UniProt Accession

 LSM6_HUMAN; P62312; Q4W5J5; Q9Y4Y8 

Genbank Protein ID

 AJ238098; AF182292; AK312126; AC097372; CH471056; CH471056; CH471056; BC016026 

Genbank Nucleotide ID

 CAB45869.1; AAD56230.1; BAG35062.1; AAY41032.1; EAX05029.1; EAX05030.1; EAX05031.1; AAH16026.1 

Protein Name

 U6 snRNA-associated Sm-like protein LSm6 

Protein Synonyms/Alias

  

Gene Name

 LSM6 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
13	QTPSDFLKQIIGRPV	ubiquitination	[1, 2]
23	IGRPVVVKLNSGVDY	ubiquitination	[1, 2]
59	VNGQLKNKYGDAFIR	acetylation	[3, 4]
59	VNGQLKNKYGDAFIR	ubiquitination	[5]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] 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 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 

Functional Description

 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, spliceosomal 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). 

Sequence Annotation

 MOD_RES 59 59 N6-acetyllysine.  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing; Spliceosome; tRNA processing. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 80 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:UniProtKB.
 GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; TAS:UniProtKB.
 GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
 GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. 

Interpro

 IPR010920; LSM_dom.
 IPR001163; Ribonucl_LSM.
 IPR006649; Ribonucl_LSM_euk/arc. 

Pfam

 PF01423; LSM 

SMART

 SM00651; Sm 

PROSITE

  

PRINTS