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Gene Review

SYNCRIP  -  synaptotagmin binding, cytoplasmic RNA...

Homo sapiens

Synonyms: GRY-RBP, GRYRBP, Glycine-and tyrosine-rich RNA-binding protein, HNRNPQ, HNRPQ, ...
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Disease relevance of SYNCRIP

  • As further evidence of the role of GRY-RBP, rat hepatoma cells treated with an antisense oligonucleotide to GRY-RBP demonstrated an increase in C to U editing of endogenous apoB RNA [1].
  • Together, these data indicate that NSAP1 modulates IRES-dependent translation of BiP mRNA through an RNA-protein interaction under heat stress conditions [2].
  • Chronic pain following whiplash injury and non-specific arm pain (NSAP, previously termed diffuse repetitive strain injury) present clinicians with problems of diagnosis and management [3].
  • BACKGROUND: Abdominal pain of uncertain aetiology (non-specific abdominal pain; NSAP) is the commonest reason for emergency surgical admission [4].
  • Post-streptococcal glomerulonephritis: studies on the interaction between nephritis strain-associated protein (NSAP), complement and the glomerulus [5].

High impact information on SYNCRIP

  • BiP mRNAs were redistributed from the heavy polysome to the light polysome in NSAP1 knockdown cells [2].
  • The amount of NSAP1 bound to the BiP IRES increased under heat stress conditions, and the IRES activity of BiP mRNA was increased [2].
  • Here we show that a cellular protein, NS1-associated protein 1 (NSAP1), augments HCV mRNA translation through a specific interaction with an adenosine-rich protein-coding region within the HCV mRNA [6].
  • An HCV replicon RNA capable of mimicking the HCV proliferation process in host cells was further used to confirm that NSAP1 enhances the translation of HCV mRNA [6].
  • An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites [7].

Biological context of SYNCRIP

  • Experiments using recombinant proteins demonstrate that GRY-RBP binds to ACF and inhibits both the binding of ACF to apoB RNA and C to U RNA editing [1].
  • By yeast two-hybrid cloning using apobec-1 as bait we identified a 69.6-kDa RNA binding protein, GRY-RBP, that contains 3 RNA-recognition motifs (RRMs) as a novel apobec-1 associating protein [8].
  • These results raise the possibility that regulation of mRNA translation or stability by insulin may involve the phosphorylation of SYNCRIP [9].
  • The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization [10].

Anatomical context of SYNCRIP

  • In vitro phosphorylation studies revealed that SYNCRIP, once extracted from low density microsomes, can be tyrosine phosphorylated using purified insulin receptor [9].
  • Furthermore, the interaction between SYNCRIP and Syt-VII, -VIII, or -IX was revealed by co-immunoprecipitation experiments using COS cells transiently expressing each Syt isoform [11].
  • Hence, we propose that pp70 and pp68 likely represent B cell homologs of SLP-76 which facilitate and coordinate B cell activation [12].
  • A two-hybrid screen identified a HeLa cell cDNA clone (NS1-associated protein 1 [NSAP1]) that interacts with NS11-276 and NS11-638 [13].
  • Short interfering RNA-mediated gene-specific knockdown of CUGBP2, GRY-RBP, and hnRNP-C1 resulted in increased editing in Caco-2 cells, consistent with their known inhibitory function [14].

Associations of SYNCRIP with chemical compounds

  • However, the induction was not inhibited by HA-1004 and H-8, relatively high-affinity inhibitors of protein kinase A. Phorbol myristate acetate and 1-oleoyl-2-acetyl-sn-glycerol, activators of protein kinase C, were able to induce pp68 in mouse peritoneal macrophages [15].
  • The fimbria-induced pp68 was inhibited dramatically by staurosporine, a potent inhibitor of protein kinase C. pp68 induction was also inhibited by H-7, a potent inhibitor of several types of protein kinase [15].

Physical interactions of SYNCRIP


Other interactions of SYNCRIP

  • ACF and GRY-RBP colocalize in the nucleus of transfected cells and, in cotransfection experiments with apobec-1, each appears to colocalize in a predominantly nuclear distribution [1].
  • Of relevance, cells transfected with RETMEN2B examined for anti-phosphotyrosine bound proteins, showed other proteins implicated in splicing: DEAD-box p68 RNA helicase, SYNCRIP, and hnRNP K [16].
  • Several well known components of FGFR-1 signaling were identified along with two novel candidates: NS-1-associated protein-1 and target of Myb 1-like protein [17].

Analytical, diagnostic and therapeutic context of SYNCRIP

  • In this present study we have identified, by MALDI mass spectrometry, pp68 as the tyrosine-phosphorylated form of synaptotagmin-binding cytoplasmic RNA-interacting protein (SYNCRIP)/NSAP1, a newly discovered cytoplasmic RNA-binding protein [9].
  • The aim of this study was to examine the role of early laparoscopy in the management of NSAP [4].
  • In this way we performed gasless laparoscopic surgery on 54 patients: cholecystectomy (n = 37), abdominal exploration for NSAP (n = 5) or tumor staging (n = 4), fenestration of liver cysts (n = 5), and appendectomy (n = 3) [18].
  • Of the 49 patients with SAP, 39 developed pancreatic or peripancreatic NSAP were reactive to skin tests on the third week, while 4% remained anergic necrosis and were operated [19].
  • SDS-PAGE and double immunodiffusion analysis showed that no NSAP occurred in the extracellular product of S. pyogenes strain Su [20].


  1. Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing. Blanc, V., Navaratnam, N., Henderson, J.O., Anant, S., Kennedy, S., Jarmuz, A., Scott, J., Davidson, N.O. J. Biol. Chem. (2001) [Pubmed]
  2. BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1. Cho, S., Park, S.M., Kim, T.D., Kim, J.H., Kim, K.T., Jang, S.K. Mol. Cell. Biol. (2007) [Pubmed]
  3. In vivo study of nerve movement and mechanosensitivity of the median nerve in whiplash and non-specific arm pain patients. Greening, J., Dilley, A., Lynn, B. Pain (2005) [Pubmed]
  4. Randomized clinical trial of early laparoscopy in the management of acute non-specific abdominal pain. Decadt, B., Sussman, L., Lewis, M.P., Secker, A., Cohen, L., Rogers, C., Patel, A., Rhodes, M. The British journal of surgery. (1999) [Pubmed]
  5. Post-streptococcal glomerulonephritis: studies on the interaction between nephritis strain-associated protein (NSAP), complement and the glomerulus. Peake, P.W., Pussell, B.A., Karplus, T.E., Riley, E.H., Charlesworth, J.A. APMIS (1991) [Pubmed]
  6. A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon. Kim, J.H., Paek, K.Y., Ha, S.H., Cho, S., Choi, K., Kim, C.S., Ryu, S.H., Jang, S.K. Mol. Cell. Biol. (2004) [Pubmed]
  7. An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites. Bannai, H., Fukatsu, K., Mizutani, A., Natsume, T., Iemura, S., Ikegami, T., Inoue, T., Mikoshiba, K. J. Biol. Chem. (2004) [Pubmed]
  8. Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome. Lau, P.P., Chang, B.H., Chan, L. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  9. Identification of pp68 as the Tyrosine-phosphorylated Form of SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein. Hresko, R.C., Mueckler, M. J. Biol. Chem. (2002) [Pubmed]
  10. The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization. Passos, D.O., Quaresma, A.J., Kobarg, J. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  11. SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms. Mizutani, A., Fukuda, M., Ibata, K., Shiraishi, Y., Mikoshiba, K. J. Biol. Chem. (2000) [Pubmed]
  12. Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation. Fu, C., Chan, A.C. J. Biol. Chem. (1997) [Pubmed]
  13. A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice. Harris, C.E., Boden, R.A., Astell, C.R. J. Virol. (1999) [Pubmed]
  14. ApoB mRNA editing is mediated by a coordinated modulation of multiple apoB mRNA editing enzyme components. Chen, Z., Eggerman, T.L., Patterson, A.P. Am. J. Physiol. Gastrointest. Liver Physiol. (2007) [Pubmed]
  15. Porphyromonas gingivalis fimbriae induce a 68-kilodalton phosphorylated protein in macrophages. Murakami, Y., Hanazawa, S., Watanabe, A., Naganuma, K., Iwasaka, H., Kawakami, K., Kitano, S. Infect. Immun. (1994) [Pubmed]
  16. RET oncoproteins induce tyrosine phosphorylation changes of proteins involved in RNA metabolism. Gorla, L., Cant??, M., Miccich??, F., Patelli, C., Mondellini, P., Pierotti, M.A., Bongarzone, I. Cell. Signal. (2006) [Pubmed]
  17. Signaling initiated by overexpression of the fibroblast growth factor receptor-1 investigated by mass spectrometry. Hinsby, A.M., Olsen, J.V., Bennett, K.L., Mann, M. Mol. Cell Proteomics (2003) [Pubmed]
  18. Gasless laparoscopy in abdominal surgery. Paolucci, V., Gutt, C.N., Schaeff, B., Encke, A. Surgical endoscopy. (1995) [Pubmed]
  19. The anergic state as a predictor of pancreatic sepsis. García-Sabrido, J.L., Valdecantos, E., Bastida, E., Tellado, J.M. Zentralblatt für Chirurgie. (1989) [Pubmed]
  20. Absence of nephritis strain-associated protein (NSAP) in the extracellular product of Streptococcus pyogenes strain Su. Ohkuni, H., Todome, Y., Yamamoto, A., Usami, H., Tada, S., Yokomuro, K., Sugawara, Y. Journal of clinical & laboratory immunology. (1987) [Pubmed]
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