SYNE2

SYNE2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSYNE2, EDMD5, NUA, NUANCE, Nesp2, Nesprin-2, SYNE-2, TROPH, spectrin repeat containing nuclear envelope protein 2, KASH2
External IDsMGI: 2449316 HomoloGene: 56700 GeneCards: SYNE2
Gene location (Human)
Chr.Chromosome 14 (human)[1]
Band14q23.2Start63,852,983 bp[1]
End64,226,433 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

23224

319565

Ensembl

ENSG00000054654

ENSMUSG00000063450

UniProt

Q8WXH0

Q6ZWQ0

RefSeq (mRNA)

NM_015180
NM_182910
NM_182912
NM_182913
NM_182914

NM_001005510

RefSeq (protein)

NP_055995
NP_878914
NP_878917
NP_878918

NP_001005510

Location (UCSC)Chr 14: 63.85 – 64.23 MbChr 12: 75.82 – 76.11 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Nesprin-2 is a protein that in humans is encoded by the SYNE2 gene.[5][6][7] The human SYNE2 gene consists of 116 exons and encodes nesprin-2, a member of the nuclear envelope (NE) spectrin-repeat (nesprin) family. Nesprins are modular proteins with a central extended spectrin-repeat (SR) rod domain and a C-terminal Klarsicht/ANC-1/Syne homology (KASH) transmembrane domain, which acts as a NE-targeting motif. Nesprin-2 (Nesp2) binds to cytoplasmic F-actin, tethering the nucleus to the cytoskeleton and maintaining the structural integrity of the nucleus.

The human SYNE2 gene encodes a protein of 6,885 amino acids (isoform 1, Nesp2 giant); alternative mRNA splicing produces transcripts encoding a larger isoform and numerous smaller isoforms, some of which are specific to various tissues; alternative start and termination sites within the mRNA also allow translation of smaller isoforms, many possessing unique N- or C-terminal sequences encoded by retained introns. Two mechanisms create splice variants of nesprin-2 with the KASH domain deleted (deltaKASH). In deltaKASH1 variants, deletion of cassette exons 111-112 results in a frame shift that disrupts the KASH domain but retains the 3' untranslated region (UTR) in exon 116 utilized for isoforms containing the KASH domain. This mechanism, which also occurs in SYNE1 mRNA encoding nesprin-1 (enaptin), generates deltaKASH1 isoforms terminating with a distinct 11-amino acid tail (GIAGHSATPPA replacing YPMLRYTNGPPPT in isoforms with KASH). Utilization of an alternative stop codon in exon 115, which is followed by a distinct 3' UTR, generates deltaKASH2 variants. This mechanism truncates larger isoforms without generating a distinct C-terminal sequence. Expression of deltaKASH1 variants occurs largely in brain and kidney, with smaller amounts in heart; deltaKASH2 variants are detected in heart and spleen.[8]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000054654 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000063450 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Jul 1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
  6. ↑ Apel ED, Lewis RM, Grady RM, Sanes JR (Nov 2000). "Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction". J Biol Chem. 275 (41): 31986–95. doi:10.1074/jbc.M004775200. PMID 10878022.
  7. ↑ "Entrez Gene: SYNE2 spectrin repeat containing, nuclear envelope 2".
  8. ↑ Rajgor D, Mellad JA, Autore F, Zhang Q, Shanahan CM (Jul 2012). "Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds". PLOS ONE. 7 (7): e40098. doi:10.1371/journal.pone.0040098. PMC 3388047. PMID 22768332.

Further reading

  • Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Zhang Q, Skepper JN, Yang F, et al. (2002). "Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues". J. Cell Sci. 114 (Pt 24): 4485–98. PMID 11792814.
  • Zhen YY, Libotte T, Munck M, et al. (2003). "NUANCE, a giant protein connecting the nucleus and actin cytoskeleton". J. Cell Sci. 115 (Pt 15): 3207–22. PMID 12118075.
  • Zhang Q, Ragnauth C, Greener MJ, et al. (2003). "The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300". Genomics. 80 (5): 473–81. doi:10.1016/S0888-7543(02)96859-X. PMID 12408964.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Heilig R, Eckenberg R, Petit JL, et al. (2003). "The DNA sequence and analysis of human chromosome 14". Nature. 421 (6923): 601–7. doi:10.1038/nature01348. PMID 12508121.
  • Schirmer EC, Florens L, Guan T, et al. (2003). "Nuclear membrane proteins with potential disease links found by subtractive proteomics". Science. 301 (5638): 1380–2. doi:10.1126/science.1088176. PMID 12958361.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Zhang Q, Ragnauth CD, Skepper JN, et al. (2005). "Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle". J. Cell Sci. 118 (Pt 4): 673–87. doi:10.1242/jcs.01642. PMID 15671068.
  • Cheng J, Kapranov P, Drenkow J, et al. (2005). "Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution". Science. 308 (5725): 1149–54. doi:10.1126/science.1108625. PMID 15790807.
  • Libotte T, Zaim H, Abraham S, et al. (2005). "Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope". Mol. Biol. Cell. 16 (7): 3411–24. doi:10.1091/mbc.E04-11-1009. PMC 1165422. PMID 15843432.
  • Padmakumar VC, Libotte T, Lu W, et al. (2005). "The inner nuclear membrane protein Sun1 mediates the anchorage of Nesprin-2 to the nuclear envelope". J. Cell Sci. 118 (Pt 15): 3419–30. doi:10.1242/jcs.02471. PMID 16079285.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
  • Wheeler MA, Davies JD, Zhang Q, et al. (2007). "Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophy". Exp. Cell Res. 313 (13): 2845–57. doi:10.1016/j.yexcr.2007.03.025. PMID 17462627.


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