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Q9UK45

- LSM7_HUMAN

UniProt

Q9UK45 - LSM7_HUMAN

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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

Functioni

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

GO - Molecular functioni

  1. U6 snRNA binding Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. RNA splicing Source: UniProtKB-KW
  3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  4. gene expression Source: Reactome
  5. mRNA metabolic process Source: Reactome
  6. mRNA processing Source: UniProtKB-KW
  7. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
Complete GO annotation...

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 Reviewed prediction

GO - Cellular componenti

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

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 LSm7
PRO_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. 21 interactions.
MINTiMINT-1036641.
STRINGi9606.ENSP00000252622.

Structurei

3D structure databases

ProteinModelPortaliQ9UK45.
SMRiQ9UK45. Positions 11-89.

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.

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. 21 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 120 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

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