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U7 snRNA-associated Sm-like protein LSm11

Known abbreviations: LSM11


Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing By similarity. Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases. Binds specifically to the Sm-binding site of U7 snRNA. 
Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Formation of the U7 snRNP is an ATP-dependent process mediated by a specialized SMN complex containing at least the Sm protein core complex and additionally, the U7-specific LSM10 and LSM11 proteins. Interacts with LSM10, SMN, SNRPB and ZNF473. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 By similarity. Interacts (via the Sm domains) with CLNS1A. Interacts with PRMT5 and WDR77 By similarity. 
The C-terminal SM 1 domain is both necessary for the binding to the Sm-binding site of U7 snRNA and U7 snRNP assembly (By similarity.) The N-terminal domain is essential for histone pre-mRNA cleavage. Amino acids 63-82 are sufficient to interact with ZNF473.
Not methylated (By similarity.)

This protein can be a part of a given complexes: Activities in which U7 snRNA-associated Sm-like protein LSm11 is involved: Pathways in which U7 snRNA-associated Sm-like protein LSm11 is involved:

NCBI GI number(s): 27735089
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P83369 P83369
KEGG hsa:134353 hsa:134353
PFAM: PF01423
InterPro: IPR010920
CATH: - -
SCOP: - -

Protein sequence:

U7 snRNA-associated Sm-like protein LSm11 (Homo sapiens) is product of expression of LSM11 gene.


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
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing. Pillai RS, Grimmler M, Meister G, Will CL, Luhrmann R, Fischer U, Schumperli D Genes Dev 2003-09-15 (17) 12975319
Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein. Pillai RS, Will CL, Luhrmann R, Schumperli D, Muller B EMBO J 2001-10-01 (20) 11574479
ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S phase. Wagner EJ, Marzluff WF Mol Cell Biol 2006-09-01 (26) 16914750
Conserved zinc fingers mediate multiple functions of ZFP100, a U7snRNP associated protein. Wagner EJ, Ospina JK, Hu Y, Dundr M, Matera AG, Marzluff WF RNA 2006-07-01 (12) 16714279

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

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