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Spectrin, alpha, non-erythrocytic 1

PDB rendering based on 1aey.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SPTAN1 ; EIEE5; NEAS; SPTA2
External IDs OMIM182810 MGI98386 HomoloGene2353 GeneCards: SPTAN1 Gene
RNA expression pattern
PBB GE SPTAN1 208611 s at tn.png
PBB GE SPTAN1 215235 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6709 20740
Ensembl ENSG00000197694 ENSMUSG00000057738
UniProt Q13813 P16546
RefSeq (mRNA) NM_001130438 NM_001076554
RefSeq (protein) NP_001123910 NP_001070022
Location (UCSC) Chr 9:
131.31 – 131.4 Mb
Chr 2:
29.97 – 30.03 Mb
PubMed search [1] [2]

Spectrin alpha chain, brain is a protein that in humans is encoded by the SPTAN1 gene.[1][1][2][3]

The spectrins are a family of widely distributed cytoskeletal proteins which are involved in actin crosslinking. The protein enocoded by this gene is a spectrin alpha-chain which heterodimerizes with tissue-specific beta-chains.[1] It is specifically expressed in nonerythrocytic cells. The encoded protein has been implicated in other cellular functions including DNA repair and cell cycle regulation. Mutations in this gene are the cause of early infantile epileptic encephalopathy-5. Alternate splicing results in multiple transcript variants.[2]

See also[edit]

Interactions[edit]

SPTAN1 has been shown to interact with Vimentin,[4] SHANK1,[5] Fanconi anemia, complementation group C,[6][7] FANCA,[6][7][8] Plectin,[4][9] GRIA2[10] and Abl gene.[11]

References[edit]

  1. ^ a b c Leto TL, Fortugno-Erikson D, Barton D, Yang-Feng TL, Francke U, Harris AS, Morrow JS, Marchesi VT, Benz EJ Jr (February 1988). "Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species". Mol Cell Biol 8 (1): 1–9. PMC 363070. PMID 3336352. 
  2. ^ a b "Entrez Gene: SPTAN1 spectrin, alpha, non-erythrocytic 1 (alpha-fodrin)". 
  3. ^ McMahon AP, Giebelhaus DH, Champion JE, et al. (1987). "cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin". Differentiation 34 (1): 68–78. doi:10.1111/j.1432-0436.1987.tb00052.x. PMID 3038643. 
  4. ^ a b Brown, M J; Hallam J A, Liu Y, Yamada K M, Shaw S (July 2001). "Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin". J. Immunol. (United States) 167 (2): 641–5. ISSN 0022-1767. PMID 11441066. 
  5. ^ 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. 
  6. ^ a b McMahon, L W; Sangerman J, Goodman S R, Kumaresan K, Lambert M W (June 2001). "Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links". Biochemistry (United States) 40 (24): 7025–34. doi:10.1021/bi002917g. ISSN 0006-2960. PMID 11401546. 
  7. ^ a b McMahon, L W; Walsh C E, Lambert M W (November 1999). "Human alpha spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex". J. Biol. Chem. (UNITED STATES) 274 (46): 32904–8. doi:10.1074/jbc.274.46.32904. ISSN 0021-9258. PMID 10551855. 
  8. ^ Sridharan, Deepa; Brown Monique, Lambert W Clark, McMahon Laura W, Lambert Muriel W (March 2003). "Nonerythroid alphaII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links". J. Cell. Sci. (England) 116 (Pt 5): 823–35. doi:10.1242/jcs.00294. ISSN 0021-9533. PMID 12571280. 
  9. ^ Herrmann, H; Wiche G (January 1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin". J. Biol. Chem. (UNITED STATES) 262 (3): 1320–5. ISSN 0021-9258. PMID 3027087. 
  10. ^ Hirai, H; Matsuda S (September 1999). "Interaction of the C-terminal domain of delta glutamate receptor with spectrin in the dendritic spines of cultured Purkinje cells". Neurosci. Res. (IRELAND) 34 (4): 281–7. doi:10.1016/S0168-0102(99)00061-9. ISSN 0168-0102. PMID 10576550. 
  11. ^ Ziemnicka-Kotula, D; Xu J, Gu H, Potempska A, Kim K S, Jenkins E C, Trenkner E, Kotula L (May 1998). "Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton". J. Biol. Chem. (UNITED STATES) 273 (22): 13681–92. doi:10.1074/jbc.273.22.13681. ISSN 0021-9258. PMID 9593709. 

Further reading[edit]

  • Chow CW (1999). "Regulation and intracellular localization of the epithelial isoforms of the Na+/H+ exchangers NHE2 and NHE3.". Clinical and investigative medicine. Médecine clinique et experimentale 22 (5): 195–206. PMID 10579058. 
  • Hayashi Y, Arakaki R, Ishimaru N (2003). "The role of caspase cascade on the development of primary Sjögren's syndrome.". J. Med. Invest. 50 (1-2): 32–8. PMID 12630566. 
  • Bennett V (1979). "Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues.". Nature 281 (5732): 597–9. doi:10.1038/281597a0. PMID 492324. 
  • Frappier T, Stetzkowski-Marden F, Pradel LA (1991). "Interaction domains of neurofilament light chain and brain spectrin.". Biochem. J. 275. ( Pt 2): 521–7. PMC 1150082. PMID 1902666. 
  • Bennett AF, Hayes NV, Baines AJ (1991). "Site specificity in the interactions of synapsin 1 with tubulin.". Biochem. J. 276. ( Pt 3): 793–9. PMC 1151074. PMID 1905928. 
  • Davis LH, Bennett V (1990). "Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin.". J. Biol. Chem. 265 (18): 10589–96. PMID 2141335. 
  • Moon RT, McMahon AP (1990). "Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin.". J. Biol. Chem. 265 (8): 4427–33. PMID 2307671. 
  • Langley RC, Cohen CM (1986). "Association of spectrin with desmin intermediate filaments.". J. Cell. Biochem. 30 (2): 101–9. doi:10.1002/jcb.240300202. PMID 2939097. 
  • Cianci CD, Giorgi M, Morrow JS (1988). "Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3.". J. Cell. Biochem. 37 (3): 301–15. doi:10.1002/jcb.240370305. PMID 2970468. 
  • Steiner JP, Bennett V (1988). "Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin.". J. Biol. Chem. 263 (28): 14417–25. PMID 2971657. 
  • Herrmann H, Wiche G (1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin.". J. Biol. Chem. 262 (3): 1320–5. PMID 3027087. 
  • McMahon AP, Giebelhaus DH, Champion JE, et al. (1987). "cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin.". Differentiation 34 (1): 68–78. doi:10.1111/j.1432-0436.1987.tb00052.x. PMID 3038643. 
  • Frappier T, Regnouf F, Pradel LA (1988). "Binding of brain spectrin to the 70-kDa neurofilament subunit protein.". Eur. J. Biochem. 169 (3): 651–7. doi:10.1111/j.1432-1033.1987.tb13657.x. PMID 3121319. 
  • McMahon AP, Moon RT (1988). "Structure and evolution of a non-erythroid spectrin, human alpha-fodrin.". Biochem. Soc. Trans. 15 (5): 804–7. PMID 3691949. 
  • Lundberg S, Björk J, Löfvenberg L, Backman L (1995). "Cloning, expression and characterization of two putative calcium-binding sites in human non-erythroid alpha-spectrin.". Eur. J. Biochem. 230 (2): 658–65. doi:10.1111/j.1432-1033.1995.0658h.x. PMID 7607240. 
  • Hughes CA, Bennett V (1995). "Adducin: a physical model with implications for function in assembly of spectrin-actin complexes.". J. Biol. Chem. 270 (32): 18990–6. doi:10.1074/jbc.270.32.18990. PMID 7642559. 
  • Gregorio CC, Repasky EA, Fowler VM, Black JD (1994). "Dynamic properties of ankyrin in T lymphocytes: colocalization with spectrin and protein kinase C beta.". J. Cell Biol. 125 (2): 345–58. doi:10.1083/jcb.125.2.345. PMC 2120020. PMID 8163551. 
  • Li X, Bennett V (1996). "Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes.". J. Biol. Chem. 271 (26): 15695–702. doi:10.1074/jbc.271.26.15695. PMID 8663089. 
  • Stabach PR, Cianci CD, Glantz SB, et al. (1997). "Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility.". Biochemistry 36 (1): 57–65. doi:10.1021/bi962034i. PMID 8993318. 



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