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Q9Y4Z0

- LSM4_HUMAN

UniProt

Q9Y4Z0 - LSM4_HUMAN

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Protein
U6 snRNA-associated Sm-like protein LSm4
Gene
LSM4
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.

GO - Molecular functioni

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

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. RNA splicing Source: ProtInc
  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 LSm4
Alternative name(s):
Glycine-rich protein
Short name:
GRP
Gene namesi
Name:LSM4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17259. LSM4.

Subcellular locationi

Nucleus Reviewed prediction

GO - Cellular componenti

  1. U6 snRNP Source: ProtInc
  2. cytosol Source: Reactome
  3. small nuclear ribonucleoprotein complex Source: ProtInc
  4. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134906569.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139U6 snRNA-associated Sm-like protein LSm4
PRO_0000125564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y4Z0.
PaxDbiQ9Y4Z0.
PeptideAtlasiQ9Y4Z0.
PRIDEiQ9Y4Z0.

PTM databases

PhosphoSiteiQ9Y4Z0.

Expressioni

Gene expression databases

ArrayExpressiQ9Y4Z0.
BgeeiQ9Y4Z0.
CleanExiHS_LSM4.
GenevestigatoriQ9Y4Z0.

Organism-specific databases

HPAiHPA040932.

Interactioni

Subunit structurei

LSm subunits form a heteromer with a doughnut shape.

Binary interactionsi

WithEntry#Exp.IntActNotes
LSM7Q9UK456EBI-372521,EBI-348372
LSM8O957774EBI-372521,EBI-347779

Protein-protein interaction databases

BioGridi117336. 46 interactions.
DIPiDIP-31209N.
IntActiQ9Y4Z0. 16 interactions.
MINTiMINT-1469332.
STRINGi9606.ENSP00000252816.

Structurei

3D structure databases

ProteinModelPortaliQ9Y4Z0.
SMRiQ9Y4Z0. Positions 14-71.

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.

Phylogenomic databases

eggNOGiCOG1958.
HOGENOMiHOG000182713.
HOVERGENiHBG000486.
InParanoidiQ9Y4Z0.
KOiK12623.
OMAiWMNIHLV.
OrthoDBiEOG747PMG.
PhylomeDBiQ9Y4Z0.
TreeFamiTF315027.

Family and domain databases

InterProiIPR027141. LSm4/Sm_D1/D3.
IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PANTHERiPTHR23338. PTHR23338. 1 hit.
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y4Z0-1 [UniParc]FASTAAdd to Basket

« Hide

MLPLSLLKTA QNHPMLVELK NGETYNGHLV SCDNWMNINL REVICTSRDG    50
DKFWRMPECY IRGSTIKYLR IPDEIIDMVK EEVVAKGRGR GGLQQQKQQK 100
GRGMGGAGRG VFGGRGRGGI PGTGRGQPEK KPGRQAGKQ 139
Length:139
Mass (Da):15,350
Last modified:November 1, 1999 - v1
Checksum:iBCEFB20247335A1B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ238096 mRNA. Translation: CAB45867.1.
AF182290 mRNA. Translation: AAD56228.1.
AF117235 mRNA. Translation: AAF17216.1.
AF251218 mRNA. Translation: AAF90055.1.
BC000387 mRNA. Translation: AAH00387.1.
BC003652 mRNA. Translation: AAH03652.1.
BC022198 mRNA. Translation: AAH22198.1.
BC023665 mRNA. Translation: AAH23665.1.
CCDSiCCDS12374.1.
RefSeqiNP_036453.1. NM_012321.4.
UniGeneiHs.515255.

Genome annotation databases

EnsembliENST00000593829; ENSP00000469468; ENSG00000130520.
GeneIDi25804.
KEGGihsa:25804.
UCSCiuc002niq.3. human.

Polymorphism databases

DMDMi10720082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ238096 mRNA. Translation: CAB45867.1 .
AF182290 mRNA. Translation: AAD56228.1 .
AF117235 mRNA. Translation: AAF17216.1 .
AF251218 mRNA. Translation: AAF90055.1 .
BC000387 mRNA. Translation: AAH00387.1 .
BC003652 mRNA. Translation: AAH03652.1 .
BC022198 mRNA. Translation: AAH22198.1 .
BC023665 mRNA. Translation: AAH23665.1 .
CCDSi CCDS12374.1.
RefSeqi NP_036453.1. NM_012321.4.
UniGenei Hs.515255.

3D structure databases

ProteinModelPortali Q9Y4Z0.
SMRi Q9Y4Z0. Positions 14-71.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117336. 46 interactions.
DIPi DIP-31209N.
IntActi Q9Y4Z0. 16 interactions.
MINTi MINT-1469332.
STRINGi 9606.ENSP00000252816.

PTM databases

PhosphoSitei Q9Y4Z0.

Polymorphism databases

DMDMi 10720082.

Proteomic databases

MaxQBi Q9Y4Z0.
PaxDbi Q9Y4Z0.
PeptideAtlasi Q9Y4Z0.
PRIDEi Q9Y4Z0.

Protocols and materials databases

DNASUi 25804.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000593829 ; ENSP00000469468 ; ENSG00000130520 .
GeneIDi 25804.
KEGGi hsa:25804.
UCSCi uc002niq.3. human.

Organism-specific databases

CTDi 25804.
GeneCardsi GC19M018417.
HGNCi HGNC:17259. LSM4.
HPAi HPA040932.
MIMi 607284. gene.
neXtProti NX_Q9Y4Z0.
PharmGKBi PA134906569.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1958.
HOGENOMi HOG000182713.
HOVERGENi HBG000486.
InParanoidi Q9Y4Z0.
KOi K12623.
OMAi WMNIHLV.
OrthoDBi EOG747PMG.
PhylomeDBi Q9Y4Z0.
TreeFami TF315027.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi LSM4. human.
GeneWikii LSM4.
GenomeRNAii 25804.
NextBioi 47015.
PROi Q9Y4Z0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y4Z0.
Bgeei Q9Y4Z0.
CleanExi HS_LSM4.
Genevestigatori Q9Y4Z0.

Family and domain databases

InterProi IPR027141. LSm4/Sm_D1/D3.
IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view ]
PANTHERi PTHR23338. PTHR23338. 1 hit.
Pfami PF01423. LSM. 1 hit.
[Graphical view ]
SMARTi SM00651. Sm. 1 hit.
[Graphical view ]
SUPFAMi SSF50182. SSF50182. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: Liver.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hypothalamus.
  4. Chan E.K.L.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Lung.
  6. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-20, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Mammary carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLSM4_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4Z0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 126 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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