S., Buck, F., Richter, D., Kreienkamp, H.J. J. Neurochem. (2004) [Pubmed]
  27. Shank vessel injuries. Rowe, V.L., Salim, A., Lipham, J., Asensio, J.A. Surg. Clin. North Am. (2002) [Pubmed]
  28. A numerical approach to evaluate the fatigue life of monolimb. Chen, N.Z., Lee, W.C., Zhang, M. Medical engineering & physics. (2006) [Pubmed]
  29. Expression of postsynaptic density proteins of the ProSAP/Shank family in the thymus. Redecker, P., Bockmann, J., B??ckers, T.M. Histochem. Cell Biol. (2006) [Pubmed]
  30. The anatomic basis for the occasional failure of transfemoral balloon catheter thromboembolectomy. Short, D., Vaughn, G.D., Jachimczyk, J., Gallagher, M.W., Garcia-Rinaldi, R. Ann. Surg. (1979) [Pubmed]
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