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O15116

- LSM1_HUMAN

UniProt

O15116 - LSM1_HUMAN

Protein

U6 snRNA-associated Sm-like protein LSm1

Gene

LSM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Plays a role in replication-dependent histone mRNA degradation. Binds specifically to the 3'-terminal U-tract of U6 snRNA.1 Publication

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    2. gene expression Source: Reactome
    3. histone mRNA catabolic process Source: UniProtKB
    4. mRNA metabolic process Source: Reactome
    5. mRNA processing Source: ProtInc
    6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    7. RNA metabolic process Source: Reactome
    8. RNA splicing Source: ProtInc
    9. RNA splicing, via transesterification reactions Source: UniProtKB

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U6 snRNA-associated Sm-like protein LSm1
    Alternative name(s):
    Cancer-associated Sm-like
    Small nuclear ribonuclear CaSm
    Gene namesi
    Name:LSM1
    Synonyms:CASM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:20472. LSM1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: Reactome
    3. nucleus Source: MGI
    4. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134864226.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 133133U6 snRNA-associated Sm-like protein LSm1PRO_0000125554Add
    BLAST

    Proteomic databases

    MaxQBiO15116.
    PaxDbiO15116.
    PeptideAtlasiO15116.
    PRIDEiO15116.

    PTM databases

    PhosphoSiteiO15116.

    Expressioni

    Tissue specificityi

    Has elevated expression in pancreatic cancer and in several cancer-derived cell lines.

    Gene expression databases

    ArrayExpressiO15116.
    BgeeiO15116.
    CleanExiHS_LSM1.
    GenevestigatoriO15116.

    Organism-specific databases

    HPAiHPA024601.

    Interactioni

    Subunit structurei

    Interacts with SLBP. Interaction with SLBP occurs when histone mRNA is being rapidly degraded during the S phase. LSm subunits form a heteromer with a doughnut shape.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM2Q9Y3333EBI-347619,EBI-347416
    LSM3P623103EBI-347619,EBI-348239

    Protein-protein interaction databases

    BioGridi118104. 34 interactions.
    DIPiDIP-31130N.
    IntActiO15116. 20 interactions.
    MINTiMINT-1036791.
    STRINGi9606.ENSP00000310596.

    Structurei

    3D structure databases

    ProteinModelPortaliO15116.
    SMRiO15116. Positions 7-123.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the snRNP Sm proteins family.Curated

    Phylogenomic databases

    eggNOGiNOG236501.
    HOGENOMiHOG000223544.
    HOVERGENiHBG027238.
    InParanoidiO15116.
    KOiK12620.
    OMAiFHQTVER.
    OrthoDBiEOG7N8ZXQ.
    PhylomeDBiO15116.
    TreeFamiTF105846.

    Family and domain databases

    InterProiIPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view]
    PfamiPF01423. LSM. 1 hit.
    [Graphical view]
    SMARTiSM00651. Sm. 1 hit.
    [Graphical view]
    SUPFAMiSSF50182. SSF50182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O15116-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNYMPGTASL IEDIDKKHLV LLRDGRTLIG FLRSIDQFAN LVLHQTVERI    50
    HVGKKYGDIP RGIFVVRGEN VVLLGEIDLE KESDTPLQQV SIEEILEEQR 100
    VEQQTKLEAE KLKVQALKDR GLSIPRADTL DEY 133
    Length:133
    Mass (Da):15,179
    Last modified:January 1, 1998 - v1
    Checksum:iFF798CDA9447037A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000177 mRNA. Translation: AAB62189.1.
    AJ238094 mRNA. Translation: CAB45865.1.
    AK312159 mRNA. Translation: BAG35093.1.
    CH471080 Genomic DNA. Translation: EAW63332.1.
    BC001767 mRNA. Translation: AAH01767.1.
    CCDSiCCDS6103.1.
    RefSeqiNP_055277.1. NM_014462.2.
    UniGeneiHs.425311.

    Genome annotation databases

    EnsembliENST00000311351; ENSP00000310596; ENSG00000175324.
    GeneIDi27257.
    KEGGihsa:27257.
    UCSCiuc003xkw.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000177 mRNA. Translation: AAB62189.1 .
    AJ238094 mRNA. Translation: CAB45865.1 .
    AK312159 mRNA. Translation: BAG35093.1 .
    CH471080 Genomic DNA. Translation: EAW63332.1 .
    BC001767 mRNA. Translation: AAH01767.1 .
    CCDSi CCDS6103.1.
    RefSeqi NP_055277.1. NM_014462.2.
    UniGenei Hs.425311.

    3D structure databases

    ProteinModelPortali O15116.
    SMRi O15116. Positions 7-123.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118104. 34 interactions.
    DIPi DIP-31130N.
    IntActi O15116. 20 interactions.
    MINTi MINT-1036791.
    STRINGi 9606.ENSP00000310596.

    PTM databases

    PhosphoSitei O15116.

    Proteomic databases

    MaxQBi O15116.
    PaxDbi O15116.
    PeptideAtlasi O15116.
    PRIDEi O15116.

    Protocols and materials databases

    DNASUi 27257.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311351 ; ENSP00000310596 ; ENSG00000175324 .
    GeneIDi 27257.
    KEGGi hsa:27257.
    UCSCi uc003xkw.3. human.

    Organism-specific databases

    CTDi 27257.
    GeneCardsi GC08M038020.
    HGNCi HGNC:20472. LSM1.
    HPAi HPA024601.
    MIMi 607281. gene.
    neXtProti NX_O15116.
    PharmGKBi PA134864226.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236501.
    HOGENOMi HOG000223544.
    HOVERGENi HBG027238.
    InParanoidi O15116.
    KOi K12620.
    OMAi FHQTVER.
    OrthoDBi EOG7N8ZXQ.
    PhylomeDBi O15116.
    TreeFami TF105846.

    Enzyme and pathway databases

    Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Miscellaneous databases

    GeneWikii LSM1.
    GenomeRNAii 27257.
    NextBioi 50202.
    PROi O15116.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15116.
    Bgeei O15116.
    CleanExi HS_LSM1.
    Genevestigatori O15116.

    Family and domain databases

    InterProi IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view ]
    Pfami PF01423. LSM. 1 hit.
    [Graphical view ]
    SMARTi SM00651. Sm. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50182. SSF50182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "CaSm: an Sm-like protein that contributes to the transformed state in cancer cells."
      Schweinfest C.W., Graber M.W., Chapman J.M., Papas T.S., Baron P.L., Watson D.K.
      Cancer Res. 57:2961-2965(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Lymph node.
    3. "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., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Substantia nigra.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Eye.
    6. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
      Mullen T.E., Marzluff W.F.
      Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY, INTERACTION WITH SLBP.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLSM1_HUMAN
    AccessioniPrimary (citable) accession number: O15116
    Secondary accession number(s): B2R5E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3