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Protein

U6 snRNA-associated Sm-like protein LSm5

Gene

Lsm5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA, thereby facilitating formation of the spliceosomal U4/U6 duplex in vitro (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-430039. mRNA decay by 5' to 3' exoribonuclease.
R-MMU-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
U6 snRNA-associated Sm-like protein LSm5
Gene namesi
Name:Lsm5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1913623. Lsm5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 9190U6 snRNA-associated Sm-like protein LSm5PRO_0000125573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP62322.
MaxQBiP62322.
PaxDbiP62322.
PRIDEiP62322.
TopDownProteomicsiP62322.

PTM databases

iPTMnetiP62322.
PhosphoSiteiP62322.

Expressioni

Gene expression databases

BgeeiP62322.
ExpressionAtlasiP62322. baseline and differential.
GenevisibleiP62322. MM.

Interactioni

Subunit structurei

LSm subunits form a heteromer with a doughnut shape.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211422. 1 interaction.
IntActiP62322. 1 interaction.
STRINGi10090.ENSMUSP00000126565.

Structurei

3D structure databases

ProteinModelPortaliP62322.
SMRiP62322. Positions 12-86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

eggNOGiKOG1775. Eukaryota.
COG1958. LUCA.
GeneTreeiENSGT00390000001455.
HOVERGENiHBG107310.
InParanoidiP62322.
KOiK12624.
OMAiSRIWIAM.
OrthoDBiEOG7NSB4W.
PhylomeDBiP62322.
TreeFamiTF313575.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62322-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANATTNPS QLLPLELVDK CIGSRIHIVM KSDKEIVGTL LGFDDFVNMV
60 70 80 90
LEDVTEFEIT PEGRRITKLD QILLNGNNIT MLVPGGEGPE V
Length:91
Mass (Da):9,937
Last modified:January 23, 2007 - v2
Checksum:i82B5C8830E64C992
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009617 mRNA. Translation: BAB26394.1.
AK011218 mRNA. Translation: BAB27475.1.
BC048459 mRNA. Translation: AAH48459.1.
BC061085 mRNA. Translation: AAH61085.1.
BC132626 mRNA. Translation: AAI32627.1.
BC132628 mRNA. Translation: AAI32629.1.
CCDSiCCDS51788.1.
RefSeqiNP_079796.1. NM_025520.3.
XP_006544600.1. XM_006544537.2.
UniGeneiMm.25642.

Genome annotation databases

EnsembliENSMUST00000170382; ENSMUSP00000126565; ENSMUSG00000091625.
GeneIDi102641341.
66373.
KEGGimmu:102641341.
mmu:66373.
UCSCiuc009cbj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009617 mRNA. Translation: BAB26394.1.
AK011218 mRNA. Translation: BAB27475.1.
BC048459 mRNA. Translation: AAH48459.1.
BC061085 mRNA. Translation: AAH61085.1.
BC132626 mRNA. Translation: AAI32627.1.
BC132628 mRNA. Translation: AAI32629.1.
CCDSiCCDS51788.1.
RefSeqiNP_079796.1. NM_025520.3.
XP_006544600.1. XM_006544537.2.
UniGeneiMm.25642.

3D structure databases

ProteinModelPortaliP62322.
SMRiP62322. Positions 12-86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211422. 1 interaction.
IntActiP62322. 1 interaction.
STRINGi10090.ENSMUSP00000126565.

PTM databases

iPTMnetiP62322.
PhosphoSiteiP62322.

Proteomic databases

EPDiP62322.
MaxQBiP62322.
PaxDbiP62322.
PRIDEiP62322.
TopDownProteomicsiP62322.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000170382; ENSMUSP00000126565; ENSMUSG00000091625.
GeneIDi102641341.
66373.
KEGGimmu:102641341.
mmu:66373.
UCSCiuc009cbj.2. mouse.

Organism-specific databases

CTDi23658.
MGIiMGI:1913623. Lsm5.

Phylogenomic databases

eggNOGiKOG1775. Eukaryota.
COG1958. LUCA.
GeneTreeiENSGT00390000001455.
HOVERGENiHBG107310.
InParanoidiP62322.
KOiK12624.
OMAiSRIWIAM.
OrthoDBiEOG7NSB4W.
PhylomeDBiP62322.
TreeFamiTF313575.

Enzyme and pathway databases

ReactomeiR-MMU-430039. mRNA decay by 5' to 3' exoribonuclease.
R-MMU-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

NextBioi321477.
PROiP62322.
SOURCEiSearch...

Gene expression databases

BgeeiP62322.
ExpressionAtlasiP62322. baseline and differential.
GenevisibleiP62322. MM.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Tongue.
  2. "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: Brain, Heart and Lung.

Entry informationi

Entry nameiLSM5_MOUSE
AccessioniPrimary (citable) accession number: P62322
Secondary accession number(s): A2RTT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.