SYMPK

SYMPK
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3O2Q, 3O2S, 3O2T, 3ODR, 3ODS, 4H3H, 4H3K
Identifiers
Aliases	SYMPK , SPK, SYM, symplekin, Pta1, symplekin scaffold protein
External IDs	OMIM: 602388; MGI: 1915438; HomoloGene: 37969; GeneCards: SYMPK; OMA:SYMPK - orthologs
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19q13.32 Start 45,815,410 bp [1] End 45,863,194 bp [1]
Gene location (Mouse) Chr. Chromosome 7 (mouse) [2] Band 7|7 A3 Start 18,758,302 bp [2] End 18,788,543 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left testis right testis anterior pituitary stromal cell of endometrium right uterine tube granulocyte mucosa of transverse colon sural nerve right lobe of thyroid gland right lobe of liver Top expressed in muscle of thigh tail of embryo ventricular zone superior frontal gyrus internal carotid artery genital tubercle external carotid artery spermatid spermatocyte seminiferous tubule More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component cytoplasm cell junction plasma membrane cytoskeleton membrane nucleus bicellular tight junction nucleoplasm cytosol nuclear stress granule Biological process mRNA polyadenylation mRNA processing cell adhesion positive regulation of protein dephosphorylation mRNA splicing, via spliceosome termination of RNA polymerase II transcription mRNA export from nucleus mRNA 3'-end processing negative regulation of protein binding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8189 68188 Ensembl ENSG00000125755 ENSMUSG00000023118 UniProt Q92797 Q80X82 RefSeq (mRNA) NM_004819 NM_026605 NM_001360713 RefSeq (protein) NP_004810 NP_001347642 NP_080881 Location (UCSC) Chr 19: 45.82 – 45.86 Mb Chr 7: 18.76 – 18.79 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Symplekin is a protein that in humans is encoded by the SYMPK gene. ^{[5] [6]}

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. ^[6]

Interactions

SYMPK has been shown to interact with CSTF2, ^[7] HSF1 ^[8] and Oct4 ^[9]

References

1. GRCh38: Ensembl release 89: ENSG00000125755 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000023118 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ueki K, Ramaswamy S, Billings SJ, Mohrenweiser HW, Louis DN (May 1997). "Chromosomal localization to 19q13.3, partial genomic structure and 5' cDNA sequence of the human symplekin gene". Somatic Cell and Molecular Genetics. 23 (3): 229–31. doi:10.1007/BF02721375. PMID   9330635. S2CID   24956684.
6. "Entrez Gene: SYMPK symplekin".
7. 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.
8. 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.
9. Yu J, Lu W, Ge T, et al., (2019). "Interaction Between Sympk and Oct4 Promotes Mouse Embryonic Stem Cell Proliferation". STEM CELLS;37(6): 743-753 https://doi.org/10.1002/stem.2992

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. S2CID   319161.
• 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. Bibcode:2004PNAS..10112130B. 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. S2CID   8289230.
• 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" (PDF). Journal of Cell Science. 119 (Pt 24): 5098–105. doi: 10.1242/jcs.03297 . PMID   17158914. S2CID   8702837.