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Protein Page:
LSM2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
LSM2 Binds specifically to the 3'-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing. Identified in the spliceosome C complex. LSm subunits form a heteromer with a doughnut shape. Belongs to the snRNP Sm proteins family. Note: This description may include information from UniProtKB.
Protein type: RNA splicing; RNA binding protein; Spliceosome
Cellular Component: nucleoplasm; cytosol
Molecular Function: protein binding; protein kinase binding; U6 snRNA binding
Biological Process: nuclear mRNA splicing, via spliceosome; RNA metabolic process; RNA splicing; gene expression; mRNA metabolic process; mRNA catabolic process, deadenylation-dependent decay
Reference #:  Q9Y333 (UniProtKB)
Alt. Names/Synonyms: C6orf28; G7B; LSM2; LSM2 homolog, U6 small nuclear RNA associated (S. cerevisiae); Protein G7b; Small nuclear ribonuclear protein D homolog; snRNP; snRNP core Sm-like protein Sm-x5; U6 snRNA-associated Sm-like protein LSm2; YBL026W
Gene Symbols: LSM2
Molecular weight: 10,835 Da
Basal Isoelectric point: 6.05  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

LSM2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 8 Y4-p ____MLFysFFkSLV
0 2 S5-p ___MLFysFFkSLVG
0 1 K8-ub MLFysFFkSLVGKDV
0 6 Y35-p TLHSVDQyLNIKLTD
0 1 S44-p NIKLTDIsVTDPEKy
0 3 Y51-p sVTDPEKyPHMLSVK
0 2 S65-p KNCFIRGsVVRYVQL
0 1 T79-p LPADEVDtQLLQDAA
0 1 K88-ub LLQDAARkEALQQkQ
0 1 K94-ub RkEALQQkQ______
  mouse

 
Y4 ____MLFYSFFKSLV
S5 ___MLFYSFFKSLVG
K8 MLFYSFFKSLVGKDV
Y35-p TLHSVDQyLNIKLTD
S44 NIKLTDISVTDPEKY
Y51 SVTDPEKYPHMLSVK
S65-p KNCFIRGsVVRYVQL
T79 LPADEVDTQLLQDAA
K88 LLQDAARKEALQQKQ
K94 RKEALQQKQ______
  rat

 
Y40 QDFVRLFYSFFKSLV
S41 DFVRLFYSFFKSLVG
K44 RLFYSFFKSLVGKDV
Y71 TLHSVDQYLNIKLTD
S80 NIKLTDISVTDPEKY
Y87 SVTDPEKYPHMLSVK
S101 KNCFIRGSVVRYVQL
T115 LPADEVDTQLLQDAA
K124 LLQDAARKEALQQKQ
K130 RKEALQQKQ______
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