SYMPK

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Symplekin is a protein that in humans is encoded by the SYMPK gene.

Function

This gene encodes a nuclear protein that functions in the regulation of polyadenylation and promotes gene expression. The protein forms a high-molecular weight complex with components of the polyadenylation machinery. It is thought to serve as a scaffold for recruiting regulatory factors to the polyadenylation complex. It also participates in 3'-end maturation of histone mRNAs, which do not undergo polyadenylation. The protein also localizes to the cytoplasmic plaques of tight junctions in some cell types.

Model organisms

Sympk knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Plasma immunoglobulins	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Brain histopathology	Normal
Salmonella infection	Normal
Citrobacter infection	Normal
All tests and analysis from

Model organisms have been used in the study of SYMPK function. A conditional knockout mouse line, called Sympk^{tm1a(EUCOMM)Wtsi} was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice and two significant abnormalities were observed. No homozygous mutant embryos were identified during gestation, and thus none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.

Interactions

SYMPK has been shown to interact with CSTF2 and HSF1.

Further reading

• Keon BH, Schäfer S, Kuhn C, Grund C, Franke WW (Aug 1996). "Symplekin, a novel type of tight junction plaque protein". The Journal of Cell Biology. 134 (4): 1003–18. doi:10.1083/jcb.134.4.1003. PMC 2120966. PMID 8769423.
• Alwazzan M, Hamshere MG, Lennon GG, Brook JD (Jun 1998). "Six transcripts map within 200 kilobases of the myotonic dystrophy expanded repeat". Mammalian Genome. 9 (6): 485–7. doi:10.1007/s003359900804. PMID 9585442.
• Faber PW, Barnes GT, Srinidhi J, Chen J, Gusella JF, MacDonald ME (Sep 1998). "Huntingtin interacts with a family of WW domain proteins". Human Molecular Genetics. 7 (9): 1463–74. doi:10.1093/hmg/7.9.1463. PMID 9700202.
• Paffenholz R, Kuhn C, Grund C, Stehr S, Franke WW (Aug 1999). "The arm-repeat protein NPRAP (neurojungin) is a constituent of the plaques of the outer limiting zone in the retina, defining a novel type of adhering junction". Experimental Cell Research. 250 (2): 452–64. doi:10.1006/excr.1999.4534. PMID 10413599.
• Takagaki Y, Manley JL (Mar 2000). "Complex protein interactions within the human polyadenylation machinery identify a novel component". Molecular and Cellular Biology. 20 (5): 1515–25. doi:10.1128/MCB.20.5.1515-1525.2000. PMC 85326. PMID 10669729.
• Langbein L, Pape UF, Grund C, Kuhn C, Praetzel S, Moll I, Moll R, Franke WW (Aug 2003). "Tight junction-related structures in the absence of a lumen: occludin, claudins and tight junction plaque proteins in densely packed cell formations of stratified epithelia and squamous cell carcinomas". European Journal of Cell Biology. 82 (8): 385–400. doi:10.1078/0171-9335-00330. PMID 14533737.
• Xing H, Mayhew CN, Cullen KE, Park-Sarge OK, Sarge KD (Mar 2004). "HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin". The Journal of Biological Chemistry. 279 (11): 10551–5. doi:10.1074/jbc.M311719200. PMID 14707147.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Barnard DC, Ryan K, Manley JL, Richter JD (Nov 2004). "Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation". Cell. 119 (5): 641–51. doi:10.1016/j.cell.2004.10.029. PMID 15550246.
• Kolev NG, Steitz JA (Nov 2005). "Symplekin and multiple other polyadenylation factors participate in 3'-end maturation of histone mRNAs". Genes & Development. 19 (21): 2583–92. doi:10.1101/gad.1371105. PMC 1276732. PMID 16230528.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Kavanagh E, Buchert M, Tsapara A, Choquet A, Balda MS, Hollande F, Matter K (Dec 2006). "Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin". Journal of Cell Science. 119 (Pt 24): 5098–105. doi:10.1242/jcs.03297. PMID 17158914.