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U6 snRNA-associated Sm-like protein LSm6

 
Known abbreviations: LSM6

 

FUNCTION:
 
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity.)
 
SUBUNIT STRUCTURE:
 
Component of the heptameric LSM1-LSM7 complex, which consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component of the heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. The LSm subunits form a seven-membered ring structure with a doughnut shape.
 
CELLULAR LOCALIZATION:
 
Cytoplasm. Nucleus (By similarity)



This protein can be a part of a given complexes: Activities in which U6 snRNA-associated Sm-like protein LSm6 is involved: Pathways in which U6 snRNA-associated Sm-like protein LSm6 is involved:

NCBI GI number(s): 5901998
154426303
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P62312 P62312
BRENDA - -
KEGG hsa:11157 hsa:11157
PFAM: PF01423
PF01423
InterPro: IPR010920
IPR001163
IPR006649
IPR010920
IPR001163
IPR006649
CATH: - -
SCOP: - -


Protein sequence:
MSLRKQTPSDFLKQIIGRPVVVKLNSGVDYRGVLACLDGYMNIALEQTEE
YVNGQLKNKYGDAFIRGNNVLYISTQKRRM

U6 snRNA-associated Sm-like protein LSm6 (Homo sapiens) is product of expression of LSM6 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. Salgado-Garrido J, Bragado-Nilsson E, Kandels-Lewis S, Seraphin B EMBO J 1999-06-15 (18) 10369684
A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. Achsel T, Brahms H, Kastner B, Bachi A, Wilm M, Luhrmann R EMBO J 1999-10-15 (18) 10523320
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science 2009-08-14 (325) 19608861
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T RNA 2002-12-01 (8) 12515382



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Last modification of this entry: Sept. 25, 2012.

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