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P62310 (LSM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
U6 snRNA-associated Sm-like protein LSm3
Gene names
Name:LSM3
ORF Names:MDS017
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length102 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds specifically to the 3'-terminal U-tract of U6 snRNA.

Subunit structure

LSm subunits form a heteromer with a doughnut shape. Identified in the spliceosome C complex. Ref.7

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the snRNP Sm proteins family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 102101U6 snRNA-associated Sm-like protein LSm3
PRO_0000125560

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.10

Sequences

Sequence LengthMass (Da)Tools
P62310 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 206B0DF0D95CD4D2

FASTA10211,845
        10         20         30         40         50         60 
MADDVDQQQT TNTVEEPLDL IRLSLDERIY VKMRNDRELR GRLHAYDQHL NMILGDVEET 

        70         80         90        100 
VTTIEIDEET YEEIYKSTKR NIPMLFVRGD GVVLVAPPLR VG 

« Hide

References

« Hide 'large scale' references
[1]"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. 18:3451-3462(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal liver and Spleen.
[2]"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., Luehrmann R.
EMBO J. 18:5789-5802(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hematopoietic stem cell.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[7]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ238095 mRNA. Translation: CAB45866.1.
AF182289 mRNA. Translation: AAD56227.1.
AF182418 mRNA. Translation: AAG14954.1.
CR457185 mRNA. Translation: CAG33466.1.
CH471055 Genomic DNA. Translation: EAW64190.1.
BC007055 mRNA. Translation: AAH07055.1.
RefSeqNP_055278.1. NM_014463.2.
UniGeneHs.111632.

3D structure databases

ProteinModelPortalP62310.
SMRP62310. Positions 16-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118105. 32 interactions.
DIPDIP-31218N.
IntActP62310. 26 interactions.
MINTMINT-1036960.
STRING9606.ENSP00000302160.

PTM databases

PhosphoSiteP62310.

Polymorphism databases

DMDM61227725.

Proteomic databases

PaxDbP62310.
PeptideAtlasP62310.
PRIDEP62310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306024; ENSP00000302160; ENSG00000170860.
GeneID27258.
KEGGhsa:27258.
UCSCuc003byn.3. human.

Organism-specific databases

CTD27258.
GeneCardsGC03P014219.
HGNCHGNC:17874. LSM3.
HPAHPA044966.
MIM607283. gene.
neXtProtNX_P62310.
PharmGKBPA134881991.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236203.
HOGENOMHOG000223550.
HOVERGENHBG052368.
InParanoidP62310.
KOK12622.
OMAGYDSHCN.
OrthoDBEOG76HQ4Q.
PhylomeDBP62310.
TreeFamTF312907.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP62310.
CleanExHS_LSM3.
GenevestigatorP62310.

Family and domain databases

InterProIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PfamPF01423. LSM. 1 hit.
[Graphical view]
SMARTSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMSSF50182. SSF50182. 1 hit.
ProtoNetSearch...

Other

ChiTaRSLSM3. human.
GeneWikiLSM3.
GenomeRNAi27258.
NextBio50206.
PROP62310.
SOURCESearch...

Entry information

Entry nameLSM3_HUMAN
AccessionPrimary (citable) accession number: P62310
Secondary accession number(s): Q6IAH0, Q9Y4Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM