SHANK1

SHANK1
Identifiers
Aliases	SHANK1, SPANK-1, SSTRIP, synamon, SH3 and multiple ankyrin repeat domains 1
External IDs	OMIM: 604999; MGI: 3613677; HomoloGene: 22949; GeneCards: SHANK1; OMA:SHANK1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.33 Start 50,659,255 bp End 50,719,802 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 B3 Start 43,959,677 bp End 44,009,996 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in anterior cingulate cortex right frontal lobe prefrontal cortex amygdala right hemisphere of cerebellum primary visual cortex dorsolateral prefrontal cortex Brodmann area 9 hippocampus proper middle temporal gyrus Top expressed in prefrontal cortex primary motor cortex temporal lobe subiculum cingulate gyrus amygdala lateral geniculate nucleus piriform cortex primary visual cortex medial dorsal nucleus More reference expression data BioGPS n/a
Gene ontology Molecular function somatostatin receptor binding SH3 domain binding ankyrin repeat binding scaffold protein binding protein C-terminus binding protein binding synaptic receptor adaptor activity identical protein binding ionotropic glutamate receptor binding signaling receptor complex adaptor activity protein-containing complex binding Cellular component cytoplasm postsynaptic membrane membrane dendritic spine synapse excitatory synapse intracellular anatomical structure NMDA selective glutamate receptor complex cell junction dendrite neuron projection ionotropic glutamate receptor complex postsynaptic density cytosol plasma membrane Schaffer collateral - CA1 synapse glutamatergic synapse neuron spine Biological process cell differentiation olfactory behavior associative learning neuromuscular process controlling balance negative regulation of actin filament bundle assembly positive regulation of dendritic spine development nervous system development regulation of AMPA receptor activity dendritic spine morphogenesis vocalization behavior adult behavior long-term memory synapse maturation positive regulation of excitatory postsynaptic potential social behavior habituation determination of affect righting reflex protein localization to synapse protein-containing complex assembly postsynapse organization synapse assembly brain morphogenesis synaptic assembly at neuromuscular junction positive regulation of synaptic transmission, glutamatergic long-term potentiation postsynaptic density assembly Sources:Amigo / QuickGO
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: 43.96 – 44.01 Mb PubMed search
Wikidata
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SH3 and multiple ankyrin repeat domains protein 1 is a protein that in humans is encoded by the SHANK1 gene.

Interactions

SHANK1 has been shown to interact with:

• ARHGEF7,
• BAIAP2,
• DNM2,
• SPTAN1, and
• Somatostatin receptor 2.

Further reading

• 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, Xiao B, Sala C, Valtschanoff J, Weinberg RJ, Worley PF, Sheng M (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. S2CID 2209372.
• Tu JC, Xiao B, Naisbitt S, Yuan JP, Petralia RS, Brakeman P, Doan A, Aakalu VK, Lanahan AA, Sheng M, Worley PF (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. S2CID 16429070.
• 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, Richter D, Bockers TM (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. S2CID 8791865.
• Lim S, Sala C, Yoon J, Park S, Kuroda S, Sheng M, Kim E (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. S2CID 45278068.
• Böckers TM, Mameza MG, Kreutz MR, Bockmann J, Weise C, Buck F, Richter D, Gundelfinger ED, Kreienkamp HJ (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, Fallon J, Vallee RB (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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. S2CID 572407.
• Park E, Na M, Choi J, Kim S, Lee JR, Yoon J, Park D, Sheng M, Kim E (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, Sanders KM, Fujino MA (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. S2CID 38146288.
• Im YJ, Lee JH, Park SH, Park SJ, Rho SH, Kang GB, Kim E, Eom SH (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, Tian QB, Sakagami H, Usuda N, Usada N, Kondo H, Fujii T, Endo S (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. S2CID 28773407.
• Fieulaine S, Juillan-Binard C, Serero A, Dardel F, Giglione C, Meinnel T, Ferrer JL (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.