Symplekin (SYMPK)

SPK; SYM

SPN	T975
HGNC	22935
MGI	1915438
PubMed	8769423
RGD	1306735
UniProt	Q92797
Wiki	SYMPK

Symplekin is 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.

The protein also localizes to the cytoplasmic plaques of tight junctions in some cell types.In testis, expressed in polar epithelia and Sertoli cells but not in vascular endothelia. The protein is detected in stomach, duodenum, pancreas, liver, fetal brain, carcinomas, lens-forming cells, fibroblasts, lymphocytes, lymphoma cells, erythroleukemia cells but not in endothelium of vessels, epidermis, intercalated disks, Purkinje fiber cells of the heart and lymph node.

Reference

"Six transcripts map within 200 kilobases of the myotonic dystrophy expanded repeat."
Mamm. Genome 9:485-487(1998) [PubMed] [Europe PMC] [Abstract]

"Chromosomal localization to 19q13.3, partial genomic structure and 5' cDNA sequence of the human symplekin gene."
Somat. Cell Mol. Genet. 23:229-231(1997) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Symplekin, a novel type of tight junction plaque protein."
J. Cell Biol. 134:1003-1018(1996) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"Complex protein interactions within the human polyadenylation machinery identify a novel component."
Mol. Cell. Biol. 20:1515-1525(2000) [PubMed] [Europe PMC] [Abstract]

"Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes."
Mol. Biol. Cell 13:1665-1676(2002) [PubMed] [Europe PMC] [Abstract]

"HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin."
J. Biol. Chem. 279:10551-10555(2004) [PubMed] [Europe PMC] [Abstract]

"Symplekin and multiple other polyadenylation factors participate in 3'-end maturation of histone mRNAs."
Genes Dev. 19:2583-2592(2005) [PubMed] [Europe PMC] [Abstract]

"Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation."
EMBO Rep. 9:1013-1018(2008) [PubMed] [Europe PMC] [Abstract]

"A quantitative atlas of mitotic phosphorylation."
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex."
Nature 467:729-733(2010) [PubMed] [Europe PMC] [Abstract]

"An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72."
Genes Dev. 26:2265-2270(2012) [PubMed] [Europe PMC] [Abstract]