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Protein

U6 snRNA-associated Sm-like protein LSm7

Gene

LSM7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • U6 snRNA binding Source: UniProtKB

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

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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:20470. LSM7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134888612.

Polymorphism and mutation databases

BioMutaiLSM7.
DMDMi10720075.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 103102U6 snRNA-associated Sm-like protein LSm7PRO_0000125579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9UK45.
MaxQBiQ9UK45.
PaxDbiQ9UK45.
PRIDEiQ9UK45.
TopDownProteomicsiQ9UK45.

PTM databases

iPTMnetiQ9UK45.
PhosphoSiteiQ9UK45.

Expressioni

Gene expression databases

BgeeiQ9UK45.
CleanExiHS_LSM7.
ExpressionAtlasiQ9UK45. baseline and differential.
GenevisibleiQ9UK45. HS.

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
DDIT4LQ96D033EBI-348372,EBI-742054
LSM2Q9Y3335EBI-348372,EBI-347416
LSM3P623104EBI-348372,EBI-348239
LSM4Q9Y4Z06EBI-348372,EBI-372521
LSM5Q9Y4Y910EBI-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. 39 interactions.
DIPiDIP-31129N.
IntActiQ9UK45. 23 interactions.
MINTiMINT-1036641.
STRINGi9606.ENSP00000252622.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JCRelectron microscopy7.0071-103[»]
ProteinModelPortaliQ9UK45.
SMRiQ9UK45. Positions 11-89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

eggNOGiKOG1781. Eukaryota.
ENOG4111VMJ. LUCA.
GeneTreeiENSGT00510000047872.
HOGENOMiHOG000223548.
HOVERGENiHBG000513.
InParanoidiQ9UK45.
KOiK12626.
OMAiDNTTEFL.
PhylomeDBiQ9UK45.
TreeFamiTF314385.

Family and domain databases

InterProiIPR017132. Lsm7/snRNP-G.
IPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[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

        10         20         30         40         50
MADKEKKKKE SILDLSKYID KTIRVKFQGG REASGILKGF DPLLNLVLDG
60 70 80 90 100
TIEYMRDPDD QYKLTEDTRQ LGLVVCRGTS VVLICPQDGM EAIPNPFIQQ

QDA
Length:103
Mass (Da):11,602
Last modified:May 1, 2000 - v1
Checksum:i7429DC0FB365C9C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JCRelectron microscopy7.0071-103[»]
ProteinModelPortaliQ9UK45.
SMRiQ9UK45. Positions 11-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119678. 39 interactions.
DIPiDIP-31129N.
IntActiQ9UK45. 23 interactions.
MINTiMINT-1036641.
STRINGi9606.ENSP00000252622.

PTM databases

iPTMnetiQ9UK45.
PhosphoSiteiQ9UK45.

Polymorphism and mutation databases

BioMutaiLSM7.
DMDMi10720075.

Proteomic databases

EPDiQ9UK45.
MaxQBiQ9UK45.
PaxDbiQ9UK45.
PRIDEiQ9UK45.
TopDownProteomicsiQ9UK45.

Protocols and materials databases

DNASUi51690.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252622; ENSP00000252622; ENSG00000130332.
GeneIDi51690.
KEGGihsa:51690.
UCSCiuc002lvp.5. human.

Organism-specific databases

CTDi51690.
GeneCardsiLSM7.
HGNCiHGNC:20470. LSM7.
HPAiHPA041850.
MIMi607287. gene.
neXtProtiNX_Q9UK45.
PharmGKBiPA134888612.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1781. Eukaryota.
ENOG4111VMJ. LUCA.
GeneTreeiENSGT00510000047872.
HOGENOMiHOG000223548.
HOVERGENiHBG000513.
InParanoidiQ9UK45.
KOiK12626.
OMAiDNTTEFL.
PhylomeDBiQ9UK45.
TreeFamiTF314385.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikiiLSM7.
GenomeRNAii51690.
NextBioi55694.
PROiQ9UK45.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UK45.
CleanExiHS_LSM7.
ExpressionAtlasiQ9UK45. baseline and differential.
GenevisibleiQ9UK45. HS.

Family and domain databases

InterProiIPR017132. Lsm7/snRNP-G.
IPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037188. U6_snRNA_Lsm7. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [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: May 11, 2016
This is version 138 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.