SHANK1

SH3 and multiple ankyrin repeat domains 1

PDB rendering based on 1q3o.

Available structures
PDB	1q3o, 1q3p

Identifiers

Symbols

SHANK1; SPANK-1; SSTRIP; synamon

External IDs

OMIM: 604999 MGI: 3613677 HomoloGene: 22949 GeneCards: SHANK1 Gene

Gene Ontology
Molecular function	• protein binding • protein C-terminus binding • receptor signaling complex scaffold activity • somatostatin receptor binding • ionotropic glutamate receptor binding
Cellular component	• intracellular • membrane fraction • cytoplasm • plasma membrane • postsynaptic density • cell junction • dendrite • synapse • postsynaptic membrane
Biological process	• cytoskeletal anchoring at plasma membrane
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
51.17 – 51.22 Mb

Chr 7:
51.57 – 51.61 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

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

References

^ ^a ^b Zitzer H, Honck HH, Bachner D, Richter D, Kreienkamp HJ (Jan 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.
^ "Entrez Gene: SHANK1 SH3 and multiple ankyrin repeat domains 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50944.
^ Böckers, T M; Mameza M G, Kreutz M R, Bockmann J, Weise C, Buck F, Richter D, Gundelfinger E D, Kreienkamp H J (Oct. 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.
^ 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.
^ 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.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2715172.

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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2715172.
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.

PDB gallery

1q3o: Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization

1q3p: Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization

SHANK1

Interactions

References

Further reading