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Q9UK45

- LSM7_HUMAN

UniProt

Q9UK45 - LSM7_HUMAN

Protein

U6 snRNA-associated Sm-like protein LSm7

Gene

LSM7

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

    Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. U6 snRNA 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. mRNA metabolic process Source: Reactome
    4. mRNA processing Source: UniProtKB-KW
    5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    6. RNA metabolic process Source: Reactome
    7. RNA splicing Source: UniProtKB-KW

    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 LSm7
    Gene namesi
    Name:LSM7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:20470. LSM7.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134888612.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 103102U6 snRNA-associated Sm-like protein LSm7PRO_0000125579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UK45.
    PaxDbiQ9UK45.
    PRIDEiQ9UK45.

    PTM databases

    PhosphoSiteiQ9UK45.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UK45.
    BgeeiQ9UK45.
    CleanExiHS_LSM7.
    GenevestigatoriQ9UK45.

    Organism-specific databases

    HPAiHPA041850.

    Interactioni

    Subunit structurei

    LSm subunits form a heteromer with a doughnut shape. Also interacts with TACC1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM2Q9Y3335EBI-348372,EBI-347416
    LSM3P623104EBI-348372,EBI-348239
    LSM4Q9Y4Z06EBI-348372,EBI-372521
    LSM5Q9Y4Y95EBI-348372,EBI-373007
    LSM6P623124EBI-348372,EBI-373310
    SNRPD3P623183EBI-348372,EBI-372789
    TACC1O75410-14EBI-348372,EBI-624252
    TACC1O75410-62EBI-348372,EBI-624278

    Protein-protein interaction databases

    BioGridi119678. 29 interactions.
    DIPiDIP-31129N.
    IntActiQ9UK45. 22 interactions.
    MINTiMINT-1036641.
    STRINGi9606.ENSP00000252622.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UK45.
    SMRiQ9UK45. Positions 11-89.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the snRNP Sm proteins family.Curated

    Phylogenomic databases

    eggNOGiNOG276686.
    HOGENOMiHOG000223548.
    HOVERGENiHBG000513.
    KOiK12626.
    OMAiKPIRVKF.
    PhylomeDBiQ9UK45.
    TreeFamiTF314385.

    Family and domain databases

    InterProiIPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    IPR017132. U6_snRNA_Lsm7.
    [Graphical view]
    PfamiPF01423. LSM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037188. U6_snRNA_Lsm7. 1 hit.
    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.

    Q9UK45-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADKEKKKKE SILDLSKYID KTIRVKFQGG REASGILKGF DPLLNLVLDG    50
    TIEYMRDPDD QYKLTEDTRQ LGLVVCRGTS VVLICPQDGM EAIPNPFIQQ 100
    QDA 103
    Length:103
    Mass (Da):11,602
    Last modified:May 1, 2000 - v1
    Checksum:i7429DC0FB365C9C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF182293 mRNA. Translation: AAD56231.1.
    AC005258 Genomic DNA. Translation: AAG45442.1.
    BC018621 mRNA. Translation: AAH18621.1.
    CCDSiCCDS45907.1.
    RefSeqiNP_057283.1. NM_016199.2.
    UniGeneiHs.512610.

    Genome annotation databases

    EnsembliENST00000252622; ENSP00000252622; ENSG00000130332.
    GeneIDi51690.
    KEGGihsa:51690.
    UCSCiuc002lvp.4. human.

    Polymorphism databases

    DMDMi10720075.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF182293 mRNA. Translation: AAD56231.1 .
    AC005258 Genomic DNA. Translation: AAG45442.1 .
    BC018621 mRNA. Translation: AAH18621.1 .
    CCDSi CCDS45907.1.
    RefSeqi NP_057283.1. NM_016199.2.
    UniGenei Hs.512610.

    3D structure databases

    ProteinModelPortali Q9UK45.
    SMRi Q9UK45. Positions 11-89.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119678. 29 interactions.
    DIPi DIP-31129N.
    IntActi Q9UK45. 22 interactions.
    MINTi MINT-1036641.
    STRINGi 9606.ENSP00000252622.

    PTM databases

    PhosphoSitei Q9UK45.

    Polymorphism databases

    DMDMi 10720075.

    Proteomic databases

    MaxQBi Q9UK45.
    PaxDbi Q9UK45.
    PRIDEi Q9UK45.

    Protocols and materials databases

    DNASUi 51690.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252622 ; ENSP00000252622 ; ENSG00000130332 .
    GeneIDi 51690.
    KEGGi hsa:51690.
    UCSCi uc002lvp.4. human.

    Organism-specific databases

    CTDi 51690.
    GeneCardsi GC19M002321.
    HGNCi HGNC:20470. LSM7.
    HPAi HPA041850.
    MIMi 607287. gene.
    neXtProti NX_Q9UK45.
    PharmGKBi PA134888612.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276686.
    HOGENOMi HOG000223548.
    HOVERGENi HBG000513.
    KOi K12626.
    OMAi KPIRVKF.
    PhylomeDBi Q9UK45.
    TreeFami TF314385.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii LSM7.
    GenomeRNAii 51690.
    NextBioi 55694.
    PROi Q9UK45.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UK45.
    Bgeei Q9UK45.
    CleanExi HS_LSM7.
    Genevestigatori Q9UK45.

    Family and domain databases

    InterProi IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    IPR017132. U6_snRNA_Lsm7.
    [Graphical view ]
    Pfami PF01423. LSM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037188. U6_snRNA_Lsm7. 1 hit.
    SMARTi SM00651. Sm. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50182. SSF50182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: B-cell.
    4. "Carcinogenesis and translational controls: TACC1 is down-regulated in human cancers and associates with mRNA regulators."
      Conte N., Charafe-Jauffret E., Delaval B., Adelaide J., Ginestier C., Geneix J., Isnardon D., Jacquemier J., Birnbaum D.
      Oncogene 21:5619-5630(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TACC1.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLSM7_HUMAN
    AccessioniPrimary (citable) accession number: Q9UK45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 121 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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