LTN1

Protein-coding gene in the species Homo sapiens
LTN1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3J92

Identifiers
AliasesLTN1, C21orf10, C21orf98, RNF160, ZNF294, listerin E3 ubiquitin protein ligase 1
External IDsOMIM: 613083; MGI: 1926163; HomoloGene: 32272; GeneCards: LTN1; OMA:LTN1 - orthologs
Gene location (Human)
Chromosome 21 (human)
Chr.Chromosome 21 (human)[1]
Chromosome 21 (human)
Genomic location for LTN1
Genomic location for LTN1
Band21q21.3Start28,928,144 bp[1]
End28,992,956 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for LTN1
Genomic location for LTN1
Band16|16 C3.3Start87,173,539 bp[2]
End87,229,500 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • decidua

  • biceps brachii

  • endothelial cell

  • mucosa of sigmoid colon

  • Skeletal muscle tissue of biceps brachii

  • skin of thigh

  • skin of hip

  • Skeletal muscle tissue of rectus abdominis

  • tail of epididymis
Top expressed in
  • cumulus cell

  • seminiferous tubule

  • lacrimal gland

  • substantia nigra

  • pineal gland

  • parotid gland

  • spermatid

  • seminal vesicula

  • ascending aorta

  • aortic valve
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • zinc ion binding
  • protein binding
  • metal ion binding
  • ubiquitin protein ligase activity
  • ubiquitin-protein transferase activity
  • transferase activity
  • ribosomal large subunit binding
Cellular component
  • cytosol
  • RQC complex
Biological process
  • protein ubiquitination
  • protein autoubiquitination
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • rescue of stalled ribosome
  • ribosome-associated ubiquitin-dependent protein catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

26046

78913

Ensembl

ENSG00000198862

ENSMUSG00000052299

UniProt

O94822

Q6A009

RefSeq (mRNA)

NM_015565
NM_001320766

NM_001081068

RefSeq (protein)

NP_001307695
NP_056380

NP_001074537

Location (UCSC)Chr 21: 28.93 – 28.99 MbChr 16: 87.17 – 87.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Listerin E3 ubiquitin protein ligase 1 (LTN1), otherwise known as listerin, is a protein that in humans is encoded by the LTN1 gene.[5]

Function

Like most RING finger proteins, listerin functions as an E3 ubiquitin ligase.[6] Listerin is a component of the ribosome quality control complex.[7][8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198862 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052299 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: Listerin E3 ubiquitin protein ligase 1".
  6. ^ Chu J, Hong NA, Masuda CA, Jenkins BV, Nelms KA, Goodnow CC, Glynne RJ, Wu H, Masliah E, Joazeiro CA, Kay SA (February 2009). "A mouse forward genetics screen identifies LISTERIN as an E3 ubiquitin ligase involved in neurodegeneration". Proceedings of the National Academy of Sciences of the United States of America. 106 (7): 2097–103. doi:10.1073/pnas.0812819106. PMC 2650114. PMID 19196968.
  7. ^ Shao S, Brown A, Santhanam B, Hegde RS (February 2015). "Structure and assembly pathway of the ribosome quality control complex". Molecular Cell. 57 (3): 433–44. doi:10.1016/j.molcel.2014.12.015. PMC 4321881. PMID 25578875.
  8. ^ Shao S, von der Malsburg K, Hegde RS (June 2013). "Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation". Molecular Cell. 50 (5): 637–48. doi:10.1016/j.molcel.2013.04.015. PMC 3719020. PMID 23685075.

Further reading

  • Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR (2010). "Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score". Molecular Medicine. 16 (7–8): 247–53. doi:10.2119/molmed.2009.00159. PMC 2896464. PMID 20379614.
  • Shao S, Brown A, Santhanam B, Hegde RS (February 2015). "Structure and assembly pathway of the ribosome quality control complex". Molecular Cell. 57 (3): 433–44. doi:10.1016/j.molcel.2014.12.015. PMC 4321881. PMID 25578875.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.